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Enzyme 1
[top]
|
| Enzyme 1 ID |
5639 |
| Enzyme 1 Name |
Histone-lysine N-methyltransferase, H3 lysine-79 specific |
| Enzyme 1 Synonyms |
- DOT1-like protein
- Histone H3-K79 methyltransferase
- H3-K79-HMTase
- Lysine N-methyltransferase 4
|
| Enzyme 1 Gene Name |
DOT1L |
| Enzyme 1 Protein Sequence |
>Histone-lysine N-methyltransferase, H3 lysine-79 specific
MGEKLELRLKSPVGAEPAVYPWPLPVYDKHHDAAHEIIETIRWVCEEIPDLKLAMENYVL
IDYDTKSFESMQRLCDKYNRAIDSIHQLWKGTTQPMKLNTRPSTGLLRHILQQVYNHSVT
DPEKLNNYEPFSPEVYGETSFDLVAQMIDEIKMTDDDLFVDLGSGVGQVVLQVAAATNCK
HHYGVEKADIPAKYAETMDREFRKWMKWYGKKHAEYTLERGDFLSEEWRERIANTSVIFV
NNFAFGPEVDHQLKERFANMKEGGRIVSSKPFAPLNFRINSRNLSDIGTIMRVVELSPLK
GSVSWTGKPVSYYLHTIDRTILENYFSSLKNPKLREEQEAARRRQQRESKSNAATPTKGP
EGKVAGPADAPMDSGAEEEKAGAATVKKPSPSKARKKKLNKKGRKMAGRKRGRPKKMNTA
NPERKPKKNQTALDALHAQTVSQTAASSPQDAYRSPHSPFYQLPPSVQRHSPNPLLVAPT
PPALQKLLESFKIQYLQFLAYTKTPQYKASLQELLGQEKEKNAQLLGAAQQLLSHCQAQK
EEIRRLFQQKLDELGVKALTYNDLIQAQKEISAHNQQLREQSEQLEQDNRALRGQSLQLL
KARCEELQLDWATLSLEKLLKEKQALKSQISEKQRHCLELQISIVELEKSQRQQELLQLK
SCVPPDDALSLHLRGKGALGRELEPDASRLHLELDCTKFSLPHLSSMSPELSMNGQAAGY
ELCGVLSRPSSKQNTPQYLASPLDQEVVPCTPSHVGRPRLEKLSGLAAPDYTRLSPAKIV
LRRHLSQDHTVPGRPAASELHSRAEHTKENGLPYQSPSVPGSMKLSPQDPRPLSPGALQL
AGEKSSEKGLRERAYGSSGELITSLPISIPLSTVQPNKLPVSIPLASVVLPSRAERARST
PSPVLQPRDPSSTLEKQIGANAHGAGSRSLALAPAGFSYAGSVAISGALAGSPASLTPGA
EPATLDESSSSGSLFATVGSRSSTPQHPLLLAQPRNSLPASPAHQLSSSPRLGGAAQGPL
PEASKGDLPSDSGFSDPESEAKRRIVFTITTGAGSAKQSPSSKHSPLTASARGDCVPSHG
QDSRRRGRRKRASAGTPSLSAGVSPKRRALPSVAGLFTQPSGSPLNLNSMVSNINQPLEI
TAISSPETSLKSSPVPYQDHDQPPVLKKERPLSQTNGAHYSPLTSDEEPGSEDEPSSARI
ERKIATISLESKSPPKTLENGGGLAGRKPAPAGEPVNSSKWKSTFSPISDIGLAKSADSP
LQASSALSQNSLFTFRPALEEPSADAKLAAHPRKGFPGSLSGADGLSPGTNPANGCTFGG
GLAADLSLHSFSDGASLPHKGPEAAGLSSPLSFPSQRGKEGSDANPFLSKRQLDGLAGLK
GEGSRGKEAGEGGLPLCGPTDKTPLLSGKAAKARDREVDLKNGHNLFISAAAVPPGSLLS
GPGLAPAASSAGGAASSAQTHRSFLGPFPPGPQFALGPMSLQANLGSVAGSSVLQSLFSS
VPAAAGLVHVSSAATRLTNSHAMGSFSGVAGGTVGGVVFNHAVPSASAHPFGARVGRGAA
CGSATLGPSPLQAAASASASSFQAPASVETRPPPPPPPPPPPLPPPAHLGRSPAGPPVLH
APPPPNAALPPPPTLLASNPEPALLQSLASLPPNQAFLPPTSAASLPPANASLSIKLTSL
PHKGARPSFTVHHQPLPRLALAQAAPGIPQASATGPSAVWVSLGMPPPYAAHLSGVKPR
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| Enzyme 1 Number of Residues |
1739 |
| Enzyme 1 Molecular Weight |
184851.2 |
| Enzyme 1 Theoretical pI |
9.88 |
| Enzyme 1 GO Classification |
| Function |
- DNA binding
- binding
- catalytic activity
- histone-lysine N-methyltransferase activity
- methyltransferase activity
- nucleic acid binding
- protein methyltransferase activity
- protein-lysine N-methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in DNA binding |
| Enzyme 1 Specific Function |
Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. Binds to DNA |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
22094135  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q8TEK3  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
DOT1L_HUMAN  |
| Enzyme 1 PDB ID |
1NW3  |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
Not Available |
| Enzyme 1 GenBank Gene ID |
Not Available |
| Enzyme 1 GeneCard ID |
DOT1L  |
| Enzyme 1 GenAtlas ID |
DOT1L  |
| Enzyme 1 HGNC ID |
HGNC:24948  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
19p13.3 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Feng Q, Wang H, Ng HH, Erdjument-Bromage H, Tempst P, Struhl K, Zhang Y: Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain. Curr Biol. 2002 Jun 25;12(12):1052-8. [PubMed
]
- Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed
]
- Nagase T, Nakayama M, Nakajima D, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2001 Apr 27;8(2):85-95. [PubMed
]
- Jikuya H, Takano J, Kikuno R, Hirosawa M, Nagase T, Nomura N, Ohara O: Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones. DNA Res. 2003 Feb 28;10(1):49-57. [PubMed
]
- Okada Y, Feng Q, Lin Y, Jiang Q, Li Y, Coffield VM, Su L, Xu G, Zhang Y: hDOT1L links histone methylation to leukemogenesis. Cell. 2005 Apr 22;121(2):167-78. [PubMed
]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed
]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
- Min J, Feng Q, Li Z, Zhang Y, Xu RM: Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase. Cell. 2003 Mar 7;112(5):711-23. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
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Enzyme 2
[top]
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| Enzyme 2 ID |
5641 |
| Enzyme 2 Name |
Histone-lysine N-methyltransferase SETD7 |
| Enzyme 2 Synonyms |
- Histone H3-K4 methyltransferase SETD7
- H3-K4-HMTase SETD7
- Lysine N-methyltransferase 7
- SET domain-containing protein 7
- SET7/9
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| Enzyme 2 Gene Name |
SETD7 |
| Enzyme 2 Protein Sequence |
>Histone-lysine N-methyltransferase SETD7
MDSDDEMVEEAVEGHLDDDGLPHGFCTVTYSSTDRFEGNFVHGEKNGRGKFFFFDGSTLE
GYYVDDALQGQGVYTYEDGGVLQGTYVDGELNGPAQEYDTDGRLIFKGQYKDNIRHGVCW
IYYPDGGSLVGEVNEDGEMTGEKIAYVYPDERTALYGKFIDGEMIEGKLATLMSTEEGRP
HFELMPGNSVYHFDKSTSSCISTNALLPDPYESERVYVAESLISSAGEGLFSKVAVGPNT
VMSFYNGVRITHQEVDSRDWALNGNTLSLDEETVIDVPEPYNHVSKYCASLGHKANHSFT
PNCIYDMFVHPRFGPIKCIRTLRAVEADEELTVAYGYDHSPPGKSGPEAPEWYQVELKAF
QATQQK
|
| Enzyme 2 Number of Residues |
366 |
| Enzyme 2 Molecular Weight |
40720.6 |
| Enzyme 2 Theoretical pI |
4.25 |
| Enzyme 2 GO Classification |
| Function |
- catalytic activity
- histone-lysine N-methyltransferase activity
- methyltransferase activity
- protein methyltransferase activity
- protein-lysine N-methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- biological regulation
- cellular component organization at cellular level
- cellular process
- chromatin modification
- chromatin organization
- chromosome organization
- organelle organization
- regulation of biological process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
- regulation of transcription, DNA-dependent
|
| Component |
- chromosome
- intracellular non-membrane-bounded organelle
- non-membrane-bounded organelle
- organelle
|
|
| Enzyme 2 General Function |
Involved in histone-lysine N-methyltransferase activity |
| Enzyme 2 Specific Function |
Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation. Also able to demethylated 'Lys-372' of p53/TP53 in vitro |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
Not Available |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q8WTS6  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
SETD7_HUMAN  |
| Enzyme 2 PDB ID |
1N6C  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1101 bp
ATGGATAGCGACGACGAGATGGTGGAGGAGGCGGTGGAAGGGCACCTGGACGATGACGGA
TTACCGCACGGGTTCTGCACAGTCACCTACTCCTCCACAGACAGATTTGAGGGGAACTTT
GTTCACGGAGAAAAGAACGGACGGGGGAAGTTCTTCTTCTTTGATGGCAGCACCCTGGAG
GGGTATTATGTGGATGATGCCTTGCAGGGCCAGGGAGTTTACACTTACGAAGATGGGGGA
GTTCTCCAGGGCACGTATGTAGACGGAGAGCTGAACGGTCCAGCCCAGGAATATGACACA
GATGGGAGACTGATCTTCAAGGGGCAGTATAAAGATAACATTCGTCATGGAGTGTGCTGG
ATATATTACCCAGATGGAGGAAGCCTTGTAGGAGAAGTAAATGAAGATGGGGAGATGACT
GGAGAGAAGATAGCCTATGTGTACCCTGATGAGAGGACCGCACTTTATGGGAAATTTATT
GATGGAGAGATGATAGAAGGCAAACTGGCTACCCTTATGTCCACTGAAGAAGGGAGGCCT
CACTTTGAACTGATGCCTGGAAATTCAGTGTACCACTTTGATAAGTCGACTTCATCTTGC
ATTTCTACCAATGCTCTTCTTCCAGATCCTTATGAATCAGAAAGGGTTTATGTTGCTGAA
TCTCTTATTTCCAGTGCTGGAGAAGGACTTTTTTCAAAGGTAGCTGTGGGACCTAATACT
GTTATGTCTTTTTATAATGGAGTTCGAATTACACACCAAGAGGTTGACAGCAGGGACTGG
GCCCTTAATGGGAACACCCTCTCCCTTGATGAAGAAACGGTCATTGATGTGCCTGAGCCC
TATAACCACGTATCCAAGTACTGTGCCTCCTTGGGACACAAGGCAAATCACTCCTTCACT
CCAAACTGCATCTACGATATGTTTGTCCACCCCCGTTTTGGGCCCATCAAATGCATCCGC
ACCCTGAGAGCAGTGGAGGCCGATGAAGAGCTCACCGTTGCCTATGGCTATGACCACAGC
CCCCCCGGGAAGAGTGGGCCTGAAGCCCCTGAGTGGTACCAGGTGGAGCTGAAGGCCTTC
CAGGCCACCCAGCAAAAGTGA
|
| Enzyme 2 GenBank Gene ID |
AF448510  |
| Enzyme 2 GeneCard ID |
SETD7  |
| Enzyme 2 GenAtlas ID |
SETD7  |
| Enzyme 2 HGNC ID |
HGNC:30412  |
| Enzyme 2 Chromosome Location |
4 |
| Enzyme 2 Locus |
4q28 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Wang H, Cao R, Xia L, Erdjument-Bromage H, Borchers C, Tempst P, Zhang Y: Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase. Mol Cell. 2001 Dec;8(6):1207-17. [PubMed
]
- Nishioka K, Chuikov S, Sarma K, Erdjument-Bromage H, Allis CD, Tempst P, Reinberg D: Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. Genes Dev. 2002 Feb 15;16(4):479-89. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Nagase T, Kikuno R, Hattori A, Kondo Y, Okumura K, Ohara O: Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Dec 31;7(6):347-55. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Martens JH, Verlaan M, Kalkhoven E, Zantema A: Cascade of distinct histone modifications during collagenase gene activation. Mol Cell Biol. 2003 Mar;23(5):1808-16. [PubMed
]
- Kouskouti A, Scheer E, Staub A, Tora L, Talianidis I: Gene-specific modulation of TAF10 function by SET9-mediated methylation. Mol Cell. 2004 Apr 23;14(2):175-82. [PubMed
]
- Francis J, Chakrabarti SK, Garmey JC, Mirmira RG: Pdx-1 links histone H3-Lys-4 methylation to RNA polymerase II elongation during activation of insulin transcription. J Biol Chem. 2005 Oct 28;280(43):36244-53. Epub 2005 Sep 1. [PubMed
]
- Huang J, Perez-Burgos L, Placek BJ, Sengupta R, Richter M, Dorsey JA, Kubicek S, Opravil S, Jenuwein T, Berger SL: Repression of p53 activity by Smyd2-mediated methylation. Nature. 2006 Nov 30;444(7119):629-32. Epub 2006 Nov 15. [PubMed
]
- Hu P, Zhang Y: Catalytic mechanism and product specificity of the histone lysine methyltransferase SET7/9: an ab initio QM/MM-FE study with multiple initial structures. J Am Chem Soc. 2006 Feb 1;128(4):1272-8. [PubMed
]
- Wilson JR, Jing C, Walker PA, Martin SR, Howell SA, Blackburn GM, Gamblin SJ, Xiao B: Crystal structure and functional analysis of the histone methyltransferase SET7/9. Cell. 2002 Oct 4;111(1):105-15. [PubMed
]
- Jacobs SA, Harp JM, Devarakonda S, Kim Y, Rastinejad F, Khorasanizadeh S: The active site of the SET domain is constructed on a knot. Nat Struct Biol. 2002 Nov;9(11):833-8. [PubMed
]
- Xiao B, Jing C, Wilson JR, Walker PA, Vasisht N, Kelly G, Howell S, Taylor IA, Blackburn GM, Gamblin SJ: Structure and catalytic mechanism of the human histone methyltransferase SET7/9. Nature. 2003 Feb 6;421(6923):652-6. Epub 2003 Jan 22. [PubMed
]
- Kwon T, Chang JH, Kwak E, Lee CW, Joachimiak A, Kim YC, Lee J, Cho Y: Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet. EMBO J. 2003 Jan 15;22(2):292-303. [PubMed
]
- Chuikov S, Kurash JK, Wilson JR, Xiao B, Justin N, Ivanov GS, McKinney K, Tempst P, Prives C, Gamblin SJ, Barlev NA, Reinberg D: Regulation of p53 activity through lysine methylation. Nature. 2004 Nov 18;432(7015):353-60. Epub 2004 Nov 3. [PubMed
]
- Couture JF, Collazo E, Hauk G, Trievel RC: Structural basis for the methylation site specificity of SET7/9. Nat Struct Mol Biol. 2006 Feb;13(2):140-6. Epub 2006 Jan 15. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5647 |
| Enzyme 3 Name |
Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific |
| Enzyme 3 Synonyms |
- Androgen receptor coactivator 267 kDa protein
- Androgen receptor-associated protein of 267 kDa
- H3-K36-HMTase
- H4-K20-HMTase
- Lysine N-methyltransferase 3B
- Nuclear receptor-binding SET domain-containing protein 1
- NR-binding SET domain-containing protein
|
| Enzyme 3 Gene Name |
NSD1 |
| Enzyme 3 Protein Sequence |
>Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific
MDQTCELPRRNCLLPFSNPVNLDAPEDKDSPFGNGQSNFSEPLNGCTMQLSTVSGTSQNA
YGQDSPSCYIPLRRLQDLASMINVEYLNGSADGSESFQDPEKSDSRAQTPIVCTSLSPGG
PTALAMKQEPSCNNSPELQVKVTKTIKNGFLHFENFTCVDDADVDSEMDPEQPVTEDESI
EEIFEETQTNATCNYETKSENGVKVAMGSEQDSTPESRHGAVKSPFLPLAPQTETQKNKQ
RNEVDGSNEKAALLPAPFSLGDTNITIEEQLNSINLSFQDDPDSSTSTLGNMLELPGTSS
SSTSQELPFCQPKKKSTPLKYEVGDLIWAKFKRRPWWPCRICSDPLINTHSKMKVSNRRP
YRQYYVEAFGDPSERAWVAGKAIVMFEGRHQFEELPVLRRRGKQKEKGYRHKVPQKILSK
WEASVGLAEQYDVPKGSKNRKCIPGSIKLDSEEDMPFEDCTNDPESEHDLLLNGCLKSLA
FDSEHSADEKEKPCAKSRARKSSDNPKRTSVKKGHIQFEAHKDERRGKIPENLGLNFISG
DISDTQASNELSRIANSLTGSNTAPGSFLFSSCGKNTAKKEFETSNGDSLLGLPEGALIS
KCSREKNKPQRSLVCGSKVKLCYIGAGDEEKRSDSISICTTSDDGSSDLDPIEHSSESDN
SVLEIPDAFDRTENMLSMQKNEKIKYSRFAATNTRVKAKQKPLISNSHTDHLMGCTKSAE
PGTETSQVNLSDLKASTLVHKPQSDFTNDALSPKFNLSSSISSENSLIKGGAANQALLHS
KSKQPKFRSIKCKHKENPVMAEPPVINEECSLKCCSSDTKGSPLASISKSGKVDGLKLLN
NMHEKTRDSSDIETAVVKHVLSELKELSYRSLGEDVSDSGTSKPSKPLLFSSASSQNHIP
IEPDYKFSTLLMMLKDMHDSKTKEQRLMTAQNLVSYRSPGRGDCSTNSPVGVSKVLVSGG
STHNSEKKGDGTQNSANPSPSGGDSALSGELSASLPGLLSDKRDLPASGKSRSDCVTRRN
CGRSKPSSKLRDAFSAQMVKNTVNRKALKTERKRKLNQLPSVTLDAVLQGDRERGGSLRG
GAEDPSKEDPLQIMGHLTSEDGDHFSDVHFDSKVKQSDPGKISEKGLSFENGKGPELDSV
MNSENDELNGVNQVVPKKRWQRLNQRRTKPRKRMNRFKEKENSECAFRVLLPSDPVQEGR
DEFPEHRTPSASILEEPLTEQNHADCLDSAGPRLNVCDKSSASIGDMEKEPGIPSLTPQA
ELPEPAVRSEKKRLRKPSKWLLEYTEEYDQIFAPKKKQKKVQEQVHKVSSRCEEESLLAR
GRSSAQNKQVDENSLISTKEEPPVLEREAPFLEGPLAQSELGGGHAELPQLTLSVPVAPE
VSPRPALESEELLVKTPGNYESKRQRKPTKKLLESNDLDPGFMPKKGDLGLSKKCYEAGH
LENGITESCATSYSKDFGGGTTKIFDKPRKRKRQRHAAAKMQCKKVKNDDSSKEIPGSEG
ELMPHRTATSPKETVEEGVEHDPGMPASKKMQGERGGGAALKENVCQNCEKLGELLLCEA
QCCGAFHLECLGLTEMPRGKFICNECRTGIHTCFVCKQSGEDVKRCLLPLCGKFYHEECV
QKYPPTVMQNKGFRCSLHICITCHAANPANVSASKGRLMRCVRCPVAYHANDFCLAAGSK
ILASNSIICPNHFTPRRGCRNHEHVNVSWCFVCSEGGSLLCCDSCPAAFHRECLNIDIPE
GNWYCNDCKAGKKPHYREIVWVKVGRYRWWPAEICHPRAVPSNIDKMRHDVGEFPVLFFG
SNDYLWTHQARVFPYMEGDVSSKDKMGKGVDGTYKKALQEAAARFEELKAQKELRQLQED
RKNDKKPPPYKHIKVNRPIGRVQIFTADLSEIPRCNCKATDENPCGIDSECINRMLLYEC
HPTVCPAGGRCQNQCFSKRQYPEVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEE
CRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMNHCCQPNCETQKWSVNGDTRV
GLFALSDIKAGTELTFNYNLECLGNGKTVCKCGAPNCSGFLGVRPKNQPIATEEKSKKFK
KKQQGKRRTQGEITKEREDECFSCGDAGQLVSCKKPGCPKVYHADCLNLTKRPAGKWECP
WHQCDICGKEAASFCEMCPSSFCKQHREGMLFISKLDGRLSCTEHDPCGPNPLEPGEIRE
YVPPPVPLPPGPSTHLAEQSTGMAAQAPKMSDKPPADTNQMLSLSKKALAGTCQRPLLPE
RPLERTDSRPQPLDKVRDLAGSGTKSQSLVSSQRPLDRPPAVAGPRPQLSDKPSPVTSPS
SSPSVRSQPLERPLGTADPRLDKSIGAASPRPQSLEKTSVPTGLRLPPPDRLLITSSPKP
QTSDRPTDKPHASLSQRLPPPEKVLSAVVQTLVAKEKALRPVDQNTQSKNRAALVMDLID
LTPRQKERAASPHQVTPQADEKMPVLESSSWPASKGLGHMPRAVEKGCVSDPLQTSGKAA
APSEDPWQAVKSLTQARLLSQPPAKAFLYEPTTQASGRASAGAEQTPGPLSQSPGLVKQA
KQMVGGQQLPALAAKSGQSFRSLGKAPASLPTEEKKLVTTEQSPWALGKASSRAGLWPIV
AGQTLAQSCWSAGSTQTLAQTCWSLGRGQDPKPEQNTLPALNQAPSSHKCAESEQK
|
| Enzyme 3 Number of Residues |
2696 |
| Enzyme 3 Molecular Weight |
296649.3 |
| Enzyme 3 Theoretical pI |
8.08 |
| Enzyme 3 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- histone-lysine N-methyltransferase activity
- ion binding
- metal ion binding
- methyltransferase activity
- protein binding
- protein methyltransferase activity
- protein-lysine N-methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
- transition metal ion binding
- zinc ion binding
|
| Process |
| — |
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 3 General Function |
Involved in histone-lysine N-methyltransferase activity |
| Enzyme 3 Specific Function |
Histone methyltransferase. Preferentially methylates 'Lys-36' of histone H3 and 'Lys-20' of histone H4 (in vitro). Transcriptional intermediary factor capable of both negatively or positively influencing transcription, depending on the cellular context |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
19923586  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q96L73  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
NSD1_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>8091 bp
ATGGATCAGACCTGTGAACTACCCAGAAGAAATTGTCTGCTGCCCTTTTCCAATCCAGTG
AATTTAGATGCCCCTGAAGACAAGGACAGCCCTTTCGGTAATGGTCAATCCAATTTTTCT
GAGCCACTTAATGGGTGTACTATGCAGTTATCGACTGTCAGTGGAACATCCCAAAATGCT
TATGGACAAGATTCTCCATCTTGTTACATTCCACTGCGGAGACTACAGGATTTGGCCTCC
ATGATCAATGTAGAGTATTTAAATGGGTCTGCTGATGGATCAGAATCCTTTCAAGACCCT
GAAAAAAGTGATTCAAGAGCTCAGACGCCAATTGTTTGCACTTCCTTGAGTCCTGGTGGT
CCTACAGCACTTGCTATGAAACAGGAACCCTCTTGTAATAACTCCCCTGAACTCCAGGTA
AAAGTAACAAAGACTATCAAGAATGGCTTTCTGCACTTTGAGAATTTTACTTGTGTGGAC
GATGCAGATGTAGATTCTGAAATGGACCCAGAACAGCCAGTCACAGAGGATGAGAGTATA
GAGGAGATCTTTGAGGAAACTCAGACCAATGCCACCTGCAATTATGAGACTAAATCAGAG
AATGGTGTAAAAGTGGCCATGGGAAGTGAACAAGACAGCACACCAGAGAGTAGACACGGT
GCAGTCAAATCGCCATTCTTGCCATTAGCTCCTCAGACTGAAACACAGAAAAATAAGCAA
AGAAATGAAGTGGACGGCAGCAATGAAAAAGCAGCCCTTCTCCCAGCCCCCTTTTCACTA
GGAGACACAAACATTACAATAGAAGAGCAATTAAACTCAATAAATTTATCTTTTCAGGAT
GATCCAGATTCCAGTACCAGTACATTAGGAAACATGCTAGAATTACCTGGAACTTCATCA
TCATCTACTTCACAGGAATTGCCATTTTGTCAACCTAAGAAAAAGTCTACGCCACTGAAG
TATGAAGTTGGAGATCTCATCTGGGCAAAATTCAAGAGACGCCCATGGTGGCCCTGCAGG
ATTTGTTCTGATCCGTTGATTAACACACATTCAAAAATGAAAGTTTCCAACCGGAGGCCC
TATCGGCAGTACTACGTGGAGGCTTTTGGAGATCCTTCTGAGAGAGCCTGGGTGGCTGGA
AAAGCAATCGTCATGTTTGAAGGCAGACATCAATTCGAAGAGCTACCTGTCCTTAGGAGA
AGAGGGAAACAGAAAGAAAAAGGATATAGGCATAAGGTTCCTCAGAAAATTTTGAGTAAA
TGGGAAGCCAGTGTTGGACTTGCAGAACAGTATGATGTTCCCAAGGGGTCAAAGAACCGA
AAATGTATTCCTGGTTCAATCAAGTTGGACAGTGAAGAAGATATGCCATTTGAAGACTGC
ACAAATGATCCTGAGTCAGAACATGACCTGTTGCTTAATGGCTGTTTGAAATCACTGGCT
TTTGATTCTGAACATTCTGCAGATGAGAAGGAAAAGCCTTGCGCTAAATCTCGAGCCAGA
AAGAGCTCTGATAATCCAAAAAGGACTAGTGTGAAAAAGGGCCACATACAATTTGAAGCA
CATAAAGATGAACGGAGGGGAAAGATTCCAGAGAACCTTGGCCTAAACTTTATCTCTGGG
GATATATCTGATACGCAGGCCTCTAATGAACTTTCCAGGATAGCAAATAGCCTCACAGGG
TCCAACACTGCCCCAGGAAGTTTTCTGTTTTCTTCCTGTGGAAAAAACACTGCAAAGAAA
GAATTTGAGACTTCAAATGGTGACTCTTTATTGGGCTTGCCTGAGGGTGCTTTGATCTCA
AAGTGTTCTCGAGAGAAGAATAAACCCCAACGAAGCCTGGTGTGTGGTTCAAAAGTGAAG
CTCTGCTATATTGGAGCAGGTGATGAGGAAAAGCGAAGTGATTCCATTAGTATCTGTACC
ACTTCTGATGATGGAAGCAGTGACCTGGATCCCATAGAACACAGCTCAGAGTCTGATAAC
AGTGTCCTTGAAATTCCAGATGCTTTCGATAGAACAGAGAACATGTTATCTATGCAGAAA
AATGAAAAGATAAAGTATTCTAGGTTTGCTGCCACAAACACTAGGGTAAAAGCAAAACAG
AAGCCTCTCATTAGTAACTCACATACAGACCACTTAATGGGTTGTACTAAGAGTGCAGAG
CCTGGAACCGAGACGTCTCAGGTTAATCTCTCTGATCTGAAGGCATCTACTCTTGTTCAC
AAACCCCAGTCAGATTTTACAAATGATGCTCTCTCTCCAAAATTCAACCTGTCATCAAGC
ATATCCAGTGAGAACTCGTTAATAAAGGGTGGGGCAGCAAATCAAGCTCTATTACATTCG
AAAAGCAAACAGCCCAAGTTCCGAAGTATAAAGTGCAAACACAAAGAAAATCCAGTTATG
GCAGAACCCCCAGTTATAAATGAGGAGTGCAGTTTGAAATGCTGCTCTTCTGATACCAAA
GGCTCTCCTTTGGCCAGCATTTCTAAAAGTGGGAAAGTGGATGGTCTAAAACTACTGAAC
AATATGCATGAGAAAACCAGGGATTCAAGTGACATAGAAACAGCAGTGGTGAAACATGTT
TTATCCGAGTTGAAGGAACTCTCTTACAGATCCTTAGGTGAGGATGTCAGTGACTCTGGA
ACATCAAAGCCATCAAAACCATTACTTTTCTCTTCTGCTTCTAGTCAGAATCACATACCT
ATTGAACCAGACTACAAATTCAGTACATTGCTAATGATGTTGAAAGATATGCATGATAGT
AAGACGAAGGAGCAGCGGTTGATGACTGCTCAAAACCTGGTCTCTTACCGGAGTCCTGGT
CGTGGGGACTGTTCTACTAATAGTCCTGTAGGAGTCTCTAAGGTTTTGGTTTCAGGAGGC
TCCACACACAATTCAGAGAAAAAGGGAGATGGCACTCAGAACTCCGCCAATCCTAGCCCT
AGTGGGGGTGACTCTGCATTATCTGGCGAGTTGTCTGCTTCCCTACCTGGCTTACTGTCC
GACAAGAGAGACCTCCCTGCTTCTGGTAAAAGTCGTTCAGACTGTGTTACTAGGCGCAAC
TGTGGACGATCAAAGCCTTCATCCAAATTGCGAGATGCTTTTTCAGCCCAAATGGTAAAG
AACACAGTGAACCGTAAAGCCTTAAAGACCGAGCGCAAAAGAAAACTGAATCAGCTTCCA
AGTGTGACTCTTGATGCTGTACTGCAGGGAGACCGAGAACGTGGAGGTTCATTGAGAGGT
GGGGCAGAAGATCCTAGTAAAGAGGATCCCCTTCAGATAATGGGCCACTTAACAAGTGAA
GATGGTGACCATTTTTCTGATGTGCATTTCGATAGCAAGGTTAAGCAATCTGATCCTGGT
AAAATTTCTGAAAAAGGACTCTCTTTTGAAAACGGAAAAGGCCCAGAGCTGGACTCTGTA
ATGAACAGTGAGAATGATGAACTCAATGGTGTAAATCAAGTGGTGCCTAAAAAGCGGTGG
CAGCGTTTAAACCAAAGGCGCACTAAACCTCGTAAGCGCATGAACAGATTTAAAGAGAAA
GAAAACTCTGAGTGTGCCTTTAGGGTCTTACTTCCTAGTGACCCTGTGCAGGAGGGGCGG
GATGAGTTTCCAGAGCATAGAACTCCTTCAGCAAGCATACTTGAGGAACCACTGACAGAG
CAAAATCATGCTGACTGCTTAGATTCAGCTGGGCCACGGTTAAATGTTTGTGATAAATCC
AGTGCCAGCATTGGTGACATGGAAAAGGAGCCAGGAATTCCCAGTTTGACACCACAGGCT
GAGCTCCCTGAACCAGCTGTGCGGTCAGAGAAGAAACGCCTTAGGAAGCCAAGCAAGTGG
CTTTTGGAATATACAGAAGAATATGATCAGATATTTGCTCCTAAGAAAAAACAAAAGAAG
GTACAGGAGCAGGTGCACAAGGTAAGTTCCCGCTGTGAAGAGGAAAGCCTTCTAGCCCGA
GGTCGATCTAGTGCTCAGAACAAGCAGGTGGACGAGAATTCTTTGATTTCAACCAAAGAA
GAGCCTCCAGTTCTTGAAAGGGAGGCTCCGTTTTTGGAGGGCCCCTTGGCTCAGTCAGAA
CTTGGAGGTGGACATGCTGAGTTGCCGCAGCTGACCTTGTCTGTGCCTGTGGCTCCGGAA
GTCTCTCCACGGCCTGCCCTTGAGTCTGAGGAATTGCTAGTTAAAACGCCAGGAAATTAT
GAAAGTAAACGTCAAAGAAAACCAACTAAGAAACTTCTTGAATCCAATGATTTAGACCCT
GGATTTATGCCCAAGAAGGGGGACCTTGGCCTTTCTAAAAAGTGCTATGAAGCTGGTCAC
CTGGAGAATGGCATAACTGAATCTTGTGCCACATCTTATTCAAAAGATTTTGGTGGAGGC
ACTACCAAGATATTTGACAAGCCAAGGAAGCGAAAACGACAGAGGCATGCTGCAGCCAAG
ATGCAGTGTAAAAAAGTGAAAAATGATGACTCGTCAAAAGAGATTCCAGGCTCAGAGGGA
GAACTAATGCCTCACAGGACGGCCACAAGCCCCAAGGAGACTGTTGAGGAAGGTGTAGAA
CACGATCCCGGGATGCCTGCCTCTAAAAAAATGCAGGGTGAACGCGGTGGAGGAGCTGCA
CTCAAGGAGAATGTCTGTCAGAATTGTGAAAAATTGGGTGAGCTGCTGTTATGTGAGGCT
CAGTGCTGTGGGGCTTTCCACCTGGAGTGCCTTGGATTGACTGAGATGCCAAGAGGAAAA
TTTATCTGCAATGAATGTCGCACAGGAATCCATACCTGTTTTGTATGTAAGCAGAGTGGG
GAAGATGTTAAAAGGTGCCTTCTACCCTTGTGTGGAAAGTTTTACCATGAAGAGTGTGTC
CAGAAGTACCCACCCACTGTTATGCAGAACAAGGGCTTCCGGTGCTCCCTCCACATCTGT
ATAACCTGTCATGCTGCTAATCCAGCCAATGTTTCTGCATCTAAAGGTCGGTTGATGCGC
TGTGTCCGCTGTCCTGTGGCATACCACGCCAATGACTTTTGCCTGGCTGCTGGGTCAAAG
ATCCTTGCATCTAATAGTATCATCTGCCCTAATCACTTTACCCCTAGGCGGGGCTGCCGA
AATCATGAGCATGTTAATGTTAGCTGGTGCTTTGTGTGCTCAGAAGGAGGCAGCCTTCTG
TGCTGTGATTCTTGCCCTGCTGCTTTTCATCGTGAATGCCTGAACATTGATATCCCTGAA
GGAAACTGGTATTGCAATGACTGTAAAGCAGGCAAAAAGCCACACTACAGGGAGATTGTC
TGGGTAAAAGTTGGACGATACAGGTGGTGGCCAGCTGAGATCTGCCATCCTCGAGCTGTT
CCTTCCAACATTGATAAGATGAGACATGATGTGGGAGAGTTCCCAGTCCTCTTTTTTGGA
TCTAATGACTATTTGTGGACTCACCAGGCCCGAGTCTTCCCTTACATGGAGGGTGACGTG
AGCAGCAAGGATAAGATGGGCAAAGGAGTGGATGGGACATATAAAAAAGCTCTTCAGGAA
GCTGCAGCAAGGTTTGAGGAATTAAAGGCCCAAAAAGAGCTAAGACAGCTGCAGGAAGAC
CGAAAGAATGACAAGAAGCCACCACCTTATAAACATATAAAGGTAAACCGTCCTATTGGC
AGGGTACAGATCTTCACTGCAGACTTATCTGAAATACCCCGTTGCAACTGTAAAGCTACT
GATGAGAACCCCTGTGGGATAGACTCTGAATGCATCAACCGCATGCTGCTCTATGAGTGC
CACCCCACAGTGTGTCCTGCCGGAGGGCGCTGTCAAAACCAGTGCTTTTCCAAGCGCCAA
TATCCAGAGGTTGAAATTTTCCGCACATTACAGCGGGGTTGGGGTCTACGGACAAAAACA
GATATTAAAAAGGGTGAATTTGTGAATGAGTATGTGGGTGAGCTTATAGATGAAGAAGAA
TGCAGAGCTCGAATTCGCTATGCTCAAGAACATGATATCACTAATTTCTATATGCTCACC
CTAGACAAAGACCGAATCATTGATGCTGGTCCCAAAGGAAACTATGCTCGGTTCATGAAT
CATTGCTGCCAGCCCAACTGTGAAACACAGAAGTGGTCTGTGAATGGAGATACCCGTGTA
GGCCTTTTTGCACTAAGTGACATTAAAGCAGGCACTGAACTTACCTTCAACTACAACCTA
GAATGTCTTGGGAATGGAAAGACTGTTTGCAAATGTGGAGCCCCGAACTGCAGTGGCTTC
TTGGGTGTAAGGCCAAAGAATCAACCCATTGCCACGGAAGAAAAGTCAAAGAAATTCAAG
AAGAAGCAACAGGGAAAGCGCAGGACCCAGGGTGAAATCACAAAGGAGCGAGAAGATGAG
TGTTTTAGTTGTGGGGATGCTGGCCAGCTCGTCTCCTGCAAGAAACCAGGCTGCCCAAAA
GTTTACCACGCAGACTGTCTCAATCTGACCAAGCGACCAGCAGGGAAATGGGAATGTCCG
TGGCATCAGTGTGACATCTGCGGGAAGGAAGCAGCCTCCTTCTGTGAGATGTGCCCCAGC
TCCTTTTGTAAGCAGCATCGAGAAGGGATGCTTTTCATTTCCAAACTGGATGGGCGTCTG
TCTTGTACTGAGCATGACCCCTGTGGGCCCAATCCTCTGGAACCTGGGGAGATCCGTGAG
TATGTGCCTCCCCCAGTACCGCTGCCTCCAGGGCCAAGCACTCACCTGGCAGAGCAATCA
ACAGGAATGGCTGCTCAGGCACCCAAAATGTCAGATAAACCTCCTGCTGACACCAACCAG
ATGCTGTCGCTCTCCAAAAAAGCTCTGGCAGGGACTTGTCAGAGGCCATTGCTACCTGAA
AGACCTCTTGAGAGAACTGACTCCAGGCCCCAGCCTTTAGATAAGGTCAGAGACCTCGCT
GGGTCAGGGACCAAATCCCAATCCTTGGTTTCCAGCCAGAGGCCACTGGACAGGCCACCA
GCAGTGGCAGGACCAAGACCCCAGCTAAGCGACAAACCCTCTCCAGTGACCAGCCCAAGC
TCCTCACCCTCAGTCAGGTCCCAACCACTGGAAAGACCTCTGGGGACGGCTGACCCAAGG
CTGGATAAATCCATAGGTGCTGCCAGCCCAAGGCCCCAGTCACTGGAGAAAACCTCAGTT
CCCACTGGCCTGAGACTTCCGCCGCCAGACAGACTGCTCATTACTAGCAGTCCCAAACCC
CAGACTTCAGACAGGCCTACTGACAAACCCCATGCCTCTTTGTCCCAGAGACTCCCACCT
CCTGAGAAAGTACTATCAGCTGTGGTCCAGACCCTTGTAGCTAAAGAAAAAGCACTGAGG
CCTGTGGACCAGAATACTCAGTCAAAAAATAGAGCTGCTTTGGTGATGGATCTCATAGAC
CTAACTCCTCGCCAGAAGGAGCGGGCAGCTTCACCTCATCAGGTCACACCACAGGCTGAT
GAGAAGATGCCAGTGTTGGAGTCAAGTTCATGGCCTGCCAGCAAAGGTCTGGGGCATATG
CCGAGAGCTGTTGAGAAAGGCTGTGTGTCAGATCCTCTTCAGACATCTGGGAAAGCAGCA
GCCCCTTCAGAGGACCCCTGGCAAGCTGTTAAATCACTCACCCAGGCCAGACTTCTTTCT
CAGCCTCCTGCCAAGGCCTTTTTATATGAGCCAACAACTCAGGCCTCAGGAAGAGCTTCT
GCAGGGGCTGAGCAGACCCCAGGGCCTCTTAGCCAATCCCCGGGCCTGGTGAAGCAGGCG
AAGCAGATGGTCGGAGGCCAGCAACTACCTGCACTTGCCGCCAAGAGTGGGCAATCTTTT
AGGTCTCTCGGGAAGGCCCCAGCCTCCCTCCCCACTGAAGAAAAGAAGTTGGTAACCACA
GAGCAAAGTCCCTGGGCCCTGGGAAAAGCCTCATCACGGGCAGGGCTCTGGCCCATAGTG
GCTGGACAGACACTGGCACAGTCTTGCTGGTCTGCTGGGAGCACACAGACATTGGCACAG
ACTTGCTGGTCTCTTGGAAGAGGGCAAGACCCCAAACCAGAGCAAAATACACTTCCAGCT
CTTAACCAGGCTCCTTCCAGTCACAAGTGTGCAGAATCAGAACAGAAGTAG
|
| Enzyme 3 GenBank Gene ID |
NM_022455.4  |
| Enzyme 3 GeneCard ID |
NSD1  |
| Enzyme 3 GenAtlas ID |
NSD1  |
| Enzyme 3 HGNC ID |
HGNC:14234  |
| Enzyme 3 Chromosome Location |
5 |
| Enzyme 3 Locus |
5q35 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Wang X, Yeh S, Wu G, Hsu CL, Wang L, Chiang T, Yang Y, Guo Y, Chang C: Identification and characterization of a novel androgen receptor coregulator ARA267-alpha in prostate cancer cells. J Biol Chem. 2001 Nov 2;276(44):40417-23. Epub 2001 Aug 16. [PubMed
]
- Kurotaki N, Harada N, Yoshiura K, Sugano S, Niikawa N, Matsumoto N: Molecular characterization of NSD1, a human homologue of the mouse Nsd1 gene. Gene. 2001 Nov 28;279(2):197-204. [PubMed
]
- Jaju RJ, Fidler C, Haas OA, Strickson AJ, Watkins F, Clark K, Cross NC, Cheng JF, Aplan PD, Kearney L, Boultwood J, Wainscoat JS: A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in de novo childhood acute myeloid leukemia. Blood. 2001 Aug 15;98(4):1264-7. [PubMed
]
- Kurotaki N, Imaizumi K, Harada N, Masuno M, Kondoh T, Nagai T, Ohashi H, Naritomi K, Tsukahara M, Makita Y, Sugimoto T, Sonoda T, Hasegawa T, Chinen Y, Tomita Ha HA, Kinoshita A, Mizuguchi T, Yoshiura Ki K, Ohta T, Kishino T, Fukushima Y, Niikawa N, Matsumoto N: Haploinsufficiency of NSD1 causes Sotos syndrome. Nat Genet. 2002 Apr;30(4):365-6. Epub 2002 Mar 18. [PubMed
]
- Baujat G, Rio M, Rossignol S, Sanlaville D, Lyonnet S, Le Merrer M, Munnich A, Gicquel C, Cormier-Daire V, Colleaux L: Paradoxical NSD1 mutations in Beckwith-Wiedemann syndrome and 11p15 anomalies in Sotos syndrome. Am J Hum Genet. 2004 Apr;74(4):715-20. Epub 2004 Mar 1. [PubMed
]
- La Starza R, Gorello P, Rosati R, Riezzo A, Veronese A, Ferrazzi E, Martelli MF, Negrini M, Mecucci C: Cryptic insertion producing two NUP98/NSD1 chimeric transcripts in adult refractory anemia with an excess of blasts. Genes Chromosomes Cancer. 2004 Dec;41(4):395-9. [PubMed
]
- Giorgianni F, Zhao Y, Desiderio DM, Beranova-Giorgianni S: Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line. Electrophoresis. 2007 Jun;28(12):2027-34. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed
]
- Douglas J, Hanks S, Temple IK, Davies S, Murray A, Upadhyaya M, Tomkins S, Hughes HE, Cole TR, Rahman N: NSD1 mutations are the major cause of Sotos syndrome and occur in some cases of Weaver syndrome but are rare in other overgrowth phenotypes. Am J Hum Genet. 2003 Jan;72(1):132-43. Epub 2002 Dec 2. [PubMed
]
- Rio M, Clech L, Amiel J, Faivre L, Lyonnet S, Le Merrer M, Odent S, Lacombe D, Edery P, Brauner R, Raoul O, Gosset P, Prieur M, Vekemans M, Munnich A, Colleaux L, Cormier-Daire V: Spectrum of NSD1 mutations in Sotos and Weaver syndromes. J Med Genet. 2003 Jun;40(6):436-40. [PubMed
]
- Ley TJ, Mardis ER, Ding L, Fulton B, McLellan MD, Chen K, Dooling D, Dunford-Shore BH, McGrath S, Hickenbotham M, Cook L, Abbott R, Larson DE, Koboldt DC, Pohl C, Smith S, Hawkins A, Abbott S, Locke D, Hillier LW, Miner T, Fulton L, Magrini V, Wylie T, Glasscock J, Conyers J, Sander N, Shi X, Osborne JR, Minx P, Gordon D, Chinwalla A, Zhao Y, Ries RE, Payton JE, Westervelt P, Tomasson MH, Watson M, Baty J, Ivanovich J, Heath S, Shannon WD, Nagarajan R, Walter MJ, Link DC, Graubert TA, DiPersio JF, Wilson RK: DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome. Nature. 2008 Nov 6;456(7218):66-72. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5648 |
| Enzyme 4 Name |
Histone-lysine N-methyltransferase SETDB1 |
| Enzyme 4 Synonyms |
- ERG-associated protein with SET domain
- ESET
- Histone H3-K9 methyltransferase 4
- H3-K9-HMTase 4
- Lysine N-methyltransferase 1E
- SET domain bifurcated 1
|
| Enzyme 4 Gene Name |
SETDB1 |
| Enzyme 4 Protein Sequence |
>Histone-lysine N-methyltransferase SETDB1
MSSLPGCIGLDAATATVESEEIAELQQAVVEELGISMEELRHFIDEELEKMDCVQQRKKQ
LAELETWVIQKESEVAHVDQLFDDASRAVTNCESLVKDFYSKLGLQYRDSSSEDESSRPT
EIIEIPDEDDDVLSIDSGDAGSRTPKDQKLREAMAALRKSAQDVQKFMDAVNKKSSSQDL
HKGTLSQMSGELSKDGDLIVSMRILGKKRTKTWHKGTLIAIQTVGPGKKYKVKFDNKGKS
LLSGNHIAYDYHPPADKLYVGSRVVAKYKDGNQVWLYAGIVAETPNVKNKLRFLIFFDDG
YASYVTQSELYPICRPLKKTWEDIEDISCRDFIEEYVTAYPNRPMVLLKSGQLIKTEWEG
TWWKSRVEEVDGSLVRILFLDDKRCEWIYRGSTRLEPMFSMKTSSASALEKKQGQLRTRP
NMGAVRSKGPVVQYTQDLTGTGTQFKPVEPPQPTAPPAPPFPPAPPLSPQAGDSDLESQL
AQSRKQVAKKSTSFRPGSVGSGHSSPTSPALSENVSGGKPGINQTYRSPLGSTASAPAPS
ALPAPPAPPVFHGMLERAPAEPSYRAPMEKLFYLPHVCSYTCLSRVRPMRNEQYRGKNPL
LVPLLYDFRRMTARRRVNRKMGFHVIYKTPCGLCLRTMQEIERYLFETGCDFLFLEMFCL
DPYVLVDRKFQPYKPFYYILDITYGKEDVPLSCVNEIDTTPPPQVAYSKERIPGKGVFIN
TGPEFLVGCDCKDGCRDKSKCACHQLTIQATACTPGGQINPNSGYQYKRLEECLPTGVYE
CNKRCKCDPNMCTNRLVQHGLQVRLQLFKTQNKGWGIRCLDDIAKGSFVCIYAGKILTDD
FADKEGLEMGDEYFANLDHIESVENFKEGYESDAPCSSDSSGVDLKDQEDGNSGTEDPEE
SNDDSSDDNFCKDEDFSTSSVWRSYATRRQTRGQKENGLSETTSKDSHPPDLGPPHIPVP
PSIPVGGCNPPSSEETPKNKVASWLSCNSVSEGGFADSDSHSSFKTNEGGEGRAGGSRME
AEKASTSGLGIKDEGDIKQAKKEDTDDRNKMSVVTESSRNYGYNPSPVKPEGLRRPPSKT
SMHQSRRLMASAQSNPDDVLTLSSSTESEGESGTSRKPTAGQTSATAVDSDDIQTISSGS
EGDDFEDKKNMTGPMKRQVAVKSTRGFALKSTHGIAIKSTNMASVDKGESAPVRKNTRQF
YDGEESCYIIDAKLEGNLGRYLNHSCSPNLFVQNVFVDTHDLRFPWVAFFASKRIRAGTE
LTWDYNYEVGSVEGKELLCCCGAIECRGRLL
|
| Enzyme 4 Number of Residues |
1291 |
| Enzyme 4 Molecular Weight |
143155.6 |
| Enzyme 4 Theoretical pI |
5.84 |
| Enzyme 4 GO Classification |
| Function |
- DNA binding
- binding
- catalytic activity
- cation binding
- histone-lysine N-methyltransferase activity
- ion binding
- metal ion binding
- methyltransferase activity
- nucleic acid binding
- protein methyltransferase activity
- protein-lysine N-methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
- transition metal ion binding
- zinc ion binding
|
| Process |
- cellular component organization at cellular level
- cellular process
- chromatin modification
- chromatin organization
- chromosome organization
- organelle organization
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 4 General Function |
Involved in DNA binding |
| Enzyme 4 Specific Function |
Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
55960634  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q15047  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
SETB1_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>3876 bp
ATGTCTTCCCTTCCTGGGTGCATTGGTTTGGATGCAGCAACAGCTACAGTGGAGTCTGAA
GAGATTGCAGAGCTGCAACAGGCAGTGGTTGAGGAACTGGGTATCTCTATGGAGGAACTT
CGGCATTTCATCGATGAGGAACTGGAGAAGATGGATTGTGTACAGCAACGCAAGAAGCAG
CTAGCAGAGTTAGAGACATGGGTAATACAGAAAGAATCTGAGGTGGCTCACGTTGACCAA
CTCTTTGATGATGCATCCAGGGCAGTGACTAATTGTGAGTCTTTGGTGAAGGACTTCTAC
TCCAAGCTGGGACTACAATACCGGGACAGTAGCTCTGAGGACGAATCTTCCCGGCCTACA
GAAATAATTGAGATTCCTGATGAAGATGATGATGTCCTCAGTATTGATTCAGGTGATGCT
GGGAGCAGAACTCCAAAAGACCAGAAGCTCCGTGAAGCTATGGCTGCCTTAAGAAAGTCA
GCTCAAGATGTTCAGAAGTTCATGGATGCTGTCAACAAGAAGAGCAGTTCCCAGGATCTG
CATAAAGGAACCTTGAGTCAGATGTCTGGAGAACTAAGCAAAGATGGTGACCTGATAGTC
AGCATGCGAATTCTGGGCAAGAAGAGAACTAAGACTTGGCACAAAGGCACCCTTATTGCC
ATCCAGACAGTTGGGCCAGGGAAGAAATACAAGGTGAAATTTGACAACAAAGGAAAGAGT
CTACTGTCGGGGAACCATATTGCCTATGATTACCACCCTCCTGCTGACAAGCTGTATGTG
GGCAGTCGGGTGGTCGCCAAATACAAAGATGGGAATCAGGTCTGGCTCTATGCTGGCATT
GTAGCTGAGACACCAAACGTCAAAAACAAGCTCAGGTTTCTCATTTTCTTTGATGATGGC
TATGCTTCCTATGTCACACAGTCGGAACTGTATCCCATTTGCCGGCCACTGAAAAAGACT
TGGGAGGACATAGAAGACATCTCCTGCCGTGACTTCATAGAGGAGTATGTCACTGCCTAC
CCCAACCGCCCCATGGTACTGCTCAAGAGTGGCCAGCTTATCAAGACTGAGTGGGAAGGC
ACGTGGTGGAAGTCCCGAGTTGAGGAGGTGGATGGCAGCCTAGTCAGGATCCTCTTCCTG
GATGACAAAAGATGTGAGTGGATCTATCGAGGCTCTACACGGCTGGAGCCCATGTTCAGC
ATGAAAACATCCTCAGCCTCTGCACTGGAGAAGAAGCAAGGACAGCTCAGGACACGTCCA
AATATGGGTGCTGTGAGGAGCAAAGGCCCTGTTGTCCAGTACACACAGGATCTGACCGGT
ACTGGAACCCAGTTCAAGCCAGTGGAACCCCCACAGCCTACAGCTCCACCTGCCCCACCT
TTCCCACCTGCTCCACCTCTATCCCCCCAAGCAGGTGACAGTGACTTGGAAAGCCAGCTT
GCCCAGTCACGGAAGCAGGTAGCCAAAAAGAGCACGTCCTTTCGACCAGGATCTGTGGGC
TCTGGTCATTCCTCCCCTACATCTCCTGCACTCAGTGAAAATGTCTCTGGTGGGAAACCT
GGGATCAACCAGACATATAGATCACCTTTAGGCTCCACAGCCTCTGCCCCAGCACCCTCA
GCACTCCCGGCCCCTCCAGCACCCCCAGTCTTCCATGGCATGCTGGAGCGGGCCCCAGCA
GAGCCCTCCTACCGTGCTCCCATGGAGAAGCTTTTCTACTTACCTCATGTCTGCAGCTAT
ACCTGTCTGTCTCGAGTCAGACCTATGAGGAATGAGCAGTACCGGGGCAAGAACCCTCTG
CTGGTCCCGTTACTATATGACTTCCGGCGGATGACAGCCCGGCGTCGAGTTAACCGCAAG
ATGGGCTTTCATGTTATCTATAAGACACCTTGTGGTCTCTGCCTTCGGACAATGCAGGAG
ATAGAACGCTACCTTTTCGAGACTGGCTGTGACTTCCTCTTCCTGGAGATGTTCTGTTTG
GATCCATATGTTCTTGTGGACCGAAAGTTTCAGCCCTATAAGCCTTTTTACTATATTTTG
GACATCACTTATGGGAAGGAAGATGTTCCCCTATCCTGTGTCAATGAGATTGACACAACC
CCTCCACCCCAGGTGGCCTACAGCAAGGAACGTATCCCGGGCAAGGGTGTTTTCATTAAC
ACAGGCCCTGAATTTCTGGTTGGCTGTGACTGCAAGGATGGGTGTCGGGACAAGTCCAAG
TGTGCCTGCCATCAACTAACTATCCAGGCTACAGCCTGTACCCCAGGAGGCCAAATCAAC
CCTAACTCTGGCTACCAGTACAAGAGACTAGAAGAGTGTCTACCCACAGGGGTATATGAG
TGTAACAAACGCTGCAAATGTGACCCAAACATGTGCACAAACCGGTTGGTGCAACATGGA
CTACAAGTTCGGCTACAGCTATTCAAGACACAGAACAAGGGCTGGGGTATCCGCTGCTTG
GATGACATTGCCAAAGGCTCTTTTGTTTGTATTTATGCAGGCAAAATCCTGACAGATGAC
TTTGCAGACAAGGAGGGTCTGGAAATGGGTGATGAGTACTTTGCAAATCTGGACCATATC
GAGAGCGTGGAGAACTTCAAAGAAGGATATGAGAGTGATGCCCCCTGTTCCTCTGACAGC
AGTGGTGTAGACTTGAAGGACCAGGAAGATGGCAACAGCGGTACAGAGGACCCTGAAGAG
TCCAATGATGATAGCTCAGATGATAACTTCTGTAAGGATGAGGACTTCAGCACCAGTTCA
GTGTGGCGGAGCTATGCTACCCGGAGGCAGACCCGGGGCCAGAAAGAGAACGGACTCTCT
GAGACAACTTCCAAGGACTCCCACCCCCCAGATCTTGGACCCCCACATATTCCTGTTCCT
CCCTCAATCCCTGTAGGTGGCTGCAATCCACCTTCCTCCGAAGAGACACCCAAGAACAAG
GTGGCCTCATGGTTGAGCTGCAATAGTGTCAGTGAAGGTGGTTTTGCTGACTCTGATAGC
CATTCATCCTTCAAGACTAATGAAGGTGGGGAGGGCCGGGCTGGGGGAAGCCGAATGGAG
GCTGAGAAGGCCTCCACCTCAGGACTAGGCATCAAGGATGAGGGAGACATCAAACAGGCC
AAGAAAGAGGACACTGACGACCGAAACAAGATGTCAGTAGTTACTGAAAGCTCTCGAAAT
TACGGTTACAATCCTTCTCCTGTGAAGCCTGAAGGACTTCGCCGCCCACCTAGTAAGACT
AGTATGCATCAAAGCCGAAGACTCATGGCTTCTGCTCAGTCCAACCCTGATGATGTCCTG
ACACTGTCCAGCAGCACAGAAAGTGAGGGGGAAAGTGGGACCAGCCGAAAGCCCACTGCT
GGTCAGACTTCGGCTACAGCGGTTGACAGTGATGATATCCAGACCATATCCTCTGGCTCT
GAAGGGGATGACTTTGAGGACAAGAAGAACATGACTGGTCCAATGAAGCGTCAAGTGGCA
GTAAAATCAACCCGAGGCTTTGCTCTTAAATCAACCCATGGGATTGCAATTAAATCAACC
AACATGGCCTCTGTGGACAAGGGGGAGAGCGCACCTGTTCGTAAGAACACACGCCAATTC
TATGATGGCGAGGAGTCTTGCTACATCATTGATGCCAAGCTTGAAGGCAACCTGGGCCGC
TACCTCAACCACAGTTGCAGCCCCAACCTGTTTGTCCAGAATGTCTTCGTGGATACCCAT
GATCTTCGCTTCCCCTGGGTGGCCTTCTTTGCCAGCAAAAGAATCCGGGCTGGGACAGAA
CTTACTTGGGACTACAACTACGAGGTGGGCAGTGTGGAAGGCAAGGAGCTACTCTGTTGC
TGTGGGGCCATTGAATGCAGAGGACGTCTTCTTTAG
|
| Enzyme 4 GenBank Gene ID |
AL590133  |
| Enzyme 4 GeneCard ID |
SETDB1  |
| Enzyme 4 GenAtlas ID |
SETDB1  |
| Enzyme 4 HGNC ID |
HGNC:10761  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
1q21 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Nomura N, Nagase T, Miyajima N, Sazuka T, Tanaka A, Sato S, Seki N, Kawarabayasi Y, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1994;1(5):223-9. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Schultz DC, Ayyanathan K, Negorev D, Maul GG, Rauscher FJ 3rd: SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins. Genes Dev. 2002 Apr 15;16(8):919-32. [PubMed
]
- Ayyanathan K, Lechner MS, Bell P, Maul GG, Schultz DC, Yamada Y, Tanaka K, Torigoe K, Rauscher FJ 3rd: Regulated recruitment of HP1 to a euchromatic gene induces mitotically heritable, epigenetic gene silencing: a mammalian cell culture model of gene variegation. Genes Dev. 2003 Aug 1;17(15):1855-69. Epub 2003 Jul 17. [PubMed
]
- Wang H, An W, Cao R, Xia L, Erdjument-Bromage H, Chatton B, Tempst P, Roeder RG, Zhang Y: mAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9 of histone H3 to cause transcriptional repression. Mol Cell. 2003 Aug;12(2):475-87. [PubMed
]
- Sarraf SA, Stancheva I: Methyl-CpG binding protein MBD1 couples histone H3 methylation at lysine 9 by SETDB1 to DNA replication and chromatin assembly. Mol Cell. 2004 Aug 27;15(4):595-605. [PubMed
]
- Verschure PJ, van der Kraan I, de Leeuw W, van der Vlag J, Carpenter AE, Belmont AS, van Driel R: In vivo HP1 targeting causes large-scale chromatin condensation and enhanced histone lysine methylation. Mol Cell Biol. 2005 Jun;25(11):4552-64. [PubMed
]
- Gevaert K, Staes A, Van Damme J, De Groot S, Hugelier K, Demol H, Martens L, Goethals M, Vandekerckhove J: Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC. Proteomics. 2005 Sep;5(14):3589-99. [PubMed
]
- Lyst MJ, Nan X, Stancheva I: Regulation of MBD1-mediated transcriptional repression by SUMO and PIAS proteins. EMBO J. 2006 Nov 15;25(22):5317-28. Epub 2006 Oct 26. [PubMed
]
- Ichimura T, Watanabe S, Sakamoto Y, Aoto T, Fujita N, Nakao M: Transcriptional repression and heterochromatin formation by MBD1 and MCAF/AM family proteins. J Biol Chem. 2005 Apr 8;280(14):13928-35. Epub 2005 Feb 2. [PubMed
]
- Li H, Rauch T, Chen ZX, Szabo PE, Riggs AD, Pfeifer GP: The histone methyltransferase SETDB1 and the DNA methyltransferase DNMT3A interact directly and localize to promoters silenced in cancer cells. J Biol Chem. 2006 Jul 14;281(28):19489-500. Epub 2006 May 8. [PubMed
]
- Rosendorff A, Sakakibara S, Lu S, Kieff E, Xuan Y, DiBacco A, Shi Y, Shi Y, Gill G: NXP-2 association with SUMO-2 depends on lysines required for transcriptional repression. Proc Natl Acad Sci U S A. 2006 Apr 4;103(14):5308-13. Epub 2006 Mar 27. [PubMed
]
- Ryu H, Lee J, Hagerty SW, Soh BY, McAlpin SE, Cormier KA, Smith KM, Ferrante RJ: ESET/SETDB1 gene expression and histone H3 (K9) trimethylation in Huntington's disease. Proc Natl Acad Sci U S A. 2006 Dec 12;103(50):19176-81. Epub 2006 Dec 1. [PubMed
]
- Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed
]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed
]
- Meierhofer D, Wang X, Huang L, Kaiser P: Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J Proteome Res. 2008 Oct;7(10):4566-76. Epub 2008 Sep 10. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5656 |
| Enzyme 5 Name |
Histone-lysine N-methyltransferase, H3 lysine-9 specific 3 |
| Enzyme 5 Synonyms |
- Euchromatic histone-lysine N-methyltransferase 2
- HLA-B-associated transcript 8
- Histone H3-K9 methyltransferase 3
- H3-K9-HMTase 3
- Lysine N-methyltransferase 1C
- Protein G9a
|
| Enzyme 5 Gene Name |
EHMT2 |
| Enzyme 5 Protein Sequence |
>Histone-lysine N-methyltransferase, H3 lysine-9 specific 3
MAAAAGAAAAAAAEGEAPAEMGALLLEKETRGATERVHGSLGDTPRSEETLPKATPDSLE
PAGPSSPASVTVTVGDEGADTPVGATPLIGDESENLEGDGDLRGGRILLGHATKSFPSSP
SKGGSCPSRAKMSMTGAGKSPPSVQSLAMRLLSMPGAQGAAAAGSEPPPATTSPEGQPKV
HRARKTMSKPGNGQPPVPEKRPPEIQHFRMSDDVHSLGKVTSDLAKRRKLNSGGGLSEEL
GSARRSGEVTLTKGDPGSLEEWETVVGDDFSLYYDSYSVDERVDSDSKSEVEALTEQLSE
EEEEEEEEEEEEEEEEEEEEEEEDEESGNQSDRSGSSGRRKAKKKWRKDSPWVKPSRKRR
KREPPRAKEPRGVNGVGSSGPSEYMEVPLGSLELPSEGTLSPNHAGVSNDTSSLETERGF
EELPLCSCRMEAPKIDRISERAGHKCMATESVDGELSGCNAAILKRETMRPSSRVALMVL
CETHRARMVKHHCCPGCGYFCTAGTFLECHPDFRVAHRFHKACVSQLNGMVFCPHCGEDA
SEAQEVTIPRGDGVTPPAGTAAPAPPPLSQDVPGRADTSQPSARMRGHGEPRRPPCDPLA
DTIDSSGPSLTLPNGGCLSAVGLPLGPGREALEKALVIQESERRKKLRFHPRQLYLSVKQ
GELQKVILMLLDNLDPNFQSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRT
PLMEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGQVDVNA
QDSGGWTPIIWAAEHKHIEVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNA
RCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDLTPERSDVWFA
LQLNRKLRLGVGNRAIRTEKIICRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCETS
TMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQA
CSCWRNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVR
EDDSYLFDLDNKDGEVYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFS
SRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQSRLARLDPHPELLP
ELGSLPPVNT
|
| Enzyme 5 Number of Residues |
1210 |
| Enzyme 5 Molecular Weight |
132369.2 |
| Enzyme 5 Theoretical pI |
5.14 |
| Enzyme 5 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- histone-lysine N-methyltransferase activity
- ion binding
- metal ion binding
- methyltransferase activity
- protein methyltransferase activity
- protein-lysine N-methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
- transition metal ion binding
- zinc ion binding
|
| Process |
- cellular component organization at cellular level
- cellular process
- chromatin modification
- chromatin organization
- chromosome organization
- organelle organization
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 5 General Function |
Involved in zinc ion binding |
| Enzyme 5 Specific Function |
Histone methyltransferase. Preferentially methylates 'Lys-9' of histone H3 and 'Lys-27' of histone H3 (in vitro). H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. Also methylates histone H1 |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
15917538  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q96KQ7  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
EHMT2_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>3633 bp
ATGGCGGCGGCGGCGGGAGCTGCAGCGGCGGCGGCCGCCGAGGGGGAGGCCCCCGCTGAG
ATGGGGGCGCTGCTGCTGGAGAAGGAAACCAGAGGAGCCACCGAGAGAGTTCATGGCTCT
TTGGGGGACACCCCTCGTAGTGAAGAAACCCTGCCCAAGGCCAACCCCGACTCCCTGGAG
CCTGCTGGCCCCTCATCTCCAGCCTCTGTCACTGTCACTGTTGGTGATGAGGGGGCTGAC
ACCCCTGTAGGGGCTACACCACTCATTGGGGATGAATCTGAGAATCTTGAGGGAGATGGG
GACCTCCGTGGGGGCCGGATCCTGCTGGGCCATGCCACAAAGTCATTCCCCTCTTCCCCC
AGCAAGGGGGGTTCCTGTCCTAGCCGGGCCAAGATGTCAATGACAGGGGCGGGAAAATCA
CCTCCATCTGTCCAGAGTTTGGCTATGAGGCTACTGAGTATGCCAGGAGCCCAGGGAGCT
GCAGCAGCAGGGTCTGAACCCCCTCCAGCCACCACGAGCCCAGAGGGACAGTCCAAGGTC
CACCGAGCCCGCAAAACCATGTCCAAACCAGGAAATGGACAGCCCCCGGTCCCTGAGAAG
CGGCCCCCTGAAATACAGCATTTCCGCATGAGTGATGATGTCCACTCACTGGGAAAGGTG
ACCTCAGATCTGGCCAAAAGGAGGAAGCTGAACTCAGGAGGTGGCCTGTCGGAGGAGTTA
GGTTCTGCCCGGCGTTCAGGAGAAGTGACCCTGACGAAAGGGGACCCCGGGTCCCTGGAG
GAGTGGGAGACGGTGGTGGGTGATGACTTCAGTCTCTACTATGATTCCTACTCTGTGGAT
GAGCGCGTGGACTCCGACAGCAAGTCTGAAGTTGAAGCTCTAACTGAACAACTAAGTGAA
GAGGAGGAGGAGGAAGAGGAGGAAGAAGAAGAAGAGGAAGAGGAGGAGGAAGAGGAAGAA
GAAGAGGAAGATGAGGAGTCAGGGAATCAGTCAGATAGGAGTGGTTCCAGTGGCCGGCGC
AAGGCCAAGAAGAAATGGCGAAAAGACAGCCCATGGGTGAAGCCGTCTCGGAAACGGCGC
AAGCGGGAGCCTCCGCGGGCCAAGGAGCCACGAGGAGTGAATGGTGTGGGCTCCTCAGGC
CCCAGTGAGTACATGGAGGTCCCTCTGGGGTCCCTGGAGCTGCCCAGCGAGGGGACCCTC
TCCCCCAACCACGCTGGGGTGTCCAATGACACATCTTCGCTGGAGACAGAGCGAGGGTTT
GAGGAGTTGCCCCTGTGCAGCTGCCGCATGGAGGCACCCAAGATTGACCGCATCAGCGAG
AGGGCGGGGCACAAGTGCATGGCCACTGAGAGTGTGGACGGAGAGCTGTCAGGCTGCAAT
GCCGCCATCCTCAAGCGGGAGACCATGAGGCCATCCAGCCGTGTGGCCCTGATGGTGCTC
TGTGAGACCCACCGCGCCCGCATGGTCAAACACCACTGCTGCCCGGGCTGCGGCTACTTC
TGCACGGCGGGCACCTTCCTGGAGTGCCACCCTGACTTCCGTGTGGCCCACCGCTTCCAC
AAGGCCTGTGTGTCTCAGCTGAATGGGATGGTCTTCTGTCCCCACTGTGGGGAGGATGCT
TCTGAAGCTCAAGAGGTGACCATCCCCCGGGGTGACGGGGTGACCCCACCGGCCGGCACT
GCAGCTCCTGCACCCCCACCCCTGTCCCAGGATGTCCCCGGGAGAGCAGACACTTCTCAG
CCCAGTGCCCGGATGCGAGGGCATGGGGAACCCCGGCGCCCGCCCTGCGATCCCCTGGCT
GACACCATTGACAGCTCAGGGCCCTCCCTGACCCTGCCCAATGGGGGCTGCCTTTCAGCC
GTGGGGCTGCCACTGGGGCCAGGCCGGGAGGCCCTGGAAAAGGCCCTGGTCATCCAGGAG
TCAGAGAGGCGGAAGAAGCTCCGTTTCCACCCTCGGCAGTTGTACCTGTCCGTGAAGCAG
GGCGAGCTGCAGAAGGTGATCCTGATGCTGTTGGACAACCTGGACCCCAACTTCCAGAGC
GACCAGCAGAGCAAGCGCACGCCCCTGCATGCAGCCGCCCAGAAGGGCTCCGTGGAGATC
TGCCATGTGCTGCTGCAGGCTGGAGCCAACATAAATGCAGTGGACAAACAGCAGCGGACG
CCACTGATGGAGGCCGTGGTGAACAACCACCTGGAGGTAGCCCGTTACATGGTGCAGCGT
GGTGGCTGTGTCTATAGCAAGGAGGAGGACGGTTCCACCTGCCTCCACCACGCAGCCAAA
ATCGGGAACTTGGAGATGGTCAGCCTGCTGCTGAGCACAGGACAGGTGGACGTCAACGCC
CAGGACAGTGGGGGGTGGACGCCCATCATCTGGGCTGCAGAGCACAAGCACATCGAGGTG
ATCCGCATGCTACTGACGCGGGGCGCCGACGTCACCCTCACTGACAACGAGGAGAACATC
TGCCTGCACTGGGCCTCCTTCACGGGCAGCGCCGCCATCGCCGAAGTCCTTCTGAATGCG
CGCTGTGACCTCCATGCTGTCAACTACCATGGGGACACCCCCCTGCACATCGCAGCTCGG
GAGAGCTACCATGACTGCGTGCTGTTATTCCTGTCACGTGGGGCCAACCCTGAGCTGCGG
AACAAAGAGGGGGACACAGCATGGGACCTGACTCCCGAGCGCTCCGACGTGTGGTTTGCG
CTTCAACTCAACCGCAAGCTCCGACTTGGGGTGGGAAATCGGGCCATCCGCACAGAGAAG
ATCATCTGCCGGGACGTGGCTCGGGGCTATGAGAACGTGCCCATTCCCTGTGTCAACGGT
GTGGATGGGGAGCCCTGCCCTGAGGATTACAAGTACATCTCAGAGAACTGCGAGACGTCC
ACCATGAACATCGATCGCAACATCACCCACCTGCAGCACTGCACGTGTGTGGACGACTGC
TCTAGCTCCAACCGCCTGTGCGGCCAGCTCAGCATCCGGTGCTGGTATGACAAGGATGGG
CGATTGCTCCAGGAATTTAACAAGATTGAGCCTCCGCTGATTTTCGAGTGTAACCAGGCG
TGCTCATGCTGGAGAAACTGCAAGAACCGGGTCGTACAGAGTGGCATCAAGGTGCGGCTA
CAGCTCTACCGAACAGCCAAGATGGGCTGGGGGGTCCGCGCCCTGCAGACCATCCCACAG
GGGACCTTCATCTGCGAGTATGTCGGGGAGCTGATCTCTGATGCTGAGGCTGATGTGAGA
GAGGATGATTCTTACCTCTTCGACTTAGACAACAAGGATGGAGAGGTGTACTGCATAGAT
GCCCGTTACTATGGCAACATCAGCCGCTTCATCAACCACCTGTGTGACCCCAACATCATT
CCCGTCCGGGTCTTCATGCTGCACCAAGACCTGCGATTTCCACGCATCGCCTTCTTCAGT
TCCCGAGACATCCGGACTGGGGAGGAGCTAGGGTTTGACTATGGCGACCGCTTCTGGGAC
ATCAAAAGCAAATATTTCACCTGCCAATGTGGCTCTGAGAAGTGCAAGCACTCAGCCGAA
GCCATTGCCCTGGAGCAGAGCCGTCTGGCCCGCCTGGACCCACACCCTGAGCTGCTGCCC
GAGCTCGGCTCCCTGCCCCCTGTCAACACATGA
|
| Enzyme 5 GenBank Gene ID |
AJ315532  |
| Enzyme 5 GeneCard ID |
EHMT2  |
| Enzyme 5 GenAtlas ID |
EHMT2  |
| Enzyme 5 HGNC ID |
HGNC:14129  |
| Enzyme 5 Chromosome Location |
6 |
| Enzyme 5 Locus |
6p21.31 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Brown SE, Campbell RD, Sanderson CM: Novel NG36/G9a gene products encoded within the human and mouse MHC class III regions. Mamm Genome. 2001 Dec;12(12):916-24. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Xie T, Rowen L, Aguado B, Ahearn ME, Madan A, Qin S, Campbell RD, Hood L: Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse. Genome Res. 2003 Dec;13(12):2621-36. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Milner CM, Campbell RD: The G9a gene in the human major histocompatibility complex encodes a novel protein containing ankyrin-like repeats. Biochem J. 1993 Mar 15;290 ( Pt 3):811-8. [PubMed
]
- Tachibana M, Sugimoto K, Fukushima T, Shinkai Y: Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3. J Biol Chem. 2001 Jul 6;276(27):25309-17. Epub 2001 Apr 20. [PubMed
]
- Ogawa H, Ishiguro K, Gaubatz S, Livingston DM, Nakatani Y: A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells. Science. 2002 May 10;296(5570):1132-6. [PubMed
]
- Vassen L, Fiolka K, Moroy T: Gfi1b alters histone methylation at target gene promoters and sites of gamma-satellite containing heterochromatin. EMBO J. 2006 Jun 7;25(11):2409-19. Epub 2006 May 11. [PubMed
]
- Ueda J, Tachibana M, Ikura T, Shinkai Y: Zinc finger protein Wiz links G9a/GLP histone methyltransferases to the co-repressor molecule CtBP. J Biol Chem. 2006 Jul 21;281(29):20120-8. Epub 2006 May 15. [PubMed
]
- Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed
]
- Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed
]
- Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed
]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5662 |
| Enzyme 6 Name |
Histone-lysine N-methyltransferase, H3 lysine-9 specific 5 |
| Enzyme 6 Synonyms |
- Euchromatic histone-lysine N-methyltransferase 1
- Eu-HMTase1
- G9a-like protein 1
- GLP1
- Histone H3-K9 methyltransferase 5
- H3-K9-HMTase 5
- Lysine N-methyltransferase 1D
|
| Enzyme 6 Gene Name |
EHMT1 |
| Enzyme 6 Protein Sequence |
>Histone-lysine N-methyltransferase, H3 lysine-9 specific 5
MAADEGSAEKQAGEAHMAADGETNGSCENSDASSHANAAKHTQDSARVNPQDGTNTLTRI
AENGVSERDSEAAKQNHVTADDFVQTSVIGSNGYILNKPALQAQPLRTTSTLASSLPGHA
AKTLPGGAGKGRTPSAFPQTPAAPPATLGEGSADTEDRKLPAPGADVKVHRARKTMPKSV
VGLHAASKDPREVREARDHKEPKEEINKNISDFGRQQLLPPFPSLHQSLPQNQCYMATTK
SQTACLPFVLAAAVSRKKKRRMGTYSLVPKKKTKVLKQRTVIEMFKSITHSTVGSKGEKD
LGASSLHVNGESLEMDSDEDDSEELEEDDGHGAEQAAAFPTEDSRTSKESMSEADRAQKM
DGESEEEQESVDTGEEEEGGDESDLSSESSIKKKFLKRKGKTDSPWIKPARKRRRRSRKK
PSGALGSESYKSSAGSAEQTAPGDSTGYMEVSLDSLDLRVKGILSSQAEGLANGPDVLET
DGLQEVPLCSCRMETPKSREITTLANNQCMATESVDHELGRCTNSVVKYELMRPSNKAPL
LVLCEDHRGRMVKHQCCPGCGYFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCG
EESSKAKEVTIAKADTTSTVTPVPGQEKGSALEGRADTTTGSAAGPPLSEDDKLQGAASH
VPEGFDPTGPAGLGRPTPGLSQGPGKETLESALIALDSEKPKKLRFHPKQLYFSARQGEL
QKVLLMLVDGIDPNFKMEHQNKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLM
EAAENNHLEAVKYLIKAGALVDPKDAEGSTCLHLAAKKGHYEVVQYLLSNGQMDVNCQDD
GGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCD
LHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNSQVWSALQM
SKALQDSAPDRPSPVERIVSRDIARGYERIPIPCVNAVDSEPCPSNYKYVSQNCVTSPMN
IDRNITHLQYCVCIDDCSSSNCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSC
WRNCRNRVVQNGLRARLQLYRTRDMGWGVRSLQDIPPGTFVCEYVGELISDSEADVREED
SYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEPNLVPVRVFMAHQDLRFPRIAFFSTRL
IEAGEQLGFDYGERFWDIKGKLFSCRCGSPKCRHSSAALAQRQASAAQEAQEDGLPDTSS
AAAADPL
|
| Enzyme 6 Number of Residues |
1267 |
| Enzyme 6 Molecular Weight |
138252.4 |
| Enzyme 6 Theoretical pI |
5.78 |
| Enzyme 6 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- histone-lysine N-methyltransferase activity
- ion binding
- metal ion binding
- methyltransferase activity
- protein methyltransferase activity
- protein-lysine N-methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
- transition metal ion binding
- zinc ion binding
|
| Process |
- cellular component organization at cellular level
- cellular process
- chromatin modification
- chromatin organization
- chromosome organization
- organelle organization
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 6 General Function |
Involved in zinc ion binding |
| Enzyme 6 Specific Function |
Histone methyltransferase. Methylates 'Lys-9' of histone H3 (in vitro). H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. During G0 phase, it probably contributes to silencing of MYC- and E2F-responsive genes, suggesting a role in G0/G1 transition in cell cycle |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
224465233  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q9H9B1  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
EHMT1_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>3897 bp
ATGGCCGCCGCCGATGCCGAGGCAGTTCCGGCGAGGGGGGAGCCTCAGCAGGATTGCTGT
GTGAAAACCGAGCTGCTGGGAGAAGAGACACCTATGGCTGCCGATGAAGGCTCAGCAGAG
AAACAGGCAGGAGAGGCCCACATGGCTGCGGACGGTGAGACCAATGGGTCTTGTGAAAAC
AGCGATGCCAGCAGTCATGCAAATGCTGCAAAGCACACTCAGGACAGCGCAAGGGTCAAC
CCCCAGGATGGCACCAACACACTAACTCGGATAGCGGAAAATGGGGTTTCAGAAAGAGAC
TCAGAAGCGGCGAAGCAAAACCACGTCACTGCCGACGACTTTGTGCAGACTTCTGTCATC
GGCAGCAACGGATACATCTTAAATAAGCCGGCCCTACAGGCACAGCCCTTGAGGACTACC
AGCACTCTGGCCTCTTCGCTGCCTGGCCATGCTGCAAAAACCCTTCCTGGAGGGGCTGGC
AAAGGCAGGACTCCAAGCGCTTTTCCCCAGACGCCAGCCGCCCCACCAGCCACCCTTGGG
GAGGGGAGTGCTGACACAGAGGACAGGAAGCTCCCGGCCCCTGGCGCCGACGTCAAGGTC
CACAGGGCACGCAAGACCATGCCGAAGTCCGTCGTGGGCCTGCATGCAGCCAGTAAAGAT
CCCAGAGAAGTTCGAGAAGCTAGAGATCATAAGGAACCAAAAGAGGAGATCAACAAAAAC
ATTTCTGACTTTGGACGACAGCAGCTTTTACCCCCCTTCCCATCCCTTCATCAGTCGCTA
CCTCAGAACCAGTGCTACATGGCCACCACAAAATCACAGACAGCTTGCTTGCCTTTTGTT
TTAGCAGCTGCAGTATCTCGGAAGAAAAAACGAAGAATGGGAACCTATAGCCTGGTTCCT
AAGAAAAAGACCAAAGTATTAAAACAGAGGACGGTGATTGAGATGTTTAAGAGCATAACT
CATTCCACTGTGGGTTCCAAGGGGGAGAAGGACCTGGGCGCCAGCAGCCTGCACGTGAAT
GGGGAGAGCCTGGAGATGGACTCGGATGAGGACGACTCAGAGGAGCTCGAGGAGGACGAC
GGCCATGGTGCAGAGCAGGCGGCCGCGTTCCCCACAGAGGACAGCAGGACTTCCAAGGAG
AGCATGTCGGAGGCTGATCGCGCCCAGAAGATGGACGGGGAGTCCGAGGAGGAGCAGGAG
TCCGTGGACACCGGGGAGGAGGAGGAAGGCGGTGACGAGTCTGACCTGAGTTCGGAATCC
AGCATTAAGAAGAAATTTCTCAAGAGGAAAGGAAAGACCGACAGTCCCTGGATCAAGCCA
GCCAGGAAAAGGAGGCGGAGAAGTAGAAAGAAGCCCAGCGGTGCCCTCGGTTCTGAGTCG
TATAAGTCATCTGCAGGAAGCGCTGAGCAGACGGCACCAGGAGACAGCACAGGGTACATG
GAAGTTTCTCTGGACTCCCTGGATCTCCGAGTCAAAGGAATTCTGTCTTCACAAGCAGAA
GGGTTGGCCAACGGTCCAGATGTGCTGGAGACAGACGGCCTCCAGGAAGTGCCTCTCTGC
AGCTGCCGGATGGAAACACCGAAGAGTCGAGAGATCACCACACTGGCCAACAACCAGTGC
ATGGCTACAGAGAGCGTGGACCATGAATTGGGCCGGTGCACAAACAGCGTGGTCAAGTAT
GAGCTGATGCGCCCCTCCAACAAGGCCCCGCTCCTCGTGCTGTGTGAAGACCACCGGGGC
CGCATGGTGAAGCACCAGTGCTGTCCTGGCTGTGGCTACTTCTGCACAGCGGGTAATTTT
ATGGAGTGTCAGCCCGAGAGCAGCATCTCTCACCGTTTCCACAAAGACTGTGCCTCTCGA
GTCAATAACGCCAGCTATTGTCCCCACTGTGGGGAGGAGAGCTCCAAGGCCAAAGAGGTG
ACGATAGCTAAAGCAGACACCACCTCGACCGTGACACCAGTCCCCGGGCAGGAGAAGGGC
TCGGCCCTGGAGGGCAGGGCCGACACCACAACGGGCAGTGCTGCCGGGCCACCACTCTCG
GAGGACGACAAGCTGCAGGGTGCAGCCTCCCACGTGCCCGAGGGCTTTGATCCAACGGGA
CCTGCTGGGCTTGGGAGGCCAACTCCCGGCCTTTCCCAGGGACCAGGGAAGGAAACCTTG
GAGAGCGCTCTCATCGCCCTCGACTCGGAAAAACCCAAGAAGCTTCGCTTCCACCCAAAG
CAGCTGTACTTCTCCGCCAGGCAAGGGGAGCTTCAGAAGGTGCTCCTCATGCTGGTGGAC
GGAATTGACCCCAACTTCAAAATGGAGCACCAGAATAAGCGCTCTCCACTGCACGCCGCG
GCAGAGGCTGGACACGTGGACATCTGCCACATGCTGGTTCAGGCGGGCGCTAATATTGAC
ACCTGCTCAGAAGACCAGAGGACCCCGTTGATGGAAGCAGCCGAAAACAACCATCTGGAA
GCAGTGAAGTACCTCATCAAGGCTGGGGCCCTGGTGGATCCCAAGGACGCAGAGGGCTCT
ACGTGTTTGCACCTGGCTGCCAAGAAAGGCCACTACGAAGTGGTCCAGTACCTGCTTTCA
AATGGACAGATGGACGTCAACTGTCAGGATGACGGAGGCTGGACACCCATGATCTGGGCC
ACAGAGTACAAGCACGTGGACCTCGTGAAGCTGCTGCTGTCCAAGGGCTCTGACATCAAC
ATCCGAGACAACGAGGAGAACATTTGCCTGCACTGGGCGGCGTTCTCCGGCTGCGTGGAC
ATAGCCGAGATCCTGCTGGCTGCCAAGTGCGACCTCCACGCCGTGAACATCCACGGAGAC
TCGCCACTGCACATTGCCGCCCGGGAGAACCGCTACGACTGTGTCGTCCTCTTTCTTTCT
CGGGATTCAGATGTCACCTTAAAGAACAAGGAAGGAGAGACGCCCCTGCAGTGTGCGAGC
CTCAACTCTCAGGTGTGGAGCGCTCTGCAGATGAGCAAGGCTCTGCAGGACTCGGCCCCC
GACAGGCCCAGCCCCGTGGAGAGGATAGTGAGCAGGGACATCGCTCGAGGCTACGAGCGC
ATCCCCATCCCCTGTGTCAACGCCGTGGACAGCGAGCCATGCCCCAGCAACTACAAGTAC
GTCTCTCAGAACTGCGTGACGTCCCCCATGAACATCGACAGAAATATCACTCATCTGCAG
TACTGCGTGTGCATCGACGACTGCTCCTCCAGCAACTGCATGTGCGGCCAGCTCAGCATG
CGCTGCTGGTACGACAAGGATGGCCGGCTCCTGCCAGAGTTCAACATGGCGGAGCCTCCC
TTGATCTTCGAATGCAACCACGCGTGCTCCTGCTGGAGGAACTGCCGAAATCGCGTCGTA
CAGAATGGTCTCAGGGCAAGGCTGCAGCTCTACCGGACGCGGGACATGGGCTGGGGCGTG
CGGTCCCTGCAGGACATCCCACCAGGCACCTTTGTCTGCGAGTATGTTGGGGAGCTGATT
TCAGACTCAGAAGCCGACGTTCGAGAGGAAGATTCTTACCTCTTTGATCTCGACAATAAG
GACGGGGAGGTTTACTGCATCGACGCGCGGTTCTACGGGAACGTCAGCCGGTTCATCAAC
CACCACTGCGAGCCCAACCTGGTGCCCGTGCGCGTGTTCATGGCCCACCAGGACCTGCGG
TTCCCCCGGATCGCCTTCTTCAGCACCCGCCTGATCGAGGCCGGCGAGCAGCTCGGGTTT
GACTATGGAGAGCGCTTCTGGGACATCAAAGGCAAGCTCTTCAGCTGCCGCTGCGGCTCC
CCCAAGTGCCGGCACTCGAGCGCGGCCCTGGCCCAGCGTCAGGCCAGCGCGGCCCAGGAG
GCCCAGGAGGACGGCTTGCCCGACACCAGCTCCGCGGCTGCCGCCGACCCCCTATGA
|
| Enzyme 6 GenBank Gene ID |
NM_024757  |
| Enzyme 6 GeneCard ID |
EHMT1  |
| Enzyme 6 GenAtlas ID |
EHMT1  |
| Enzyme 6 HGNC ID |
HGNC:24650  |
| Enzyme 6 Chromosome Location |
9 |
| Enzyme 6 Locus |
9q34.3 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Ogawa H, Ishiguro K, Gaubatz S, Livingston DM, Nakatani Y: A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells. Science. 2002 May 10;296(5570):1132-6. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed
]
- Nagase T, Nakayama M, Nakajima D, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2001 Apr 27;8(2):85-95. [PubMed
]
- Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Kleefstra T, Brunner HG, Amiel J, Oudakker AR, Nillesen WM, Magee A, Genevieve D, Cormier-Daire V, van Esch H, Fryns JP, Hamel BC, Sistermans EA, de Vries BB, van Bokhoven H: Loss-of-function mutations in euchromatin histone methyl transferase 1 (EHMT1) cause the 9q34 subtelomeric deletion syndrome. Am J Hum Genet. 2006 Aug;79(2):370-7. Epub 2006 Jun 13. [PubMed
]
- Ueda J, Tachibana M, Ikura T, Shinkai Y: Zinc finger protein Wiz links G9a/GLP histone methyltransferases to the co-repressor molecule CtBP. J Biol Chem. 2006 Jul 21;281(29):20120-8. Epub 2006 May 15. [PubMed
]
- Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5699 |
| Enzyme 7 Name |
Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 |
| Enzyme 7 Synonyms |
- Lysyl hydroxylase 1
- LH1
|
| Enzyme 7 Gene Name |
PLOD1 |
| Enzyme 7 Protein Sequence |
>Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1
MRPLLLLALLGWLLLAEAKGDAKPEDNLLVLTVATKETEGFRRFKRSAQFFNYKIQALGL
GEDWNVEKGTSAGGGQKVRLLKKALEKHADKEDLVILFADSYDVLFASGPRELLKKFRQA
RSQVVFSAEELIYPDRRLETKYPVVSDGKRFLGSGGFIGYAPNLSKLVAEWEGQDSDSDQ
LFYTKIFLDPEKREQINITLDHRCRIFQNLDGALDEVVLKFEMGHVRARNLAYDTLPVLI
HGNGPTKLQLNYLGNYIPRFWTFETGCTVCDEGLRSLKGIGDEALPTVLVGVFIEQPTPF
VSLFFQRLLRLHYPQKHMRLFIHNHEQHHKAQVEEFLAQHGSEYQSVKLVGPEVRMANAD
ARNMGADLCRQDRSCTYYFSVDADVALTEPNSLRLLIQQNKNVIAPLMTRHGRLWSNFWG
ALSADGYYARSEDYVDIVQGRRVGVWNVPYISNIYLIKGSALRGELQSSDLFHHSKLDPD
MAFCANIRQQDVFMFLTNRHTLGHLLSLDSYRTTHLHNDLWEVFSNPEDWKEKYIHQNYT
KALAGKLVETPCPDVYWFPIFTEVACDELVEEMEHFGQWSLGNNKDNRIQGGYENVPTID
IHMNQIGFEREWHKFLLEYIAPMTEKLYPGYYTRAQFDLAFVVRYKPDEQPSLMPHHDAS
TFTINIALNRVGVDYEGGGCRFLRYNCSIRAPRKGWTLMHPGRLTHYHEGLPTTRGTRYI
AVSFVDP
|
| Enzyme 7 Number of Residues |
727 |
| Enzyme 7 Molecular Weight |
83549.5 |
| Enzyme 7 Theoretical pI |
6.94 |
| Enzyme 7 GO Classification |
| Function |
- L-ascorbic acid binding
- binding
- catalytic activity
- cation binding
- ion binding
- iron ion binding
- metal ion binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
- peptidyl-lysine 5-dioxygenase activity
- procollagen-lysine 5-dioxygenase activity
- transition metal ion binding
- vitamin binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
- endoplasmic reticulum
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- organelle
|
|
| Enzyme 7 General Function |
Involved in oxidoreductase activity |
| Enzyme 7 Specific Function |
Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- L-lysine-[procollagen] + 2-oxoglutarate + O2 = (2S,5R)- 5-hydroxy-L-lysine-[procollagen] + succinate + CO2
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
20149013  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q02809  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
PLOD1_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>2184 bp
ATGCGGCCCCTGCTGCTACTGGCCCTGCTGGGCTGGCTGCTGCTGGCCGAAGCGAAGGGC
GACGCCAAGCCGGAGGACAACCTTTTAGTCCTCACGGTGGCCACTAAGGAGACCGAGGGA
TTCCGTCGCTTCAAGCGCTCAGCTCAGTTCTTCAACTACAAGATCCAGGCGCTTGGCCTA
GGGGAGGACTGGAATGTGGAGAAGGGGACGTCGGCAGGTGGAGGGCAGAAGGTCCGGCTG
CTGAAGAAAGCTCTGGAGAAGCACGCAGACAAGGAGGATCTGGTCATTCTCTTTGCAGAC
AGCTATGACGTGCTGTTTGCATCGGGGCCCCGGGAGCTCCTGAAGAAGTTCCGGCAGGCC
AGGAGCCAGGTGGTCTTCTCTGCTGAGGAGCTCATCTACCCAGACCGCAGGCTGGAGACC
AAGTATCCGGTGGTGTCCGATGGCAAGAGGTTCCTGGGCTCTGGAGGCTTCATCGGTTAT
GCCCCCAACCTCAGCAAACTGGTGGCCGAGTGGGAGGGCCAGGACAGCGACAGCGATCAG
CTGTTTTACACCAAGATCTTCTTGGACCCGGAGAAGAGGGAGCAGATCAATATCACCCTG
GACCACCGCTGCCGTATCTTCCAGAACCTGGATGGAGCCTTGGATGAGGTCGTGCTCAAG
TTTGAAATGGGCCATGTGAGAGCGAGGAACCTGGCCTATGACACCCTCCCGGTCCTGATC
CATGGCAACGGGCCAACCAAGCTGCAGTTGAACTACCTGGGCAACTACATCCCGCGCTTC
TGGACCTTCGAAACAGGCTGCACCGTGTGTGACGAAGGCTTGCGCAGCCTCAAGGGCATT
GGGGATGAAGCTCTGCCCACGGTCCTGGTCGGCGTGTTCATCGAACAGCCCACGCCGTTT
GTGTCCCTGTTCTTCCAGCGGCTCCTGCGGCTCCACTACCCCCAGAAACACATGCGACTT
TTCATCCACAACCACGAGCAGCACCACAAGGCTCAGGTGGAAGAGTTCCTGGCACAGCAT
GGCAGCGAGTACCAGTCTGTGAAGCTGGTGGGCCCTGAGGTGCGGATGGCGAATGCAGAT
GCCAGGAACATGGGCGCAGACCTGTGCCGGCAGGACCGCAGCTGCACCTACTACTTCAGC
GTGGATGCTGACGTGGCCCTGACCGAGCCCAACAGCCTGCGGCTGCTGATCCAACAGAAC
AAGAATGTCATTGCCCCGCTGATGACCCGGCATGGGAGGCTGTGGTCGAACTTCTGGGGG
GCTCTCAGTGCAGATGGCTACTATGCCCGTTCCGAGGACTACGTGGACATTGTGCAGGGG
CGGCGTGTTGGTGTCTGGAATGTGCCCTATATTTCAAACATCTACTTGATCAAGGGCAGT
GCCCTGCGGGGTGAGCTGCAGTCCTCAGATCTCTTCCACCACAGCAAGCTGGACCCCGAC
ATGGCCTTCTGTGCCAACATCCGGCAGCAGGATGTGTTCATGTTCCTGACCAACCGGCAC
ACCCTTGGCCATCTGCTCTCCCTAGACAGCTACCGCACCACCCACCTGCACAACGACCTC
TGGGAGGTGTTCAGCAACCCCGAGGACTGGAAGGAGAAGTACATCCACCAGAACTACACC
AAAGCCCTGGCAGGGAAGCTGGTGGAGACGCCCTGCCCGGATGTCTATTGGTTCCCCATC
TTCACGGAGGTGGCCTGTGATGAGCTGGTGGAGGAGATGGAGCACTTTGGCCAGTGGTCT
CTGGGCAACAACAAGGACAACCGCATCCAGGGTGGCTACGAGAACGTGCCGACTATTGAC
ATCCACATGAACCAGATCGGCTTTGAGCGGGAGTGGCACAAATTCCTGCTGGAGTACATT
GCGCCCATGACGGAGAAGCTCTACCCCGGCTACTACACCAGGGCCCAGTTTGACCTGGCC
TTTGTCGTCCGCTACAAGCCTGATGAGCAGCCCTCACTGATGCCACACCATGATGCCTCC
ACCTTCACCATCAACATCGCCCTGAACCGAGTCGGGGTGGATTACGAGGGCGGGGGCTGT
CGGTTCCTGCGCTACAACTGTTCCATCCGAGCCCCAAGGAAGGGCTGGACCCTCATGCAC
CCTGGACGACTCACGCATTACCATGAGGGGCTCCCCACCACCAGGGGCACCCGCTACATC
GCAGTCTCCTTCGTCGATCCCTAA
|
| Enzyme 7 GenBank Gene ID |
AF490527  |
| Enzyme 7 GeneCard ID |
PLOD1  |
| Enzyme 7 GenAtlas ID |
PLOD1  |
| Enzyme 7 HGNC ID |
HGNC:9081  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
1p36.22 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Hautala T, Byers MG, Eddy RL, Shows TB, Kivirikko KI, Myllyla R: Cloning of human lysyl hydroxylase: complete cDNA-derived amino acid sequence and assignment of the gene (PLOD) to chromosome 1p36.3----p36.2. Genomics. 1992 May;13(1):62-9. [PubMed
]
- Heikkinen J, Hautala T, Kivirikko KI, Myllyla R: Structure and expression of the human lysyl hydroxylase gene (PLOD): introns 9 and 16 contain Alu sequences at the sites of recombination in Ehlers-Danlos syndrome type VI patients. Genomics. 1994 Dec;24(3):464-71. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Pirskanen A, Kaimio AM, Myllyla R, Kivirikko KI: Site-directed mutagenesis of human lysyl hydroxylase expressed in insect cells. Identification of histidine residues and an aspartic acid residue critical for catalytic activity. J Biol Chem. 1996 Apr 19;271(16):9398-402. [PubMed
]
- Ha VT, Marshall MK, Elsas LJ, Pinnell SR, Yeowell HN: A patient with Ehlers-Danlos syndrome type VI is a compound heterozygote for mutations in the lysyl hydroxylase gene. J Clin Invest. 1994 Apr;93(4):1716-21. [PubMed
]
- Brinckmann J, Acil Y, Feshchenko S, Katzer E, Brenner R, Kulozik A, Kugler S: Ehlers-Danlos syndrome type VI: lysyl hydroxylase deficiency due to a novel point mutation (W612C). Arch Dermatol Res. 1998 Apr;290(4):181-6. [PubMed
]
- Yeowell HN, Allen JD, Walker LC, Overstreet MA, Murad S, Thai SF: Deletion of cysteine 369 in lysyl hydroxylase 1 eliminates enzyme activity and causes Ehlers-Danlos syndrome type VI. Matrix Biol. 2000 Feb;19(1):37-46. [PubMed
]
- Giunta C, Randolph A, Al-Gazali LI, Brunner HG, Kraenzlin ME, Steinmann B: Nevo syndrome is allelic to the kyphoscoliotic type of the Ehlers-Danlos syndrome (EDS VIA). Am J Med Genet A. 2005 Mar 1;133A(2):158-64. [PubMed
]
- Walker LC, Overstreet MA, Siddiqui A, De Paepe A, Ceylaner G, Malfait F, Symoens S, Atsawasuwan P, Yamauchi M, Ceylaner S, Bank RA, Yeowell HN: A novel mutation in the lysyl hydroxylase 1 gene causes decreased lysyl hydroxylase activity in an Ehlers-Danlos VIA patient. J Invest Dermatol. 2005 May;124(5):914-8. [PubMed
]
- Giunta C, Randolph A, Steinmann B: Mutation analysis of the PLOD1 gene: an efficient multistep approach to the molecular diagnosis of the kyphoscoliotic type of Ehlers-Danlos syndrome (EDS VIA). Mol Genet Metab. 2005 Sep-Oct;86(1-2):269-76. Epub 2005 Jun 24. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5700 |
| Enzyme 8 Name |
Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 |
| Enzyme 8 Synonyms |
- Lysyl hydroxylase 2
- LH2
|
| Enzyme 8 Gene Name |
PLOD2 |
| Enzyme 8 Protein Sequence |
>Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2
MGGCTVKPQLLLLALVLHPWNPCLGADSEKPSSIPTDKLLVITVATKESDGFHRFMQSAK
YFNYTVKVLGQGEEWRGGDGINSIGGGQKVRLMKEVMEHYADQDDLVVMFTECFDVIFAG
GPEEVLKKFQKANHKVVFAADGILWPDKRLADKYPVVHIGKRYLNSGGFIGYAPYVNRIV
QQWNLQDNDDDQLFYTKVYIDPLKREAINITLDHKCKIFQTLNGAVDEVVLKFENGKARA
KNTFYETLPVAINGNGPTKILLNYFGNYVPNSWTQDNGCTLCEFDTVDLSAVDVHPNVSI
GVFIEQPTPFLPRFLDILLTLDYPKEALKLFIHNKEVYHEKDIKVFFDKAKHEIKTIKIV
GPEENLSQAEARNMGMDFCRQDEKCDYYFSVDADVVLTNPRTLKILIEQNRKIIAPLVTR
HGKLWSNFWGALSPDGYYARSEDYVDIVQGNRVGVWNVPYMANVYLIKGKTLRSEMNERN
YFVRDKLDPDMALCRNAREMGVFMYISNRHEFGRLLSTANYNTSHYNNDLWQIFENPVDW
KEKYINRDYSKIFTENIVEQPCPDVFWFPIFSEKACDELVEEMEHYGKWSGGKHHDSRIS
GGYENVPTDDIHMKQVDLENVWLHFIREFIAPVTLKVFAGYYTKGFALLNFVVKYSPERQ
RSLRPHHDASTFTINIALNNVGEDFQGGGCKFLRYNCSIESPRKGWSFMHPGRLTHLHEG
LPVKNGTRYIAVSFIDP
|
| Enzyme 8 Number of Residues |
737 |
| Enzyme 8 Molecular Weight |
84685.1 |
| Enzyme 8 Theoretical pI |
6.69 |
| Enzyme 8 GO Classification |
| Function |
- L-ascorbic acid binding
- binding
- catalytic activity
- cation binding
- ion binding
- iron ion binding
- metal ion binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
- peptidyl-lysine 5-dioxygenase activity
- procollagen-lysine 5-dioxygenase activity
- transition metal ion binding
- vitamin binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
- endoplasmic reticulum
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- organelle
|
|
| Enzyme 8 General Function |
Involved in oxidoreductase activity |
| Enzyme 8 Specific Function |
Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- L-lysine-[procollagen] + 2-oxoglutarate + O2 = (2S,5R)- 5-hydroxy-L-lysine-[procollagen] + succinate + CO2
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
2138314  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
O00469  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
PLOD2_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>2214 bp
ATGGGGGGATGCACGGTGAAGCCTCAGCTGCTGCTCCTGGCGCTCGTCCTCCACCCCTGG
AATCCCTGTCTGGGTGCGGACTCGGAGAAGCCCTCGAGCATCCCCACAGATAAATTATTA
GTCATAACTGTAGCAACAAAAGAAAGTGATGGATTCCATCGATTTATGCAGTCAGCCAAA
TATTTCAATTATACTGTGAAGGTCCTTGGTCAAGGAGAAGAATGGAGAGGTGGTGATGGA
ATTAATAGTATTGGAGGGGGCCAGAAAGTGAGATTAATGAAAGAAGTCATGGAACACTAT
GCTGATCAAGATGATCTGGTTGTCATGTTTACTGAATGCTTTGATGTCATATTTGCTGGT
GGTCCAGAAGAAGTTCTAAAAAAATTCCAAAAGGCAAACCACAAAGTGGTCTTTGCAGCA
GATGGAATTTTGTGGCCAGATAAAAGACTAGCAGACAAGTATCCTGTTGTGCACATTGGG
AAACGCTATCTGAATTCAGGAGGATTTATTGGCTATGCTCCATATGTCAACCGTATAGTT
CAACAATGGAATCTCCAGGATAATGATGATGATCAGCTCTTTTACACTAAAGTTTACATT
GATCCACTGAAAAGGGAAGCTATTAACATCACATTGGATCACAAATGCAAAATTTTCCAG
ACCTTAAATGGAGCTGTAGATGAAGTTGTTTTAAAATTTGAAAATGGCAAAGCCAGAGCT
AAGAATACATTTTATGAAACATTACCAGTGGCAATTAATGGAAATGGACCCACCAAGATT
CTCCTGAATTATTTTGGAAACTATGTACCCAATTCATGGACACAGGATAATGGCTGCACT
CTTTGTGAATTCGATACAGTCGACTTGTCTGCAGTAGATGTCCATCCAAACGTATCAATA
GGTGTTTTTATTGAGCAACCAACCCCTTTTCTACCTCGGTTTCTGGACATATTGTTGACA
CTGGATTACCCAAAAGAAGCACTTAAACTTTTTATTCATAACAAAGAAGTTTATCATGAA
AAGGACATCAAGGTATTTTTTGATAAAGCTAAGCATGAAATCAAAACTATAAAAATAGTA
GGACCAGAAGAAAATCTAAGTCAAGCGGAAGCCAGAAACATGGGAATGGACTTTTGCCGT
CAGGATGAAAAGTGTGATTATTACTTTAGTGTGGATGCAGATGTTGTTTTGACAAATCCA
AGGACTTTAAAAATTTTGATTGAACAAAACAGAAAGATCATTGCTCCTCTTGTAACTCGT
CATGGAAAGCTGTGGTCCAATTTCTGGGGAGCATTGAGTCCTGATGGATACTATGCACGA
TCTGAAGATTATGTGGATATTGTTCAAGGGAATAGAGTAGGAGTATGGAATGTCCCATAT
ATGGCTAATGTGTACTTAATTAAAGGAAAGACACTCCGATCAGAGATGAATGAAAGGAAC
TATTTTGTTCGTGATAAACTGGATCCTGATATGGCTCTTTGCCGAAATGCTAGAGAAATG
GGTGTATTTATGTACATTTCTAATAGACATGAATTTGGAAGGCTATTATCCACTGCTAAT
TACAATACTTCCCATTATAACAATGACCTCTGGCAGATTTTTGAAAATCCTGTGGACTGG
AAGGAAAAGTATATAAACCGTGATTATTCAAAGATTTTCACTGAAAATATAGTTGAACAG
CCCTGTCCAGATGTCTTTTGGTTCCCCATATTTTCTGAAAAAGCCTGTGATGAATTGGTA
GAAGAAATGGAACATTACGGCAAATGGTCTGGGGGAAAACATCATGATAGCCGTATATCT
GGTGGTTATGAAAATGTCCCAACTGATGATATCCACATGAAGCAAGTTGATCTGGAGAAT
GTATGGCTTGATTTTATCCGGGAGTTCATTGCACCAGTTACACTGAAGGTCTTTGCAGGC
TATTATACGAAGGGATTTGCACTACTGAATTTTGTAGTAAAATACTCCCCTGAACGACAG
CGTTCTCTTCGTCCTCATCATGATGCTTCTACATTTACCATAAACATTGCACTTAATAAC
GTGGGAGAAGACTTTCAGGGAGGTGGTTGCAAATTTCTAAGGTACAATTGCTCTATTGAG
TCACCACGAAAAGGCTGGAGCTTCATGCATCCTGGGAGACTCACACATTTGCATGAAGGA
CTTCCTGTTAAAAATGGAACAAGATACATTGCAGTGTCATTTATAGATCCCTAA
|
| Enzyme 8 GenBank Gene ID |
U84573  |
| Enzyme 8 GeneCard ID |
PLOD2  |
| Enzyme 8 GenAtlas ID |
PLOD2  |
| Enzyme 8 HGNC ID |
HGNC:9082  |
| Enzyme 8 Chromosome Location |
3 |
| Enzyme 8 Locus |
3q23-q24 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Valtavaara M, Papponen H, Pirttila AM, Hiltunen K, Helander H, Myllyla R: Cloning and characterization of a novel human lysyl hydroxylase isoform highly expressed in pancreas and muscle. J Biol Chem. 1997 Mar 14;272(11):6831-4. [PubMed
]
- Yeowell HN, Walker LC: Tissue specificity of a new splice form of the human lysyl hydroxylase 2 gene. Matrix Biol. 1999 Apr;18(2):179-87. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed
]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed
]
- van der Slot AJ, Zuurmond AM, Bardoel AF, Wijmenga C, Pruijs HE, Sillence DO, Brinckmann J, Abraham DJ, Black CM, Verzijl N, DeGroot J, Hanemaaijer R, TeKoppele JM, Huizinga TW, Bank RA: Identification of PLOD2 as telopeptide lysyl hydroxylase, an important enzyme in fibrosis. J Biol Chem. 2003 Oct 17;278(42):40967-72. Epub 2003 Jul 24. [PubMed
]
- Ha-Vinh R, Alanay Y, Bank RA, Campos-Xavier AB, Zankl A, Superti-Furga A, Bonafe L: Phenotypic and molecular characterization of Bruck syndrome (osteogenesis imperfecta with contractures of the large joints) caused by a recessive mutation in PLOD2. Am J Med Genet A. 2004 Dec 1;131(2):115-20. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5701 |
| Enzyme 9 Name |
Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 |
| Enzyme 9 Synonyms |
- Lysyl hydroxylase 3
- LH3
|
| Enzyme 9 Gene Name |
PLOD3 |
| Enzyme 9 Protein Sequence |
>Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3
MTSSGPGPRFLLLLPLLLPPAASASDRPRGRDPVNPEKLLVITVATAETEGYLRFLRSAE
FFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDVILAG
SPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIV
RQWKYKDDDDDQLFYTRLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRI
RNVAYDTLPIVVHGNGPTKLQLNYLGNYVPNGWTPEGGCGFCNQDRRTLPGGQPPPRVFL
AVFVEQPTPFLPRFLQRLLLLDYPPDRVTLFLHNNEVFHEPHIADSWPQLQDHFSAVKLV
GPEEALSPGEARDMAMDLCRQDPECEFYFSLDADAVLTNLQTLRILIEENRKVIAPMLSR
HGKLWSNFWGALSPDEYYARSEDYVELVQRKRVGVWNVPYISQAYVIRGDTLRMELPQRD
VFSGSDTDPDMAFCKSFRDKGIFLHLSNQHEFGRLLATSRYDTEHLHPDLWQIFDNPVDW
KEQYIHENYSRALEGEGIVEQPCPDVYWFPLLSEQMCDELVAEMEHYGQWSGGRHEDSRL
AGGYENVPTVDIHMKQVGYEDQWLQLLRTYVGPMTESLFPGYHTKARAVMNFVVRYRPDE
QPSLRPHHDSSTFTLNVALNHKGLDYEGGGCRFLRYDCVISSPRKGWALLHPGRLTHYHE
GLPTTWGTRYIMVSFVDP
|
| Enzyme 9 Number of Residues |
738 |
| Enzyme 9 Molecular Weight |
84784.5 |
| Enzyme 9 Theoretical pI |
5.95 |
| Enzyme 9 GO Classification |
| Function |
- L-ascorbic acid binding
- binding
- catalytic activity
- cation binding
- ion binding
- iron ion binding
- metal ion binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors
- peptidyl-lysine 5-dioxygenase activity
- procollagen-lysine 5-dioxygenase activity
- transition metal ion binding
- vitamin binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
- endoplasmic reticulum
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- organelle
|
|
| Enzyme 9 General Function |
Involved in oxidoreductase activity |
| Enzyme 9 Specific Function |
Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- L-lysine-[procollagen] + 2-oxoglutarate + O2 = (2S,5R)- 5-hydroxy-L-lysine-[procollagen] + succinate + CO2
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
3153235  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
O60568  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
PLOD3_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>2217 bp
ATGACCTCCTCGGGGCCTGGACCCCGGTTCCTGCTGCTGCTGCCGCTGCTGCTGCCCCCT
GCGGCCTCAGCCTCCGACCGGCCCCGGGGCCGAGACCCGGTCAACCCAGAGAAGCTGCTG
GTGATCACTGTGGCCACAGCTGAAACCGAGGGGTACCTGCGTTTCCTGCGCTCTGCGGAG
TTCTTCAACTACACTGTGCGGACCCTGGGCCTGGGAGAGGAGTGGCGAGGGGGTGATGTG
GCTCGAACAGTTGGTGGAGGACAGAAGGTCCGGTGGTTAAAGAAGGAAATGGAGAAATAC
GCTGACCGGGAGGATATGATCATCATGTTTGTGGATAGCTACGACGTGATTCTGGCCGGC
AGCCCCACAGAGCTGCTGAAGAAGTTCGTCCAGAGTGGCAGCCGCCTGCTCTTCTCTGCA
GAGAGCTTCTGCTGGCCCGAGTGGGGGCTGGCGGAGCAGTACCCTGAGGTGGGCACGGGG
AAGCGCTTCCTCAATTCTGGTGGATTCATCGGTTTTGCCACCACCATCCACCAAATCGTG
CGCCAGTGGAAGTACAAGGATGATGACGACGACCAGCTGTTCTACACACGGCTCTACCTG
GACCCAGGACTGAGGGAGAAACTCAGCCTTAATCTGGATCATAAGTCTCGGATCTTTCAG
AACCTCAACGGGGCTTTAGATGAAGTGGTTTTAAAGTTTGATCGGAACCGTGTGCGTATC
CGGAACGTGGCCTACGACACGCTCCCCATTGTGGTCCATGGAAACGGTCCCACTAAGCTG
CAGCTCAACTACCTGGGAAACTACGTCCCCAATGGCTGGACTCCTGAGGGAGGCTGTGGC
TTCTGCAACCAGGACCGGAGGACACTCCCGGGGGGGCAGCCTCCCCCCCGGGTGTTTCTG
GCCGTGTTTGTGGAACAGCCTACTCCGTTTCTGCCCCGCTTCCTGCAGCGGCTGCTACTC
CTGGACTATCCCCCCGACAGGGTCACCCTTTTCCTGCACAACAACGAGGTCTTCCATGAA
CCCCACATCGCTGACTCCTGGCCGCAGCTCCAGGACCACTTCTCAGCTGTGAAGCTCGTG
GGGCCGGAGGAGGCTCTGAGCCCAGGCGAGGCCAGGGACATGGCCATGGACCTGTGTCGG
CAGGACCCCGAGTGTGAGTTCTACTTCAGCCTGGACGCCGACGCTGTCCTCACCAACCTG
CAGACCCTGCGTATCCTCATTGAGGAGAACAGGAAGGTGATCGCCCCCATGCTGTCCCGC
CACGGCAAGCTGTGGTCCAACTTCTGGGGCGCCCTGAGCCCCGATGAGTACTACGCCCGC
TCCGAGGACTACGTGGAGCTGGTGCAGCGGAAGCGAGTGGGTGTGTGGAATGTACCATAC
ATCTCCCAGGCCTATGTGATCCGGGGTGATACCCTGCGGATGGAGCTGCCCCAGAGGGAT
GTGTTCTCGGGCAGTGACACAGACCCGGACATGGCCTTCTGTAAGAGCTTTCGAGACAAG
GGCATCTTCCTCCATCTGAGCAATCAGCATGAATTTGGCCGGCTCCTGGCCACTTCCAGA
TACGACACGGAGCACCTGCACCCCGACCTCTGGCAGATCTTCGACAACCCCGTCGACTGG
AAGGAGCAGTACATCCACGAGAACTACAGCCGGGCCCTGGAAGGGGAAGGAATCGTGGAG
CAGCCATGCCCGGACGTGTACTGGTTCCCACTGCTGTCAGAACAAATGTGTGATGAGCTG
GTGGCAGAGATGGAGCACTACGGCCAGTGGTCAGGCGGCCGGCATGAGGATTCAAGGCTG
GCTGGAGGCTACGAGAATGTGCCCACCGTGGACATCCACATGAAGCAGGTGGGGTACGAG
GACCAGTGGCTGCAGCTGCTGCGGACGTATGTGGGCCCCATGACCGAGAGCCTGTTTCCC
GGTTACCACACCAAGGCGCGGGCGGTGATGAACTTTGTGGTTCGCTACCGGCCAGACGAG
CAGCCGTCTCTGCGGCCACACCACGACTCATCCACCTTCACCCTCAACGTTGCCCTCAAC
CACAAGGGCCTGGACTATGAGGGAGGTGGCTGCCGCTTCCTGCGCTACGACTGTGTGATC
TCCTCCCCGAGGAAGGGCTGGGCACTCCTGCACCCCGGCCGCCTCACCCACTACCACGAG
GGGCTGCCAACGACCTGGGGCACACGCTACATCATGGTGTCCTTTGTCGACCCCTGA
|
| Enzyme 9 GenBank Gene ID |
AF046889  |
| Enzyme 9 GeneCard ID |
PLOD3  |
| Enzyme 9 GenAtlas ID |
PLOD3  |
| Enzyme 9 HGNC ID |
HGNC:9083  |
| Enzyme 9 Chromosome Location |
7 |
| Enzyme 9 Locus |
7q22 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Valtavaara M, Szpirer C, Szpirer J, Myllyla R: Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3) J Biol Chem. 1998 May 22;273(21):12881-6. [PubMed
]
- Passoja K, Rautavuoma K, Ala-Kokko L, Kosonen T, Kivirikko KI: Cloning and characterization of a third human lysyl hydroxylase isoform. Proc Natl Acad Sci U S A. 1998 Sep 1;95(18):10482-6. [PubMed
]
- Rautavuoma K, Passoja K, Helaakoski T, Kivirikko KI: Complete exon-intron organization of the gene for human lysyl hydroxylase 3 (LH3). Matrix Biol. 2000 Feb;19(1):73-9. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Salo AM, Cox H, Farndon P, Moss C, Grindulis H, Risteli M, Robins SP, Myllyla R: A connective tissue disorder caused by mutations of the lysyl hydroxylase 3 gene. Am J Hum Genet. 2008 Oct;83(4):495-503. Epub 2008 Oct 2. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
5817 |
| Enzyme 10 Name |
Biotinidase |
| Enzyme 10 Synonyms |
- Biotinase
|
| Enzyme 10 Gene Name |
BTD |
| Enzyme 10 Protein Sequence |
>Biotinidase
MAHAHIQGGRRAKSRFVVCIMSGARSKLALFLCGCYVVALGAHTGEESVADHHEAEYYVA
AVYEHPSILSLNPLALISRQEALELMNQNLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNF
TRTSIYPFLDFMPSPQVVRWNPCLEPHRFNDTEVLQRLSCMAIRGDMFLVANLGTKEPCH
SSDPRCPKDGRYQFNTNVVFSNNGTLVDRYRKHNLYFEAAFDVPLKVDLITFDTPFAGRF
GIFTCFDILFFDPAIRVLRDYKVKHVVYPTAWMNQLPLLAAIEIQKAFAVAFGINVLAAN
VHHPVLGMTGSGIHTPLESFWYHDMENPKSHLIIAQVAKNPVGLIGAENATGETDPSHSK
FLKILSGDPYCEKDAQEVHCDEATKWNVNAPPTFHSEMMYDNFTLVPVWGKEGYLHVCSN
GLCCYLLYERPTLSKELYALGVFDGLHTVHGTYYIQVCALVRCGGLGFDTCGQEITEATG
IFEFHLWGNFSTSYIFPLFLTSGMTLEVPDQLGWENDHYFLRKSRLSSGLVTAALYGRLY
ERD
|
| Enzyme 10 Number of Residues |
543 |
| Enzyme 10 Molecular Weight |
61132.4 |
| Enzyme 10 Theoretical pI |
6.22 |
| Enzyme 10 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
|
| Process |
- metabolic process
- nitrogen compound metabolic process
|
| Component |
| — |
|
| Enzyme 10 General Function |
Involved in hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| Enzyme 10 Specific Function |
Catalytic release of biotin from biocytin, the product of biotin-dependent carboxylases degradation |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- biotin amide + H2O = biotin + NH3 [RN:R01076]
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
4557373  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P43251  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
BTD_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1632 bp
ATGGCGCATGCGCATATTCAGGGCGGAAGGCGCGCTAAGAGCAGATTTGTGGTCTGCATT
ATGTCTGGAGCCAGAAGTAAGCTTGCTCTTTTCCTCTGCGGCTGTTACGTGGTTGCCCTG
GGAGCCCACACCGGGGAGGAGAGCGTGGCTGACCATCACGAGGCTGAATATTATGTGGCT
GCCGTGTATGAGCATCCATCCATCCTGAGTCTGAACCCTCTGGCTCTCATCAGCCGCCAA
GAGGCCTTGGAGCTCATGAACCAGAACCTTGACATCTATGAACAGCAAGTGATGACTGCA
GCCCAAAAGGATGTACAGATTATAGTGTTTCCAGAAGATGGCATTCATGGATTCAACTTT
ACAAGAACATCCATTTATCCATTTTTGGACTTCATGCCGTCTCCCCAGGTGGTCAGGTGG
AACCCATGCCTGGAGCCTCACCGCTTCAATGACACAGAGGTGCTCCAGCGCCTGAGTTGT
ATGGCCATCAGGGGAGATATGTTCTTGGTGGCCAATCTTGGGACAAAGGAGCCTTGTCAT
AGCAGTGACCCAAGGTGCCCAAAAGATGGGAGATACCAGTTCAACACAAATGTCGTGTTC
AGCAATAATGGAACCCTTGTTGACCGCTACCGTAAACACAACCTCTACTTTGAGGCAGCA
TTCGATGTTCCTCTTAAAGTGGATCTCATCACCTTTGATACCCCCTTTGCTGGCAGGTTT
GGCATCTTCACATGCTTTGATATATTGTTCTTTGACCCTGCCATCAGAGTCCTCAGAGAC
TACAAGGTGAAGCATGTTGTGTACCCAACTGCCTGGATGAACCAGCTCCCACTCTTGGCA
GCAATTGAGATTCAGAAAGCTTTTGCTGTTGCCTTTGGCATCAACGTTCTGGCAGCTAAT
GTCCACCACCCAGTTCTGGGGATGACAGGAAGTGGCATACACACCCCTCTGGAGTCCTTT
TGGTACCATGACATGGAAAATCCCAAAAGTCACCTTATAATTGCCCAGGTGGCCAAAAAT
CCAGTGGGTCTCATTGGTGCAGAGAATGCAACAGGTGAAACGGACCCATCCCATAGTAAG
TTTTTAAAAATTTTGTCAGGCGATCCGTACTGTGAGAAGGATGCTCAGGAAGTCCACTGT
GATGAGGCCACCAAGTGGAACGTGAATGCTCCTCCCACATTTCACTCTGAGATGATGTAT
GACAATTTCACCCTGGTCCCTGTCTGGGGAAAGGAAGGCTATCTCCACGTCTGTTCCAAT
GGCCTCTGCTGTTATTTACTTTACGAGAGGCCCACCTTATCCAAAGAGCTGTATGCCCTG
GGGGTCTTTGATGGGCTTCACACAGTACATGGCACTTACTACATCCAAGTGTGTGCCCTG
GTCAGGTGTGGGGGTCTTGGCTTCGACACCTGTGGACAGGAAATCACAGAGGCCACGGGG
ATATTTGAGTTTCACCTGTGGGGCAACTTCAGTACTTCCTATATCTTTCCTTTGTTTCTG
ACCTCAGGGATGACCCTAGAAGTCCCTGACCAGCTTGGCTGGGAGAATGACCACTATTTC
CTGAGGAAAAGTAGGCTGTCCTCTGGGCTGGTGACGGCGGCTCTCTATGGGCGCTTGTAT
GAGAGGGACTAG
|
| Enzyme 10 GenBank Gene ID |
NM_000060.2  |
| Enzyme 10 GeneCard ID |
BTD  |
| Enzyme 10 GenAtlas ID |
BTD  |
| Enzyme 10 HGNC ID |
HGNC:1122  |
| Enzyme 10 Chromosome Location |
3 |
| Enzyme 10 Locus |
3p25 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Cole H, Reynolds TR, Lockyer JM, Buck GA, Denson T, Spence JE, Hymes J, Wolf B: Human serum biotinidase. cDNA cloning, sequence, and characterization. J Biol Chem. 1994 Mar 4;269(9):6566-70. [PubMed
]
- Knight HC, Reynolds TR, Meyers GA, Pomponio RJ, Buck GA, Wolf B: Structure of the human biotinidase gene. Mamm Genome. 1998 Apr;9(4):327-30. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed
]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed
]
- Pomponio RJ, Norrgard KJ, Hymes J, Reynolds TR, Buck GA, Baumgartner R, Suormala T, Wolf B: Arg538 to Cys mutation in a CpG dinucleotide of the human biotinidase gene is the second most common cause of profound biotinidase deficiency in symptomatic children. Hum Genet. 1997 Apr;99(4):506-12. [PubMed
]
- Swango KL, Demirkol M, Huner G, Pronicka E, Sykut-Cegielska J, Schulze A, Mayatepek E, Wolf B: Partial biotinidase deficiency is usually due to the D444H mutation in the biotinidase gene. Hum Genet. 1998 May;102(5):571-5. [PubMed
]
- Norrgard KJ, Pomponio RJ, Swango KL, Hymes J, Reynolds T, Buck GA, Wolf B: Double mutation (A171T and D444H) is a common cause of profound biotinidase deficiency in children ascertained by newborn screening the the United States. Mutations in brief no. 128. Online. Hum Mutat. 1998;11(5):410. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
5885 |
| Enzyme 11 Name |
Lysyl-tRNA synthetase |
| Enzyme 11 Synonyms |
- Lysine--tRNA ligase
- LysRS
|
| Enzyme 11 Gene Name |
KARS |
| Enzyme 11 Protein Sequence |
>Lysyl-tRNA synthetase
MAAVQAAEVKVDGSEPKLSKNELKRRLKAEKKVAEKEAKQKELSEKQLSQATAAATNHTT
DNGVGPEEESVDPNQYYKIRSQAIHQLKVNGEDPYPHKFHVDISLTDFIQKYSHLQPGDH
LTDITLKVAGRIHAKRASGGKLIFYDLRGEGVKLQVMANSRNYKSEEEFIHINNKLRRGD
IIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDFV
RQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNELDMNLYMRIAP
ELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSG
MVKHITGSYKVTYHPDGPEGQAYDVDFTPPFRRINMVEELEKALGMKLPETNLFETEETR
KILDDICVAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKE
GLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEYG
LPPTAGWGMGIDRVAMFLTDSNNIKEVLLFPAMKPEDKKENVATTDTLESTTVGTSV
|
| Enzyme 11 Number of Residues |
597 |
| Enzyme 11 Molecular Weight |
68047.5 |
| Enzyme 11 Theoretical pI |
6.31 |
| Enzyme 11 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- aminoacyl-tRNA ligase activity
- binding
- catalytic activity
- ligase activity
- ligase activity, forming aminoacyl-tRNA and related compounds
- ligase activity, forming carbon-oxygen bonds
- lysine-tRNA ligase activity
- nucleic acid binding
- nucleoside binding
- nucleotide binding
- purine nucleoside binding
|
| Process |
- RNA metabolic process
- biosynthetic process
- cellular macromolecule biosynthetic process
- cellular macromolecule metabolic process
- lysyl-tRNA aminoacylation
- macromolecule biosynthetic process
- macromolecule metabolic process
- metabolic process
- ncRNA metabolic process
- tRNA aminoacylation
- tRNA aminoacylation for protein translation
- tRNA metabolic process
- translation
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 11 General Function |
Involved in nucleotide binding |
| Enzyme 11 Specific Function |
Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction:the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages. Catalyzes the synthesis of diadenosine oligophosphate (Ap4A), a signaling molecule involved in the activation of MITF transcriptional activity. Interacts with HIV-1 virus GAG protein, facilitating the selective packaging of tRNA(3)(Lys), the primer for reverse transcription initiation |
| Enzyme 11 Pathways |
|
| Enzyme 11 Reactions |
- ATP + L-lysine + tRNALys = AMP + diphosphate + L-lysyl-tRNALys [RN:R03658]
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
5031815  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q15046  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
SYK_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1794 bp
ATGGCGGCCGTGCAGGCGGCCGAGGTGAAAGTGGATGGCAGCGAGCCGAAACTGAGCAAG
AATGAGCTGAAGAGACGCCTGAAAGCTGAGAAGAAAGTAGCAGAGAAGGAGGCCAAACAG
AAAGAGCTCAGTGAGAAACAGCTAAGCCAAGCCACTGCTGCTGCCACCAACCACACCACT
GATAATGGTGTGGGTCCTGAGGAAGAGAGCGTGGACCCAAATCAATACTACAAAATCCGC
AGTCAAGCAATTCATCAGCTGAAGGTCAATGGGGAAGACCCATACCCACACAAGTTCCAT
GTAGACATCTCACTCACTGACTTCATCCAAAAATATAGTCACCTGCAGCCTGGGGATCAC
CTGACTGACATCACCTTAAAGGTGGCAGGTAGGATCCATGCCAAAAGAGCTTCTGGGGGA
AAGCTCATCTTCTATGATCTTCGAGGAGAGGGGGTGAAGTTGCAAGTCATGGCCAATTCC
AGAAATTATAAATCAGAAGAAGAATTTATTCATATTAATAACAAACTGCGTCGGGGAGAC
ATAATTGGAGTTCAGGGGAATCCTGGTAAAACCAAGAAGGGTGAGCTGAGCATCATTCCG
TATGAGATCACACTGCTGTCTCCCTGTTTGCATATGTTACCTCATCTTCACTTTGGCCTC
AAAGACAAGGAAACAAGGTATCGCCAGAGATACTTGGACTTGATCCTGAATGACTTTGTG
AGGCAGAAATTTATCATCCGCTCTAAGATCATCACATATATAAGAAGTTTCTTAGATGAG
CTGGGATTCCTAGAGATTGAAACTCCCATGATGAACATCATCCCAGGGGGAGCCGTGGCC
AAGCCTTTCATCACTTATCACAACGAGCTGGACATGAACTTATATATGAGAATTGCTCCA
GAACTCTATCATAAGATGCTTGTGGTTGGTGGCATCGACCGGGTTTATGAAATTGGACGC
CAGTTCCGGAATGAGGGGATTGATTTGACGCACAATCCTGAGTTCACCACCTGTGAGTTC
TACATGGCCTATGCAGACTATCACGATCTCATGGAAATCACGGAGAAGATGGTTTCAGGG
ATGGTGAAGCATATTACAGGCAGTTACAAGGTCACCTACCACCCAGATGGCCCAGAGGGC
CAAGCCTACGATGTTGACTTCACCCCACCCTTCCGGCGAATCAACATGGTAGAAGAGCTT
GAGAAAGCCCTGGGGATGAAGCTGCCAGAAACGAACCTCTTTGAAACTGAAGAAACTCGC
AAAATTCTTGATGATATCTGTGTGGCAAAAGCTGTTGAATGCCCTCCACCTCGGACCACA
GCCAGGCTCCTTGACAAGCTTGTTGGGGAGTTCCTGGAAGTGACTTGCATCAATCCTACA
TTCATCTGTGATCACCCACAGATAATGAGCCCTTTGGCTAAATGGCACCGCTCTAAAGAG
GGTCTGACTGAGCGCTTTGAGCTGTTTGTCATGAAGAAAGAGATATGCAATGCGTATACT
GAGCTGAATGATCCCATGCGGCAGCGGCAGCTTTTTGAAGAACAGGCCAAGGCCAAGGCT
GCAGGTGATGATGAGGCCATGTTCATAGATGAAAACTTCTGTACTGCCCTGGAATATGGG
CTGCCCCCCACAGCTGGCTGGGGCATGGGCATTGATCGAGTCGCCATGTTTCTCACGGAC
TCCAACAACATCAAGGAAGTACTTCTGTTTCCTGCCATGAAACCCGAAGACAAGAAGGAG
AATGTAGCAACCACTGATACACTGGAAAGCACAACAGTTGGCACTTCTGTCTAG
|
| Enzyme 11 GenBank Gene ID |
NM_005548.2  |
| Enzyme 11 GeneCard ID |
KARS  |
| Enzyme 11 GenAtlas ID |
KARS  |
| Enzyme 11 HGNC ID |
HGNC:6215  |
| Enzyme 11 Chromosome Location |
1 |
| Enzyme 11 Locus |
16q23.1 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Shiba K, Stello T, Motegi H, Noda T, Musier-Forsyth K, Schimmel P: Human lysyl-tRNA synthetase accepts nucleotide 73 variants and rescues Escherichia coli double-defective mutant. J Biol Chem. 1997 Sep 5;272(36):22809-16. [PubMed
]
- Tolkunova E, Park H, Xia J, King MP, Davidson E: The human lysyl-tRNA synthetase gene encodes both the cytoplasmic and mitochondrial enzymes by means of an unusual alternative splicing of the primary transcript. J Biol Chem. 2000 Nov 10;275(45):35063-9. [PubMed
]
- Nomura N, Nagase T, Miyajima N, Sazuka T, Tanaka A, Sato S, Seki N, Kawarabayasi Y, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1994;1(5):223-9. [PubMed
]
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Zamecnik PC, Stephenson ML, Janeway CM, Randerath K: Enzymatic synthesis of diadenosine tetraphosphate and diadenosine triphosphate with a purified lysyl-sRNA synthetase. Biochem Biophys Res Commun. 1966 Jul 6;24(1):91-7. [PubMed
]
- Quevillon S, Robinson JC, Berthonneau E, Siatecka M, Mirande M: Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein. J Mol Biol. 1999 Jan 8;285(1):183-95. [PubMed
]
- Tan M, Wei C, Price CM: The telomeric protein Rap1 is conserved in vertebrates and is expressed from a bidirectional promoter positioned between the Rap1 and KARS genes. Gene. 2003 Dec 24;323:1-10. [PubMed
]
- Lee YN, Nechushtan H, Figov N, Razin E: The function of lysyl-tRNA synthetase and Ap4A as signaling regulators of MITF activity in FcepsilonRI-activated mast cells. Immunity. 2004 Feb;20(2):145-51. [PubMed
]
- Javanbakht H, Halwani R, Cen S, Saadatmand J, Musier-Forsyth K, Gottlinger H, Kleiman L: The interaction between HIV-1 Gag and human lysyl-tRNA synthetase during viral assembly. J Biol Chem. 2003 Jul 25;278(30):27644-51. Epub 2003 May 19. [PubMed
]
- Halwani R, Cen S, Javanbakht H, Saadatmand J, Kim S, Shiba K, Kleiman L: Cellular distribution of Lysyl-tRNA synthetase and its interaction with Gag during human immunodeficiency virus type 1 assembly. J Virol. 2004 Jul;78(14):7553-64. [PubMed
]
- Park SG, Kim HJ, Min YH, Choi EC, Shin YK, Park BJ, Lee SW, Kim S: Human lysyl-tRNA synthetase is secreted to trigger proinflammatory response. Proc Natl Acad Sci U S A. 2005 May 3;102(18):6356-61. Epub 2005 Apr 25. [PubMed
]
- Guzzo CM, Yang DC: Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA synthetase and p38 in vitro. Biochem Biophys Res Commun. 2008 Jan 25;365(4):718-23. Epub 2007 Nov 20. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Guo M, Ignatov M, Musier-Forsyth K, Schimmel P, Yang XL: Crystal structure of tetrameric form of human lysyl-tRNA synthetase: Implications for multisynthetase complex formation. Proc Natl Acad Sci U S A. 2008 Feb 19;105(7):2331-6. Epub 2008 Feb 13. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
6133 |
| Enzyme 12 Name |
Alpha-aminoadipic semialdehyde synthase, mitochondrial |
| Enzyme 12 Synonyms |
- LKR/SDH
- Lysine ketoglutarate reductase
- LKR
- LOR
- Saccharopine dehydrogenase
- SDH
|
| Enzyme 12 Gene Name |
AASS |
| Enzyme 12 Protein Sequence |
>Alpha-aminoadipic semialdehyde synthase, mitochondrial
MLQVHRTGLGRLGVSLSKGLHHKAVLAVRREDVNAWERRAPLAPKHIKGITNLGYKVLIQ
PSNRRAIHDKDYVKAGGILQEDISEACLILGVKRPPEEKLMSRKTYAFFSHTIKAQEANM
GLLDEILKQEIRLIDYEKMVDHRGVRVVAFGQWAGVAGMINILHGMGLRLLALGHHTPFM
HIGMAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQAIFNELPC
EYVEPHELKEVSQTGDLRKVYGTVLSRHHHLVRKTDAVYDPAEYDKHPERYISRFNTDIA
PYTTCLINGIYWEQNTPRLLTRQDAQSLLAPGKFSPAGVEGCPALPHKLVAICDISADTG
GSIEFMTECTTIEHPFCMYDADQHIIHDSVEGSGILMCSIDNLPAQLPIEATECFGDMLY
PYVEEMILSDATQPLESQNFSPVVRDAVITSNGTLPDKYKYIQTLRESRERAQSLSMGTR
RKVLVLGSGYISEPVLEYLSRDGNIEITVGSDMKNQIEQLGKKYNINPVSMDICKQEEKL
GFLVAKQDLVISLLPYVLHPLVAKACITNKVNMVTASYITPALKELEKSVEDAGITIIGE
LGLDPGLDHMLAMETIDKAKEVGATIESYISYCGGLPAPEHSNNPLRYKFSWSPVGVLMN
VMQSATYLLDGKVVNVAGGISFLDAVTSMDFFPGLNLEGYPNRDSTKYAEIYGISSAHTL
LRGTLRYKGYMKALNGFVKLGLINREALPAFRPEANPLTWKQLLCDLVGISPSSEHDVLK
EAVLKKLGGDNTQLEAAEWLGLLGDEQVPQAESILDALSKHLVMKLSYGPEEKDMIVMRD
SFGIRHPSGHLEHKTIDLVAYGDINGFSAMAKTVGLPTAMAAKMLLDGEIGAKGLMGPFS
KEIYGPILERIKAEGIIYTTQSTIKP
|
| Enzyme 12 Number of Residues |
926 |
| Enzyme 12 Molecular Weight |
102130.9 |
| Enzyme 12 Theoretical pI |
6.62 |
| Enzyme 12 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 12 General Function |
Involved in oxidoreductase activity |
| Enzyme 12 Specific Function |
Bifunctional enzyme that catalyzes the first two steps in lysine degradation. The N-terminal and the C-terminal contain lysine-ketoglutarate reductase and saccharopine dehydrogenase activity, respectively |
| Enzyme 12 Pathways |
|
| Enzyme 12 Reactions |
- N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H+ [RN:R02313]
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
Not Available |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q9UDR5  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
AASS_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>2781 bp
ATGCTGCAAGTACATAGGACTGGACTGGGCAGGCTGGGGGTCAGCCTCTCCAAGGGTCTT
CACCACAAAGCTGTGTTGGCCGTCCGGAGGGAGGATGTGAACGCCTGGGAGAGAAGGGCC
CCGCTAGCTCCCAAGCACATCAAAGGCATCACCAATCTGGGATACAAGGTCTTGATACAG
CCTTCGAATCGGCGGGCCATTCATGATAAGGACTATGTCAAAGCTGGTGGCATTCTTCAG
GAGGATATTTCTGAAGCTTGTCTAATTTTAGGAGTTAAAAGACCTCCAGAGGAAAAATTA
ATGTCCAGGAAGACTTATGCATTTTTCTCCCACACAATAAAAGCTCAGGAGGCCAATATG
GGCTTGTTGGATGAGATTCTAAAACAGGAAATTCGCCTTATTGATTATGAGAAAATGGTG
GATCATAGAGGAGTACGGGTAGTGGCATTTGGACAGTGGGCTGGTGTGGCAGGAATGATC
AACATTTTACATGGAATGGGTTTAAGGCTCCTTGCTTTGGGACATCACACACCTTTTATG
CACATTGGCATGGCTCATAACTACAGGAATAGCAGTCAGGCTGTGCAAGCTGTCCGTGAT
GCTGGCTATGAAATATCTTTGGGTTTGATGCCTAAGTCAATAGGACCCTTAACATTTGTG
TTCACAGGAACTGGTAATGTTTCTAAGGGAGCCCAAGCAATCTTTAATGAGCTACCTTGT
GAATATGTGGAGCCCCATGAATTAAAAGAAGTTTCCCAAACTGGAGACCTCAGAAAAGTG
TATGGGACGGTGTTAAGTCGTCATCATCATCTTGTCAGGAAAACAGATGCTGTGTATGAT
CCTGCAGAGTATGACAAACATCCGGAGCGCTACATAAGTCGTTTTAATACTGATATTGCA
CCCTATACAACTTGCTTAATTAATGGAATCTACTGGGAACAAAACACTCCTCGCCTCCTA
ACCCGCCAAGATGCTCAGAGTCTCCTGGCTCCGGGCAAGTTCTCACCTGCTGGTGTGGAA
GGCTGCCCTGCATTACCACACAAACTCGTGGCAATATGTGACATTTCAGCTGACACAGGA
GGGTCTATAGAGTTTATGACTGAGTGTACAACAATAGAGCATCCCTTTTGCATGTATGAT
GCAGACCAGCATATTATTCATGACAGTGTTGAAGGCTCGGGGATCCTGATGTGTTCCATT
GACAATTTGCCGGCACAGCTCCCAATTGAAGCTACAGAATGCTTTGGAGACATGCTTTAC
CCTTATGTTGAAGAAATGATATTATCAGACGCGACACAGCCTCTTGAAAGTCAGAATTTT
TCTCCTGTGGTGAGAGATGCAGTGATTACATCCAACGGTACATTACCTGATAAATATAAA
TATATCCAGACACTCCGGGAGAGCAGGGAACGTGCTCAGTCACTTTCAATGGGCACCAGG
AGAAAGGTTTTGGTTCTTGGATCTGGCTACATATCTGAGCCTGTATTAGAATATTTATCA
AGAGATGGCAATATAGAAATAACAGTAGGATCTGACATGAAGAATCAAATTGAACAGTTA
GGCAAGAAATATAATATTAATCCTGTTAGCATGGACATTTGTAAACAAGAAGAGAAGCTG
GGCTTCTTGGTGGCAAAACAGGATCTTGTCATCAGCTTGTTGCCTTATGTATTGCACCCT
CTTGTGGCCAAGGCCTGCATCACAAACAAAGTTAACATGGTCACTGCAAGCTACATCACA
CCAGCACTAAAAGAATTGGAAAAGAGTGTGGAAGATGCTGGCATCACAATCATTGGTGAA
TTGGGATTGGACCCTGGTCTGGATCACATGTTAGCAATGGAAACAATAGATAAAGCCAAG
GAAGTGGGAGCCACGATTGAATCATATATTTCCTACTGTGGTGGGCTTCCAGCCCCTGAA
CATTCAAACAATCCATTGAGATATAAATTTAGCTGGAGTCCAGTGGGAGTTTTGATGAAT
GTAATGCAGTCTGCCACCTATCTGCTCGATGGAAAGGTTGTGAATGTTGCAGGAGGCATC
TCCTTTCTTGATGCCGTTACGTCCATGGATTTTTTTCCAGGATTAAATTTGGAAGGCTAT
CCTAACAGAGACAGTACGAAATATGCTGAGATTTATGGCATTTCTTCTGCTCACACTTTG
TTGCGGGGGACACTGAGATATAAGGGATATATGAAAGCTTTGAATGGATTTGTAAAATTA
GGTCTTATAAACAGAGAAGCGCTTCCTGCCTTTAGACCTGAGGCCAACCCTCTCACCTGG
AAACAACTCCTCTGTGACCTAGTTGGGATTTCACCCTCCTCTGAGCATGATGTGTTGAAG
GAAGCTGTTCTTAAGAAACTAGGAGGAGACAATACCCAGTTGGAGGCTGCTGAATGGTTG
GGCTTACTTGGGGATGAACAAGTTCCTCAGGCAGAGTCCATTCTGGATGCCCTCTCCAAG
CATTTGGTCATGAAGCTTTCCTATGGTCCTGAAGAAAAAGATATGATTGTGATGAGAGAC
AGCTTTGGAATCAGACATCCTTCTGGACATTTAGAACATAAAACGATTGATCTTGTGGCT
TATGGGGACATCAATGGCTTTTCAGCCATGGCTAAAACCGTGGGGTTACCCACCGCCATG
GCAGCCAAAATGTTGCTTGATGGTGAAATTGGAGCCAAAGGCCTAATGGGGCCCTTTTCA
AAGGAGATCTATGGACCAATATTGGAGCGAATTAAAGCAGAAGGCATTATATATACTACA
CAGAGTACAATTAAACCATAA
|
| Enzyme 12 GenBank Gene ID |
AF229180  |
| Enzyme 12 GeneCard ID |
AASS  |
| Enzyme 12 GenAtlas ID |
AASS  |
| Enzyme 12 HGNC ID |
HGNC:17366  |
| Enzyme 12 Chromosome Location |
7 |
| Enzyme 12 Locus |
7q31.3 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Sacksteder KA, Biery BJ, Morrell JC, Goodman BK, Geisbrecht BV, Cox RP, Gould SJ, Geraghty MT: Identification of the alpha-aminoadipic semialdehyde synthase gene, which is defective in familial hyperlysinemia. Am J Hum Genet. 2000 Jun;66(6):1736-43. Epub 2000 Apr 20. [PubMed
]
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
7261 |
| Enzyme 13 Name |
PR domain zinc finger protein 2 |
| Enzyme 13 Synonyms |
- GATA-3-binding protein G3B
- Lysine N-methyltransferase 8
- MTB-ZF
- MTE-binding protein
- PR domain-containing protein 2
- Retinoblastoma protein-interacting zinc finger protein
- Zinc finger protein RIZ
|
| Enzyme 13 Gene Name |
PRDM2 |
| Enzyme 13 Protein Sequence |
>PR domain zinc finger protein 2
MNQNTTEPVAATETLAEVPEHVLRGLPEEVRLFPSAVDKTRIGVWATKPILKGKKFGPFV
GDKKKRSQVKNNVYMWEVYYPNLGWMCIDATDPEKGNWLRYVNWACSGEEQNLFPLEINR
AIYYKTLKPIAPGEELLVWYNGEDNPEIAAAIEEERASARSKRSSPKSRKGKKKSQENKN
KGNKIQDIQLKTSEPDFTSANMRDSAEGPKEDEEKPSASALEQPATLQEVASQEVPPELA
TPAPAWEPQPEPDERLEAAACEVNDLGEEEEEEEEEDEEEEEDDDDDELEDEGEEEASMP
NENSVKEPEIRCDEKPEDLLEEPKTTSEETLEDCSEVTPAMQIPRTKEEANGDVFETFMF
PCQHCERKFTTKQGLERHMHIHISTVNHAFKCKYCGKAFGTQINRRRHERRHEAGLKRKP
SQTLQPSEDLADGKASGENVASKDDSSPPSLGPDCLIMNSEKASQDTINSSVVEENGEVK
ELHPCKYCKKVFGTHTNMRRHQRRVHERHLIPKGVRRKGGLEEPQPPAEQAQATQNVYVP
STEPEEEGEADDVYIMDISSNISENLNYYIDGKIQTNNNTSNCDVIEMESASADLYGINC
LLTPVTVEITQNIKTTQVPVTEDLPKEPLGSTNSEAKKRRTASPPALPKIKAETDSDPMV
PSCSLSLPLSISTTEAVSFHKEKSVYLSSKLKQLLQTQDKLTPAGISATEIAKLGPVCVS
APASMLPVTSSRFKRRTSSPPSSPQHSPALRDFGKPSDGKAAWTDAGLTSKKSKLESHSD
SPAWSLSGRDERETVSPPCFDEYKMSKEWTASSAFSSVCNQQPLDLSSGVKQKAEGTGKT
PVQWESVLDLSVHKKHCSDSEGKEFKESHSVQPTCSAVKKRKPTTCMLQKVLLNEYNGID
LPVENPADGTRSPSPCKSLEAQPDPDLGPGSGFPAPTVESTPDVCPSSPALQTPSLSSGQ
LPPLLIPTDPSSPPPCPPVLTVATPPPPLLPTVPLPAPSSSASPHPCPSPLSNATAQSPL
PILSPTVSPSPSPIPPVEPLMSAASPGPPTLSSSSSSSSSSSSFSSSSSSSSPSPPPLSA
ISSVVSSGDNLEASLPMISFKQEELENEGLKPREEPQSAAEQDVVVQETFNKNFVCNVCE
SPFLSIKDLTKHLSIHAEEWPFKCEFCVQLFKDKTDLSEHRFLLHGVGNIFVCSVCKKEF
AFLCNLQQHQRDLHPDKVCTHHEFESGTLRPQNFTDPSKAHVEHMQSLPEDPLETSKEEE
ELNDSSEELYTTIKIMASGIKTKDPDVRLGLNQHYPSFKPPPFQYHHRNPMGIGVTATNF
TTHNIPQTFTTAIRCTKCGKGVDNMPELHKHILACASASDKKRYTPKKNPVPLKQTVQPK
NGVVVLDNSGKNAFRRMGQPKRLNFSVELSKMSSNKLKLNALKKKNQLVQKAILQKNKSA
KQKADLKNACESSSHICPYCNREFTYIGSLNKHAAFSCPKKPLSPPKKKVSHSSKKGGHS
SPASSDKNSNSNHRRRTADAEIKMQSMQTPLGKTRARSSGPTQVPLPSSSFRSKQNVKFA
ASVKSKKPSSSSLRNSSPIRMAKITHVEGKKPKAVAKNHSAQLSSKTSRSLHVRVQKSKA
VLQSKSTLASKKRTDRFNIKSRERSGGPVTRSLQLAAAADLSENKREDGSAKQELKDFSY
SLRLASRCSPPAAPYITRQYRKVKAPAAAQFQGPFFKE
|
| Enzyme 13 Number of Residues |
1718 |
| Enzyme 13 Molecular Weight |
188913.7 |
| Enzyme 13 Theoretical pI |
7.33 |
| Enzyme 13 GO Classification |
| Function |
- DNA binding
- binding
- cation binding
- ion binding
- metal ion binding
- nucleic acid binding
- transcription regulator activity
- transition metal ion binding
- zinc ion binding
|
| Process |
- biological regulation
- regulation of biological process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
|
| Component |
- cell part
- intracellular
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 13 General Function |
Involved in DNA binding |
| Enzyme 13 Specific Function |
S-adenosyl-L-methionine-dependent histone methyltransferase that specifically methylates 'Lys-9' of histone H3. May function as a DNA-binding transcription factor. Binds to the macrophage-specific TPA-responsive element (MTE) of the HMOX1 (heme oxygenase 1) gene and may act as a transcriptional activator of this gene |
| Enzyme 13 Pathways |
Not Available |
| Enzyme 13 Reactions |
- S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
56417724  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q13029  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
PRDM2_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>5157 bp
ATGAATCAGAACACTACTGAGCCTGTGGCGGCCACCGAGACCCTGGCTGAGGTACCCGAA
CATGTGCTGCGAGGACTTCCGGAGGAAGTGAGGCTTTTCCCTTCTGCTGTTGACAAGACC
CGGATTGGTGTCTGGGCCACTAAACCAATTTTAAAAGGCAAAAAATTTGGGCCATTTGTT
GGTGATAAGAAAAAAAGATCTCAGGTTAAGAATAATGTATACATGTGGGAGGTGTATTAC
CCAAATTTGGGATGGATGTGCATTGATGCCACTGATCCAGAGAAGGGAAACTGGCTGCGA
TATGTGAATTGGGCTTGCTCAGGAGAAGAGCAAAATTTATTCCCACTGGAAATCAACAGA
GCCATTTACTATAAAACTTTAAAGCCAATCGCGCCGGGCGAGGAGCTCCTGGTCTGGTAC
AATGGGGAAGACAACCCTGAGATAGCAGCTGCGATTGAGGAAGAGCGAGCCAGCGCCCGG
AGCAAGCGGAGCTCCCCCAAGAGCCGGAAAGGGAAGAAAAAATCCCAGGAAAATAAAAAC
AAAGGAAACAAAATCCAAGACATACAACTGAAGACAAGTGAGCCAGATTTCACCTCTGCA
AATATGAGAGATTCTGCAGAAGGTCCTAAAGAAGACGAAGAGAAGCCTTCAGCCTCAGCA
CTTGAGCAGCCGGCCACCCTCCAGGAGGTGGCCAGTCAGGAGGTGCCTCCAGAACTAGCA
ACCCCTGCCCCTGCCTGGGAGCCACAGCCAGAACCAGACGAGCGATTAGAAGCGGCAGCT
TGTGAGGTGAATGATTTGGGGGAAGAGGAGGAGGAGGAAGAGGAGGAGGATGAAGAAGAA
GAAGAAGATGATGATGATGATGAGTTGGAAGACGAGGGGGAAGAAGAAGCCAGCATGCCA
AATGAAAATTCTGTGAAAGAGCCAGAAATACGGTGTGATGAGAAGCCAGAAGATTTATTA
GAGGAACCAAAAACAACTTCAGAAGAAACTCTTGAAGACTGCTCAGAGGTAACACCTGCC
ATGCAAATCCCCAGAACTAAAGAAGAGGCCAATGGTGATGTATTTGAAACGTTTATGTTT
CCGTGTCAACATTGTGAAAGGAAGTTTACAACCAAACAGGGGCTTGAGCGTCACATGCAT
ATCCATATATCCACCGTCAATCATGCTTTCAAATGCAAGTACTGTGGGAAAGCCTTTGGC
ACACAGATTAACCGGCGGCGACATGAGCGGCGCCATGAAGCAGGGTTAAAGCGGAAACCC
AGCCAAACACTACAGCCGTCAGAGGATCTGGCTGATGGCAAAGCATCTGGAGAAAACGTT
GCTTCAAAAGATGATTCGAGTCCTCCCAGTCTTGGGCCAGACTGTCTGATCATGAATTCA
GAGAAGGCTTCCCAAGACACAATAAATTCTTCTGTCGTAGAAGAGAATGGGGAAGTTAAA
GAACTTCATCCGTGCAAATATTGTAAAAAGGTTTTTGGAACTCATACTAATATGAGACGG
CATCAGCGTAGAGTTCACGAACGTCATCTGATTCCCAAAGGTGTACGGCGAAAAGGAGGC
CTTGAAGAGCCCCAGCCTCCAGCAGAACAGGCCCAGGCCACCCAGAACGTGTATGTACCA
AGCACAGAGCCGGAGGAGGAAGGGGAAGCAGATGATGTGTACATCATGGACATTTCTAGC
AATATCTCTGAAAACTTAAATTACTATATTGATGGTAAAATTCAAACTAATAACAACACT
AGTAACTGTGATGTGATTGAGATGGAGTCTGCTTCGGCAGATTTGTATGGTATAAATTGT
CTGCTCACTCCAGTTACAGTGGAAATTACTCAAAATATAAAGACCACACAGGTCCCTGTA
ACAGAAGATCTTCCTAAAGAGCCTTTGGGCAGCACAAATAGTGAGGCCAAGAAGCGGAGA
ACTGCGAGCCCACCTGCACTGCCCAAAATTAAGGCCGAAACAGACTCTGACCCCATGGTC
CCCTCTTGCTCTTTAAGTCTTCCTCTTAGCATATCAACAACAGAGGCAGTGTCTTTCCAC
AAAGAGAAAAGTGTTTATTTGTCATCAAAGCTCAAACAACTTCTTCAAACCCAAGATAAA
CTAACTCCTGCAGGGATTTCAGCAACTGAAATAGCTAAATTAGGTCCTGTTTGTGTGTCT
GCTCCTGCATCAATGTTGCCTGTGACCTCAAGTAGGTTTAAGAGGCGGACCAGCTCTCCT
CCCAGTTCTCCACAGCACAGTCCTGCCCTTCGAGACTTTGGAAAGCCAAGTGATGGGAAA
GCAGCATGGACCGATGCCGGGCTGACTTCCAAAAAATCCAAATTAGAAAGTCACAGCGAC
TCACCAGCATGGAGTTTGTCTGGGAGAGATGAGAGAGAAACTGTGAGCCCTCCATGCTTT
GATGAATATAAAATGTCTAAAGAGTGGACAGCTAGTTCTGCTTTTAGCAGTGTGTGCAAC
CAGCAGCCACTGGATTTATCCAGCGGTGTCAAACAGAAGGCTGAGGGTACAGGCAAGACT
CCAGTCCAGTGGGAATCTGTCTTAGATCTCAGTGTGCATAAAAAGCATTGTAGTGACTCT
GAAGGCAAGGAATTCAAAGAAAGTCATTCAGTGCAGCCTACGTGTAGTGCTGTAAAGAAA
AGGAAACCAACCACCTGCATGCTGCAGAAGGTTCTTCTCAATGAATATAATGGCATCGAT
TTACCTGTAGAAAACCCTGCAGATGGGACCAGGAGCCCAAGTCCTTGTAAATCCCTAGAA
GCTCAGCCAGATCCTGACCTCGGTCCGGGCTCTGGTTTCCCTGCCCCTACTGTTGAGTCC
ACACCTGATGTTTGTCCTTCATCACCTGCCCTGCAGACACCCTCCCTTTCATCCGGTCAG
CTGCCTCCTCTCTTGATCCCCACAGATCCCTCTTCCCCTCCACCCTGTCCCCCGGTATTA
ACTGTTGCCACTCCGCCCCCTCCCCTCCTTCCTACCGTACCTCTTCCAGCCCCCTCTTCC
AGTGCATCTCCACACCCATGCCCCTCTCCACTCTCAAATGCCACCGCACAGTCCCCACTT
CCAATTCTGTCCCCAACAGTGTCCCCCTCTCCCTCTCCCATTCCTCCCGTGGAGCCCCTG
ATGTCTGCCGCCTCACCCGGGCCTCCAACACTTTCTTCTTCCTCCTCTTCATCTTCCTCC
TCCTCTTCGTTTTCTTCTTCATCTTCCTCCTCTTCTCCTTCTCCACCTCCTCTCTCCGCA
ATATCATCTGTTGTTTCCTCTGGTGATAATCTGGAGGCTTCTCTCCCCATGATATCTTTC
AAACAGGAGGAATTAGAGAATGAAGGTCTGAAACCCAGGGAAGAGCCCCAGTCTGCTGCT
GAACAGGATGTTGTTGTTCAGGAAACATTCAACAAAAACTTTGTTTGCAACGTCTGTGAA
TCACCTTTTCTTTCCATTAAAGATCTAACCAAACATTTATCTATTCATGCTGAAGAATGG
CCCTTCAAATGTGAATTTTGTGTGCAGCTTTTTAAGGATAAAACGGACTTGTCAGAACAT
CGCTTTTTGCTTCATGGAGTTGGGAATATCTTTGTGTGTTCTGTTTGTAAAAAAGAATTT
GCTTTTTTGTGCAATTTGCAGCAGCACCAGCGAGATCTCCACCCAGATAAGGTGTGCACA
CATCACGAGTTTGAAAGCGGGACTCTGAGGCCCCAGAACTTTACAGATCCCAGCAAGGCC
CATGTAGAGCATATGCAGAGCTTGCCAGAAGATCCTTTAGAAACTTCTAAAGAAGAAGAG
GAGTTAAATGATTCCTCTGAAGAGCTTTACACGACTATAAAAATAATGGCTTCTGGAATA
AAGACAAAAGATCCAGATGTTCGATTGGGCCTCAATCAGCATTACCCAAGCTTTAAACCA
CCTCCATTTCAGTACCATCACCGTAACCCCATGGGGATTGGTGTGACAGCCACAAATTTC
ACTACACACAATATTCCACAGACTTTCACTACCGCCATTCGCTGCACAAAGTGTGGAAAA
GGTGTCGACAATATGCCGGAGTTGCACAAACATATCCTGGCTTGTGCTTCTGCAAGTGAC
AAGAAGAGGTACACGCCTAAGAAAAACCCAGTACCATTAAAACAAACTGTGCAACCCAAA
AATGGCGTGGTGGTTTTAGATAACTCTGGGAAAAATGCCTTCCGACGAATGGGACAGCCC
AAAAGGCTTAACTTTAGTGTTGAGCTCAGCAAAATGTCGTCGAATAAGCTCAAATTAAAT
GCATTGAAGAAAAAAAATCAGCTAGTACAGAAAGCAATTCTTCAGAAAAACAAATCTGCA
AAGCAGAAGGCCGACTTGAAAAATGCTTGTGAGTCATCCTCTCACATCTGCCCTTACTGT
AATCGAGAGTTCACTTACATTGGAAGCCTGAATAAACACGCCGCCTTCAGCTGTCCCAAA
AAACCCCTTTCTCCTCCCAAAAAAAAAGTTTCTCATTCATCTAAGAAAGGTGGACACTCA
TCACCTGCAAGTAGTGACAAAAACAGTAACAGCAACCACCGCAGACGGACAGCGGATGCG
GAGATTAAAATGCAAAGCATGCAGACTCCGTTGGGCAAGACCAGAGCCCGCAGCTCAGGC
CCCACCCAAGTCCCACTTCCCTCCTCATCCTTCAGGTCCAAGCAGAACGTCAAGTTTGCA
GCTTCGGTGAAATCCAAAAAACCAAGCTCCTCCTCTTTAAGGAACTCCAGCCCGATAAGA
ATGGCCAAAATAACTCATGTTGAGGGGAAAAAACCTAAAGCTGTGGCCAAGAATCATTCT
GCTCAGCTTTCCAGCAAAACATCACGGAGCCTGCACGTGAGGGTACAGAAAAGCAAAGCT
GTTTTACAAAGCAAATCCACCTTGGCGAGTAAGAAAAGAACAGACCGGTTCAATATAAAA
TCTAGAGAGCGGAGTGGGGGGCCAGTCACCCGGAGCCTTCAGCTGGCAGCTGCTGCTGAC
TTGAGTGAGAACAAGAGAGAGGACGGCAGCGCCAAGCAGGAGCTGAAGGACTTCAGCTAC
AGCCTCCGCTTGGCGTCCCGATGCTCTCCACCAGCGGCCCCGTACATCACCAGGCAGTAT
AGGAAGGTCAAAGCTCCAGCTGCAGCCCAGTTCCAGGGACCATTCTTCAAAGAGTAG
|
| Enzyme 13 GenBank Gene ID |
AL031277  |
| Enzyme 13 GeneCard ID |
PRDM2  |
| Enzyme 13 GenAtlas ID |
PRDM2  |
| Enzyme 13 HGNC ID |
HGNC:9347  |
| Enzyme 13 Chromosome Location |
1 |
| Enzyme 13 Locus |
1p36.21 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Buyse IM, Shao G, Huang S: The retinoblastoma protein binds to RIZ, a zinc-finger protein that shares an epitope with the adenovirus E1A protein. Proc Natl Acad Sci U S A. 1995 May 9;92(10):4467-71. [PubMed
]
- Liu L, Shao G, Steele-Perkins G, Huang S: The retinoblastoma interacting zinc finger gene RIZ produces a PR domain-lacking product through an internal promoter. J Biol Chem. 1997 Jan 31;272(5):2984-91. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Shapiro VS, Lee P, Winoto A: Identification and cloning of the G3B cDNA encoding a 3' segment of a protein binding to GATA-3. Gene. 1995 Oct 3;163(2):329-30. [PubMed
]
- Muraosa Y, Takahashi K, Yoshizawa M, Shibahara S: cDNA cloning of a novel protein containing two zinc-finger domains that may function as a transcription factor for the human heme-oxygenase-1 gene. Eur J Biochem. 1996 Feb 1;235(3):471-9. [PubMed
]
- Kim KC, Geng L, Huang S: Inactivation of a histone methyltransferase by mutations in human cancers. Cancer Res. 2003 Nov 15;63(22):7619-23. [PubMed
]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed
]
- Briknarova K, Zhou X, Satterthwait A, Hoyt DW, Ely KR, Huang S: Structural studies of the SET domain from RIZ1 tumor suppressor. Biochem Biophys Res Commun. 2008 Feb 15;366(3):807-13. Epub 2007 Dec 17. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
7398 |
| Enzyme 14 Name |
Histone-lysine N-methyltransferase MLL |
| Enzyme 14 Synonyms |
- ALL-1
- CXXC-type zinc finger protein 7
- Lysine N-methyltransferase 2A
- KMT2A
- Trithorax-like protein
- Zinc finger protein HRX
- MLL cleavage product N320
- N-terminal cleavage product of 320 kDa
- p320
- MLL cleavage product C180
- C-terminal cleavage product of 180 kDa
- p180
|
| Enzyme 14 Gene Name |
MLL |
| Enzyme 14 Protein Sequence |
>Histone-lysine N-methyltransferase MLL
MAHSCRWRFPARPGTTGGGGGGGRRGLGGAPRQRVPALLLPPGPPVGGGGPGAPPSPPAV
AAAAAAAGSSGAGVPGGAAAASAASSSSASSSSSSSSSASSGPALLRVGPGFDAALQVSA
AIGTNLRRFRAVFGESGGGGGSGEDEQFLGFGSDEEVRVRSPTRSPSVKTSPRKPRGRPR
SGSDRNSAILSDPSVFSPLNKSETKSGDKIKKKDSKSIEKKRGRPPTFPGVKIKITHGKD
ISELPKGNKEDSLKKIKRTPSATFQQATKIKKLRAGKLSPLKSKFKTGKLQIGRKGVQIV
RRRGRPPSTERIKTPSGLLINSELEKPQKVRKDKEGTPPLTKEDKTVVRQSPRRIKPVRI
IPSSKRTDATIAKQLLQRAKKGAQKKIEKEAAQLQGRKVKTQVKNIRQFIMPVVSAISSR
IIKTPRRFIEDEDYDPPIKIARLESTPNSRFSAPSCGSSEKSSAASQHSSQMSSDSSRSS
SPSVDTSTDSQASEEIQVLPEERSDTPEVHPPLPISQSPENESNDRRSRRYSVSERSFGS
RTTKKLSTLQSAPQQQTSSSPPPPLLTPPPPLQPASSISDHTPWLMPPTIPLASPFLPAS
TAPMQGKRKSILREPTFRWTSLKHSRSEPQYFSSAKYAKEGLIRKPIFDNFRPPPLTPED
VGFASGFSASGTAASARLFSPLHSGTRFDMHKRSPLLRAPRFTPSEAHSRIFESVTLPSN
RTSAGTSSSGVSNRKRKRKVFSPIRSEPRSPSHSMRTRSGRLSSSELSPLTPPSSVSSSL
SISVSPLATSALNPTFTFPSHSLTQSGESAEKNQRPRKQTSAPAEPFSSSSPTPLFPWFT
PGSQTERGRNKDKAPEELSKDRDADKSVEKDKSRERDREREKENKRESRKEKRKKGSEIQ
SSSALYPVGRVSKEKVVGEDVATSSSAKKATGRKKSSSHDSGTDITSVTLGDTTAVKTKI
LIKKGRGNLEKTNLDLGPTAPSLEKEKTLCLSTPSSSTVKHSTSSIGSMLAQADKLPMTD
KRVASLLKKAKAQLCKIEKSKSLKQTDQPKAQGQESDSSETSVRGPRIKHVCRRAAVALG
RKRAVFPDDMPTLSALPWEEREKILSSMGNDDKSSIAGSEDAEPLAPPIKPIKPVTRNKA
PQEPPVKKGRRSRRCGQCPGCQVPEDCGVCTNCLDKPKFGGRNIKKQCCKMRKCQNLQWM
PSKAYLQKQAKAVKKKEKKSKTSEKKDSKESSVVKNVVDSSQKPTPSAREDPAPKKSSSE
PPPRKPVEEKSEEGNVSAPGPESKQATTPASRKSSKQVSQPALVIPPQPPTTGPPRKEVP
KTTPSEPKKKQPPPPESGPEQSKQKKVAPRPSIPVKQKPKEKEKPPPVNKQENAGTLNIL
STLSNGNSSKQKIPADGVHRIRVDFKEDCEAENVWEMGGLGILTSVPITPRVVCFLCASS
GHVEFVYCQVCCEPFHKFCLEENERPLEDQLENWCCRRCKFCHVCGRQHQATKQLLECNK
CRNSYHPECLGPNYPTKPTKKKKVWICTKCVRCKSCGSTTPGKGWDAQWSHDFSLCHDCA
KLFAKGNFCPLCDKCYDDDDYESKMMQCGKCDRWVHSKCENLSDEMYEILSNLPESVAYT
CVNCTERHPAEWRLALEKELQISLKQVLTALLNSRTTSHLLRYRQAAKPPDLNPETEESI
PSRSSPEGPDPPVLTEVSKQDDQQPLDLEGVKRKMDQGNYTSVLEFSDDIVKIIQAAINS
DGGQPEIKKANSMVKSFFIRQMERVFPWFSVKKSRFWEPNKVSSNSGMLPNAVLPPSLDH
NYAQWQEREENSHTEQPPLMKKIIPAPKPKGPGEPDSPTPLHPPTPPILSTDRSREDSPE
LNPPPGIEDNRQCALCLTYGDDSANDAGRLLYIGQNEWTHVNCALWSAEVFEDDDGSLKN
VHMAVIRGKQLRCEFCQKPGATVGCCLTSCTSNYHFMCSRAKNCVFLDDKKVYCQRHRDL
IKGEVVPENGFEVFRRVFVDFEGISLRRKFLNGLEPENIHMMIGSMTIDCLGILNDLSDC
EDKLFPIGYQCSRVYWSTTDARKRCVYTCKIVECRPPVVEPDINSTVEHDENRTIAHSPT
SFTESSSKESQNTAEIISPPSPDRPPHSQTSGSCYYHVISKVPRIRTPSYSPTQRSPGCR
PLPSAGSPTPTTHEIVTVGDPLLSSGLRSIGSRRHSTSSLSPQRSKLRIMSPMRTGNTYS
RNNVSSVSTTGTATDLESSAKVVDHVLGPLNSSTSLGQNTSTSSNLQRTVVTVGNKNSHL
DGSSSSEMKQSSASDLVSKSSSLKGEKTKVLSSKSSEGSAHNVAYPGIPKLAPQVHNTTS
RELNVSKIGSFAEPSSVSFSSKEALSFPHLHLRGQRNDRDQHTDSTQSANSSPDEDTEVK
TLKLSGMSNRSSIINEHMGSSSRDRRQKGKKSCKETFKEKHSSKSFLEPGQVTTGEEGNL
KPEFMDEVLTPEYMGQRPCNNVSSDKIGDKGLSMPGVPKAPPMQVEGSAKELQAPRKRTV
KVTLTPLKMENESQSKNALKESSPASPLQIESTSPTEPISASENPGDGPVAQPSPNNTSC
QDSQSNNYQNLPVQDRNLMLPDGPKPQEDGSFKRRYPRRSARARSNMFFGLTPLYGVRSY
GEEDIPFYSSSTGKKRGKRSAEGQVDGADDLSTSDEDDLYYYNFTRTVISSGGEERLASH
NLFREEEQCDLPKISQLDGVDDGTESDTSVTATTRKSSQIPKRNGKENGTENLKIDRPED
AGEKEHVTKSSVGHKNEPKMDNCHSVSRVKTQGQDSLEAQLSSLESSRRVHTSTPSDKNL
LDTYNTELLKSDSDNNNSDDCGNILPSDIMDFVLKNTPSMQALGESPESSSSELLNLGEG
LGLDSNREKDMGLFEVFSQQLPTTEPVDSSVSSSISAEEQFELPLELPSDLSVLTTRSPT
VPSQNPSRLAVISDSGEKRVTITEKSVASSESDPALLSPGVDPTPEGHMTPDHFIQGHMD
ADHISSPPCGSVEQGHGNNQDLTRNSSTPGLQVPVSPTVPIQNQKYVPNSTDSPGPSQIS
NAAVQTTPPHLKPATEKLIVVNQNMQPLYVLQTLPNGVTQKIQLTSSVSSTPSVMETNTS
VLGPMGGGLTLTTGLNPSLPTSQSLFPSASKGLLPMSHHQHLHSFPAATQSSFPPNISNP
PSGLLIGVQPPPDPQLLVSESSQRTDLSTTVATPSSGLKKRPISRLQTRKNKKLAPSSTP
SNIAPSDVVSNMTLINFTPSQLPNHPSLLDLGSLNTSSHRTVPNIIKRSKSSIMYFEPAP
LLPQSVGGTAATAAGTSTISQDTSHLTSGSVSGLASSSSVLNVVSMQTTTTPTSSASVPG
HVTLTNPRLLGTPDIGSISNLLIKASQQSLGIQDQPVALPPSSGMFPQLGTSQTPSTAAI
TAASSICVLPSTQTTGITAASPSGEADEHYQLQHVNQLLASKTGIHSSQRDLDSASGPQV
SNFTQTVDAPNSMGLEQNKALSSAVQASPTSPGGSPSSPSSGQRSASPSVPGPTKPKPKT
KRFQLPLDKGNGKKHKVSHLRTSSSEAHIPDQETTSLTSGTGTPGAEAEQQDTASVEQSS
QKECGQPAGQVAVLPEVQVTQNPANEQESAEPKTVEEEESNFSSPLMLWLQQEQKRKESI
TEKKPKKGLVFEISSDDGFQICAESIEDAWKSLTDKVQEARSNARLKQLSFAGVNGLRML
GILHDAVVFLIEQLSGAKHCRNYKFRFHKPEEANEPPLNPHGSARAEVHLRKSAFDMFNF
LASKHRQPPEYNPNDEEEEEVQLKSARRATSMDLPMPMRFRHLKKTSKEAVGVYRSPIHG
RGLFCKRNIDAGEMVIEYAGNVIRSIQTDKREKYYDSKGIGCYMFRIDDSEVVDATMHGN
AARFINHSCEPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKFPIEDASNKLPCNCG
AKKCRKFLN
|
| Enzyme 14 Number of Residues |
3969 |
| Enzyme 14 Molecular Weight |
431760.5 |
| Enzyme 14 Theoretical pI |
9.56 |
| Enzyme 14 GO Classification |
| Function |
- DNA binding
- binding
- catalytic activity
- cation binding
- histone methyltransferase activity (H3-K4 specific)
- histone-lysine N-methyltransferase activity
- ion binding
- metal ion binding
- methyltransferase activity
- nucleic acid binding
- protein binding
- protein methyltransferase activity
- protein-lysine N-methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
- transition metal ion binding
- zinc ion binding
|
| Process |
- biological regulation
- cellular component organization at cellular level
- cellular process
- chromatin modification
- chromatin organization
- chromosome organization
- organelle organization
- regulation of biological process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
- regulation of transcription, DNA-dependent
|
| Component |
- histone methyltransferase complex
- intracellular membrane-bounded organelle
- macromolecular complex
- membrane-bounded organelle
- methyltransferase complex
- nucleus
- organelle
- protein complex
|
|
| Enzyme 14 General Function |
Involved in DNA binding |
| Enzyme 14 Specific Function |
Histone methyltransferase that plays an essential role in early development and hematopoiesis. Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac). In the MLL1/MLL complex, it specifically mediates H3K4me, a specific tag for epigenetic transcriptional activation. Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity. Has no activity toward histone H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward H3 acetylated on 'Lys-9'. Required for transcriptional activation of HOXA9. Promotes PPP1R15A-induced apoptosis |
| Enzyme 14 Pathways |
Not Available |
| Enzyme 14 Reactions |
- S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
34305635  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q03164  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
MLL1_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>11910 bp
ATGGCGCACAGCTGTCGGTGGCGCTTCCCCGCCCGACCCGGGACCACCGGGGGCGGCGGC
GGCGGGGGGCGCCGGGGCCTAGGGGGCGCCCCGCGGCAACGCGTCCCGGCCCTGCTGCTT
CCCCCCGGGCCCCCGGTCGGCGGTGGCGGCCCCGGGGCGCCCCCCTCCCCCCCGGCTGTG
GCGGCCGCGGCGGCGGCGGCGGGAAGCAGCGGGGCTGGGGTTCCAGGGGGAGCGGCCGCC
GCCTCAGCAGCCTCCTCGTCGTCCGCCTCGTCTTCGTCTTCGTCATCGTCCTCAGCCTCT
TCAGGGCCGGCCCTGCTCCGGGTGGGCCCGGGCTTCGACGCGGCGCTGCAGGTCTCGGCC
GCCATCGGCACCAACCTGCGCCGGTTCCGGGCCGTGTTTGGGGAGAGCGGCGGGGGAGGC
GGCAGCGGAGAGGATGAGCAATTCTTAGGTTTTGGCTCAGATGAAGAAGTCAGAGTGCGA
AGTCCCACAAGGTCTCCTTCAGTTAAAACTAGTCCTCGAAAACCTCGTGGGAGACCTAGA
AGTGGCTCTGACCGAAATTCAGCTATCCTCTCAGATCCATCTGTGTTTTCCCCTCTAAAT
AAATCAGAGACCAAATCTGGAGATAAGATCAAGAAGAAAGATTCTAAAAGTATAGAAAAG
AAGAGAGGAAGACCTCCCACCTTCCCTGGAGTAAAAATCAAAATAACACATGGAAAGGAC
ATTTCAGAGTTACCAAAGGGAAACAAAGAAGATAGCCTGAAAAAAATTAAAAGGACACCT
TCTGCTACGTTTCAGCAAGCCACAAAGATTAAAAAATTAAGAGCAGGTAAACTCTCTCCT
CTCAAGTCTAAGTTTAAGACAGGGAAGCTTCAAATAGGAAGGAAGGGGGTACAAATTGTA
CGACGGAGAGGAAGGCCTCCATCAACAGAAAGGATAAAGACCCCTTCGGGTCTCCTCATT
AATTCTGAACTGGAAAAGCCCCAGAAAGTCCGGAAAGACAAGGAAGGAACACCTCCACTT
ACAAAAGAAGATAAGACAGTTGTCAGACAAAGCCCTCGAAGGATTAAGCCAGTTAGGATT
ATTCCTTCTTCAAAAAGGACAGATGCAACCATTGCTAAGCAACTCTTACAGAGGGCAAAA
AAGGGGGCTCAAAAGAAAATTGAAAAAGAAGCAGCTCAGCTGCAGGGAAGAAAGGTGAAG
ACACAGGTCAAAAATATTCGACAGTTCATCATGCCTGTTGTCAGTGCTATCTCCTCGCGG
ATCATTAAGACCCCTCGGCGGTTTATAGAGGATGAGGATTATGACCCTCCAATTAAAATT
GCCCGATTAGAGTCTACACCGAATAGTAGATTCAGTGCCCCGTCCTGTGGATCTTCTGAA
AAATCAAGTGCAGCTTCTCAGCACTCCTCTCAAATGTCTTCAGACTCCTCTCGATCTAGT
AGCCCCAGTGTTGATACCTCCACAGACTCTCAGGCTTCTGAGGAGATTCAGGTACTTCCT
GAGGAGCGGAGCGATACCCCTGAAGTTCATCCTCCACTGCCCATTTCCCAGTCCCCAGAA
AATGAGAGTAATGATAGGAGAAGCAGAAGGTATTCAGTGTCGGAGAGAAGTTTTGGATCT
AGAACGACGAAAAAATTATCAACTCTACAAAGTGCCCCCCAGCAGCAGACCTCCTCGTCT
CCACCTCCACCTCTGCTGACTCCACCGCCACCACTGCAGCCAGCCTCCAGTATCTCTGAC
CACACACCTTGGCTTATGCCTCCAACAATCCCCTTAGCATCACCATTTTTGCCTGCTTCC
ACTGCTCCTATGCAAGGGAAGCGAAAATCTATTTTGCGAGAACCGACATTTAGGTGGACT
TCTTTAAAGCATTCTAGGTCAGAGCCACAATACTTTTCCTCAGCAAAGTATGCCAAAGAA
GGTCTTATTCGCAAACCAATATTTGATAATTTCCGACCCCCTCCACTAACTCCCGAGGAC
GTTGGCTTTGCATCTGGTTTTTCTGCATCTGGTACCGCTGCTTCAGCCCGATTGTTTTCG
CCACTCCATTCTGGAACAAGGTTTGATATGCACAAAAGGAGCCCTCTTCTGAGAGCTCCA
AGATTTACTCCAAGTGAGGCTCACTCTAGAATATTTGAGTCTGTAACCTTGCCTAGTAAT
CGAACTTCTGCTGGAACATCTTCTTCAGGAGTATCCAATAGAAAAAGGAAAAGAAAAGTG
TTTAGTCCTATTCGATCTGAACCAAGATCTCCTTCTCACTCCATGAGGACAAGAAGTGGA
AGGCTTAGTAGTTCTGAGCTCTCACCTCTCACCCCCCCGTCTTCTGTCTCTTCCTCGTTA
AGCATTTCTGTTAGTCCTCTTGCCACTAGTGCCTTAAACCCAACTTTTACTTTTCCTTCT
CATTCCCTGACTCAGTCTGGGGAATCTGCAGAGAAAAATCAGAGACCAAGGAAGCAGACT
AGTGCTCCGGCAGAGCCATTTTCATCAAGTAGTCCTACTCCTCTCTTCCCTTGGTTTACC
CCAGGCTCTCAGACTGAAAGAGGGAGAAATAAAGACAAGGCCCCCGAGGAGCTGTCCAAA
GATCGAGATGCTGACAAGAGCGTGGAGAAGGACAAGAGTAGAGAGAGAGACCGGGAGAGA
GAAAAGGAGAATAAGCGGGAGTCAAGGAAAGAGAAAAGGAAAAAGGGATCAGAAATTCAG
AGTAGTTCTGCTTTGTATCCTGTGGGTAGGGTTTCCAAAGAGAAGGTTGTTGGTGAAGAT
GTTGCCACTTCATCTTCTGCCAAAAAAGCAACAGGGCGGAAGAAGTCTTCATCACATGAT
TCTGGGACTGATATTACTTCTGTGACTCTTGGGGATACAACAGCTGTCAAAACCAAAATA
CTTATAAAGAAAGGGAGAGGAAATCTGGAAAAAACCAACTTGGACCTCGGCCCAACTGCC
CCATCCCTGGAGAAGGAGAAAACCCTCTGCCTTTCCACTCCTTCATCTAGCACTGTTAAA
CATTCCACTTCCTCCATAGGCTCCATGTTGGCTCAGGCAGACAAGCTTCCAATGACTGAC
AAGAGGGTTGCCAGCCTCCTAAAAAAGGCCAAAGCTCAGCTCTGCAAGATTGAGAAGAGT
AAGAGTCTTAAACAAACCGACCAGCCCAAAGCACAGGGTCAAGAAAGTGACTCATCAGAG
ACCTCTGTGCGAGGACCCCGGATTAAACATGTCTGCAGAAGAGCAGCTGTTGCCCTTGGC
CGAAAACGAGCTGTGTTTCCTGATGACATGCCCACCCTGAGTGCCTTACCATGGGAAGAA
CGAGAAAAGATTTTGTCTTCCATGGGGAATGATGACAAGTCATCAATTGCTGGCTCAGAA
GATGCTGAACCTCTTGCTCCACCCATCAAACCAATTAAACCTGTCACTAGAAACAAGGCA
CCCCAGGAACCTCCAGTAAAGAAAGGACGTCGATCGAGGCGGTGTGGGCAGTGTCCCGGC
TGCCAGGTGCCTGAGGACTGTGGTGTTTGTACTAATTGCTTAGATAAGCCCAAGTTTGGT
GGTCGCAATATAAAGAAGCAGTGCTGCAAGATGAGAAAATGTCAGAATCTACAATGGATG
CCTTCCAAAGCCTACCTGCAGAAGCAAGCTAAAGCTGTGAAAAAGAAAGAGAAAAAGTCT
AAGACCAGTGAAAAGAAAGACAGCAAAGAGAGCAGTGTTGTGAAGAACGTGGTGGACTCT
AGTCAGAAACCTACCCCATCAGCAAGAGAGGATCCTGCCCCAAAGAAAAGCAGTAGTGAG
CCTCCTCCACGAAAGCCCGTCGAGGAAAAGAGTGAAGAAGGGAATGTCTCGGCCCCTGGG
CCTGAATCCAAACAGGCCACCACTCCAGCTTCCAGGAAGTCAAGCAAGCAGGTCTCCCAG
CCAGCACTGGTCATCCCGCCTCAGCCACCTACTACAGGACCGCCAAGAAAAGAAGTTCCC
AAAACCACTCCTAGTGAGCCCAAGAAAAAGCAGCCTCCACCACCAGAATCAGGTCCAGAG
CAGAGCAAACAGAAAAAAGTGGCTCCCCGCCCAAGTATCCCTGTAAAACAAAAACCAAAA
GAAAAGGAAAAACCACCTCCGGTCAATAAGCAGGAGAATGCAGGCACTTTGAACATCCTC
AGCACTCTCTCCAATGGCAATAGTTCTAAGCAAAAAATTCCAGCAGATGGAGTCCACAGG
ATCAGAGTGGACTTTAAGGAGGATTGTGAAGCAGAAAATGTGTGGGAGATGGGAGGCTTA
GGAATCTTGACTTCTGTTCCTATAACACCCAGGGTGGTTTGCTTTCTCTGTGCCAGTAGT
GGGCATGTAGAGTTTGTGTATTGCCAAGTCTGTTGTGAGCCCTTCCACAAGTTTTGTTTA
GAGGAGAACGAGCGCCCTCTGGAGGACCAGCTGGAAAATTGGTGTTGTCGTCGTTGCAAA
TTCTGTCACGTTTGTGGAAGGCAACATCAGGCTACAAAGCAGCTGCTGGAGTGTAATAAG
TGCCGAAACAGCTATCACCCTGAGTGCCTGGGACCAAACTACCCCACCAAACCCACAAAG
AAGAAGAAAGTCTGGATCTGTACCAAGTGTGTTCGCTGTAAGAGCTGTGGATCCACAACT
CCAGGCAAAGGGTGGGATGCACAGTGGTCTCATGATTTCTCACTGTGTCATGATTGCGCC
AAGCTCTTTGCTAAAGGAAACTTCTGCCCTCTCTGTGACAAATGTTATGATGATGATGAC
TATGAGAGTAAGATGATGCAATGTGGAAAGTGTGATCGCTGGGTCCATTCCAAATGTGAG
AATCTTTCAGATGAGATGTATGAGATTCTATCTAATCTGCCAGAAAGTGTGGCCTACACT
TGTGTGAACTGTACTGAGCGGCACCCTGCAGAGTGGCGACTGGCCCTTGAAAAAGAGCTG
CAGATTTCTCTGAAGCAAGTTCTGACAGCTTTGTTGAATTCTCGGACTACCAGCCATTTG
CTACGCTACCGGCAGGCTGCCAAGCCTCCAGACTTAAATCCCGAGACAGAGGAGAGTATA
CCTTCCCGCAGCTCCCCCGAAGGACCTGATCCACCAGTTCTTACTGAGGTCAGCAAACAG
GATGATCAGCAGCCTTTAGATCTAGAAGGAGTCAAGAGGAAGATGGACCAAGGGAATTAC
ACATCTGTGTTGGAGTTCAGTGATGATATTGTGAAGATCATTCAAGCAGCCATTAATTCA
GATGGAGGACAGCCAGAAATTAAAAAAGCCAACAGCATGGTCAAGTCCTTCTTCATTCGG
CAAATGGAACGTGTTTTTCCATGGTTCAGTGTCAAAAAGTCCAGGTTTTGGGAGCCAAAT
AAAGTATCAAGCAACAGTGGGATGTTACCAAACGCAGTGCTTCCACCTTCACTTGACCAT
AATTATGCTCAGTGGCAGGAGCGAGAGGAAAACAGCCACACTGAGCAGCCTCCTTTAATG
AAGAAAATCATTCCAGCTCCCAAACCCAAAGGTCCTGGAGAACCAGACTCACCAACTCCT
CTGCATCCTCCTACACCACCAATTTTGAGTACTGATAGGAGTCGAGAAGACAGTCCAGAG
CTGAACCCACCCCCAGGCATAGAAGACAATAGACAGTGTGCGTTATGTTTGACTTATGGT
GATGACAGTGCTAATGATGCTGGTCGTTTACTATATATTGGCCAAAATGAGTGGACACAT
GTAAATTGTGCTTTGTGGTCAGCGGAAGTGTTTGAAGATGATGACGGATCACTAAAGAAT
GTGCATATGGCTGTGATCAGGGGCAAGCAGCTGAGATGTGAATTCTGCCAAAAGCCAGGA
GCCACCGTGGGTTGCTGTCTCACATCCTGCACCAGCAACTATCACTTCATGTGTTCCCGA
GCCAAGAACTGTGTCTTTCTGGATGATAAAAAAGTATATTGCCAACGACATCGGGATTTG
ATCAAAGGCGAAGTGGTTCCTGAGAATGGATTTGAAGTTTTCAGAAGAGTGTTTGTGGAC
TTTGAAGGAATCAGCTTGAGAAGGAAGTTTCTCAATGGCTTGGAACCAGAAAATATCCAC
ATGATGATTGGGTCTATGACAATCGACTGCTTAGGAATTCTAAATGATCTCTCCGACTGT
GAAGATAAGCTCTTTCCTATTGGATATCAGTGTTCCAGGGTATACTGGAGCACCACAGAT
GCTCGCAAGCGCTGTGTATATACATGCAAGATAGTGGAGTGCCGTCCTCCAGTCGTAGAG
CCGGATATCAACAGCACTGTTGAACATGATGAAAACAGGACCATTGCCCATAGTCCAACA
TCTTTTACAGAAAGTTCATCAAAAGAGAGTCAAAACACAGCTGAAATTATAAGTCCTCCA
TCACCAGACCGACCTCCTCATTCACAAACCTCTGGCTCCTGTTATTATCATGTCATCTCA
AAGGTCCCCAGGATTCGAACACCCAGTTATTCTCCAACACAGAGATCCCCTGGCTGTCGA
CCGTTGCCTTCTGCAGGAAGTCCTACCCCAACCACTCATGAAATAGTCACAGTAGGTGAT
CCTTTACTCTCCTCTGGACTTCGAAGCATTGGCTCCAGGCGTCACAGTACCTCTTCCTTA
TCACCCCAGCGGTCCAAACTCCGGATAATGTCTCCAATGAGAACTGGGAATACTTACTCT
AGGAATAATGTTTCCTCAGTCTCCACCACCGGGACCGCTACTGATCTTGAATCAAGTGCC
AAAGTAGTTGATCATGTCTTAGGGCCACTGAATTCAAGTACTAGTTTAGGGCAAAACACT
TCCACCTCTTCAAATTTGCAAAGGACAGTGGTTACTGTAGGCAATAAAAACAGTCACTTG
GATGGATCTTCATCTTCAGAAATGAAGCAGTCCAGTGCTTCAGACTTGGTGTCCAAGAGC
TCCTCTTTAAAGGGAGAGAAGACCAAAGTGCTGAGTTCCAAGAGCTCAGAGGGATCTGCA
CATAATGTGGCTTACCCTGGAATTCCTAAACTGGCCCCACAGGTTCATAACACAACATCT
AGAGAACTGAATGTTAGTAAAATCGGCTCCTTTGCTGAACCCTCTTCAGTGTCGTTTTCT
TCTAAAGAGGCCCTCTCCTTCCCACACCTCCATTTGAGAGGGCAAAGGAATGATCGAGAC
CAACACACAGATTCTACCCAATCAGCAAACTCCTCTCCAGATGAAGATACTGAAGTCAAA
ACCTTGAAGCTATCTGGAATGAGCAACAGATCATCCATTATCAACGAACATATGGGATCT
AGTTCCAGAGATAGGAGACAGAAAGGGAAAAAATCCTGTAAAGAAACTTTCAAAGAAAAG
CATTCCAGTAAATCTTTTTTGGAACCTGGTCAGGTGACAACTGGTGAGGAAGGAAACTTG
AAGCCAGAGTTTATGGATGAGGTTTTGACTCCTGAGTATATGGGCCAACGACCATGTAAC
AATGTTTCTTCTGATAAGATTGGTGATAAAGGCCTTTCTATGCCAGGAGTCCCCAAAGCT
CCACCCATGCAAGTAGAAGGATCTGCCAAGGAATTACAGGCACCACGGAAACGCACAGTC
AAAGTGACACTGACACCTCTAAAAATGGAAAATGAGAGTCAATCCAAAAATGCCCTGAAA
GAAAGTAGTCCTGCTTCCCCTTTGCAAATAGAGTCAACATCTCCCACAGAACCAATTTCA
GCCTCTGAAAATCCAGGAGATGGTCCAGTGGCCCAACCAAGCCCCAATAATACCTCATGC
CAGGATTCTCAAAGTAACAACTATCAGAATCTTCCAGTACAGGACAGAAACCTAATGCTT
CCAGATGGCCCCAAACCTCAGGAGGATGGCTCTTTTAAAAGGAGGTATCCCCGTCGCAGT
GCCCGTGCACGTTCTAACATGTTTTTTGGGCTTACCCCACTCTATGGAGTAAGATCCTAT
GGTGAAGAAGACATTCCATTCTACAGCAGCTCAACTGGGAAGAAGCGAGGCAAGAGATCA
GCTGAAGGACAGGTGGATGGGGCCGATGACTTAAGCACTTCAGATGAAGACGACTTATAC
TATTACAACTTCACTAGAACAGTGATTTCTTCAGGTGGAGAGGAACGACTGGCATCCCAT
AATTTATTTCGGGAGGAGGAACAGTGTGATCTTCCAAAAATCTCACAGTTGGATGGTGTT
GATGATGGGACAGAGAGTGATACTAGTGTCACAGCCACAACAAGGAAAAGCAGCCAGATT
CCAAAAAGAAATGGTAAAGAAAATGGAACAGAGAACTTAAAGATTGATAGACCTGAAGAT
GCTGGGGAGAAAGAACATGTCACTAAGAGTTCTGTTGGCCACAAAAATGAGCCAAAGATG
GATAACTGCCATTCTGTAAGCAGAGTTAAAACACAGGGACAAGATTCCTTGGAAGCTCAG
CTCAGCTCATTGGAGTCAAGCCGCAGAGTCCACACAAGTACCCCCTCCGACAAAAATTTA
CTGGACACCTATAATACTGAGCTCCTGAAATCAGATTCAGACAATAACAACAGTGATGAC
TGTGGGAATATCCTGCCTTCAGACATTATGGACTTTGTACTAAAGAATACTCCATCCATG
CAGGCTTTGGGTGAGAGCCCAGAGTCATCTTCATCAGAACTCCTGAATCTTGGTGAAGGA
TTGGGTCTTGACAGTAATCGTGAAAAAGACATGGGTCTTTTTGAAGTATTTTCTCAGCAG
CTGCCTACAACAGAACCTGTGGATAGTAGTGTCTCTTCCTCTATCTCAGCAGAGGAACAG
TTTGAGTTGCCTCTAGAGCTACCATCTGATCTGTCTGTCTTGACCACCCGGAGTCCCACT
GTCCCCAGCCAGAATCCCAGTAGACTAGCTGTTATCTCAGACTCAGGGGAGAAGAGAGTA
ACCATCACAGAAAAATCTGTAGCCTCCTCTGAAAGTGACCCAGCACTGCTGAGCCCAGGA
GTAGATCCAACTCCTGAAGGCCACATGACTCCTGATCATTTTATCCAAGGACACATGGAT
GCAGACCACATCTCTAGCCCTCCTTGTGGTTCAGTAGAGCAAGGTCATGGCAACAATCAG
GATTTAACTAGGAACAGTAGCACCCCTGGCCTTCAGGTACCTGTTTCCCCAACTGTTCCC
ATCCAGAACCAGAAGTATGTGCCCAATTCTACTGATAGTCCTGGCCCGTCTCAGATTTCC
AATGCAGCTGTCCAGACCACTCCACCCCACCTGAAGCCAGCCACTGAGAAACTCATAGTT
GTTAACCAGAACATGCAGCCACTTTATGTTCTCCAAACTCTTCCAAATGGAGTGACCCAA
AAAATCCAATTGACCTCTTCTGTTAGTTCTACACCCAGTGTGATGGAGACAAATACTTCA
GTATTGGGACCCATGGGAGGTGGTCTCACCCTTACCACAGGACTAAATCCAAGCTTGCCA
ACTTCTCAATCTTTGTTCCCTTCTGCTAGCAAAGGATTGCTACCCATGTCTCATCACCAG
CACTTACATTCCTTCCCTGCAGCTACTCAAAGTAGTTTCCCACCAAACATCAGCAATCCT
CCTTCAGGCCTGCTTATTGGGGTTCAGCCTCCTCCGGATCCCCAACTTTTGGTTTCAGAA
TCCAGCCAGAGGACAGACCTCAGTACCACAGTAGCCACTCCATCCTCTGGACTCAAGAAA
AGACCCATATCTCGTCTACAGACCCGAAAGAATAAAAAACTTGCTCCCTCTAGTACCCCT
TCAAACATTGCCCCTTCTGATGTGGTTTCTAATATGACATTGATTAACTTCACACCCTCC
CAGCTTCCTAATCATCCAAGTCTGTTAGATTTGGGGTCACTTAATACTTCATCTCACCGA
ACTGTCCCCAACATCATAAAAAGATCTAAATCTAGCATCATGTATTTTGAACCGGCACCC
CTGTTACCACAGAGTGTGGGAGGAACTGCTGCCACAGCGGCAGGCACATCAACAATAAGC
CAGGATACTAGCCACCTCACATCAGGGTCTGTGTCTGGCTTGGCATCCAGTTCCTCTGTC
TTGAATGTTGTATCCATGCAAACTACCACAACCCCTACAAGTAGTGCGTCAGTTCCAGGA
CACGTCACCTTAACCAACCCAAGGTTGCTTGGTACCCCAGATATTGGCTCAATAAGCAAT
CTTTTAATCAAAGCTAGCCAGCAGAGCCTGGGGATTCAGGACCAGCCTGTGGCTTTACCG
CCAAGTTCAGGAATGTTTCCACAACTGGGGACATCACAGACCCCCTCTACTGCTGCAATA
ACAGCGGCATCTAGCATCTGTGTGCTCCCCTCCACTCAGACTACGGGCATAACAGCCGCT
TCACCTTCTGGGGAAGCAGACGAACACTATCAGCTTCAGCATGTGAACCAGCTCCTTGCC
AGCAAAACTGGGATTCATTCTTCCCAGCGTGATCTTGATTCTGCTTCAGGGCCCCAGGTA
TCCAACTTTACCCAGACGGTAGACGCTCCTAATAGCATGGGACTGGAGCAGAACAAGGCT
TTATCCTCAGCTGTGCAAGCCAGCCCCACCTCTCCTGGGGGTTCTCCATCCTCTCCATCT
TCTGGACAGCGGTCAGCAAGCCCTTCAGTGCCGGGTCCCACTAAACCCAAACCAAAAACC
AAACGGTTTCAGCTGCCTCTAGACAAAGGGAATGGCAAGAAGCACAAAGTTTCCCATTTG
CGGACCAGTTCTTCTGAAGCACACATTCCAGACCAAGAAACGACATCCCTGACCTCAGGC
ACAGGGACTCCAGGAGCAGAGGCTGAGCAGCAGGATACAGCTAGCGTGGAGCAGTCCTCC
CAGAAGGAGTGTGGGCAACCTGCAGGGCAAGTCGCTGTTCTTCCGGAAGTTCAGGTGACC
CAAAATCCAGCAAATGAACAAGAAAGTGCAGAACCTAAAACAGTGGAAGAAGAGGAAAGT
AATTTCAGCTCCCCACTGATGCTTTGGCTTCAGCAAGAACAAAAGCGGAAGGAAAGCATT
ACTGAGAAAAAACCCAAGAAAGGACTTGTTTTTGAAATTTCCAGTGATGATGGCTTTCAG
ATCTGTGCAGAAAGTATTGAAGATGCCTGGAAGTCATTGACAGATAAAGTCCAGGAAGCT
CGATCAAATGCCCGCCTAAAGCAGCTCTCATTTGCAGGTGTTAACGGTTTGAGGATGCTG
GGGATTCTCCATGATGCAGTTGTGTTCCTCATTGAGCAGCTGTCTGGTGCCAAGCACTGT
CGAAATTACAAATTCCGTTTCCACAAGCCAGAGGAGGCCAATGAACCCCCCTTGAACCCT
CACGGCTCAGCCAGGGCTGAAGTCCACCTCAGGAAGTCAGCATTTGACATGTTTAACTTC
CTGGCTTCTAAACATCGTCAGCCTCCTGAATACAACCCCAATGATGAAGAAGAGGAGGAG
GTACAGCTGAAGTCAGCTCGGAGGGCAACTAGCATGGATCTGCCAATGCCCATGCGCTTC
CGGCACTTAAAAAAGACTTCTAAGGAGGCAGTTGGTGTCTACAGGTCTCCCATCCATGGC
CGGGGTCTTTTCTGTAAGAGAAACATTGATGCAGGTGAGATGGTGATTGAGTATGCCGGC
AACGTCATCCGCTCCATCCAGACTGACAAGCGGGAAAAGTATTACGACAGCAAGGGCATT
GGTTGCTATATGTTCCGAATTGATGACTCAGAGGTAGTGGATGCCACCATGCATGGAAAT
GCTGCACGCTTCATCAATCACTCGTGTGAGCCTAACTGCTATTCTCGGGTCATCAATATT
GATGGGCAGAAGCACATTGTCATCTTTGCCATGCGTAAGATCTACCGAGGAGAGGAACTC
ACTTACGACTATAAGTTCCCCATTGAGGATGCCAGCAACAAGCTGCCCTGCAACTGTGGC
GCCAAGAAATGCCGGAAGTTCCTAAACTAA
|
| Enzyme 14 GenBank Gene ID |
AY373585  |
| Enzyme 14 GeneCard ID |
MLL  |
| Enzyme 14 GenAtlas ID |
MLL  |
| Enzyme 14 HGNC ID |
HGNC:7132  |
| Enzyme 14 Chromosome Location |
1 |
| Enzyme 14 Locus |
11q23 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Tkachuk DC, Kohler S, Cleary ML: Involvement of a homolog of Drosophila trithorax by 11q23 chromosomal translocations in acute leukemias. Cell. 1992 Nov 13;71(4):691-700. [PubMed
]
- Nilson I, Lochner K, Siegler G, Greil J, Beck JD, Fey GH, Marschalek R: Exon/intron structure of the human ALL-1 (MLL) gene involved in translocations to chromosomal region 11q23 and acute leukaemias. Br J Haematol. 1996 Jun;93(4):966-72. [PubMed
]
- Yamamoto K, Seto M, Komatsu H, Iida S, Akao Y, Kojima S, Kodera Y, Nakazawa S, Ariyoshi Y, Takahashi T, et al.: Two distinct portions of LTG19/ENL at 19p13 are involved in t(11;19) leukemia. Oncogene. 1993 Oct;8(10):2617-25. [PubMed
]
- Gu Y, Nakamura T, Alder H, Prasad R, Canaani O, Cimino G, Croce CM, Canaani E: The t(4;11) chromosome translocation of human acute leukemias fuses the ALL-1 gene, related to Drosophila trithorax, to the AF-4 gene. Cell. 1992 Nov 13;71(4):701-8. [PubMed
]
- Djabali M, Selleri L, Parry P, Bower M, Young BD, Evans GA: A trithorax-like gene is interrupted by chromosome 11q23 translocations in acute leukaemias. Nat Genet. 1992 Oct;2(2):113-8. [PubMed
]
- Djabali M, Selleri L, Parry P, Bower M, Young B, Evans GA: A trithorax-like gene is interrupted by chromosome 11q23 translocations in acute leukaemias. Nat Genet. 1993 Aug;4(4):431. [PubMed
]
- Marschalek R, Greil J, Lochner K, Nilson I, Siegler G, Zweckbronner I, Beck JD, Fey GH: Molecular analysis of the chromosomal breakpoint and fusion transcripts in the acute lymphoblastic SEM cell line with chromosomal translocation t(4;11). Br J Haematol. 1995 Jun;90(2):308-20. [PubMed
]
- Mbangkollo D, Burnett R, McCabe N, Thirman M, Gill H, Yu H, Rowley JD, Diaz MO: The human MLL gene: nucleotide sequence, homology to the Drosophila trx zinc-finger domain, and alternative splicing. DNA Cell Biol. 1995 Jun;14(6):475-83. [PubMed
]
- Gu Y, Alder H, Nakamura T, Schichman SA, Prasad R, Canaani O, Saito H, Croce CM, Canaani E: Sequence analysis of the breakpoint cluster region in the ALL-1 gene involved in acute leukemia. Cancer Res. 1994 May 1;54(9):2326-30. [PubMed
]
- Forster A, Rabbitts TH: A method for identifying genes within yeast artificial chromosomes: application to isolation of MLL fusion cDNAs from acute leukaemia translocations. Oncogene. 1993 Nov;8(11):3157-60. [PubMed
]
- Hsieh JJ, Ernst P, Erdjument-Bromage H, Tempst P, Korsmeyer SJ: Proteolytic cleavage of MLL generates a complex of N- and C-terminal fragments that confers protein stability and subnuclear localization. Mol Cell Biol. 2003 Jan;23(1):186-94. [PubMed
]
- Taki T, Hayashi Y, Taniwaki M, Seto M, Ueda R, Hanada R, Suzukawa K, Yokota J, Morishita K: Fusion of the MLL gene with two different genes, AF-6 and AF-5alpha, by a complex translocation involving chromosomes 5, 6, 8 and 11 in infant leukemia. Oncogene. 1996 Nov 21;13(10):2121-30. [PubMed
]
- Taki T, Shibuya N, Taniwaki M, Hanada R, Morishita K, Bessho F, Yanagisawa M, Hayashi Y: ABI-1, a human homolog to mouse Abl-interactor 1, fuses the MLL gene in acute myeloid leukemia with t(10;11)(p11.2;q23). Blood. 1998 Aug 15;92(4):1125-30. [PubMed
]
- Cui X, De Vivo I, Slany R, Miyamoto A, Firestein R, Cleary ML: Association of SET domain and myotubularin-related proteins modulates growth control. Nat Genet. 1998 Apr;18(4):331-7. [PubMed
]
- Adler HT, Chinery R, Wu DY, Kussick SJ, Payne JM, Fornace AJ Jr, Tkachuk DC: Leukemic HRX fusion proteins inhibit GADD34-induced apoptosis and associate with the GADD34 and hSNF5/INI1 proteins. Mol Cell Biol. 1999 Oct;19(10):7050-60. [PubMed
]
- Taki T, Kano H, Taniwaki M, Sako M, Yanagisawa M, Hayashi Y: AF5q31, a newly identified AF4-related gene, is fused to MLL in infant acute lymphoblastic leukemia with ins(5;11)(q31;q13q23). Proc Natl Acad Sci U S A. 1999 Dec 7;96(25):14535-40. [PubMed
]
- Sano K, Hayakawa A, Piao JH, Kosaka Y, Nakamura H: Novel SH3 protein encoded by the AF3p21 gene is fused to the mixed lineage leukemia protein in a therapy-related leukemia with t(3;11) (p21;q23). Blood. 2000 Feb 1;95(3):1066-8. [PubMed
]
- Pegram LD, Megonigal MD, Lange BJ, Nowell PC, Rowley JD, Rappaport EF, Felix CA: t(3;11) translocation in treatment-related acute myeloid leukemia fuses MLL with the GMPS (GUANOSINE 5' MONOPHOSPHATE SYNTHETASE) gene. Blood. 2000 Dec 15;96(13):4360-2. [PubMed
]
- Megonigal MD, Cheung NK, Rappaport EF, Nowell PC, Wilson RB, Jones DH, Addya K, Leonard DG, Kushner BH, Williams TM, Lange BJ, Felix CA: Detection of leukemia-associated MLL-GAS7 translocation early during chemotherapy with DNA topoisomerase II inhibitors. Proc Natl Acad Sci U S A. 2000 Mar 14;97(6):2814-9. [PubMed
]
- Daheron L, Veinstein A, Brizard F, Drabkin H, Lacotte L, Guilhot F, Larsen CJ, Brizard A, Roche J: Human LPP gene is fused to MLL in a secondary acute leukemia with a t(3;11) (q28;q23). Genes Chromosomes Cancer. 2001 Aug;31(4):382-9. [PubMed
]
- Ono R, Taki T, Taketani T, Taniwaki M, Kobayashi H, Hayashi Y: LCX, leukemia-associated protein with a CXXC domain, is fused to MLL in acute myeloid leukemia with trilineage dysplasia having t(10;11)(q22;q23). Cancer Res. 2002 Jul 15;62(14):4075-80. [PubMed
]
- Nakamura T, Mori T, Tada S, Krajewski W, Rozovskaia T, Wassell R, Dubois G, Mazo A, Croce CM, Canaani E: ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation. Mol Cell. 2002 Nov;10(5):1119-28. [PubMed
]
- Hsieh JJ, Cheng EH, Korsmeyer SJ: Taspase1: a threonine aspartase required for cleavage of MLL and proper HOX gene expression. Cell. 2003 Oct 31;115(3):293-303. [PubMed
]
- Chinwalla V, Chien A, Odero M, Neilly MB, Zeleznik-Le NJ, Rowley JD: A t(11;15) fuses MLL to two different genes, AF15q14 and a novel gene MPFYVE on chromosome 15. Oncogene. 2003 Mar 6;22(9):1400-10. [PubMed
]
- Kuefer MU, Chinwalla V, Zeleznik-Le NJ, Behm FG, Naeve CW, Rakestraw KM, Mukatira ST, Raimondi SC, Morris SW: Characterization of the MLL partner gene AF15q14 involved in t(11;15)(q23;q14). Oncogene. 2003 Mar 6;22(9):1418-24. [PubMed
]
- von Bergh AR, Wijers PM, Groot AJ, van Zelderen-Bhola S, Falkenburg JH, Kluin PM, Schuuring E: Identification of a novel RAS GTPase-activating protein (RASGAP) gene at 9q34 as an MLL fusion partner in a patient with de novo acute myeloid leukemia. Genes Chromosomes Cancer. 2004 Apr;39(4):324-34. [PubMed
]
- Kojima K, Sakai I, Hasegawa A, Niiya H, Azuma T, Matsuo Y, Fujii N, Tanimoto M, Fujita S: FLJ10849, a septin family gene, fuses MLL in a novel leukemia cell line CNLBC1 derived from chronic neutrophilic leukemia in transformation with t(4;11)(q21;q23). Leukemia. 2004 May;18(5):998-1005. [PubMed
]
- Yokoyama A, Wang Z, Wysocka J, Sanyal M, Aufiero DJ, Kitabayashi I, Herr W, Cleary ML: Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression. Mol Cell Biol. 2004 Jul;24(13):5639-49. [PubMed
]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed
]
- Hayette S, Cornillet-Lefebvre P, Tigaud I, Struski S, Forissier S, Berchet A, Doll D, Gillot L, Brahim W, Delabesse E, Magaud JP, Rimokh R: AF4p12, a human homologue to the furry gene of Drosophila, as a novel MLL fusion partner. Cancer Res. 2005 Aug 1;65(15):6521-5. [PubMed
]
- Dou Y, Milne TA, Tackett AJ, Smith ER, Fukuda A, Wysocka J, Allis CD, Chait BT, Hess JL, Roeder RG: Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF. Cell. 2005 Jun 17;121(6):873-85. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Nousiainen M, Sillje HH, Sauer G, Nigg EA, Korner R: Phosphoproteome analysis of the human mitotic spindle. Proc Natl Acad Sci U S A. 2006 Apr 4;103(14):5391-6. Epub 2006 Mar 24. [PubMed
]
- Cho YW, Hong T, Hong S, Guo H, Yu H, Kim D, Guszczynski T, Dressler GR, Copeland TD, Kalkum M, Ge K: PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex. J Biol Chem. 2007 Jul 13;282(28):20395-406. Epub 2007 May 11. [PubMed
]
- Vasilescu J, Zweitzig DR, Denis NJ, Smith JC, Ethier M, Haines DS, Figeys D: The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells. J Proteome Res. 2007 Jan;6(1):298-305. [PubMed
]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed
]
- Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed
]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Patel A, Dharmarajan V, Vought VE, Cosgrove MS: On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex. J Biol Chem. 2009 Sep 4;284(36):24242-56. Epub 2009 Jun 25. [PubMed
]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Allen MD, Grummitt CG, Hilcenko C, Min SY, Tonkin LM, Johnson CM, Freund SM, Bycroft M, Warren AJ: Solution structure of the nonmethyl-CpG-binding CXXC domain of the leukaemia-associated MLL histone methyltransferase. EMBO J. 2006 Oct 4;25(19):4503-12. Epub 2006 Sep 21. [PubMed
]
- De Guzman RN, Goto NK, Dyson HJ, Wright PE: Structural basis for cooperative transcription factor binding to the CBP coactivator. J Mol Biol. 2006 Feb 3;355(5):1005-13. Epub 2005 Oct 5. [PubMed
]
- Patel A, Dharmarajan V, Cosgrove MS: Structure of WDR5 bound to mixed lineage leukemia protein-1 peptide. J Biol Chem. 2008 Nov 21;283(47):32158-61. Epub 2008 Oct 1. [PubMed
]
- Southall SM, Wong PS, Odho Z, Roe SM, Wilson JR: Structural basis for the requirement of additional factors for MLL1 SET domain activity and recognition of epigenetic marks. Mol Cell. 2009 Jan 30;33(2):181-91. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
8738 |
| Enzyme 15 Name |
Histone-lysine N-methyltransferase MLL3 |
| Enzyme 15 Synonyms |
- Homologous to ALR protein
- Lysine N-methyltransferase 2C
- KMT2C
- Myeloid/lymphoid or mixed-lineage leukemia protein 3
|
| Enzyme 15 Gene Name |
MLL3 |
| Enzyme 15 Protein Sequence |
>Histone-lysine N-methyltransferase MLL3
MSSEEDKSVEQPQPPPPPPEEPGAPAPSPAAADKRPRGRPRKDGASPFQRARKKPRSRGK
TAVEDEDSMDGLETTETETIVETEIKEQSAEEDAEAEVDNSKQLIPTLQRSVSEESANSL
VSVGVEAKISEQLCAFCYCGEKSSLGQGDLKQFRITPGFILPWRNQPSNKKDIDDNSNGT
YEKMQNSAPRKQRGQRKERSPQQNIVSCVSVSTQTASDDQAGKLWDELSLVGLPDAIDIQ
ALFDSTGTCWAHHRCVEWSLGVCQMEEPLLVNVDKAVVSGSTERCAFCKHLGATIKCCEE
KCTQMYHYPCAAGAGTFQDFSHIFLLCPEHIDQAPERSKEDANCAVCDSPGDLLDQFFCT
TCGQHYHGMCLDIAVTPLKRAGWQCPECKVCQNCKQSGEDSKMLVCDTCDKGYHTFCLQP
VMKSVPTNGWKCKNCRICIECGTRSSSQWHHNCLICDNCYQQQDNLCPFCGKCYHPELQK
DMLHCNMCKRWVHLECDKPTDHELDTQLKEEYICMYCKHLGAEMDRLQPGEEVEIAELTT
DYNNEMEVEGPEDQMVFSEQAANKDVNGQESTPGIVPDAVQVHTEEQQKSHPSESLDTDS
LLIAVSSQHTVNTELEKQISNEVDSEDLKMSSEVKHICGEDQIEDKMEVTENIEVVTHQI
TVQQEQLQLLEEPETVVSREESRPPKLVMESVTLPLETLVSPHEESISLCPEEQLVIERL
QGEKEQKENSELSTGLMDSEMTPTIEGCVKDVSYQGGKSIKLSSETESSFSSSADISKAD
VSSSPTPSSDLPSHDMLHNYPSALSSSAGNIMPTTYISVTPKIGMGKPAITKRKFSPGRP
RSKQGAWSTHNTVSPPSWSPDISEGREIFKPRQLPGSAIWSIKVGRGSGFPGKRRPRGAG
LSGRGGRGRSKLKSGIGAVVLPGVSTADISSNKDDEENSMHNTVVLFSSSDKFTLNQDMC
VVCGSFGQGAEGRLLACSQCGQCYHPYCVSIKITKVVLSKGWRCLECTVCEACGKATDPG
RLLLCDDCDISYHTYCLDPPLQTVPKGGWKCKWCVWCRHCGATSAGLRCEWQNNYTQCAP
CASLSSCPVCYRNYREEDLILQCRQCDRWMHAVCQNLNTEEEVENVADIGFDCSMCRPYM
PASNVPSSDCCESSLVAQIVTKVKELDPPKTYTQDGVCLTESGMTQLQSLTVTVPRRKRS
KPKLKLKIINQNSVAVLQTPPDIQSEHSRDGEMDDSREGELMDCDGKSESSPEREAVDDE
TKGVEGTDGVKKRKRKPYRPGIGGFMVRQRSRTGQGKTKRSVIRKDSSGSISEQLPCRDD
GWSEQLPDTLVDESVSVTESTEKIKKRYRKRKNKLEETFPAYLQEAFFGKDLLDTSRQSK
ISLDNLSEDGAQLLYKTNMNTGFLDPSLDPLLSSSSAPTKSGTHGPADDPLADISEVLNT
DDDILGIISDDLAKSVDHSDIGPVTDDPSSLPQPNVNQSSRPLSEEQLDGILSPELDKMV
TDGAILGKLYKIPELGGKDVEDLFTAVLSPANTQPTPLPQPPPPTQLLPIHNQDAFSRMP
LMNGLIGSSPHLPHNSLPPGSGLGTFSAIAQSSYPDARDKNSAFNPMASDPNNSWTSSAP
TVEGENDTMSNAQRSTLKWEKEEALGEMATVAPVLYTNINFPNLKEEFPDWTTRVKQIAK
LWRKASSQERAPYVQKARDNRAALRINKVQMSNDSMKRQQQQDSIDPSSRIDSELFKDPL
KQRESEHEQEWKFRQQMRQKSKQQAKIEATQKLEQVKNEQQQQQQQQFGSQHLLVQSGSD
TPSSGIQSPLTPQPGNGNMSPAQSFHKELFTKQPPSTPTSTSSDDVFVKPQAPPPPPAPS
RIPIQDSLSQAQTSQPPSPQVFSPGSSNSRPPSPMDPYAKMVGTPRPPPVGHSFSRRNSA
APVENCTPLSSVSRPLQMNETTANRPSPVRDLCSSSTTNNDPYAKPPDTPRPVMTDQFPK
SLGLSRSPVVSEQTAKGPIAAGTSDHFTKPSPRADVFQRQRIPDSYARPLLTPAPLDSGP
GPFKTPMQPPPSSQDPYGSVSQASRRLSVDPYERPALTPRPIDNFSHNQSNDPYSQPPLT
PHPAVNESFAHPSRAFSQPGTISRPTSQDPYSQPPGTPRPVVDSYSQSSGTARSNTDPYS
QPPGTPRPTTVDPYSQQPQTPRPSTQTDLFVTPVTNQRHSDPYAHPPGTPRPGISVPYSQ
PPATPRPRISEGFTRSSMTRPVLMPNQDPFLQAAQNRGPALPGPLVRPPDTCSQTPRPPG
PGLSDTFSRVSPSAARDPYDQSPMTPRSQSDSFGTSQTAHDVADQPRPGSEGSFCASSNS
PMHSQGQQFSGVSQLPGPVPTSGVTDTQNTVNMAQADTEKLRQRQKLREIILQQQQQKKI
AGRQEKGSQDSPAVPHPGPLQHWQPENVNQAFTRPPPPYPGNIRSPVAPPLGPRYAVFPK
DQRGPYPPDVASMGMRPHGFRFGFPGGSHGTMPSQERFLVPPQQIQGSGVSPQLRRSVSV
DMPRPLNNSQMNNPVGLPQHFSPQSLPVQQHNILGQAYIELRHRAPDGRQRLPFSAPPGS
VVEASSNLRHGNFIPRPDFPGPRHTDPMRRPPQGLPNQLPVHPDLEQVPPSQQEQGHSVH
SSSMVMRTLNHPLGGEFSEAPLSTSVPSETTSDNLQITTQPSDGLEEKLDSDDPSVKELD
VKDLEGVEVKDLDDEDLENLNLDTEDGKVVELDTLDNLETNDPNLDDLLRSGEFDIIAYT
DPELDMGDKKSMFNEELDLPIDDKLDNQCVSVEPKKKEQENKTLVLSDKHSPQKKSTVTN
EVKTEVLSPNSKVESKCETEKNDENKDNVDTPCSQASAHSDLNDGEKTSLHPCDPDLFEK
RTNRETAGPSANVIQASTQLPAQDVINSCGITGSTPVLSSLLANEKSDNSDIRPSGSPPP
PTLPASPSNHVSSLPPFIAPPGRVLDNAMNSNVTVVSRVNHVFSQGVQVNPGLIPGQSTV
NHSLGTGKPATQTGPQTSQSGTSSMSGPQQLMIPQTLAQQNRERPLLLEEQPLLLQDLLD
QERQEQQQQRQMQAMIRQRSEPFFPNIDFDAITDPIMKAKMVALKGINKVMAQNNLGMPP
MVMSRFPFMGQVVTGTQNSEGQNLGPQAIPQDGSITHQISRPNPPNFGPGFVNDSQRKQY
EEWLQETQQLLQMQQKYLEEQIGAHRKSKKALSAKQRTAKKAGREFPEEDAEQLKHVTEQ
QSMVQKQLEQIRKQQKEHAELIEDYRIKQQQQCAMAPPTMMPSVQPQPPLIPGATPPTMS
QPTFPMVPQQLQHQQHTTVISGHTSPVRMPSLPGWQPNSAPAHLPLNPPRIQPPIAQLPI
KTCTPAPGTVSNANPQSGPPPRVEFDDNNPFSESFQERERKERLREQQERQRIQLMQEVD
RQRALQQRMEMEQHGMVGSEISSSRTSVSQIPFYSSDLPCDFMQPLGPLQQSPQHQQQMG
QVLQQQNIQQGSINSPSTQTFMQTNERRQVGPPSFVPDSPSIPVGSPNFSSVKQGHGNLS
GTSFQQSPVRPSFTPALPAAPPVANSSLPCGQDSTITHGHSYPGSTQSLIQLYSDIIPEE
KGKKKRTRKKKRDDDAESTKAPSTPHSDITAPPTPGISETTSTPAVSTPSELPQQADQES
VEPVGPSTPNMAAGQLCTELENKLPNSDFSQATPNQQTYANSEVDKLSMETPAKTEEIKL
EKAETESCPGQEEPKLEEQNGSKVEGNAVACPVSSAQSPPHSAGAPAAKGDSGNELLKHL
LKNKKSSSLLNQKPEGSICSEDDCTKDNKLVEKQNPAEGLQTLGAQMQGGFGCGNQLPKT
DGGSETKKQRSKRTQRTGEKAAPRSKKRKKDEEEKQAMYSSTDTFTHLKQQNNLSNPPTP
PASLPPTPPPMACQKMANGFATTEELAGKAGVLVSHEVTKTLGPKPFQLPFRPQDDLLAR
ALAQGPKTVDVPASLPTPPHNNQEELRIQDHCGDRDTPDSFVPSSSPESVVGVEVSRYPD
LSLVKEEPPEPVPSPIIPILPSTAGKSSESRRNDIKTEPGTLYFASPFGPSPNGPRSGLI
SVAITLHPTAAENISSVVAAFSDLLHVRIPNSYEVSSAPDVPSMGLVSSHRINPGLEYRQ
HLLLRGPPPGSANPPRLVSSYRLKQPNVPFPPTSNGLSGYKDSSHGIAESAALRPQWCCH
CKVVILGSGVRKSFKDLTLLNKDSRESTKRVEKDIVFCSNNCFILYSSTAQAKNSENKES
IPSLPQSPMRETPSKAFHQYSNNISTLDVHCLPQLPEKASPPASPPIAFPPAFEAAQVEA
KPDELKVTVKLKPRLRAVHGGFEDCRPLNKKWRGMKWKKWSIHIVIPKGTFKPPCEDEID
EFLKKLGTSLKPDPVPKDYRKCCFCHEEGDGLTDGPARLLNLDLDLWVHLNCALWSTEVY
ETQAGALINVELALRRGLQMKCVFCHKTGATSGCHRFRCTNIYHFTCAIKAQCMFFKDKT
MLCPMHKPKGIHEQELSYFAVFRRVYVQRDEVRQIASIVQRGERDHTFRVGSLIFHTIGQ
LLPQQMQAFHSPKALFPVGYEASRLYWSTRYANRRCRYLCSIEEKDGRPVFVIRIVEQGH
EDLVLSDISPKGVWDKILEPVACVRKKSEMLQLFPAYLKGEDLFGLTVSAVARIAESLPG
VEACENYTFRYGRNPLMELPLAVNPTGCARSEPKMSAHVKRFVLRPHTLNSTSTSKSFQS
TVTGELNAPYSKQFVHSKSSQYRKMKTEWKSNVYLARSRIQGLGLYAARDIEKHTMVIEY
IGTIIRNEVANRKEKLYESQNRGVYMFRMDNDHVIDATLTGGPARYINHSCAPNCVAEVV
TFERGHKIIISSSRRIQKGEELCYDYKFDFEDDQHKIPCHCGAVNCRKWMN
|
| Enzyme 15 Number of Residues |
4911 |
| Enzyme 15 Molecular Weight |
541365.6 |
| Enzyme 15 Theoretical pI |
6.46 |
| Enzyme 15 GO Classification |
| Function |
- DNA binding
- binding
- cation binding
- ion binding
- metal ion binding
- nucleic acid binding
- protein binding
- transition metal ion binding
- zinc ion binding
|
| Process |
- biological regulation
- intracellular signaling pathway
- regulation of biological process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
- regulation of transcription, DNA-dependent
- signaling
- signaling pathway
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 15 General Function |
Involved in DNA binding |
| Enzyme 15 Specific Function |
Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Central component of the MLL2/MLL3 complex, a coactivator complex of nuclear receptors, involved in transcriptional coactivation. MLL3 may be a catalytic subunit of this complex. May be involved in leukemogenesis and developmental disorder |
| Enzyme 15 Pathways |
|
| Enzyme 15 Reactions |
- S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
91718902  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q8NEZ4  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
MLL3_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>14736 bp
ATGTCGTCGGAGGAGGACAAGAGCGTGGAGCAGCCGCAGCCGCCGCCACCACCCCCCGAG
GAGCCTGGAGCCCCGGCCCCGAGCCCCGCAGCCGCAGACAAAAGACCTCGGGGCCGGCCT
CGCAAAGATGGCGCTTCCCCTTTCCAGAGAGCCAGAAAGAAACCTCGAAGTAGGGGGAAA
ACTGCAGTGGAAGATGAGGACAGCATGGATGGGCTGGAGACAACAGAAACAGAAACGATT
GTGGAAACAGAAATCAAAGAACAATCTGCAGAAGAGGATGCTGAAGCAGAAGTGGATAAC
AGCAAACAGCTAATTCCAACTCTTCAGCGATCTGTGTCTGAGGAATCGGCAAACTCCCTG
GTCTCTGTTGGTGTAGAAGCCAAAATCAGTGAACAGCTCTGCGCTTTTTGTTACTGTGGG
GAAAAAAGTTCCTTAGGACAAGGAGACTTAAAACAATTCAGAATAACGCCTGGATTTATC
TTGCCATGGAGAAACCAACCTTCTAACAAGAAGGACATTGATGACAACAGCAATGGAACC
TATGAGAAAATGCAAAACTCAGCACCACGAAAACAAAGAGGACAGAGAAAAGAACGATCT
CCTCAGCAGAATATAGTATCTTGTGTAAGTGTAAGCACCCAGACAGCTTCAGATGATCAA
GCTGGTAAACTGTGGGATGAACTCAGTCTGGTTGGGCTTCCAGATGCCATTGATATCCAA
GCCTTATTTGATTCTACAGGCACTTGTTGGGCTCATCACCGTTGTGTGGAGTGGTCACTA
GGAGTATGCCAGATGGAAGAACCATTGTTAGTGAACGTGGACAAAGCTGTTGTCTCAGGG
AGCACAGAACGATGTGCATTTTGTAAGCACCTTGGAGCCACTATCAAATGCTGTGAAGAG
AAATGTACCCAGATGTATCATTATCCTTGTGCTGCAGGAGCCGGCACCTTTCAGGATTTC
AGTCACATCTTCCTGCTTTGTCCAGAACACATTGACCAAGCTCCTGAAAGATCGAAGGAA
GATGCAAACTGTGCAGTGTGCGACAGCCCGGGAGACCTCTTAGATCAGTTCTTTTGTACT
ACTTGTGGTCAGCACTATCATGGAATGTGCCTGGATATAGCGGTTACTCCATTAAAACGT
GCAGGTTGGCAATGTCCTGAGTGCAAAGTGTGCCAGAACTGCAAACAATCGGGAGAAGAT
AGCAAGATGCTAGTGTGTGATACGTGTGACAAAGGGTATCATACTTTTTGTCTTCAACCA
GTTATGAAATCAGTACCAACCAATGGCTGGAAATGCAAAAATTGCAGAATATGTATAGAG
TGTGGCACACGGTCTAGTTCTCAGTGGCACCACAATTGCCTGATATGTGACAATTGTTAC
CAACAGCAGGATAACTTATGTCCCTTCTGTGGGAAGTGTTATCATCCAGAATTGCAGAAA
GACATGCTTCATTGTAATATGTGCAAAAGGTGGGTTCACCTAGAGTGTGACAAACCAACA
GATCATGAACTGGATACTCAGCTCAAAGAAGAGTATATCTGCATGTATTGTAAACACCTG
GGAGCTGAGATGGATCGTTTACAGCCAGGTGAGGAAGTGGAGATAGCTGAGCTCACTACA
GATTATAACAATGAAATGGAAGTTGAAGGCCCTGAAGATCAAATGGTATTCTCAGAGCAG
GCAGCTAATAAAGATGTCAACGGTCAGGAGTCCACTCCTGGAATTGTTCCAGATGCGGTT
CAAGTCCACACTGAAGAGCAACAGAAGAGTCATCCCTCAGAAAGTCTTGACACAGATAGT
CTTCTTATTGCTGTATCATCCCAACATACAGTGAATACTGAATTGGAAAAACAGATTTCT
AATGAAGTTGATAGTGAAGACCTGAAAATGTCTTCTGAAGTGAAGCATATTTGTGGCGAA
GATCAAATTGAAGATAAAATGGAAGTGACAGAAAACATTGAAGTCGTTACACACCAGATC
ACTGTGCAGCAAGAACAACTGCAGTTGTTAGAGGAACCTGAAACAGTGGTATCCAGAGAA
GAATCAAGGCCTCCAAAATTAGTCATGGAATCTGTCACTCTTCCACTAGAAACCTTAGTG
TCCCCACATGAGGAAAGTATTTCATTATGTCCTGAGGAACAGTTGGTTATAGAAAGGCTA
CAAGGAGAAAAGGAACAGAAAGAAAATTCTGAACTTTCTACTGGATTGATGGACTCTGAA
ATGACTCCTACAATTGAGGGTTGTGTGAAAGATGTTTCATACCAAGGAGGCAAATCTATA
AAGTTATCATCTGAGACAGAGTCATCATTTTCATCATCAGCAGACATAAGCAAGGCAGAT
GTGTCTTCCTCCCCAACACCTTCTTCAGACTTGCCTTCGCATGACATGCTGCATAATTAC
CCTTCAGCTCTTAGTTCCTCTGCTGGAAACATCATGCCAACAACTTACATCTCAGTCACT
CCAAAAATTGGCATGGGTAAACCAGCTATTACTAAGAGAAAATTTTCTCCTGGTAGACCT
CGGTCCAAACAGGGGGCTTGGAGTACCCATAATACAGTGAGCCCACCTTCCTGGTCCCCA
GACATTTCAGAAGGTCGGGAAATTTTTAAACCCAGGCAGCTTCCTGGCAGTGCCATTTGG
AGCATCAAAGTGGGCCGTGGGTCTGGATTTCCAGGAAAGCGGAGACCTCGAGGTGCAGGA
CTGTCGGGGCGAGGTGGCCGAGGCAGGTCAAAGCTGAAAAGTGGAATCGGAGCTGTTGTA
TTACCTGGGGTGTCTACTGCAGATATTTCATCAAATAAGGATGATGAAGAAAACTCTATG
CACAATACAGTTGTGTTGTTTTCTAGCAGTGACAAGTTCACTTTGAATCAGGATATGTGT
GTAGTTTGTGGCAGTTTTGGCCAAGGAGCAGAAGGAAGATTACTTGCCTGTTCTCAGTGT
GGTCAGTGTTACCATCCATACTGTGTCAGTATTAAGATCACTAAAGTGGTTCTTAGCAAA
GGTTGGAGGTGTCTTGAGTGCACTGTGTGTGAGGCCTGTGGGAAGGCAACTGACCCAGGA
AGACTCCTGCTGTGTGATGACTGTGACATAAGTTATCACACCTACTGCCTAGACCCTCCA
TTGCAGACAGTTCCCAAAGGAGGCTGGAAGTGCAAATGGTGTGTTTGGTGCAGACACTGT
GGAGCAACATCTGCAGGTCTAAGATGTGAATGGCAGAACAATTACACACAGTGCGCTCCT
TGTGCAAGCTTATCTTCCTGTCCAGTCTGCTATCGAAACTATAGAGAAGAAGATCTTATT
CTGCAATGTAGACAATGTGATAGATGGATGCATGCAGTTTGTCAGAACTTAAATACTGAG
GAAGAAGTGGAAAATGTAGCAGACATTGGTTTTGATTGTAGCATGTGCAGACCCTATATG
CCTGCGTCTAATGTGCCTTCCTCAGACTGCTGTGAATCTTCACTTGTAGCACAAATTGTC
ACAAAAGTAAAAGAGCTAGACCCACCCAAGACTTATACCCAGGATGGTGTGTGTTTGACT
GAATCAGGGATGACTCAGTTACAGAGCCTCACAGTTACAGTTCCAAGAAGAAAACGGTCA
AAACCAAAATTGAAATTGAAGATTATAAATCAGAATAGCGTGGCCGTCCTTCAGACCCCT
CCAGACATCCAATCAGAGCATTCAAGGGATGGTGAAATGGATGATAGTCGAGAAGGAGAA
CTTATGGATTGTGATGGAAAATCAGAATCTAGTCCTGAGCGGGAAGCTGTGGATGATGAA
ACTAAGGGAGTGGAAGGAACAGATGGTGTCAAAAAGAGAAAAAGGAAACCATACAGACCA
GGTATTGGTGGATTTATGGTGCGGCAAAGAAGTCGAACTGGGCAAGGGAAAACCAAAAGA
TCTGTGATCAGAAAAGATTCCTCAGGCTCTATTTCCGAGCAGTTACCTTGCAGAGATGAT
GGCTGGAGTGAGCAGTTACCAGATACTTTAGTTGATGAATCTGTTTCTGTTACTGAAAGC
ACTGAAAAAATAAAGAAGAGATACCGAAAAAGGAAAAATAAGCTTGAAGAAACTTTCCCT
GCCTATTTACAAGAAGCTTTCTTTGGAAAAGATCTTCTAGATACAAGTAGACAAAGCAAG
ATAAGTTTAGATAATCTGTCAGAAGATGGAGCTCAGCTTTTATATAAAACAAACATGAAC
ACAGGTTTCTTGGATCCTTCCTTAGATCCACTACTTAGTTCATCCTCGGCTCCAACAAAA
TCTGGAACTCACGGTCCTGCTGATGACCCATTAGCTGATATTTCTGAAGTTTTAAACACA
GATGATGACATTCTTGGAATAATTTCAGATGATCTAGCAAAATCAGTTGATCATTCAGAT
ATTGGTCCTGTCACTGATGATCCTTCCTCTTTGCCTCAGCCAAATGTCAATCAGAGTTCA
CGACCATTAAGTGAAGAACAGCTAGATGGGATCCTCAGTCCTGAACTAGACAAAATGGTC
ACAGATGGAGCAATTCTTGGAAAATTATATAAAATTCCAGAGCTTGGCGGAAAAGATGTT
GAAGACTTATTTACAGCTGTACTTAGTCCTGCGAACACTCAGCCAACTCCATTGCCACAG
CCTCCCCCACCAACACAGCTGTTGCCAATACACAATCAGGATGCTTTTTCACGGATGCCT
CTCATGAATGGCCTTATTGGATCCAGTCCTCATCTCCCACATAATTCTTTGCCACCTGGA
AGCGGACTGGGAACTTTCTCTGCAATTGCACAATCCTCTTATCCTGATGCCAGGGATAAA
AATTCAGCCTTTAATCCAATGGCAAGTGATCCTAACAACTCTTGGACATCATCAGCTCCC
ACTGTGGAAGGAGAAAATGACACAATGTCGAATGCCCAGAGAAGCACGCTTAAGTGGGAG
AAAGAGGAGGCTCTGGGTGAAATGGCAACTGTTGCCCCAGTTCTCTACACCAATATTAAT
TTCCCCAACTTAAAGGAAGAATTCCCTGATTGGACTACTAGAGTGAAGCAAATTGCCAAA
TTGTGGAGAAAAGCAAGCTCACAAGAAAGAGCACCATATGTGCAAAAAGCCAGAGATAAC
AGAGCTGCTTTACGCATTAATAAAGTACAGATGTCAAATGATTCCATGAAAAGGCAGCAA
CAGCAAGATAGCATTGATCCCAGCTCTCGTATTGATTCGGAGCTTTTTAAAGATCCTTTA
AAGCAAAGAGAATCAGAACATGAACAGGAATGGAAATTTAGACAGCAAATGCGTCAGAAA
AGTAAGCAGCAAGCTAAAATTGAAGCCACACAGAAACTTGAACAGGTGAAAAATGAGCAG
CAGCAGCAGCAACAACAGCAATTTGGTTCTCAGCATCTTCTGGTGCAGTCTGGTTCAGAT
ACACCAAGTAGTGGGATACAGAGTCCCTTGACACCTCAGCCTGGCAATGGAAATATGTCT
CCTGCACAGTCATTCCATAAAGAACTGTTTACAAAACAGCCACCCAGTACCCCTACGTCT
ACATCTTCAGATGATGTGTTTGTAAAGCCACAAGCTCCACCTCCTCCTCCAGCCCCATCC
CGGATTCCCATCCAGGATAGTCTTTCTCAGGCTCAGACTTCTCAGCCACCCTCACCGCAA
GTGTTTTCACCTGGGTCCTCTAACTCACGACCACCATCTCCAATGGATCCATATGCAAAA
ATGGTTGGTACCCCTCGACCACCTCCTGTGGGCCATAGTTTTTCCAGAAGAAATTCTGCT
GCACCAGTGGAAAACTGTACACCTTTATCATCGGTATCTAGGCCCCTTCAAATGAATGAG
ACAACAGCAAATAGGCCATCCCCTGTCAGAGATTTATGTTCTTCTTCCACGACAAATAAT
GACCCCTATGCAAAACCTCCAGACACACCTAGGCCTGTGATGACAGATCAATTTCCCAAA
TCCTTGGGCCTATCCCGGTCTCCTGTAGTTTCAGAACAAACTGCAAAAGGCCCTATAGCA
GCTGGAACCAGTGATCACTTTACTAAACCATCTCCTAGGGCAGATGTGTTTCAAAGACAA
AGGATACCTGACTCATATGCACGACCCTTGTTGACACCTGCACCTCTTGATAGTGGTCCT
GGACCTTTTAAGACTCCAATGCAACCTCCTCCATCCTCTCAGGATCCTTATGGATCAGTG
TCACAGGCATCAAGGCGATTGTCTGTTGACCCTTATGAAAGGCCTGCTTTGACACCAAGA
CCTATAGATAATTTTTCTCATAATCAGTCAAATGATCCATATAGTCAGCCTCCCCTTACC
CCACATCCAGCAGTGAATGAATCTTTTGCCCATCCTTCAAGGGCTTTTTCCCAGCCTGGA
ACCATATCAAGGCCAACATCTCAGGACCCATACTCCCAACCCCCAGGAACTCCACGACCT
GTTGTAGATTCTTATTCCCAATCTTCAGGAACAGCTAGGTCCAATACAGACCCTTACTCT
CAACCTCCTGGAACTCCCCGGCCTACTACTGTTGACCCATATAGTCAGCAGCCCCAAACC
CCAAGACCATCTACACAAACTGACTTGTTTGTTACACCTGTAACAAATCAGAGGCATTCT
GATCCATATGCTCATCCTCCTGGAACACCAAGACCTGGAATTTCTGTCCCTTACTCTCAG
CCACCAGCAACACCAAGGCCAAGGATTTCAGAGGGTTTTACTAGGTCCTCAATGACAAGA
CCAGTCCTCATGCCAAATCAGGATCCTTTCCTGCAAGCAGCACAAAACCGAGGACCAGCT
TTACCTGGCCCGTTGGTAAGGCCACCTGATACATGTTCCCAGACACCTAGGCCCCCTGGA
CCTGGTCTTTCAGACACATTTAGCCGTGTTTCCCCATCTGCTGCCCGTGATCCCTATGAT
CAGTCTCCAATGACTCCAAGATCTCAGTCTGACTCTTTTGGAACAAGTCAAACTGCCCAT
GATGTTGCTGATCAGCCAAGGCCTGGATCAGAGGGGAGCTTCTGTGCATCTTCAAACTCT
CCAATGCACTCCCAAGGCCAGCAGTTCTCTGGTGTCTCCCAACTTCCTGGACCTGTGCCA
ACTTCAGGAGTAACTGATACACAGAATACTGTAAATATGGCCCAAGCAGATACAGAGAAA
TTGAGACAGCGGCAGAAGTTACGTGAAATCATTCTCCAGCAGCAACAGCAGAAGAAGATT
GCAGGTCGACAGGAGAAGGGGTCACAGGACTCACCCGCAGTGCCTCATCCAGGGCCTCTT
CAACACTGGCAACCAGAGAATGTTAACCAGGCTTTCACCAGACCCCCACCTCCCTATCCT
GGGAACATTAGGTCTCCTGTTGCCCCTCCTTTAGGACCTAGATATGCTGTTTTCCCAAAA
GATCAGCGTGGACCCTATCCTCCTGATGTTGCTAGTATGGGGATGAGACCTCATGGATTT
AGATTTGGATTTCCAGGAGGTAGTCATGGTACCATGCCGAGTCAAGAGCGCTTCCTTGTG
CCTCCTCAGCAAATACAGGGATCTGGAGTTTCTCCACAGCTAAGAAGATCAGTATCTGTA
GATATGCCTAGGCCTTTAAATAACTCACAAATGAATAATCCAGTTGGACTTCCTCAGCAT
TTTTCACCACAGAGCTTGCCAGTTCAGCAGCACAACATACTGGGCCAAGCATATATTGAA
CTGAGACATAGGGCTCCTGACGGAAGGCAACGGCTGCCTTTCAGTGCTCCACCTGGCAGC
GTTGTAGAGGCATCTTCTAATCTGAGACATGGAAACTTCATTCCCCGGCCAGACTTTCCG
GGCCCTAGACACACAGACCCCATGCGACGACCTCCCCAGGGTCTACCTAATCAGCTACCT
GTGCACCCAGATTTGGAACAAGTGCCACCATCTCAACAAGAGCAAGGTCATTCTGTCCAT
TCATCTTCTATGGTCATGAGGACTCTGAACCATCCACTAGGTGGTGAATTTTCAGAAGCT
CCTTTGTCAACATCTGTACCGTCTGAAACAACGTCTGATAATTTACAGATAACCACCCAG
CCTTCTGATGGTCTAGAGGAAAAACTTGATTCTGATGACCCTTCTGTGAAGGAACTGGAT
GTTAAAGACCTTGAGGGGGTTGAAGTCAAAGACTTAGATGATGAAGATCTTGAAAACTTA
AATTTAGATACAGAGGATGGCAAGGTAGTTGAATTGGATACTTTAGATAATTTGGAAACT
AATGATCCCAACCTGGATGACCTCTTAAGGTCAGGAGAGTTTGATATCATTGCATATACA
GATCCAGAACTTGACATGGGAGATAAGAAAAGCATGTTTAATGAGGAACTAGACCTTCCA
ATTGATGATAAGTTAGATAATCAGTGTGTATCTGTTGAACCAAAAAAAAAGGAACAAGAA
AACAAAACTCTGGTTCTCTCTGATAAACATTCACCACAGAAAAAATCCACTGTTACCAAT
GAGGTAAAAACGGAAGTACTGTCTCCAAATTCTAAGGTGGAATCCAAATGTGAAACTGAA
AAAAATGATGAGAATAAAGATAATGTTGACACTCCTTGCTCACAGGCTTCTGCTCACTCA
GACCTAAATGATGGAGAAAAGACTTCTTTGCATCCTTGTGATCCAGATCTATTTGAGAAA
AGAACCAATCGAGAAACTGCTGGCCCCAGTGCAAATGTCATTCAGGCATCCACTCAACTA
CCTGCTCAAGATGTAATAAACTCTTGTGGCATAACTGGATCAACTCCAGTTCTCTCAAGT
TTACTTGCTAATGAGAAATCTGATAATTCAGACATTAGGCCATCGGGGTCTCCACCACCA
CCAACTCTGCCGGCCTCCCCATCCAATCATGTGTCAAGTTTGCCTCCTTTCATAGCACCG
CCTGGCCGTGTTTTGGATAATGCCATGAATTCTAATGTGACAGTAGTCTCTAGGGTAAAC
CATGTTTTTTCTCAGGGTGTGCAGGTAAACCCAGGGCTCATTCCAGGTCAATCAACAGTT
AACCACAGTCTGGGGACAGGAAAACCTGCAACTCAAACTGGGCCTCAAACAAGTCAGTCT
GGTACCAGTAGCATGTCTGGACCCCAACAGCTAATGATTCCTCAAACATTAGCACAGCAG
AATAGAGAGAGGCCCCTTCTTCTAGAAGAACAGCCTCTACTTCTACAGGATCTTTTGGAT
CAAGAAAGGCAAGAACAGCAGCAGCAAAGACAGATGCAAGCCATGATTCGTCAGCGATCA
GAACCGTTCTTCCCTAATATTGATTTTGATGCAATTACAGATCCTATAATGAAAGCCAAA
ATGGTGGCCCTTAAAGGTATAAATAAAGTGATGGCACAAAACAATCTGGGCATGCCACCA
ATGGTGATGAGCAGGTTCCCTTTTATGGGCCAGGTGGTAACTGGAACACAGAACAGTGAA
GGACAGAACCTTGGACCACAGGCCATTCCTCAGGATGGCAGTATAACACATCAGATTTCT
AGGCCTAATCCTCCAAATTTTGGTCCAGGCTTTGTCAATGATTCACAGCGTAAGCAGTAT
GAAGAGTGGCTCCAGGAGACCCAACAGCTGCTTCAAATGCAGCAGAAGTATCTTGAAGAA
CAAATTGGTGCTCACAGAAAATCTAAGAAGGCCCTTTCAGCTAAACAACGTACTGCCAAG
AAAGCTGGGCGTGAATTTCCAGAGGAAGATGCAGAACAACTCAAGCATGTTACTGAACAG
CAAAGCATGGTTCAGAAACAGCTAGAACAGATTCGTAAACAACAGAAAGAACATGCTGAA
TTGATTGAAGATTATCGGATCAAACAGCAGCAGCAATGTGCAATGGCCCCACCTACCATG
ATGCCCAGTGTCCAGCCCCAGCCACCCCTAATTCCAGGTGCCACTCCACCCACCATGAGC
CAACCCACCTTTCCCATGGTGCCACAGCAGCTTCAGCACCAGCAGCACACAACAGTTATT
TCTGGCCATACTAGCCCTGTTAGAATGCCCAGTTTACCTGGATGGCAACCCAACAGTGCT
CCTGCCCACCTGCCCCTCAATCCTCCTAGAATTCAGCCCCCAATTGCCCAGTTACCAATA
AAAACTTGTACACCAGCCCCAGGGACAGTCTCAAATGCAAATCCACAGAGTGGACCACCA
CCTCGGGTAGAATTTGATGACAACAATCCCTTTAGTGAAAGTTTTCAAGAACGGGAACGT
AAGGAACGTTTACGAGAACAGCAAGAGAGACAACGGATCCAACTCATGCAGGAGGTAGAT
AGACAAAGAGCTTTGCAGCAGAGGATGGAAATGGAGCAGCATGGTATGGTGGGCTCTGAG
ATAAGTAGTAGTAGGACATCTGTGTCCCAGATTCCCTTCTACAGTTCCGACTTACCTTGT
GATTTTATGCAACCTCTAGGACCCCTTCAGCAGTCTCCACAACACCAACAGCAAATGGGG
CAGGTTTTACAGCAGCAGAATATACAACAAGGATCAATTAATTCACCCTCCACCCAAACT
TTCATGCAGACTAATGAGCGAAGGCAGGTAGGCCCTCCTTCATTTGTTCCTGATTCACCA
TCAATCCCTGTTGGAAGCCCAAATTTTTCTTCTGTGAAGCAGGGACATGGAAATCTTTCT
GGGACCAGCTTCCAGCAGTCCCCAGTGAGGCCTTCTTTTACACCTGCTTTACCAGCAGCA
CCTCCAGTAGCTAATAGCAGTCTCCCATGTGGCCAAGATTCTACTATAACCCATGGACAC
AGTTATCCGGGATCAACCCAATCGCTCATTCAGTTGTATTCTGATATAATCCCAGAGGAA
AAAGGGAAAAAGAAAAGAACAAGAAAGAAGAAAAGAGATGATGATGCAGAATCCACCAAG
GCTCCATCAACTCCCCATTCAGATATAACTGCCCCACCGACTCCAGGCATCTCAGAAACT
ACCTCTACTCCTGCAGTGAGCACACCCAGTGAGCTTCCTCAACAAGCCGACCAAGAGTCG
GTGGAACCAGTCGGCCCATCCACTCCCAATATGGCAGCAGGCCAGCTATGTACAGAATTA
GAGAACAAACTGCCCAATAGTGATTTCTCACAAGCAACTCCAAATCAACAGACGTATGCA
AATTCAGAAGTAGACAAGCTCTCCATGGAAACCCCTGCCAAAACAGAAGAGATAAAACTG
GAAAAGGCTGAGACAGAGTCCTGCCCAGGCCAAGAGGAGCCTAAATTGGAGGAACAGAAT
GGTAGTAAGGTAGAAGGAAACGCTGTAGCCTGTCCTGTCTCCTCAGCACAGAGTCCTCCC
CATTCTGCTGGGGCCCCTGCTGCCAAAGGAGACTCAGGGAATGAACTTCTGAAACACTTG
TTGAAAAATAAAAAGTCATCTTCTCTTTTGAATCAAAAACCTGAGGGCAGTATTTGTTCA
GAAGATGACTGTACAAAGGATAATAAACTAGTTGAGAAGCAGAACCCAGCTGAAGGACTG
CAAACTTTGGGGGCTCAAATGCAAGGTGGTTTTGGATGTGGCAACCAGTTGCCAAAAACA
GATGGAGGAAGTGAAACCAAGAAACAGCGAAGCAAACGGACTCAGAGGACGGGTGAGAAA
GCAGCACCTCGCTCAAAGAAAAGGAAAAAGGACGAAGAGGAGAAACAAGCTATGTACTCT
AGCACTGACACGTTTACCCACTTGAAACAGCAGAATAATTTAAGTAATCCTCCAACACCC
CCTGCCTCTCTTCCTCCTACACCACCTCCTATGGCTTGTCAGAAGATGGCCAATGGTTTT
GCAACAACTGAAGAACTTGCTGGAAAAGCCGGAGTGTTAGTGAGCCATGAAGTTACCAAA
ACTCTAGGACCTAAACCATTTCAGCTGCCCTTCAGACCCCAGGACGACTTGTTGGCCCGA
GCTCTTGCTCAGGGCCCCAAGACAGTTGATGTGCCAGCCTCCCTCCCAACACCACCTCAT
AACAATCAGGAAGAATTAAGGATACAGGATCACTGTGGTGATCGAGATACTCCTGACAGT
TTTGTTCCCTCATCCTCTCCTGAGAGTGTGGTTGGGGTAGAAGTGAGCAGGTATCCAGAT
CTGTCATTGGTCAAGGAGGAGCCTCCAGAACCGGTGCCGTCCCCCATCATTCCAATTCTT
CCTAGCACTGCTGGGAAAAGTTCAGAATCAAGAAGGAATGACATCAAAACTGAGCCAGGC
ACTTTATATTTTGCGTCACCTTTTGGTCCTTCCCCAAATGGTCCCAGATCAGGTCTTATA
TCTGTAGCAATTACTCTGCATCCTACAGCTGCTGAGAACATTAGCAGTGTTGTGGCTGCA
TTTTCCGACCTTCTTCACGTCCGAATCCCTAACAGCTATGAGGTTAGCAGTGCTCCAGAT
GTCCCATCCATGGGTTTGGTCAGTAGCCACAGAATCAACCCGGGTTTGGAGTATCGACAG
CATTTACTTCTCCGTGGGCCTCCGCCAGGATCTGCAAACCCTCCCAGATTAGTGAGCTCT
TACCGGCTGAAGCAGCCTAATGTACCATTTCCTCCAACAAGCAATGGTCTTTCTGGATAT
AAGGATTCTAGTCATGGTATTGCAGAAAGCGCAGCACTCAGACCACAGTGGTGTTGTCAT
TGTAAAGTGGTTATTCTTGGAAGTGGTGTGCGGAAATCTTTCAAAGATCTGACCCTTTTG
AACAAGGATTCCCGAGAAAGCACCAAGAGGGTAGAGAAGGACATTGTCTTCTGTAGTAAT
AACTGCTTTATTCTTTATTCATCAACTGCACAAGCGAAAAACTCAGAAAACAAGGAATCC
ATTCCTTCATTGCCACAATCACCTATGAGAGAAACGCCTTCCAAAGCATTTCATCAGTAC
AGCAACAACATCTCCACTTTGGATGTGCACTGTCTCCCCCAGCTCCCAGAGAAAGCTTCT
CCCCCTGCCTCACCACCCATCGCCTTCCCTCCTGCTTTTGAAGCAGCCCAAGTCGAGGCC
AAGCCAGATGAGCTGAAGGTGACAGTCAAGCTGAAGCCTCGGCTAAGAGCTGTCCATGGT
GGGTTTGAAGATTGCAGGCCGCTCAATAAAAAATGGAGAGGAATGAAATGGAAGAAGTGG
AGCATTCATATTGTAATCCCTAAGGGGACATTTAAACCACCTTGTGAGGATGAAATAGAT
GAATTTCTAAAGAAATTGGGCACTTCCCTTAAACCTGATCCTGTGCCCAAAGACTATCGG
AAATGTTGCTTTTGTCATGAAGAAGGTGATGGATTGACAGATGGACCAGCAAGGCTACTC
AACCTTGACTTGGATCTGTGGGTCCACTTGAACTGCGCTCTGTGGTCCACGGAGGTCTAT
GAGACTCAGGCTGGTGCCTTAATAAATGTGGAGCTAGCTCTGAGGAGAGGCCTACAAATG
AAATGTGTCTTCTGTCACAAGACGGGTGCCACTAGTGGATGCCACAGATTTCGATGCACC
AACATTTATCACTTCACTTGCGCCATTAAAGCACAATGCATGTTTTTTAAGGACAAAACT
ATGCTTTGCCCCATGCACAAACCAAAGGGAATTCATGAGCAAGAATTAAGTTACTTTGCA
GTCTTCAGGAGGGTCTATGTTCAGCGTGATGAGGTGCGACAGATTGCTAGCATCGTGCAA
CGAGGAGAACGGGACCATACCTTTCGCGTGGGTAGCCTCATCTTCCACACAATTGGTCAG
CTGCTTCCACAGCAGATGCAAGCATTCCATTCTCCTAAAGCACTCTTCCCTGTGGGCTAT
GAAGCCAGCCGGCTGTACTGGAGCACTCGCTATGCCAATAGGCGCTGCCGCTACCTGTGC
TCCATTGAGGAGAAGGATGGGCGCCCAGTGTTTGTCATCAGGATTGTGGAACAAGGCCAT
GAAGACCTGGTTCTAAGTGACATCTCACCTAAAGGTGTCTGGGATAAGATTTTGGAGCCT
GTGGCATGTGTGAGAAAAAAGTCTGAAATGCTCCAGCTTTTCCCAGCGTATTTAAAAGGA
GAGGATCTGTTTGGCCTGACCGTCTCTGCAGTGGCACGCATAGCGGAATCACTTCCTGGG
GTTGAGGCATGTGAAAATTATACCTTCCGATACGGCCGAAATCCTCTCATGGAACTTCCT
CTTGCCGTTAACCCCACAGGTTGTGCCCGTTCTGAACCTAAAATGAGTGCCCATGTCAAG
AGGTTTGTGTTAAGGCCTCACACCTTAAACAGCACCAGCACCTCAAAGTCATTTCAGAGC
ACAGTCACTGGAGAACTGAACGCACCTTATAGTAAACAGTTTGTTCACTCCAAGTCATCG
CAGTACCGGAAGATGAAAACTGAATGGAAATCCAATGTGTATCTGGCACGGTCTCGGATT
CAGGGGCTGGGCCTGTATGCTGCTCGAGACATTGAGAAACACACCATGGTCATTGAGTAC
ATCGGGACTATCATTCGAAACGAAGTAGCCAACAGGAAAGAGAAGCTTTATGAGTCTCAG
AACCGTGGTGTGTACATGTTCCGCATGGATAACGACCATGTGATTGACGCGACGCTCACA
GGAGGGCCCGCAAGGTATATCAACCATTCGTGTGCACCTAATTGTGTGGCTGAAGTGGTG
ACTTTTGAGAGAGGACACAAAATTATCATCAGCTCCAGTCGGAGAATCCAGAAAGGAGAA
GAGCTCTGCTATGACTATAAGTTTGACTTTGAAGATGACCAGCACAAGATTCCGTGTCAC
TGTGGAGCTGTGAACTGCCGGAAGTGGATGAACTGA
|
| Enzyme 15 GenBank Gene ID |
NM_170606.2  |
| Enzyme 15 GeneCard ID |
MLL3  |
| Enzyme 15 GenAtlas ID |
MLL3  |
| Enzyme 15 HGNC ID |
HGNC:13726  |
| Enzyme 15 Chromosome Location |
7 |
| Enzyme 15 Locus |
7q36.1 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Ruault M, Brun ME, Ventura M, Roizes G, De Sario A: MLL3, a new human member of the TRX/MLL gene family, maps to 7q36, a chromosome region frequently deleted in myeloid leukaemia. Gene. 2002 Feb 6;284(1-2):73-81. [PubMed
]
- Tan YC, Chow VT: Novel human HALR (MLL3) gene encodes a protein homologous to ALR and to ALL-1 involved in leukemia, and maps to chromosome 7q36 associated with leukemia and developmental defects. Cancer Detect Prev. 2001;25(5):454-69. [PubMed
]
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
- Nagase T, Kikuno R, Ishikawa K, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Apr 28;7(2):143-50. [PubMed
]
- Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Goo YH, Sohn YC, Kim DH, Kim SW, Kang MJ, Jung DJ, Kwak E, Barlev NA, Berger SL, Chow VT, Roeder RG, Azorsa DO, Meltzer PS, Suh PG, Song EJ, Lee KJ, Lee YC, Lee JW: Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins. Mol Cell Biol. 2003 Jan;23(1):140-9. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y: Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006 Aug;23(4):607-18. [PubMed
]
- Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
- Cho YW, Hong T, Hong S, Guo H, Yu H, Kim D, Guszczynski T, Dressler GR, Copeland TD, Kalkum M, Ge K: PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex. J Biol Chem. 2007 Jul 13;282(28):20395-406. Epub 2007 May 11. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
13067 |
| Enzyme 16 Name |
Aminoadipate-semialdehyde synthase |
| Enzyme 16 Synonyms |
- SubName: Aminoadipate-semialdehyde synthase, isoform CRA_a
|
| Enzyme 16 Gene Name |
AASS |
| Enzyme 16 Protein Sequence |
>Aminoadipate-semialdehyde synthase
MLQVHRTGLGRLGVSLSKGLHHKAVLAVRREDVNAWERRAPLAPKHIKGITNLGYKVLIQ
PSNRRAIHDKDYVKAGGILQEDISEACLILGVKRPPEEKLMSRKTYAFFSHTIKAQEANM
GLLDEILKQEIRLIDYEKMVDHRGVRVVAFGQWAGVAGMINILHGMGLRLLALGHHTPFM
HIGMAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQAIFNELPC
EYVEPHELKEVSQTGDLRKVYGTVLSRHHHLVRKTDAVYDPAEYDKHPERYISRFNTDIA
PYTTCLINGIYWEQNTPRLLTRQDAQSLLAPGKFSPAGVEGCPALPHKLVAICDISADTG
GSIEFMTECTTIEHPFCMYDADQHIIHDSVEGSGILMCSIDNLPAQLPIEATECFGDMLY
PYVEEMILSDATQPLESQNFSPVVRDAVITSNGTLPDKYKYIQTLRESRERAQSLSMGTR
RKVLVLGSGYISEPVLEYLSRDGNIEITVGSDMKNQIEQLGKKYNINPVSMDICKQEEKL
GFLVAKQDLVISLLPYVLHPLVAKACITNKVNMVTASYITPALKELEKSVEDAGITIIGE
LGLDPGLDHMLAMETIDKAKEVGATIESYISYCGGLPAPEHSNNPLRYKFSWSPVGVLMN
VMQSATYLLDGKVVNVAGGISFLDAVTSMDFFPGLNLEGYPNRDSTKYAEIYGISSAHTL
LRGTLRYKGYMKALNGFVKLGLINREALPAFRPEANPLTWKQLLCDLVGISPSSEHDVLK
EAVLKKLGGDNTQLEAAEWLGLLGDEQVPQAESILDALSKHLVMKLSYGPEEKDMIVMRD
SFGIRHPSGHLEHKTIDLVAYGDINGFSAMAKTVGLPTAMAAKMLLDGEIGAKGLMGPFS
KEIYGPILERIKAEGIIYTTQSTIKP
|
| Enzyme 16 Number of Residues |
926 |
| Enzyme 16 Molecular Weight |
102130.9 |
| Enzyme 16 Theoretical pI |
6.62 |
| Enzyme 16 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 16 General Function |
Involved in oxidoreductase activity |
| Enzyme 16 Specific Function |
Not Available |
| Enzyme 16 Pathways |
Not Available |
| Enzyme 16 Reactions |
Not Available |
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
13027640  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
A4D0W4  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
A4D0W4_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>2781 bp
ATGCTGCAAGTACATAGGACTGGACTGGGCAGGCTGGGGGTCAGCCTCTCCAAGGGTCTT
CACCACAAAGCTGTGTTGGCCGTCCGGAGGGAGGATGTGAACGCCTGGGAGAGAAGGGCC
CCGCTAGCTCCCAAGCACATCAAAGGCATCACCAATCTGGGATACAAGGTCTTGATACAG
CCTTCGAATCGGCGGGCCATTCATGATAAGGACTATGTCAAAGCTGGTGGCATTCTTCAG
GAGGATATTTCTGAAGCTTGTCTAATTTTAGGAGTTAAAAGACCTCCAGAGGAAAAATTA
ATGTCCAGGAAGACTTATGCATTTTTCTCCCACACAATAAAAGCTCAGGAGGCCAATATG
GGCTTGTTGGATGAGATTCTAAAACAGGAAATTCGCCTTATTGATTATGAGAAAATGGTG
GATCATAGAGGAGTACGGGTAGTGGCATTTGGACAGTGGGCTGGTGTGGCAGGAATGATC
AACATTTTACATGGAATGGGTTTAAGGCTCCTTGCTTTGGGACATCACACACCTTTTATG
CACATTGGCATGGCTCATAACTACAGGAATAGCAGTCAGGCTGTGCAAGCTGTCCGTGAT
GCTGGCTATGAAATATCTTTGGGTTTGATGCCTAAGTCAATAGGACCCTTAACATTTGTG
TTCACAGGAACTGGTAATGTTTCTAAGGGAGCCCAAGCAATCTTTAATGAGCTACCTTGT
GAATATGTGGAGCCCCATGAATTAAAAGAAGTTTCCCAAACTGGAGACCTCAGAAAAGTG
TATGGGACGGTGTTAAGTCGTCATCATCATCTTGTCAGGAAAACAGATGCTGTGTATGAT
CCTGCAGAGTATGACAAACATCCGGAGCGCTACATAAGTCGTTTTAATACTGATATTGCA
CCCTATACAACTTGCTTAATTAATGGAATCTACTGGGAACAAAACACTCCTCGCCTCCTA
ACCCGCCAAGATGCTCAGAGTCTCCTGGCTCCGGGCAAGTTCTCACCTGCTGGTGTGGAA
GGCTGCCCTGCATTACCACACAAACTCGTGGCAATATGTGACATTTCAGCTGACACAGGA
GGGTCTATAGAGTTTATGACTGAGTGTACAACAATAGAGCATCCCTTTTGCATGTATGAT
GCAGACCAGCATATTATTCATGACAGTGTTGAAGGCTCGGGGATCCTGATGTGTTCCATT
GACAATTTGCCGGCACAGCTCCCAATTGAAGCTACAGAATGCTTTGGAGACATGCTTTAC
CCTTATGTTGAAGAAATGATATTATCAGACGCGACACAGCCTCTTGAAAGTCAGAATTTT
TCTCCTGTGGTGAGAGATGCAGTGATTACATCCAACGGTACATTACCTGATAAATATAAA
TATATCCAGACACTCCGGGAGAGCAGGGAACGTGCTCAGTCACTTTCAATGGGCACCAGG
AGAAAGGTTTTGGTTCTTGGATCTGGCTACATATCTGAGCCTGTATTAGAATATTTATCA
AGAGATGGCAATATAGAAATAACAGTAGGATCTGACATGAAGAATCAAATTGAACAGTTA
GGCAAGAAATATAATATTAATCCTGTTAGCATGGACATTTGTAAACAAGAAGAGAAGCTG
GGCTTCTTGGTGGCAAAACAGGATCTTGTCATCAGCTTGTTGCCTTATGTATTGCACCCT
CTTGTGGCCAAGGCCTGCATCACAAACAAAGTTAACATGGTCACTGCAAGCTACATCACA
CCAGCACTAAAAGAATTGGAAAAGAGTGTGGAAGATGCTGGCATCACAATCATTGGTGAA
TTGGGATTGGACCCTGGTCTGGATCACATGTTAGCAATGGAAACAATAGATAAAGCCAAG
GAAGTGGGAGCCACGATTGAATCATATATTTCCTACTGTGGTGGGCTTCCAGCCCCTGAA
CATTCAAACAATCCATTGAGATATAAATTTAGCTGGAGTCCAGTGGGAGTTTTGATGAAT
GTAATGCAGTCTGCCACCTATCTGCTCGATGGAAAGGTTGTGAATGTTGCAGGAGGCATC
TCCTTTCTTGATGCCGTTACGTCCATGGATTTTTTTCCAGGATTAAATTTGGAAGGCTAT
CCTAACAGAGACAGTACGAAATATGCTGAGATTTATGGCATTTCTTCTGCTCACACTTTG
TTGCGGGGGACACTGAGATATAAGGGATATATGAAAGCTTTGAATGGATTTGTAAAATTA
GGTCTTATAAACAGAGAAGCGCTTCCTGCCTTTAGACCTGAGGCCAACCCTCTCACCTGG
AAACAACTCCTCTGTGACCTAGTTGGGATTTCACCCTCCTCTGAGCATGATGTGTTGAAG
GAAGCTGTTCTTAAGAAACTAGGAGGAGACAATACCCAGTTGGAGGCTGCTGAATGGTTG
GGCTTACTTGGGGATGAACAAGTTCCTCAGGCAGAGTCCATTCTGGATGCCCTCTCCAAG
CATTTGGTCATGAAGCTTTCCTATGGTCCTGAAGAAAAAGATATGATTGTGATGAGAGAC
AGCTTTGGAATCAGACATCCTTCTGGACATTTAGAACATAAAACGATTGATCTTGTGGCT
TATGGGGACATCAATGGCTTTTCAGCCATGGCTAAAACCGTGGGGTTACCCACCGCCATG
GCAGCCAAAATGTTGCTTGATGGTGAAATTGGAGCCAAAGGCCTAATGGGGCCCTTTTCA
AAGGAGATCTATGGACCAATATTGGAGCGAATTAAAGCAGAAGGCATTATATATACTACA
CAGAGTACAATTAAACCATAA
|
| Enzyme 16 GenBank Gene ID |
NM_005763.3  |
| Enzyme 16 GeneCard ID |
AASS  |
| Enzyme 16 GenAtlas ID |
AASS  |
| Enzyme 16 HGNC ID |
HGNC:17366  |
| Enzyme 16 Chromosome Location |
7 |
| Enzyme 16 Locus |
7q31.3 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed
]
- Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
14754 |
| Enzyme 17 Name |
Histone-lysine N-methyltransferase EZH2 |
| Enzyme 17 Synonyms |
- ENX-1
- Enhancer of zeste homolog 2
- Lysine N-methyltransferase 6
|
| Enzyme 17 Gene Name |
EZH2 |
| Enzyme 17 Protein Sequence |
>Histone-lysine N-methyltransferase EZH2
MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEW
KQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNF
MVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQ
YNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEEL
KEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFH
ATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPN
NSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKM
KPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPA
PAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQ
NFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVS
CKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDK
YMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGE
ELFFDYRYSQADALKYVGIEREMEIP
|
| Enzyme 17 Number of Residues |
746 |
| Enzyme 17 Molecular Weight |
85362.4 |
| Enzyme 17 Theoretical pI |
7.01 |
| Enzyme 17 GO Classification |
| Function |
- DNA binding
- binding
- nucleic acid binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 17 General Function |
Involved in DNA binding |
| Enzyme 17 Specific Function |
Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Compared to EZH2-containing complexes, it is more abundant in embryonic stem cells and plays a major role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1, CDKN2A and retinoic acid target genes |
| Enzyme 17 Pathways |
Not Available |
| Enzyme 17 Reactions |
- S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
1575349  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
Q15910  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
EZH2_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>2241 bp
ATGGGCCAGACTGGGAAGAAATCTGAGAAGGGACCAGTTTGTTGGCGGAAGCGTGTAAAA
TCAGAGTACATGCGACTGAGACAGCTCAAGAGGTTCAGACGAGCTGATGAAGTAAAGAGT
ATGTTTAGTTCCAATCGTCAGAAAATTTTGGAAAGAACGGAAATCTTAAACCAAGAATGG
AAACAGCGAAGGATACAGCCTGTGCACATCCTGACTTCTGTGAGCTCATTGCGCGGGACT
AGGGAGTGTTCGGTGACCAGTGACTTGGATTTTCCAACACAAGTCATCCCATTAAAGACT
CTGAATGCAGTTGCTTCAGTACCCATAATGTATTCTTGGTCTCCCCTACAGCAGAATTTT
ATGGTGGAAGATGAAACTGTTTTACATAACATTCCTTATATGGGAGATGAAGTTTTAGAT
CAGGATGGTACTTTCATTGAAGAACTAATAAAAAATTATGATGGGAAAGTACACGGGGAT
AGAGAATGTGGGTTTATAAATGATGAAATTTTTGTGGAGTTGGTGAATGCCCTTGGTCAA
TATAATGATGATGACGATGATGATGATGGAGACGATCCTGAAGAAAGAGAAGAAAAGCAG
AAAGATCTGGAGGATCACCGAGATGATAAAGAAAGCCGCCCACCTCGGAAATTTCCTTCT
GATAAAATTTTTGAAGCCATTTCCTCAATGTTTCCAGATAAGGGCACAGCAGAAGAACTA
AAGGAAAAATATAAAGAACTCACCGAACAGCAGCTCCCAGGCGCACTTCCTCCTGAATGT
ACCCCCAACATAGATGGACCAAATGCTAAATCTGTTCAGAGAGAGCAAAGCTTACACTCC
TTTCATACGCTTTTCTGTAGGCGATGTTTTAAATATGACTGCTTCCTACATCCTTTTCAT
GCAACACCCAACACTTATAAGCGGAAGAACACAGAAACAGCTCTAGACAACAAACCTTGT
GGACCACAGTGTTACCAGCATTTGGAGGGAGCAAAGGAGTTTGCTGCTGCTCTCACCGCT
GAGCGGATAAAGACCCCACCAAAACGTCCAGGAGGCCGCAGAAGAGGACGGCTTCCCAAT
AACAGTAGCAGGCCCAGCACCCCCACCATTAATGTGCTGGAATCAAAGGATACAGACAGT
GATAGGGAAGCAGGGACTGAAACGGGGGGAGAGAACAATGATAAAGAAGAAGAAGAGAAG
AAAGATGAAACTTCGAGCTCCTCTGAAGCAAATTCTCGGTGTCAAACACCAATAAAGATG
AAGCCAAATATTGAACCTCCTGAGAATGTGGAGTGGAGTGGTGCTGAAGCCTCAATGTTT
AGAGTCCTCATTGGCACTTACTATGACAATTTCTGTGCCATTGCTAGGTTAATTGGGACC
AAAACATGTAGACAGGTGTATGAGTTTAGAGTCAAAGAATCTAGCATCATAGCTCCAGCT
CCCGCTGAGGATGTGGATACTCCTCCAAGGAAAAAGAAGAGGAAACACCGGTTGTGGGCT
GCACACTGCAGAAAGATACAGCTGAAAAAGGACGGCTCCTCTAACCATGTTTACAACTAT
CAACCCTGTGATCATCCACGGCAGCCTTGTGACAGTTCGTGCCCTTGTGTGATAGCACAA
AATTTTTGTGAAAAGTTTTGTCAATGTAGTTCAGAGTGTCAAAACCGCTTTCCGGGATGC
CGCTGCAAAGCACAGTGCAACACCAAGCAGTGCCCGTGCTACCTGGCTGTCCGAGAGTGT
GACCCTGACCTCTGTCTTACTTGTGGAGCCGCTGACCATTGGGACAGTAAAAATGTGTCC
TGCAAGAACTGCAGTATTCAGCGGGGCTCCAAAAAGCATCTATTGCTGGCACCATCTGAC
GTGGCAGGCTGGGGGATTTTTATCAAAGATCCTGTGCAGAAAAATGAATTCATCTCAGAA
TACTGTGGAGAGATTATTTCTCAAGATGAAGCTGACAGAAGAGGGAAAGTGTATGATAAA
TACATGTGCAGCTTTCTGTTCAACTTGAACAATGATTTTGTGGTGGATGCAACCCGCAAG
GGTAACAAAATTCGTTTTGCAAATCATTCGGTAAATCCAAACTGCTATGCAAAAGTTATG
ATGGTTAACGGTGATCACAGGATAGGTATTTTTGCCAAGAGAGCCATCCAGACTGGCGAA
GAGCTGTTTTTTGATTACAGATACAGCCAGGCTGATGCCCTGAAGTATGTCGGCATCGAA
AGAGAAATGGAAATCCCTTGA
|
| Enzyme 17 GenBank Gene ID |
U61145  |
| Enzyme 17 GeneCard ID |
EZH2  |
| Enzyme 17 GenAtlas ID |
EZH2  |
| Enzyme 17 HGNC ID |
HGNC:3527  |
| Enzyme 17 Chromosome Location |
7 |
| Enzyme 17 Locus |
7q35-q36 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Chen H, Rossier C, Antonarakis SE: Cloning of a human homolog of the Drosophila enhancer of zeste gene (EZH2) that maps to chromosome 21q22.2. Genomics. 1996 Nov 15;38(1):30-7. [PubMed
]
- Laible G, Wolf A, Dorn R, Reuter G, Nislow C, Lebersorger A, Popkin D, Pillus L, Jenuwein T: Mammalian homologues of the Polycomb-group gene Enhancer of zeste mediate gene silencing in Drosophila heterochromatin and at S. cerevisiae telomeres. EMBO J. 1997 Jun 2;16(11):3219-32. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Hobert O, Jallal B, Ullrich A: Interaction of Vav with ENX-1, a putative transcriptional regulator of homeobox gene expression. Mol Cell Biol. 1996 Jun;16(6):3066-73. [PubMed
]
- Cardoso C, Timsit S, Villard L, Khrestchatisky M, Fontes M, Colleaux L: Specific interaction between the XNP/ATR-X gene product and the SET domain of the human EZH2 protein. Hum Mol Genet. 1998 Apr;7(4):679-84. [PubMed
]
- Sewalt RG, van der Vlag J, Gunster MJ, Hamer KM, den Blaauwen JL, Satijn DP, Hendrix T, van Driel R, Otte AP: Characterization of interactions between the mammalian polycomb-group proteins Enx1/EZH2 and EED suggests the existence of different mammalian polycomb-group protein complexes. Mol Cell Biol. 1998 Jun;18(6):3586-95. [PubMed
]
- van der Vlag J, Otte AP: Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation. Nat Genet. 1999 Dec;23(4):474-8. [PubMed
]
- Satijn DP, Hamer KM, den Blaauwen J, Otte AP: The polycomb group protein EED interacts with YY1, and both proteins induce neural tissue in Xenopus embryos. Mol Cell Biol. 2001 Feb;21(4):1360-9. [PubMed
]
- Kuzmichev A, Nishioka K, Erdjument-Bromage H, Tempst P, Reinberg D: Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein. Genes Dev. 2002 Nov 15;16(22):2893-905. [PubMed
]
- Sewalt RG, Lachner M, Vargas M, Hamer KM, den Blaauwen JL, Hendrix T, Melcher M, Schweizer D, Jenuwein T, Otte AP: Selective interactions between vertebrate polycomb homologs and the SUV39H1 histone lysine methyltransferase suggest that histone H3-K9 methylation contributes to chromosomal targeting of Polycomb group proteins. Mol Cell Biol. 2002 Aug;22(15):5539-53. [PubMed
]
- Cao R, Wang L, Wang H, Xia L, Erdjument-Bromage H, Tempst P, Jones RS, Zhang Y: Role of histone H3 lysine 27 methylation in Polycomb-group silencing. Science. 2002 Nov 1;298(5595):1039-43. Epub 2002 Sep 26. [PubMed
]
- Bracken AP, Pasini D, Capra M, Prosperini E, Colli E, Helin K: EZH2 is downstream of the pRB-E2F pathway, essential for proliferation and amplified in cancer. EMBO J. 2003 Oct 15;22(20):5323-35. [PubMed
]
- Pasini D, Bracken AP, Jensen MR, Lazzerini Denchi E, Helin K: Suz12 is essential for mouse development and for EZH2 histone methyltransferase activity. EMBO J. 2004 Oct 13;23(20):4061-71. Epub 2004 Sep 23. [PubMed
]
- Kirmizis A, Bartley SM, Kuzmichev A, Margueron R, Reinberg D, Green R, Farnham PJ: Silencing of human polycomb target genes is associated with methylation of histone H3 Lys 27. Genes Dev. 2004 Jul 1;18(13):1592-605. [PubMed
]
- Kuzmichev A, Jenuwein T, Tempst P, Reinberg D: Different EZH2-containing complexes target methylation of histone H1 or nucleosomal histone H3. Mol Cell. 2004 Apr 23;14(2):183-93. [PubMed
]
- Cao R, Zhang Y: SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex. Mol Cell. 2004 Jul 2;15(1):57-67. [PubMed
]
- Tang X, Milyavsky M, Shats I, Erez N, Goldfinger N, Rotter V: Activated p53 suppresses the histone methyltransferase EZH2 gene. Oncogene. 2004 Jul 29;23(34):5759-69. [PubMed
]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed
]
- Epping MT, Wang L, Edel MJ, Carlee L, Hernandez M, Bernards R: The human tumor antigen PRAME is a dominant repressor of retinoic acid receptor signaling. Cell. 2005 Sep 23;122(6):835-47. [PubMed
]
- Kuzmichev A, Margueron R, Vaquero A, Preissner TS, Scher M, Kirmizis A, Ouyang X, Brockdorff N, Abate-Shen C, Farnham P, Reinberg D: Composition and histone substrates of polycomb repressive group complexes change during cellular differentiation. Proc Natl Acad Sci U S A. 2005 Feb 8;102(6):1859-64. Epub 2005 Jan 31. [PubMed
]
- Cha TL, Zhou BP, Xia W, Wu Y, Yang CC, Chen CT, Ping B, Otte AP, Hung MC: Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine 27 in histone H3. Science. 2005 Oct 14;310(5746):306-10. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Bracken AP, Dietrich N, Pasini D, Hansen KH, Helin K: Genome-wide mapping of Polycomb target genes unravels their roles in cell fate transitions. Genes Dev. 2006 May 1;20(9):1123-36. Epub 2006 Apr 17. [PubMed
]
- Martin C, Cao R, Zhang Y: Substrate preferences of the EZH2 histone methyltransferase complex. J Biol Chem. 2006 Mar 31;281(13):8365-70. Epub 2006 Jan 23. [PubMed
]
- Vire E, Brenner C, Deplus R, Blanchon L, Fraga M, Didelot C, Morey L, Van Eynde A, Bernard D, Vanderwinden JM, Bollen M, Esteller M, Di Croce L, de Launoit Y, Fuks F: The Polycomb group protein EZH2 directly controls DNA methylation. Nature. 2006 Feb 16;439(7078):871-4. Epub 2005 Dec 14. [PubMed
]
- Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed
]
- Kim DH, Villeneuve LM, Morris KV, Rossi JJ: Argonaute-1 directs siRNA-mediated transcriptional gene silencing in human cells. Nat Struct Mol Biol. 2006 Sep;13(9):793-7. Epub 2006 Aug 27. [PubMed
]
- Nousiainen M, Sillje HH, Sauer G, Nigg EA, Korner R: Phosphoproteome analysis of the human mitotic spindle. Proc Natl Acad Sci U S A. 2006 Apr 4;103(14):5391-6. Epub 2006 Mar 24. [PubMed
]
- Kotake Y, Cao R, Viatour P, Sage J, Zhang Y, Xiong Y: pRB family proteins are required for H3K27 trimethylation and Polycomb repression complexes binding to and silencing p16INK4alpha tumor suppressor gene. Genes Dev. 2007 Jan 1;21(1):49-54. [PubMed
]
- Bracken AP, Kleine-Kohlbrecher D, Dietrich N, Pasini D, Gargiulo G, Beekman C, Theilgaard-Monch K, Minucci S, Porse BT, Marine JC, Hansen KH, Helin K: The Polycomb group proteins bind throughout the INK4A-ARF locus and are disassociated in senescent cells. Genes Dev. 2007 Mar 1;21(5):525-30. [PubMed
]
- Schlesinger Y, Straussman R, Keshet I, Farkash S, Hecht M, Zimmerman J, Eden E, Yakhini Z, Ben-Shushan E, Reubinoff BE, Bergman Y, Simon I, Cedar H: Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for de novo methylation in cancer. Nat Genet. 2007 Feb;39(2):232-6. Epub 2006 Dec 31. [PubMed
]
- Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed
]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
- Margueron R, Li G, Sarma K, Blais A, Zavadil J, Woodcock CL, Dynlacht BD, Reinberg D: Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms. Mol Cell. 2008 Nov 21;32(4):503-18. [PubMed
]
- Cao R, Wang H, He J, Erdjument-Bromage H, Tempst P, Zhang Y: Role of hPHF1 in H3K27 methylation and Hox gene silencing. Mol Cell Biol. 2008 Mar;28(5):1862-72. Epub 2007 Dec 17. [PubMed
]
- Sarma K, Margueron R, Ivanov A, Pirrotta V, Reinberg D: Ezh2 requires PHF1 to efficiently catalyze H3 lysine 27 trimethylation in vivo. Mol Cell Biol. 2008 Apr;28(8):2718-31. Epub 2008 Feb 19. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
14761 |
| Enzyme 18 Name |
Histone-lysine N-methyltransferase MLL2 |
| Enzyme 18 Synonyms |
- ALL1-related protein
- Lysine N-methyltransferase 2B
- KMT2B
- Myeloid/lymphoid or mixed-lineage leukemia protein 2
|
| Enzyme 18 Gene Name |
MLL2 |
| Enzyme 18 Protein Sequence |
>Histone-lysine N-methyltransferase MLL2
MDSQNLAGEDKDSQPAADGPAASEDPSATESDLPNPHVGEVSVLSSGSPRLQETPQDCSG
GPVRRCALCNCGEPALHGQRELRRFELPFDWPRCPVVSPGGSPGPNEAVLPSEDLSQIGF
PEGLTPAHLGEPGGSCWAHHWCAAWSAGVWGQEGPQLCGVDKAIFSGISQRCSHCTRLGA
SIPCRSPGCPRLYHFPCATASGSFLSMKTLQLLCPEHSEGAAYLEEARCAVCEGPGELCD
LFFCTSCGHHYHGACLDTALTARKRAGWQCPECKVCQACRKPGNDSKMLVCETCDKGYHT
FCLKPPMEELPAHSWKCKACRVCRACGAGSAELNPNSEWFENYSLCHRCHKAQGGQTIRS
VAEQHTPVCSRFSPPEPGDTPTDEPDALYVACQGQPKGGHVTSMQPKEPGPLQCEAKPLG
KAGVQLEPQLEAPLNEEMPLLPPPEESPLSPPPEESPTSPPPEASRLSPPPEELPASPLP
EALHLSRPLEESPLSPPPEESPLSPPPESSPFSPLEESPLSPPEESPPSPALETPLSPPP
EASPLSPPFEESPLSPPPEELPTSPPPEASRLSPPPEESPMSPPPEESPMSPPPEASRLF
PPFEESPLSPPPEESPLSPPPEASRLSPPPEDSPMSPPPEESPMSPPPEVSRLSPLPVVS
RLSPPPEESPLSPPALSPLGELEYPFGAKGDSDPESPLAAPILETPISPPPEANCTDPEP
VPPMILPPSPGSPVGPASPILMEPLPPQCSPLLQHSLVPQNSPPSQCSPPALPLSVPSPL
SPIGKVVGVSDEAELHEMETEKVSEPECPALEPSATSPLPSPMGDLSCPAPSPAPALDDF
SGLGEDTAPLDGIDAPGSQPEPGQTPGSLASELKGSPVLLDPEELAPVTPMEVYPECKQT
AGRGSPCEEQEEPRAPVAPTPPTLIKSDIVNEISNLSQGDASASFPGSEPLLGSPDPEGG
GSLSMELGVSTDVSPARDEGSLRLCTDSLPETDDSLLCDAGTAISGGKAEGEKGRRRSSP
ARSRIKQGRSSSFPGRRRPRGGAHGGRGRGRARLKSTASSIETLVVADIDSSPSKEEEEE
DDDTMQNTVVLFSNTDKFVLMQDMCVVCGSFGRGAEGHLLACSQCSQCYHPYCVNSKITK
VMLLKGWRCVECIVCEVCGQASDPSRLLLCDDCDISYHTYCLDPPLLTVPKGGWKCKWCV
SCMQCGAASPGFHCEWQNSYTHCGPCASLVTCPICHAPYVEEDLLIQCRHCERWMHAGCE
SLFTEDDVDHAPDEGFDCVSCQPYVVKPVAPVAPPELVPMKVKEPEPQYFRFEGVWLTET
GMALLRNLTMSPLHKRRQRRGRLGLPGEAGLEGSEPSDALGPDDKKDGDLDTDELLKGEG
GVEHMECEIKLEGPVSPDVEPGKEETEESKKRKRKPYRPGIGGFMVRQRKSHTRTKKGPA
AQAEVLSGDGQPDEVIPADLPAEGAVEQSLAEGDEKKKQQRRGRKRSKLEGMFPAYLQEA
FFGKELLDLSRKALFAVGVGRPSFGLGTPKAKGDGGSERKELPTSQKGDDGPDIADEESR
GLEGKADTPGPEDGGVKASPVPSDPEKPGTPGEGMLSSDLDRISTEELPKMESKDLQQLF
KDVLGSEREQHLGCGTPGLEGSRTPLQRPFLQGGLPLGNLPSSSPMDSYPGLCQSPFLDS
RERGGFFSPEPGEPDSPWTGSGGTTPSTPTTPTTEGEGDGLSYNQRSLQRWEKDEELGQL
STISPVLYANINFPNLKQDYPDWSSRCKQIMKLWRKVPAADKAPYLQKAKDNRAAHRINK
VQKQAESQINKQTKVGDIARKTDRPALHLRIPPQPGALGSPPPAAAPTIFIGSPTTPAGL
STSADGFLKPPAGSVPGPDSPGELFLKLPPQVPAQAPSQDPFGLAPAYPLEPRFPTAPPT
YPPYPSPTGAPAQPPMLGASSRPGAGQPGEFHTTPPGTPRHQPSTPDPFLKPRCPSLDNL
AVPESPGVGGGKASEPLLSPPPFGESRKALEVKKEELGASSPSYGPPNLGFVDSPSSGTH
LGGLELKTPDVFKAPLTPRASQVEPQSPGLGLRPQEPPPAQALAPSPPSHPDIFRPGSYT
DPYAQPPLTPRPQPPPPESCCALPPRSLPSDPFSRVPVSPQSQSSSQSPLTPRPLSAEAF
CPSPVTPRFQSPDPYSRPPSRPQSRDPFAPLHKPPRPQPPEVAFKAGSLAHTSLGAGGFP
AALPAGPAGELHAKVPSGQPPNFVRSPGTGAFVGTPSPMRFTFPQAVGEPSLKPPVPQPG
LPPPHGINSHFGPGPTLGKPQSTNYTVATGNFHPSGSPLGPSSGSTGESYGLSPLRPPSV
LPPPAPDGSLPYLSHGASQRSGITSPVEKREDPGTGMGSSLATAELPGTQDPGMSGLSQT
ELEKQRQRQRLRELLIRQQIQRNTLRQEKETAAAAAGAVGPPGSWGAEPSSPAFEQLSRG
QTPFAGTQDKSSLVGLPPSKLSGPILGPGSFPSDDRLSRPPPPATPSSMDVNSRQLVGGS
QAFYQRAPYPGSLPLQQQQQQLWQQQQATAATSMRFAMSARFPSTPGPELGRQALGSPLA
GISTRLPGPGEPVPGPAGPAQFIELRHNVQKGLGPGGTPFPGQGPPQRPRFYPVSEDPHR
LAPEGLRGLAVSGLPPQKPSAPPAPELNNSLHPTPHTKGPTLPTGLELVNRPPSSTELGR
PNPLALEAGKLPCEDPELDDDFDAHKALEDDEELAHLGLGVDVAKGDDELGTLENLETND
PHLDDLLNGDEFDLLAYTDPELDTGDKKDIFNEHLRLVESANEEAEREALLRGVEPGPLG
PEERPPPAADASEPRLASVLPEVKPKVEEGGRHPSPCQFTIATPKVEPAPAANSLGLGLK
PGQSMMGSRDTRMGTGPFSSSGHTAEKASFGATGGPPAHLLTPSPLSGPGGSSLLEKFEL
ESGALTLPGGPAASGDELDKMESSLVASELPLLIEDLLEHEKKELQKKQQLSAQLQPAQQ
QQQQQQQHSLLPAPGPAQAMSLPHEGSSPSLAGSQQQLSLGLAVARQPGLPQPLMPTQPP
AHALQQRLAPSMAMVSNQGHMLSGQHGGQAGLVPQQSSQPVLSQKPMGTMPPSMCMKPQQ
LAMQQQLANSFFPDTDLDKFAAEDIIGPIAKAKMVALKGIKKVMAQGSIGVAPGMNRQQV
SLLAQRLSGGPSSDLQNHVAAGSGQERSAGDPSQPRPNPPTFAQGVINEADQRQYEEWLF
HTQQLLQMQLKVLEEQIGVHRKSRKALCAKQRTAKKAGREFPEADAEKLKLVTEQQSKIQ
KQLDQVRKQQKEHTNLMAEYRNKQQQQQQQQQQQQQQHSAVLALSPSQSPRLLTKLPGQL
LPGHGLQPPQGPPGGQAGGLRLTPGGMALPGQPGGPFLNTALAQQQQQQHSGGAGSLAGP
SGGFFPGNLALRSLGPDSRLLQERQLQLQQQRMQLAQKLQQQQQQQQQQQHLLGQVAIQQ
QQQQGPGVQTNQALGPKPQGLMPPSSHQGLLVQQLSPQPPQGPQGMLGPAQVAVLQQQHP
GALGPQGPHRQVLMTQSRVLSSPQLAQQGQGLMGHRLVTAQQQQQQQQHQQQGSMAGLSH
LQQSLMSHSGQPKLSAQPMGSLQQLQQQQQLQQQQQLQQQQQQQLQQQQQLQQQQLQQQQ
QQQQLQQQQQQQLQQQQQQLQQQQQQQQQQFQQQQQQQQMGLLNQSRTLLSPQQQQQQQV
ALGPGMPAKPLQHFSSPGALGPTLLLTGKEQNTVDPAVSSEATEGPSTHQGGPLAIGTTP
ESMATEPGEVKPSLSGDSQLLLVQPQPQPQPSSLQLQPPLRLPGQQQQQVSLLHTAGGGS
HGQLGSGSSSEASSVPHLLAQPSVSLGDQPGSMTQNLLGPQQPMLERPMQNNTGPQPPKP
GPVLQSGQGLPGVGIMPTVGQLRAQLQGVLAKNPQLRHLSPQQQQQLQALLMQRQLQQSQ
AVRQTPPYQEPGTQTSPLQGLLGCQPQLGGFPGPQTGPLQELGAGPRPQGPPRLPAPPGA
LSTGPVLGPVHPTPPPSSPQEPKRPSQLPSPSSQLPTEAQLPPTHPGTPKPQGPTLEPPP
GRVSPAAAQLADTLFSKGLGPWDPPDNLAETQKPEQSSLVPGHLDQVNGQVVPEASQLSI
KQEPREEPCALGAQSVKREANGEPIGAPGTSNHLLLAGPRSEAGHLLLQKLLRAKNVQLS
TGQGSEGLRAEINGHIDSKLAGLEQKLQGTPSNKEDAAARKPLTPKPKRVQKASDRLVSS
RKKLRKEDGVRASEALLKQLKQELSLLPLTEPAITANFSLFAPFGSGCPVNGQSQLRGAF
GSGALPTGPDYYSQLLTKNNLSNPPTPPSSLPPTPPPSVQQKMVNGVTPSEELGEHPKDA
ASARDSERALRDTSEVKSLDLLAALPTPPHNQTEDVRMESDEDSDSPDSIVPASSPESIL
GEEAPRFPHLGSGRWEQEDRALSPVIPLIPRDSIPVFPDTKPYGALGLEVPGKLPVTTWE
KGKGSEVSVMLTVSAAADKNLNGVMVAVAELLSMKIPNSYEVLFPESPARGGTEPKKGEA
EGPGGKEKGLEGKSPDTGPDWLKQFDAVLAGYTLKRQLDILSLLKQESPAPEPPTQHRYT
YNVSNLDVRQLSAPPPEEPSPPPSPLAPSPASPPTEPLVELPTEPLAEPPVPSPLPLASS
PESARPKPRARPPEEGEDTRPPRLKKWKGVRWKRLRLLLTIQKGSGRQEDEREVAEFMEQ
LGTALRPDKVPRDMRRCCFCHEEGDGATDGPARLLNLDLDLWVHLNCALWSTEVYETQGG
ALMNVEVALHRGLLTKCSLCQRTGATSSCNRMRCPNVYHFGCAIRAKCMFFKDKTMLCPM
HKIKGPCEQELSSFAVFRRVYIERDEVKQIASIIQRGERLHMFRVGGLVFHAIGQLLPHQ
MADFHSATALYPVGYEATRIYWSLRTNNRRCCYRCSIGENNGRPEFVIKVIEQGLEDLVF
TDASPQAVWNRIIEPVAAMRKEADMLRLFPEYLKGEELFGLTVHAVLRIAESLPGVESCQ
NYLFRYGRHPLMELPLMINPTGCARSEPKILTHYKRPHTLNSTSMSKAYQSTFTGETNTP
YSKQFVHSKSSQYRRLRTEWKNNVYLARSRIQGLGLYAAKDLEKHTMVIEYIGTIIRNEV
ANRREKIYEEQNRGIYMFRINNEHVIDATLTGGPARYINHSCAPNCVAEVVTFDKEDKII
IISSRRIPKGEELTYDYQFDFEDDQHEIPCHCGAWNCRKWMN
|
| Enzyme 18 Number of Residues |
5262 |
| Enzyme 18 Molecular Weight |
564180.6 |
| Enzyme 18 Theoretical pI |
5.79 |
| Enzyme 18 GO Classification |
| Function |
- DNA binding
- binding
- cation binding
- ion binding
- metal ion binding
- nucleic acid binding
- protein binding
- transition metal ion binding
- zinc ion binding
|
| Process |
| — |
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 18 General Function |
Involved in DNA binding |
| Enzyme 18 Specific Function |
Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in beta-globin locus transcription regulation by being recruited by NFE2. Acts as a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription |
| Enzyme 18 Pathways |
Not Available |
| Enzyme 18 Reactions |
- S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
2358285  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
O14686  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
MLL2_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>15789 bp
ATGGACAGCCAGAACCTGGCTGGTGAGGATAAAGATTCACAACCGGCAGCTGATGGACCT
GCAGCCTCTGAGGACCCAAGTGCCACTGAGTCAGACCTGCCCAACCCACATGTGGGAGAG
GTCTCTGTCCTTAGTTCTGGGAGTCCCAGGCTTCAGGAGACTCCTCAGGACTGCAGTGGG
GGTCCGGTGCGGCGTTGTGCTCTCTGTAACTGCGGGGAGCCCGCTCTACACGGGCAGCGG
GAGCTACGGCGCTTTGAGTTGCCATTTGATTGGCCCCGGTGTCCAGTGGTGTCCCCTGGG
GGGAGCCCAGGGCCCAATGAGGCAGTGCTGCCCAGTGAGGACCTATCACAGATTGGTTTC
CCTGAGGGCCTTACACCTGCCCACCTAGGAGAACCTGGAGGGTCCTGCTGGGCTCACCAT
TGGTGTGCTGCATGGTCGGCAGGCGTATGGGGGCAGGAGGGCCCACAACTATGTGGTGTG
GACAAGGCCATCTTCTCAGGGATCTCACAGCGCTGCTCCCACTGCACCAGGCTCGGTGCC
TCCATCCCTTGCCGCTCACCTGGATGTCCACGGCTTTACCACTTCCCCTGCGCGACTGCC
AGCGGTTCCTTCCTATCCATGAAAACACTGCAGCTGCTATGCCCAGAGCACAGTGAGGGG
GCTGCATATCTGGAGGAGGCTCGCTGTGCAGTGTGTGAGGGGCCAGGGGAGCTGTGTGAC
CTGTTCTTCTGTACCAGCTGTGGGCATCACTATCACGGGGCCTGCCTGGACACTGCTCTG
ACTGCCCGCAAACGTGCTGGCTGGCAGTGCCCTGAATGCAAAGTGTGCCAAGCCTGCAGG
AAACCTGGGAATGACTCTAAGATGTTGGTTTGCGAGACGTGTGACAAAGGATACCATACT
TTCTGCCTAAAACCACCCATGGAGGAACTGCCTGCTCACTCTTGGAAGTGCAAGGCGTGC
CGGGTGTGCCGGGCCTGTGGGGCGGGCTCAGCAGAACTGAATCCCAACTCGGAGTGGTTT
GAGAACTACTCTCTCTGTCACCGCTGTCACAAAGCCCAGGGAGGTCAGACTATCCGCTCC
GTTGCTGAGCAGCATACCCCGGTGTGTAGCAGATTTTCACCCCCAGAGCCTGGCGATACC
CCCACTGACGAGCCCGATGCTCTGTACGTTGCATGCCAAGGGCAGCCAAAGGGTGGGCAC
GTGACCTCTATGCAACCCAAGGAACCAGGGCCCCTGCAATGTGAAGCCAAACCACTAGGG
AAAGCAGGGGTCCAACTTGAGCCCCAGTTGGAGGCCCCCCTAAACGAGGAGATGCCACTG
CTGCCCCCACCTGAGGAGTCACCCCTGTCCCCACCACCTGAGGAATCACCCACGTCCCCA
CCACCTGAGGCATCACGCCTGTCGCCACCACCTGAGGAATTGCCCGCATCCCCACTTCCT
GAGGCATTGCACCTGTCCCGGCCGCTGGAGGAATCGCCCCTCTCTCCGCCGCCTGAGGAG
TCTCCTCTGTCTCCCCCACCTGAATCATCACCTTTTTCTCCACTGGAGGAGTCGCCCTTG
TCTCCACCGGAAGAGTCACCCCCATCTCCTGCACTTGAGACGCCTCTATCCCCACCACCT
GAAGCATCGCCCCTGTCCCCACCATTTGAAGAATCTCCTTTGTCCCCGCCACCTGAGGAA
TTGCCCACTTCCCCGCCACCTGAAGCATCTCGCCTGTCTCCACCACCTGAGGAGTCACCC
ATGTCCCCTCCACCTGAAGAGTCACCCATGTCTCCACCACCGGAGGCATCTCGTCTGTTC
CCACCATTTGAAGAGTCTCCTCTGTCCCCTCCACCTGAGGAGTCTCCCCTTTCCCCACCA
CCTGAGGCATCACGCCTGTCCCCACCACCTGAGGACTCGCCTATGTCCCCACCACCTGAA
GAATCACCTATGTCCCCCCCACCTGAGGTATCGCGCCTATCCCCCCTGCCTGTGGTGTCA
CGCCTGTCTCCACCGCCTGAGGAATCTCCCTTGTCCCCACCGGCCCTGTCTCCTTTGGGG
GAGTTAGAGTACCCCTTTGGTGCCAAAGGGGACAGTGACCCTGAGTCACCGTTGGCTGCC
CCCATCCTGGAGACACCCATCAGCCCTCCACCAGAAGCTAACTGCACTGACCCTGAGCCT
GTCCCCCCTATGATCCTTCCCCCATCTCCAGGCTCCCCAGTGGGGCCGGCTTCTCCCATC
CTGATGGAGCCCCTTCCTCCTCAGTGTTCGCCACTCCTTCAGCATTCCCTGGTTCCCCAA
AACTCCCCTCCTTCCCAGTGCTCTCCTCCTGCCCTACCACTGTCCGTTCCCTCCCCGTTG
AGTCCCATAGGGAAGGTAGTGGGGGTCTCAGATGAGGCTGAGCTGCACGAGATGGAGACT
GAGAAAGTTTCAGAACCTGAATGCCCAGCCTTGGAACCCAGTGCCACCAGTCCTCTCCCT
TCCCCAATGGGGGACCTTTCCTGCCCCGCCCCCAGCCCTGCCCCAGCCCTGGATGACTTC
TCTGGCCTAGGGGAAGACACAGCCCCTCTGGATGGGATTGATGCTCCGGGTTCACAGCCA
GAGCCTGGACAGACCCCTGGCAGTTTGGCTAGTGAACTTAAAGGCTCCCCTGTGCTCCTG
GACCCCGAGGAGCTGGCCCCTGTGACCCCTATGGAGGTCTACCCCGAATGCAAGCAGACA
GCAGGGCGGGGCTCACCATGTGAAGAACAGGAAGAGCCACGTGCACCGGTGGCCCCCACA
CCACCCACTCTCATCAAATCCGACATCGTTAACGAGATCTCTAATCTGAGCCAGGGTGAT
GCCAGTGCCAGTTTTCCTGGCTCAGAGCCCCTCCTGGGCTCTCCAGACCCGGAGGGGGGT
GGCTCCCTGTCCATGGAGTTGGGGGTCTCTACGGATGTTAGTCCAGCCCGAGATGAGGGC
TCCCTACGGCTCTGTACTGACTCACTGCCAGAGACTGATGACTCACTATTGTGCGATGCT
GGGACAGCTATCAGCGGAGGCAAAGCTGAGGGGGAGAAGGGGCGGCGGCGCAGCTCCCCA
GCCCGTTCCCGCATCAAACAGGGTCGCAGCAGCAGTTTCCCAGGAAGACGCCGGCCTCGT
GGAGGAGCCCATGGAGGGCGTGGTAGAGGACGGGCCCGGCTAAAGTCAACTGCTTCTTCC
ATTGAGACTCTGGTAGTTGCTGACATTGATAGCTCTCCCAGTAAGGAGGAGGAGGAAGAA
GATGATGACACCATGCAGAATACCGTGGTTCTCTTCTCCAACACAGACAAATTTGTCCTA
ATGCAGGACATGTGTGTGGTATGTGGCAGCTTTGGCCGGGGGGCAGAGGGCCACCTCCTT
GCCTGTTCGCAGTGCTCTCAGTGCTATCACCCTTACTGTGTCAACAGCAAGATCACCAAG
GTGATGCTGCTCAAGGGCTGGCGTTGTGTGGAGTGTATTGTGTGTGAGGTGTGTGGCCAG
GCCTCCGACCCCTCACGCCTGCTGCTCTGTGATGACTGTGATATTAGCTACCACACATAC
TGCCTGGACCCCCCACTGCTCACCGTCCCCAAGGGCGGCTGGAAGTGCAAGTGGTGTGTG
TCCTGTATGCAGTGTGGGGCTGCTTCCCCTGGCTTCCACTGTGAATGGCAGAATAGTTAC
ACACACTGTGGGCCCTGTGCCAGCCTGGTGACCTGCCCTATCTGTCATGCTCCTTACGTA
GAAGAGGACCTACTAATCCAGTGCCGCCACTGTGAACGGTGGATGCATGCAGGCTGTGAG
AGCCTCTTCACAGAGGACGATGTGGACCACGCACCCGATGAAGGCTTTGACTGTGTCTCC
TGCCAGCCCTACGTGGTAAAGCCTGTGGCGCCTGTTGCACCTCCAGAGCTGGTGCCCATG
AAGGTGAAAGAGCCAGAGCCCCAGTACTTTCGCTTCGAAGGCGTGTGGCTGACAGAAACT
GGCATGGCCTTGCTGCGTAACCTGACCATGTCACCACTGCACAAGCGGCGCCAACGGCGA
GGACGGCTTGGCCTCCCAGGCGAGGCAGGATTGGAGGGTTCTGAGCCCTCAGATGCCCTT
GGCCCTGATGACAAGAAGGATGGGGACCTGGACACCGATGAGCTGCTCAAGGGTGAAGGT
GGTGTGGAGCACATGGAGTGCGAAATTAAACTGGAGGGCCCCGTCAGCCCTGATGTGGAG
CCTGGCAAAGAGGAGACCGAGGAAAGCAAAAAACGCAAGCGTAAACCATATCGGCCTGGC
ATTGGTGGTTTCATGGTGCGACAGCGGAAATCCCACACACGCACGAAAAAGGGGCCTGCT
GCACAGGCGGAGGTGTTGAGTGGGGATGGGCAGCCCGACGAGGTGATACCTGCTGACCTG
CCTGCAGAGGGCGCCGTGGAGCAGAGCTTAGCTGAAGGGGATGAGAAGAAGAAGCAACAG
CGGCGAGGGCGCAAGAGGAGCAAACTGGAGGGCATGTTCCCTGCTTACTTGCAGGAAGCC
TTCTTTGGGAAGGAGCTGCTGGACCTGAGCCGTAAGGCCCTTTTTGCAGTTGGGGTGGGC
CGGCCAAGCTTTGGACTAGGGACCCCAAAAGCCAAGGGAGATGGAGGCTCAGAAAGGAAG
GAACTCCCCACATCGCAGAAAGGAGATGATGGTCCAGATATTGCAGATGAAGAATCCCGT
GGCCTCGAGGGCAAAGCCGATACACCAGGACCTGAGGATGGGGGCGTGAAGGCATCCCCA
GTGCCCAGTGACCCTGAGAAGCCAGGCACCCCAGGTGAAGGGATGCTTAGCTCTGACTTA
GACAGGATTTCCACAGAAGAACTGCCCAAGATGGAATCCAAGGACCTGCAGCAGCTCTTC
AAGGATGTTCTGGGCTCTGAACGAGAACAGCATCTGGGTTGTGGAACCCCTGGCCTAGAA
GGCAGCCGTACGCCACTGCAGAGGCCCTTTCTTCAAGGTGGACTCCCTTTGGGCAATCTG
CCCTCCAGCAGCCCAATGGACTCCTACCCAGGCCTCTGCCAGTCCCCGTTCCTGGATTCT
AGGGAGCGCGGGGGCTTCTTTAGCCCGGAACCCGGTGAGCCCGACAGCCCCTGGACGGGC
TCAGGTGGCACCACGCCCTCCACCCCCACAACCCCCACCACGGAGGGTGAGGGCGACGGA
CTCTCCTATAACCAGCGGAGTCTTCAGCGCTGGGAGAAGGATGAGGAGTTGGGCCAGCTG
TCCACCATCTCGCCTGTGCTCTATGCCAACATTAATTTTCCTAATCTCAAGCAAGACTAC
CCAGACTGGTCAAGCCGTTGCAAACAAATCATGAAGCTCTGGAGAAAGGTTCCAGCAGCT
GACAAAGCCCCCTACCTGCAAAAGGCCAAAGATAACCGGGCAGCTCACCGCATCAACAAG
GTGCAGAAGCAGGCTGAGAGCCAGATCAACAAGCAGACCAAGGTGGGCGACATAGCCCGT
AAGACTGACCGACCGGCCCTACATCTCCGCATTCCCCCGCAGCCAGGGGCACTGGGCAGC
CCGCCCCCCGCTGCTGCCCCCACCATTTTCATTGGCAGCCCCACTACCCCCGCCGGCTTG
TCTACCTCTGCGGACGGGTTCCTGAAGCCGCCGGCGGGCTCGGTGCCTGGCCCTGACTCG
CCTGGTGAGCTCTTCCTCAAGCTCCCACCCCAGGTGCCCGCCCAAGCGCCTTCGCAGGAC
CCCTTTGGACTGGCCCCTGCCTATCCCCTGGAGCCCCGCTTCCCCACGGCACCGCCCACC
TATCCCCCCTATCCTAGTCCTACGGGGGCCCCTGCGCAGCCCCCGATGCTGGGCGCCTCA
TCTCGTCCTGGGGCTGGCCAGCCAGGGGAATTCCACACTACCCCACCTGGCACCCCCAGA
CACCAGCCCTCCACACCTGACCCGTTCCTCAAACCCCGCTGCCCCTCGCTGGATAACTTG
GCTGTGCCTGAGAGCCCTGGGGTAGGGGGAGGCAAAGCTTCCGAGCCCCTGCTCTCGCCC
CCACCTTTTGGGGAGTCCCGGAAGGCCCTAGAGGTGAAGAAGGAAGAGCTTGGGGCATCC
TCTCCTAGCTATGGGCCCCCAAACCTGGGCTTTGTTGACTCACCCTCCTCAGGCACCCAC
CTGGGTGGCCTGGAGTTAAAGACACCTGATGTCTTCAAAGCCCCCCTGACCCCTCGGGCA
TCTCAGGTAGAGCCCCAGAGCCCGGGCTTGGGCCTAAGGCCCCAGGAGCCACCCCCTGCC
CAGGCTTTGGCACCTTCTCCTCCAAGTCACCCAGACATCTTTCGCCCTGGCTCCTACACT
GACCCATATGCTCAGCCCCCATTGACTCCTCGGCCCCAACCTCCGCCCCCTGAGAGCTGC
TGTGCTCTGCCCCCTCGCTCACTGCCCTCCGACCCTTTCTCCCGAGTGCCTGTCAGTCCT
CAGTCCCAGTCCAGCTCCCAGTCTCCACTGACACCCCGGCCTCTGTCTGCTGAAGCTTTT
TGCCCATCACCCGTTACCCCTCGCTTCCAGTCCCCTGACCCTTATTCTCGCCCACCCTCA
CGCCCTCAGTCCCGTGACCCATTTGCCCCATTGCATAAGCCACCCCGACCCCAGCCCCCT
GAAGTTGCCTTTAAGGCTGGGTCTCTAGCCCACACTTCGCTGGGGGCTGGGGGGTTCCCA
GCAGCCCTGCCCGCGGGGCCAGCAGGTGAGCTCCATGCCAAGGTCCCAAGTGGGCAGCCC
CCCAATTTTGTCCGGTCCCCTGGGACGGGTGCATTTGTGGGCACCCCCTCTCCCATGCGT
TTCACTTTCCCTCAGGCAGTAGGGGAGCCTTCCCTAAAGCCCCCTGTCCCTCAGCCTGGT
CTCCCGCCACCCCATGGGATCAACAGCCATTTTGGGCCCGGCCCCACCTTGGGCAAGCCT
CAAAGCACAAACTACACAGTAGCCACAGGGAACTTCCACCCATCGGGCAGCCCCCTGGGG
CCCAGCAGCGGGTCCACAGGGGAGAGCTATGGGCTGTCCCCACTACGCCCTCCGTCGGTT
CTGCCACCACCTGCACCCGACGGATCCCTCCCCTACCTGTCCCATGGAGCCTCACAGCGA
TCAGGCATCACCTCTCCTGTCGAAAAGCGAGAAGACCCAGGGACTGGAATGGGTAGCTCT
TTGGCGACAGCTGAACTCCCAGGTACCCAGGACCCAGGCATGTCCGGCCTTAGCCAAACA
GAGCTGGAGAAGCAACGGCAGCGCCAGCGGCTACGAGAGCTGCTGATTCGGCAGCAGATC
CAGCGCAACACCCTGCGGCAGGAGAAGGAAACAGCTGCAGCAGCTGCGGGAGCAGTGGGG
CCTCCAGGCAGCTGGGGTGCTGAGCCCAGCAGCCCTGCCTTTGAGCAGCTGAGTCGAGGC
CAGACCCCCTTTGCTGGGACACAGGACAAGAGCAGCCTTGTGGGGTTGCCCCCAAGCAAG
CTGAGTGGCCCCATCCTGGGGCCAGGGTCCTTCCCTAGCGATGACCGACTCTCCCGGCCA
CCTCCACCAGCCACGCCTTCCTCTATGGATGTGAACAGCCGGCAACTGGTAGGAGGCTCC
CAAGCTTTCTATCAGCGAGCACCCTATCCTGGGTCCCTGCCCTTACAGCAGCAACAGCAA
CAACTGTGGCAGCAACAACAGGCAACAGCAGCAACCTCCATGCGATTTGCCATGTCAGCT
CGCTTTCCATCAACTCCTGGACCTGAACTTGGCCGCCAAGCCCTAGGTTCCCCGTTGGCG
GGAATTTCCACCCGTCTGCCAGGCCCTGGTGAGCCAGTGCCTGGTCCAGCTGGTCCTGCC
CAGTTCATTGAGCTGCGGCACAATGTACAGAAAGGACTGGGACCTGGGGGCACTCCGTTT
CCTGGTCAGGGCCCACCTCAGAGACCCCGTTTTTACCCTGTAAGTGAGGACCCCCACCGA
CTGGCTCCTGAAGGGCTTCGGGGCCTGGCGGTATCAGGTCTTCCCCCACAGAAACCCTCA
GCCCCACCGGCCCCTGAATTGAACAACAGTCTTCATCCAACACCCCACACCAAGGGTCCT
ACCCTGCCAACTGGTTTGGAGCTGGTCAACCGGCCCCCGTCGAGCACTGAGCTTGGCCGC
CCCAATCCTCTGGCCCTGGAAGCTGGGAAGTTGCCCTGTGAGGATCCCGAGCTGGATGAC
GATTTTGATGCCCACAAGGCCCTAGAGGATGATGAAGAGCTTGCTCACCTGGGTCTGGGT
GTGGATGTGGCCAAGGGTGATGATGAACTTGGCACCTTAGAAAACCTGGAGACCAATGAC
CCCCACTTGGATGACCTGCTCAATGGAGACGAGTTTGACCTGCTGGCATATACTGATCCT
GAGCTGGACACTGGGGACAAGAAGGATATCTTCAATGAGCACCTGAGGCTGGTAGAATCG
GCTAATGAGGAGGCTGAACGGGAGGCCCTGCTGCGGGGGGTGGAGCCAGGACCCTTGGGC
CCTGAGGAGCGCCCTCCCCCTGCTGCTGATGCCTCTGAACCCCGCCTGGCATCTGTGCTC
CCTGAGGTGAAGCCCAAGGTGGAGGAGGGTGGACGCCACCCTTCTCCTTGCCAATTCACC
ATTGCTACCCCCAAGGTAGAGCCCGCACCTGCTGCCAATTCCCTTGGCCTGGGGCTAAAG
CCAGGACAGAGCATGATGGGCAGCCGGGATACCCGGATGGGCACAGGGCCATTTTCTAGC
AGTGGGCACACAGCTGAGAAGGCCTCCTTTGGGGCCACGGGAGGGCCACCAGCTCACCTG
CTGACCCCCAGCCCACTGAGTGGCCCAGGAGGATCCTCCCTGCTGGAAAAGTTTGAGCTC
GAGAGTGGGGCTTTGACCTTGCCTGGTGGACCTGCAGCATCTGGGGATGAGCTAGACAAG
ATGGAGAGCTCACTGGTAGCCAGCGAGTTACCCCTGCTCATTGAGGACCTGTTGGAGCAT
GAGAAGAAGGAGCTGCAGAAGAAGCAGCAGCTTTCAGCACAGTTGCAGCCTGCCCAGCAG
CAGCAGCAACAGCAGCAGCAGCATTCCCTACTGCCTGCACCAGGCCCTGCCCAGGCCATG
TCTTTGCCACATGAGGGCTCTTCTCCCAGTTTGGCTGGGTCCCAACAGCAGCTTTCCCTG
GGTCTTGCAGTTGCCCGACAGCCAGGTTTGCCCCAGCCACTGATGCCCACCCAGCCACCA
GCTCATGCCCTCCAGCAACGCCTGGCTCCATCCATGGCTATGGTGTCCAATCAAGGGCAT
ATGCTAAGTGGGCAGCATGGAGGGCAGGCAGGCTTGGTACCCCAGCAGAGCTCACAGCCA
GTGCTATCACAGAAGCCCATGGGCACCATGCCACCTTCCATGTGCATGAAGCCGCAGCAA
TTGGCAATGCAGCAGCAGCTGGCAAACAGCTTCTTCCCAGATACAGACCTGGACAAATTT
GCTGCAGAAGATATCATTGGTCCCATTGCAAAGGCCAAGATGGTGGCTTTGAAAGGCATC
AAGAAAGTGATGGCTCAGGGCAGCATTGGGGTGGCACCTGGTATGAACAGACAGCAAGTG
TCTCTGCTAGCCCAGAGGCTCTCGGGGGGACCTAGCAGTGATCTGCAGAACCATGTGGCA
GCTGGGAGTGGCCAGGAGCGGAGTGCTGGTGATCCCTCCCAGCCTCGTCCCAACCCGCCC
ACTTTTGCTCAGGGAGTGATCAATGAAGCTGACCAGCGGCAGTATGAGGAGTGGCTGTTC
CATACCCAGCAGCTCCTACAGATGCAGCTGAAGGTGCTAGAGGAGCAGATTGGTGTACAC
CGCAAGTCCCGGAAGGCTCTGTGTGCCAAGCAGCGCACTGCCAAAAAAGCTGGCCGTGAG
TTCCCAGAAGCTGATGCTGAGAAGCTCAAGCTGGTTACAGAGCAGCAGAGCAAGATCCAG
AAACAACTGGATCAGGTCCGGAAACAGCAGAAGGAGCACACTAATCTCATGGCAGAATAT
CGGAACAAGCAGCAGCAACAACAGCAGCAGCAGCAGCAACAACAGCAACAGCACTCAGCT
GTGCTGGCTCTCAGCCCTTCCCAGAGTCCCCGGCTGCTCACCAAGCTCCCTGGTCAGCTG
CTCCCTGGCCATGGGCTGCAGCCACCACAGGGGCCTCCGGGTGGGCAAGCCGGAGGTCTT
CGCCTGACCCCTGGGGGTATGGCACTACCTGGACAGCCTGGTGGCCCCTTCCTTAATACA
GCTCTGGCCCAACAGCAGCAACAGCAACATTCTGGTGGGGCTGGATCCCTGGCTGGCCCT
TCAGGGGGCTTCTTCCCTGGCAACCTTGCTCTTCGAAGCCTCGGACCTGATTCAAGGCTT
TTACAGGAAAGGCAGCTGCAGCTGCAGCAGCAACGTATGCAGCTGGCCCAGAAACTGCAG
CAGCAGCAGCAGCAGCAACAGCAGCAGCAGCACCTTCTAGGACAGGTGGCAATCCAGCAG
CAACAGCAGCAGGGTCCTGGAGTACAGACAAACCAAGCTCTGGGTCCCAAGCCCCAGGGC
CTTATGCCTCCCAGCAGCCACCAAGGCCTCCTGGTCCAGCAGCTGTCCCCTCAACCACCC
CAGGGGCCCCAGGGCATGCTGGGCCCTGCCCAGGTGGCTGTGTTGCAGCAGCAGCACCCT
GGAGCTTTGGGCCCCCAGGGCCCTCACAGACAGGTGCTTATGACCCAGTCCCGGGTGCTC
AGTTCCCCCCAGCTGGCACAGCAGGGTCAGGGCCTTATGGGACACAGGCTGGTCACAGCC
CAGCAGCAGCAGCAGCAACAACAGCACCAACAGCAAGGGTCCATGGCAGGGCTGTCCCAT
CTTCAGCAAAGTCTGATGTCACACAGTGGGCAGCCCAAACTGAGCGCTCAGCCCATGGGC
TCTTTACAGCAGCTTCAGCAGCAGCAGCAGCTGCAACAGCAACAGCAACTTCAGCAGCAG
CAGCAGCAGCAGCTACAACAGCAACAGCAACTTCAGCAGCAACAGCTTCAACAGCAGCAA
CAGCAGCAGCAGCTTCAACAACAGCAGCAGCAACAGCTTCAACAGCAGCAACAGCAGCTA
CAACAGCAACAGCAACAACAACAGCAGCAGTTTCAACAGCAGCAGCAACAGCAGCAGATG
GGCCTTTTAAACCAGAGTCGAACTTTACTGTCCCCTCAGCAACAACAGCAGCAGCAAGTG
GCACTTGGCCCTGGCATGCCAGCAAAGCCTCTTCAACACTTTTCTAGCCCTGGAGCCCTG
GGTCCAACCCTCCTCCTGACGGGCAAGGAACAAAACACCGTAGACCCAGCCGTTTCTTCA
GAGGCCACTGAGGGGCCCTCTACACATCAGGGAGGGCCGTTAGCAATAGGAACTACCCCT
GAGTCAATGGCCACTGAACCAGGAGAGGTAAAGCCCTCACTCTCTGGGGACTCACAACTC
CTGCTTGTCCAACCCCAGCCCCAGCCTCAGCCCAGCTCTCTGCAGCTGCAGCCACCTCTG
AGGCTTCCAGGACAACAGCAGCAGCAAGTTAGCCTGCTCCACACAGCAGGTGGAGGAAGC
CATGGGCAGCTAGGCAGTGGATCATCTTCTGAGGCCTCATCTGTGCCCCACCTGCTGGCT
CAGCCCTCTGTTTCCTTAGGGGATCAGCCTGGGTCCATGACCCAGAACCTTCTGGGCCCC
CAACAGCCCATGCTAGAGCGGCCCATGCAAAATAATACAGGGCCACAACCTCCCAAACCA
GGACCTGTCCTCCAGTCTGGGCAGGGTCTGCCTGGGGTTGGAATCATGCCTACGGTGGGT
CAGCTTCGAGCACAGCTCCAAGGAGTCCTGGCCAAAAACCCACAGCTGCGGCACTTAAGT
CCTCAGCAGCAGCAGCAGCTACAGGCACTCCTCATGCAGCGGCAGCTGCAGCAGAGTCAG
GCAGTACGCCAGACCCCACCCTACCAGGAGCCTGGGACCCAGACCTCTCCCCTCCAGGGC
CTCCTGGGCTGCCAACCTCAACTTGGGGGCTTCCCTGGACCACAGACAGGCCCCCTCCAG
GAGCTAGGGGCAGGGCCTCGACCTCAGGGCCCACCCCGGCTCCCTGCCCCACCAGGAGCC
TTATCTACAGGACCAGTCCTTGGCCCTGTCCATCCCACACCTCCACCATCCAGCCCTCAA
GAGCCAAAGAGACCTTCACAATTACCTTCCCCCAGCTCCCAGCTTCCCACTGAGGCCCAG
CTCCCTCCCACCCATCCAGGGACCCCCAAACCTCAGGGGCCAACCTTGGAGCCGCCTCCT
GGGAGGGTCTCACCTGCTGCTGCCCAGCTTGCAGATACCTTGTTTAGCAAGGGTCTGGGA
CCTTGGGATCCCCCAGACAACCTAGCAGAAACCCAGAAGCCAGAGCAGAGCAGCCTGGTA
CCTGGGCATCTGGACCAGGTGAATGGACAGGTGGTGCCTGAGGCATCCCAACTCAGCATC
AAGCAGGAACCTCGGGAAGAGCCATGTGCCCTGGGAGCCCAGTCAGTGAAGAGGGAGGCC
AATGGGGAGCCAATAGGGGCACCAGGAACCAGCAACCACCTCCTGCTGGCAGGCCCTCGC
TCAGAAGCTGGGCATCTGCTCTTGCAGAAGCTACTCCGGGCAAAGAATGTGCAACTCAGC
ACTGGGCAGGGGTCCGAGGGGCTGCGAGCTGAGATCAACGGGCACATTGACAGCAAGCTG
GCTGGGCTGGAGCAGAAACTACAGGGTACCCCCAGCAACAAGGAGGATGCAGCAGCAAGG
AAGCCTTTGACACCGAAGCCCAAGCGGGTACAGAAGGCAAGCGACAGGTTGGTGAGCTCC
CGAAAGAAGCTGCGGAAGGAGGACGGCGTCAGGGCCAGCGAGGCCTTGCTGAAACAGCTG
AAACAGGAGCTGTCCCTGCTGCCCCTAACGGAGCCTGCTATCACCGCCAATTTTAGCCTC
TTTGCCCCCTTTGGCAGTGGCTGCCCAGTCAATGGGCAGAGCCAGCTGAGGGGGGCCTTT
GGAAGTGGGGCGCTGCCCACTGGCCCTGACTACTATTCCCAGCTGCTTACCAAGAATAAC
CTGAGTAACCCGCCGACACCACCCTCGTCGCTGCCCCCCACCCCACCCCCATCGGTGCAG
CAGAAGATGGTGAATGGCGTCACCCCATCTGAAGAGCTGGGGGAGCACCCCAAGGATGCT
GCCTCTGCCCGGGATAGTGAAAGGGCACTGAGGGATACTTCAGAGGTGAAGAGTCTAGAC
CTGCTGGCTGCCTTGCCTACACCCCCTCACAATCAGACTGAGGATGTCAGGATGGAGAGT
GATGAGGATAGCGATTCTCCTGACAGCATTGTGCCAGCTTCATCCCCTGAGAGCATCTTG
GGGGAGGAGGCCCCTCGTTTCCCTCATCTGGGCTCAGGCCGGTGGGAGCAAGAGGACCGG
GCCCTCTCCCCTGTCATCCCCCTCATTCCTCGGGACAGCATCCCAGTCTTCCCAGATACC
AAACCTTATGGGGCCCTTGGCCTGGAGGTCCCTGGAAAGCTGCCTGTCACAACTTGGGAA
AAGGGCAAAGGAAGTGAGGTGTCAGTCATGCTCACAGTCTCTGCTGCTGCAGACAAGAAC
CTGAATGGCGTGATGGTGGCAGTGGCGGAGCTGCTGAGCATGAAGATCCCCAACTCCTAT
GAGGTGCTGTTCCCAGAGAGCCCCGCCCGGGGAGGCACTGAGCCAAAGAAGGGGGAAGCT
GAGGGTCCTGGTGGGAAGGAAAAGGGTCTGGAAGGCAAGAGCCCAGACACTGGCCCTGAT
TGGCTGAAGCAGTTTGATGCAGTGTTGGCTGGCTATACCCTGAAGAGGCAACTAGACATC
TTGAGCCTCCTGAAACAGGAGAGCCCCGCCCCAGAGCCACCCACTCAGCACAGGTATACC
TACAATGTCTCCAATCTGGATGTGCGACAGCTCTCGGCCCCACCTCCTGAAGAACCCTCC
CCGCCCCCTTCCCCCTTGGCACCTTCTCCTGCCAGTCCCCCTACTGAGCCCTTGGTTGAA
CTTCCCACCGAACCCTTGGCTGAGCCACCCGTCCCCTCACCTCTGCCACTGGCCTCATCC
CCTGAATCAGCCCGACCCAAGCCCCGTGCCCGGCCCCCTGAAGAAGGTGAAGATACCCGT
CCTCCTCGCCTCAAGAAATGGAAAGGAGTGCGCTGGAAGCGGCTTCGGCTGCTGCTGACC
ATCCAGAAGGGCAGTGGACGGCAGGAGGATGAGCGGGAAGTGGCAGAGTTTATGGAGCAG
CTTGGCACAGCCTTGCGACCTGACAAGGTACCGCGAGACATGCGTCGCTGCTGTTTCTGT
CATGAGGAGGGTGACGGGGCCACTGATGGGCCTGCCCGTCTGCTGAACCTGGACCTGGAC
CTGTGGGTGCACCTCAACTGTGCCCTTTGGTCCACGGAGGTGTATGAGACCCAGGGCGGA
GCACTGATGAATGTGGAGGTTGCCCTGCACCGAGGACTGCTAACCAAGTGCTCCCTGTGC
CAGCGAACTGGTGCCACCAGCAGCTGCAATCGCATGCGTTGCCCCAATGTCTACCATTTT
GGTTGTGCCATCCGCGCCAAGTGCATGTTCTTCAAGGACAAGACCATGCTGTGTCCAATG
CATAAGATCAAGGGGCCCTGTGAGCAAGAGCTGAGCTCTTTTGCTGTCTTCCGGCGGGTC
TACATTGAGCGGGACGAGGTGAAGCAAATCGCTAGCATCATTCAGCGGGGAGAACGGCTG
CACATGTTCCGTGTGGGGGGGCTTGTGTTCCACGCCATCGGACAGCTGCTGCCTCACCAG
ATGGCTGACTTTCATAGTGCCACTGCCCTCTATCCCGTGGGCTACGAGGCCACGCGCATC
TATTGGAGCCTCCGCACCAACAATCGTCGCTGCTGCTATCGCTGTTCTATTGGTGAGAAC
AACGGGCGGCCGGAGTTTGTAATCAAAGTCATCGAGCAGGGCCTGGAGGACCTGGTCTTC
ACTGACGCCTCTCCCCAGGCCGTGTGGAATCGCATCATTGAGCCTGTGGCTGCCATGAGA
AAAGAGGCTGACATGCTGCGACTCTTCCCTGAGTATCTGAAGGGCGAGGAGCTCTTTGGG
CTGACGGTGCATGCCGTGCTTCGCATAGCTGAATCACTGCCCGGGGTGGAGAGCTGTCAA
AACTATTTATTCCGCTATGGGCGCCACCCCCTTATGGAGCTGCCACTCATGATCAACCCC
ACTGGCTGTGCCCGATCAGAGCCTAAAATCCTCACACACTACAAACGGCCCCATACCCTG
AACAGCACCAGCATGTCTAAGGCATATCAGAGCACCTTCACAGGCGAGACCAACACCCCC
TACAGCAAGCAGTTTGTGCACTCCAAGTCATCTCAGTACCGGCGGCTGCGCACCGAATGG
AAGAACAACGTGTACCTGGCTCGCTCCCGTATCCAGGGCCTGGGGCTCTATGCAGCCAAG
GACCTAGAAAAGCACACAATGGTTATCGAGTACATTGGCACCATCATTCGGAACGAGGTG
GCCAACCGGCGGGAGAAAATCTACGAAGAGCAGAATCGAGGCATCTACATGTTCCGAATA
AACAATGAACATGTGATTGATGCTACGTTGACCGGCGGCCCTGCCAGGTACATTAACCAT
TCCTGTGCCCCTAACTGTGTGGCCGAAGTCGTGACATTTGACAAAGAGGACAAAATCATC
ATCATCTCCAGCCGGCGAATCCCCAAAGGAGAGGAGCTAACCTATGACTATCAGTTTGAT
TTTGAGGACGATCAGCACGAGATCCCCTGCCACTGTGGAGCCTGGAATTGTCGGAAATGG
ATGAACTAA
|
| Enzyme 18 GenBank Gene ID |
AF010403  |
| Enzyme 18 GeneCard ID |
MLL2  |
| Enzyme 18 GenAtlas ID |
MLL2  |
| Enzyme 18 HGNC ID |
HGNC:7133  |
| Enzyme 18 Chromosome Location |
1 |
| Enzyme 18 Locus |
12q12-q14 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Prasad R, Zhadanov AB, Sedkov Y, Bullrich F, Druck T, Rallapalli R, Yano T, Alder H, Croce CM, Huebner K, Mazo A, Canaani E: Structure and expression pattern of human ALR, a novel gene with strong homology to ALL-1 involved in acute leukemia and to Drosophila trithorax. Oncogene. 1997 Jul 31;15(5):549-60. [PubMed
]
- Goo YH, Sohn YC, Kim DH, Kim SW, Kang MJ, Jung DJ, Kwak E, Barlev NA, Berger SL, Chow VT, Roeder RG, Azorsa DO, Meltzer PS, Suh PG, Song EJ, Lee KJ, Lee YC, Lee JW: Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins. Mol Cell Biol. 2003 Jan;23(1):140-9. [PubMed
]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Mo R, Rao SM, Zhu YJ: Identification of the MLL2 complex as a coactivator for estrogen receptor alpha. J Biol Chem. 2006 Jun 9;281(23):15714-20. Epub 2006 Apr 7. [PubMed
]
- Cho YW, Hong T, Hong S, Guo H, Yu H, Kim D, Guszczynski T, Dressler GR, Copeland TD, Kalkum M, Ge K: PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex. J Biol Chem. 2007 Jul 13;282(28):20395-406. Epub 2007 May 11. [PubMed
]
- Demers C, Chaturvedi CP, Ranish JA, Juban G, Lai P, Morle F, Aebersold R, Dilworth FJ, Groudine M, Brand M: Activator-mediated recruitment of the MLL2 methyltransferase complex to the beta-globin locus. Mol Cell. 2007 Aug 17;27(4):573-84. [PubMed
]
- Lan F, Bayliss PE, Rinn JL, Whetstine JR, Wang JK, Chen S, Iwase S, Alpatov R, Issaeva I, Canaani E, Roberts TM, Chang HY, Shi Y: A histone H3 lysine 27 demethylase regulates animal posterior development. Nature. 2007 Oct 11;449(7163):689-94. Epub 2007 Sep 12. [PubMed
]
- Lee MG, Villa R, Trojer P, Norman J, Yan KP, Reinberg D, Di Croce L, Shiekhattar R: Demethylation of H3K27 regulates polycomb recruitment and H2A ubiquitination. Science. 2007 Oct 19;318(5849):447-50. Epub 2007 Aug 30. [PubMed
]
- Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed
]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
14762 |
| Enzyme 19 Name |
Histone-lysine N-methyltransferase MLL4 |
| Enzyme 19 Synonyms |
- Lysine N-methyltransferase 2D
- KMT2D
- Myeloid/lymphoid or mixed-lineage leukemia protein 4
- Trithorax homolog 2
- WW domain-binding protein 7
- WBP-7
|
| Enzyme 19 Gene Name |
WBP7 |
| Enzyme 19 Protein Sequence |
>Histone-lysine N-methyltransferase MLL4
MAAAAGGGSCPGPGSARGRFPGRPRGAGGGGGRGGRGNGAERVRVALRRGGGATGPGGAE
PGEDTALLRLLGLRRGLRRLRRLWAGPRVQRGRGRGRGRGWGPSRGCVPEEESSDGESDE
EEFQGFHSDEDVAPSSLRSALRSQRGRAPRGRGRKHKTTPLPPPRLADVAPTPPKTPARK
RGEEGTERMVQALTELLRRAQAPQAPRSRACEPSTPRRSRGRPPGRPAGPCRRKQQAVVV
AEAAVTIPKPEPPPPVVPVKHQTGSWKCKEGPGPGPGTPRRGGQSSRGGRGGRGRGRGGG
LPFVIKFVSRAKKVKMGQLSLGLESGQGQGQHEESWQDVPQRRVGSGQGGSPCWKKQEQK
LDDEEEEKKEEEEKDKEGEEKEERAVAEEMMPAAEKEEAKLPPPPLTPPAPSPPPPLPPP
STSPPPPLCPPPPPPVSPPPLPSPPPPPAQEEQEESPPPVVPATCSRKRGRPPLTPSQRA
EREAARAGPEGTSPPTPTPSTATGGPPEDSPTVAPKSTTFLKNIRQFIMPVVSARSSRVI
KTPRRFMDEDPPKPPKVEVSPVLRPPITTSPPVPQEPAPVPSPPRAPTPPSTPVPLPEKR
RSILREPTFRWTSLTRELPPPPPAPPPPPAPSPPPAPATSSRRPLLLRAPQFTPSEAHLK
IYESVLTPPPLGAPEAPEPEPPPADDSPAEPEPRAVGRTNHLSLPRFAPVVTTPVKAEVS
PHGAPALSNGPQTQAQLLQPLQALQTQLLPQALPPPQPQLQPPPSPQQMPPLEKARIAGV
GSLPLSGVEEKMFSLLKRAKVQLFKIDQQQQQKVAASMPLSPGGQMEEVAGAVKQISDRG
PVRSEDESVEAKRERPSGPESPVQGPRIKHVCRHAAVALGQARAMVPEDVPRLSALPLRD
RQDLATEDTSSASETESVPSRSRRGKVEAAGPGGESEPTGSGGTLAHTPRRSLPSHHGKK
MRMARCGHCRGCLRVQDCGSCVNCLDKPKFGGPNTKKQCCVYRKCDKIEARKMERLAKKG
RTIVKTLLPWDSDESPEASPGPPGPRRGAGAGGPREEVVAHPGPEEQDSLLQRKSARRCV
KQRPSYDIFEDSDDSEPGGPPAPRRRTPRENELPLPEPEEQSRPRKPTLQPVLQLKARRR
LDKDALAPGPFASFPNGWTGKQKSPDGVHRVRVDFKEDCDLENVWLMGGLSVLTSVPGGP
PMVCLLCASKGLHELVFCQVCCDPFHPFCLEEAERPLPQHHDTWCCRRCKFCHVCGRKGR
GSKHLLECERCRHAYHPACLGPSYPTRATRKRRHWICSACVRCKSCGATPGKNWDVEWSG
DYSLCPRCTQLYEKGNYCPICTRCYEDNDYESKMMQCAQCDHWVHAKCEGLSDEDYEILS
GLPDSVLYTCGPCAGAAQPRWREALSGALQGGLRQVLQGLLSSKVVGPLLLCTQCGPDGK
QLHPGPCGLQAVSQRFEDGHYKSVHSFMEDMVGILMRHSEEGETPDRRAGGQMKGLLLKL
LESAFGWFDAHDPKYWRRSTRLPNGVLPNAVLPPSLDHVYAQWRQQEPETPESGQPPGDP
SAAFQGKDPAAFSHLEDPRQCALCLKYGDADSKEAGRLLYIGQNEWTHVNCAIWSAEVFE
ENDGSLKNVHAAVARGRQMRCELCLKPGATVGCCLSSCLSNFHFMCARASYCIFQDDKKV
FCQKHTDLLDGKEIVNPDGFDVLRRVYVDFEGINFKRKFLTGLEPDAINVLIGSIRIDSL
GTLSDLSDCEGRLFPIGYQCSRLYWSTVDARRRCWYRCRILEYRPWGPREEPAHLEAAEE
NQTIVHSPAPSSEPPGGEDPPLDTDVLVPGAPERHSPIQNLDPPLRPDSGSAPPPAPRSF
SGARIKVPNYSPSRRPLGGVSFGPLPSPGSPSSLTHHIPTVGDPDFPAPPRRSRRPSPLA
PRPPPSRWASPPLKTSPQLRVPPPTSVVTALTPTSGELAPPGPAPSPPPPEDLGPDFEDM
EVVSGLSAADLDFAASLLGTEPFQEEIVAAGAMGSSHGGPGDSSEEESSPTSRYIHFPVT
VVSAPGLAPSATPGAPRIEQLDGVDDGTDSEAEAVQQPRGQGTPPSGPGVVRAGVLGAAG
DRARPPEDLPSEIVDFVLKNLGGPGDGGAGPREESLPPAPPLANGSQPSQGLTASPADPT
RTFAWLPGAPGVRVLSLGPAPEPPKPATSKIILVNKLGQVFVKMAGEGEPVPPPVKQPPL
PPTISPTAPTSWTLPPGPLLGVLPVVGVVRPAPPPPPPPLTLVLSSGPASPPRQAIRVKR
VSTFSGRSPPAPPPYKAPRLDEDGEASEDTPQVPGLGSGGFSRVRMKTPTVRGVLDLDRP
GEPAGEESPGPLQERSPLLPLPEDGPPQVPDGPPDLLLESQWHHYSGEASSSEEEPPSPD
DKENQAPKRTGPHLRFEISSEDGFSVEAESLEGAWRTLIEKVQEARGHARLRHLSFSGMS
GARLLGIHHDAVIFLAEQLPGAQRCQHYKFRYHQQGEGQEEPPLNPHGAARAEVYLRKCT
FDMFNFLASQHRVLPEGATCDEEEDEVQLRSTRRATSLELPMAMRFRHLKKTSKEAVGVY
RSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIGCYMFRMDDFDVVD
ATMHGNAARFINHSCEPNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKFPIEDASNK
LPCNCGAKRCRRFLN
|
| Enzyme 19 Number of Residues |
2715 |
| Enzyme 19 Molecular Weight |
293512.1 |
| Enzyme 19 Theoretical pI |
8.26 |
| Enzyme 19 GO Classification |
| Function |
- DNA binding
- binding
- catalytic activity
- cation binding
- histone methyltransferase activity (H3-K4 specific)
- histone-lysine N-methyltransferase activity
- ion binding
- metal ion binding
- methyltransferase activity
- nucleic acid binding
- protein binding
- protein methyltransferase activity
- protein-lysine N-methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
- transition metal ion binding
- zinc ion binding
|
| Process |
- biological regulation
- cellular component organization at cellular level
- cellular process
- chromatin modification
- chromatin organization
- chromosome organization
- organelle organization
- regulation of biological process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
- regulation of transcription, DNA-dependent
|
| Component |
- histone methyltransferase complex
- intracellular membrane-bounded organelle
- macromolecular complex
- membrane-bounded organelle
- methyltransferase complex
- nucleus
- organelle
- protein complex
|
|
| Enzyme 19 General Function |
Involved in DNA binding |
| Enzyme 19 Specific Function |
Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation |
| Enzyme 19 Pathways |
Not Available |
| Enzyme 19 Reactions |
- S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
7662046  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q9UMN6  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
MLL4_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>8148 bp
ATGGCGGCGGCGGCGGGCGGCGGCAGTTGCCCCGGGCCTGGCTCCGCGCGGGGCCGCTTC
CCGGGCCGGCCGCGGGGCGCCGGCGGGGGCGGGGGCCGCGGCGGACGGGGCAACGGGGCC
GAAAGAGTGCGGGTAGCTCTGCGGCGCGGCGGTGGCGCGACGGGGCCGGGCGGAGCCGAG
CCCGGGGAGGACACGGCCCTGCTCCGTTTGCTGGGGCTCCGCCGGGGCCTGCGCCGGCTC
CGCCGCCTGTGGGCCGGCCCGCGGGTCCAGCGGGGCCGGGGACGGGGTCGGGGCCGGGGC
TGGGGCCCGAGTCGAGGCTGCGTGCCGGAGGAGGAGAGCAGTGACGGGGAATCCGACGAG
GAGGAGTTTCAGGGTTTTCATTCAGATGAAGATGTGGCCCCCAGTTCCCTGCGCTCTGCG
CTCCGATCCCAGCGAGGTCGAGCGCCCCGAGGTCGGGGTCGCAAGCATAAGACGACCCCC
CTTCCTCCTCCTCGCCTAGCAGATGTGGCTCCTACCCCCCCAAAGACCCCTGCCCGGAAA
CGGGGTGAGGAAGGCACAGAACGGATGGTGCAGGCACTGACTGAACTTCTCCGGCGGGCC
CAGGCACCCCAAGCACCCCGGAGCCGGGCATGTGAGCCCTCCACCCCCCGGCGGTCTCGG
GGACGGCCCCCAGGACGGCCAGCAGGCCCCTGCAGGAGGAAGCAGCAAGCAGTAGTGGTG
GCAGAAGCAGCTGTGACAATCCCCAAACCTGAGCCCCCACCTCCTGTGGTTCCAGTGAAA
CATCAGACTGGCAGCTGGAAATGCAAGGAGGGGCCCGGTCCAGGACCTGGGACCCCCAGG
CGTGGAGGACAGTCAAGCCGTGGAGGCCGTGGAGGCAGGGGCCGCGGCCGAGGTGGTGGG
CTCCCCTTTGTGATCAAGTTTGTTTCAAGGGCCAAAAAAGTAAAGATGGGACAATTGTCC
TTGGGACTCGAATCAGGTCAAGGTCAAGGTCAACATGAGGAAAGTTGGCAGGATGTCCCC
CAAAGAAGAGTTGGATCTGGACAGGGAGGGAGCCCTTGCTGGAAAAAGCAGGAACAGAAG
CTGGATGACGAGGAAGAAGAGAAGAAAGAAGAAGAAGAAAAAGACAAGGAGGGAGAAGAG
AAGGAAGAAAGAGCTGTAGCTGAGGAGATGATGCCAGCTGCGGAAAAGGAAGAGGCAAAG
CTGCCACCACCGCCTCTGACTCCTCCAGCCCCTTCACCTCCTCCACCCCTCCCACCCCCT
TCGACATCTCCTCCACCCCCACTCTGCCCTCCACCACCACCCCCAGTGTCCCCACCACCT
CTACCATCCCCTCCACCGCCTCCTGCCCAAGAGGAGCAGGAGGAATCCCCTCCTCCTGTG
GTCCCAGCTACGTGCTCCAGGAAGAGGGGCCGGCCTCCCCTGACTCCCAGCCAGCGGGCG
GAGCGGGAAGCTGCTCGGGCAGGGCCAGAGGGCACCTCTCCTCCCACTCCAACCCCCAGC
ACCGCCACGGGAGGCCCTCCGGAAGACAGTCCCACCGTGGCCCCCAAAAGCACCACCTTC
CTGAAGAATATCCGGCAGTTTATTATGCCTGTGGTGAGTGCCCGCTCCTCCCGTGTCATC
AAGACACCCCGGCGATTTATGGATGAAGACCCCCCCAAACCCCCAAAGGTGGAGGTCTCA
CCTGTCCTGCGACCTCCCATTACCACCTCCCCACCTGTTCCCCAGGAGCCAGCACCAGTC
CCCTCTCCACCACGTGCCCCAACTCCTCCATCTACCCCAGTTCCACTCCCTGAGAAGAGA
CGGTCCATCCTAAGGGAACCCACATTTCGCTGGACCTCACTGACCCGGGAGCTGCCCCCT
CCTCCCCCAGCCCCTCCACCTCCCCCGGCCCCCTCCCCACCCCCTGCTCCTGCCACCTCC
TCCCGGAGGCCCCTACTCCTTCGGGCCCCTCAGTTTACCCCAAGCGAAGCCCACCTGAAG
ATCTACGAATCGGTGCTTACTCCTCCTCCTCTTGGGGCTCCTGAAGCCCCTGAGCCAGAG
CCTCCTCCTGCCGATGACTCTCCAGCTGAGCCTGAGCCTCGGGCAGTGGGCCGCACCAAC
CACCTCAGCCTGCCTCGATTCGCCCCTGTGGTCACCACTCCTGTTAAGGCCGAGGTGTCC
CCTCACGGGGCTCCAGCTCTGAGCAACGGGCCACAGACACAGGCTCAGCTACTGCAGCCC
CTGCAGGCCTTGCAAACCCAGCTCCTGCCCCAGGCACTACCGCCACCACAGCCACAGCTG
CAGCCACCGCCGTCACCACAGCAGATGCCTCCCCTGGAAAAAGCCCGGATTGCGGGCGTG
GGTTCCTTGCCGCTGTCTGGGGTAGAGGAGAAGATGTTCAGCCTCCTCAAGAGAGCCAAA
GTGCAGCTATTCAAGATCGATCAGCAGCAGCAGCAGAAGGTGGCAGCTTCCATGCCGCTG
AGCCCTGGAGGGCAGATGGAGGAGGTGGCCGGGGCTGTCAAGCAGATCTCCGACAGAGGC
CCTGTCCGGTCTGAAGATGAGTCGGTGGAAGCTAAGAGAGAGCGGCCCTCAGGTCCCGAG
TCCCCTGTGCAAGGTCCCCGCATCAAACATGTCTGCCGTCATGCTGCTGTGGCCCTGGGT
CAGGCCCGGGCCATGGTGCCTGAAGATGTCCCTCGCCTCAGTGCCCTCCCTCTCCGGGAT
CGGCAGGACCTCGCCACAGAGGATACATCATCGGCGTCCGAGACTGAGAGTGTCCCGTCA
CGGTCCCGGCGGGGAAAGGTGGAGGCAGCAGGCCCTGGGGGAGAATCAGAGCCCACAGGT
TCTGGAGGGACCCTGGCCCACACACCCCGGCGCTCACTGCCCTCCCATCACGGCAAGAAG
ATGCGCATGGCTCGATGTGGACACTGTCGGGGCTGCCTACGTGTGCAGGACTGTGGGTCC
TGTGTCAACTGCCTAGACAAGCCCAAGTTTGGGGGCCCTAACACCAAGAAGCAGTGCTGT
GTATACCGGAAGTGTGACAAAATAGAGGCTCGGAAGATGGAACGACTGGCTAAAAAAGGC
CGGACGATAGTGAAGACGCTGTTGCCCTGGGATTCCGATGAATCTCCTGAGGCCTCCCCT
GGTCCTCCAGGCCCACGCCGGGGGGCGGGAGCTGGGGGGCCCCGGGAGGAGGTGGTGGCC
CACCCAGGGCCCGAGGAGCAGGACTCCCTCCTGCAGCGCAAGTCAGCTCGGCGCTGCGTC
AAACAGCGACCCTCCTATGATATCTTCGAGGATTCGGATGACTCGGAGCCCGGGGGCCCC
CCTGCTCCTCGGCGTCGGACCCCCCGAGAAAATGAGCTGCCACTGCCAGAACCTGAGGAG
CAGAGCCGGCCCCGCAAACCTACCCTGCAGCCTGTGTTGCAGCTCAAGGCCCGAAGGCGC
CTGGACAAGGATGCTTTGGCCCCTGGCCCCTTTGCTTCTTTTCCCAATGGCTGGACTGGA
AAGCAGAAGTCTCCCGATGGTGTGCACCGCGTCCGTGTGGATTTTAAGGAGGATTGTGAT
TTAGAGAACGTGTGGCTGATGGGGGGCCTGAGTGTGCTCACCTCTGTGCCAGGGGGCCCC
CCGATGGTGTGCTTGCTGTGTGCCAGCAAAGGACTCCACGAGCTGGTGTTCTGTCAAGTC
TGCTGTGACCCATTCCACCCATTCTGCCTGGAGGAGGCCGAGCGGCCCCTGCCCCAGCAT
CACGACACCTGGTGCTGCCGTCGCTGCAAATTCTGCCACGTCTGTGGACGCAAAGGTCGT
GGATCCAAGCACCTCCTGGAGTGCGAGCGCTGCCGCCATGCATACCACCCGGCCTGTCTG
GGGCCCAGCTATCCAACCCGGGCCACGCGCAAACGGCGCCACTGGATCTGTTCAGCCTGT
GTGCGCTGTAAGAGCTGTGGGGCAACTCCAGGCAAGAACTGGGACGTCGAGTGGTCTGGA
GATTACAGCCTCTGCCCCAGGTGCACCCAGCTATATGAGAAAGGAAACTACTGCCCGATC
TGTACACGCTGCTATGAAGACAACGACTATGAGAGCAAGATGATGCAGTGCGCACAGTGC
GATCACTGGGTGCATGCCAAGTGCGAGGGGCTCTCAGATGAAGACTACGAGATCCTTTCA
GGACTGCCAGACTCGGTGCTGTACACCTGCGGACCGTGTGCTGGGGCAGCGCAGCCCCGC
TGGCGAGAGGCCCTGAGCGGGGCCCTCCAGGGGGGCCTGCGCCAGGTGCTCCAGGGCCTG
CTGAGCTCCAAGGTGGTGGGCCCACTGCTGCTCTGCACCCAGTGTGGGCCAGATGGGAAG
CAACTGCACCCAGGACCCTGCGGCCTGCAAGCTGTGAGTCAGCGCTTCGAGGATGGCCAC
TACAAGTCTGTGCACAGCTTCATGGAGGACATGGTGGGCATCCTCATGCGGCACTCGGAG
GAGGGAGAGACCCCGGACCGCCGGGCTGGAGGCCAGATGAAGGGGCTCCTGCTGAAGCTG
CTAGAATCTGCGTTCGGCTGGTTCGACGCCCACGACCCCAAGTACTGGCGACGGAGTACC
CGGCTGCCAAACGGAGTCCTTCCCAATGCGGTGTTGCCCCCATCCCTGGATCATGTCTAT
GCGCAGTGGAGACAGCAGGAACCAGAGACCCCAGAATCAGGGCAGCCTCCAGGGGATCCC
TCAGCAGCATTCCAGGGCAAGGATCCGGCTGCCTTCTCACACCTGGAGGACCCCCGTCAG
TGTGCACTCTGCCTCAAATACGGGGATGCAGACTCCAAGGAGGCGGGGCGGCTCTTGTAC
ATCGGGCAGAACGAGTGGACACACGTCAACTGTGCCATCTGGTCGGCGGAAGTCTTCGAG
GAGAACGACGGCTCCCTCAAGAATGTGCATGCTGCTGTGGCCCGAGGGAGGCAGATGCGC
TGCGAGCTCTGCCTGAAGCCTGGCGCCACGGTGGGCTGCTGCCTGTCCTCCTGCCTCAGC
AACTTCCACTTCATGTGTGCCCGGGCCAGCTACTGCATCTTCCAGGATGACAAGAAAGTC
TTCTGCCAGAAACACACTGATCTCCTGGATGGCAAGGAAATTGTGAACCCCGATGGTTTT
GATGTTCTCCGCCGAGTCTATGTGGACTTCGAGGGCATCAACTTCAAGCGGAAGTTCTTG
ACGGGGCTTGAACCCGATGCCATCAACGTGCTCATTGGTTCCATCCGCATTGACTCCCTG
GGTACTCTGTCTGATCTCTCGGACTGCGAGGGACGGCTCTTCCCCATTGGCTACCAGTGC
TCCCGTCTGTACTGGAGCACAGTGGATGCTCGGAGGCGCTGCTGGTATCGGTGCCGAATT
CTGGAGTATCGGCCATGGGGGCCGAGGGAAGAGCCAGCTCACCTGGAGGCTGCAGAGGAG
AACCAGACCATTGTGCACAGCCCCGCCCCTTCCTCAGAGCCCCCAGGTGGTGAGGACCCC
CCACTGGACACAGATGTTCTTGTCCCTGGAGCTCCTGAGCGCCACTCGCCCATTCAGAAC
CTGGACCCTCCACTGCGGCCAGATTCAGGCAGCGCCCCTCCTCCAGCCCCCCGTTCTTTT
TCGGGGGCTCGAATCAAAGTGCCCAACTACTCGCCATCCCGGAGGCCCTTGGGGGGTGTC
TCCTTTGGCCCCCTGCCCTCCCCTGGAAGTCCATCTTCACTGACCCACCACATCCCCACA
GTGGGAGACCCGGACTTCCCAGCTCCCCCCAGACGTTCCCGTCGTCCCAGCCCTTTGGCT
CCCAGGCCGCCTCCATCACGGTGGGCCTCCCCTCCTCTAAAAACCTCCCCTCAGCTCAGG
GTGCCCCCTCCTACCTCAGTCGTCACAGCCCTCACACCTACCTCAGGGGAGCTGGCTCCC
CCTGGCCCGGCCCCATCTCCACCACCCCCTGAAGACCTGGGCCCAGACTTCGAGGACATG
GAGGTGGTGTCAGGACTGAGTGCTGCTGACCTGGACTTCGCGGCCAGCCTGCTGGGGACT
GAGCCCTTCCAGGAAGAGATTGTAGCCGCTGGGGCCATGGGGAGCAGCCACGGGGGCCCG
GGGGACAGCTCCGAGGAGGAGTCCAGCCCCACCTCCCGCTACATCCACTTCCCTGTGACT
GTGGTGTCCGCCCCTGGTCTGGCCCCCAGCGCTACCCCTGGAGCCCCCCGCATTGAACAG
CTGGACGGCGTGGACGACGGCACTGACAGTGAGGCTGAGGCGGTGCAGCAGCCTCGGGGC
CAGGGCACGCCTCCTTCGGGGCCAGGAGTAGTCCGGGCAGGGGTCCTTGGGGCTGCAGGG
GACAGGGCCCGGCCTCCTGAGGACCTGCCATCGGAAATTGTGGATTTTGTGTTGAAGAAC
CTAGGGGGTCCTGGGGATGGAGGTGCTGGCCCTAGAGAGGAGTCACTCCCCCCGGCGCCT
CCCCTGGCTAATGGCAGCCAGCCCTCCCAAGGCCTGACCGCCAGCCCAGCTGACCCCACC
CGCACATTTGCCTGGCTCCCAGGGGCCCCAGGGGTCCGGGTGTTAAGCCTTGGCCCTGCC
CCTGAGCCCCCCAAACCCGCCACATCCAAAATCATACTTGTCAACAAGCTGGGGCAAGTA
TTTGTGAAGATGGCTGGGGAGGGTGAACCTGTCCCACCCCCAGTGAAGCAGCCACCTTTG
CCCCCCACCATTTCCCCCACGGCTCCCACCTCCTGGACTCTGCCCCCAGGCCCCCTCCTC
GGCGTGCTGCCCGTGGTCGGAGTGGTCCGCCCTGCCCCGCCCCCGCCACCCCCTCCCCTG
ACGCTGGTGCTGAGCAGTGGGCCAGCCAGCCCGCCCCGCCAGGCCATCCGCGTCAAGAGG
GTGTCCACTTTCTCCGGCCGGTCCCCGCCAGCACCTCCCCCATACAAAGCCCCCCGGCTG
GATGAAGATGGAGAGGCCTCAGAGGATACCCCTCAGGTTCCAGGGCTTGGCAGTGGCGGG
TTTAGCCGTGTGAGGATGAAAACCCCCACAGTGCGTGGGGTCCTTGACCTGGATCGGCCT
GGGGAGCCCGCTGGGGAAGAAAGTCCTGGGCCCCTCCAGGAACGGTCCCCTTTGCTGCCA
CTTCCGGAAGATGGTCCTCCCCAGGTCCCCGATGGTCCCCCAGACCTGCTGCTTGAGTCC
CAGTGGCACCACTATTCAGGTGAGGCTTCGAGCTCTGAGGAAGAGCCTCCATCCCCAGAT
GATAAAGAGAACCAGGCCCCAAAACGGACTGGCCCACATCTGCGCTTCGAGATCAGCAGT
GAGGATGGGTTCAGCGTTGAGGCAGAGAGCTTGGAGGGGGCGTGGAGAACTCTGATCGAG
AAAGTGCAAGAGGCCCGAGGGCATGCCCGACTCAGACATCTCTCCTTTAGTGGAATGAGT
GGGGCGAGACTCCTGGGCATCCACCATGATGCTGTCATCTTCCTGGCCGAGCAGCTCCCC
GGAGCCCAGCGTTGCCAGCACTATAAGTTCCGTTACCACCAGCAGGGAGAGGGCCAGGAG
GAGCCGCCCCTGAATCCCCATGGGGCTGCTCGGGCAGAGGTCTATCTCCGGAAGTGCACC
TTTGACATGTTCAACTTCCTGGCCTCCCAGCACCGGGTGCTCCCTGAGGGGGCCACCTGT
GATGAGGAAGAGGATGAGGTGCAGCTCAGGTCAACCAGACGTGCCACCAGCCTGGAGCTG
CCCATGGCCATGCGTTTTCGTCACCTTAAGAAGACGTCCAAAGAAGCTGTGGGTGTCTAC
AGATCAGCCATCCACGGGCGAGGCCTGTTCTGTAAGCGCAACATCGACGCGGGGGAGATG
GTCATCGAGTACTCTGGCATTGTCATCCGCTCGGTGTTGACTGACAAGCGGGAGAAGTTC
TACGATGGGAAGGGCATCGGGTGCTATATGTTCCGCATGGATGACTTTGATGTAGTGGAC
GCCACGATGCATGGCAATGCCGCCCGCTTCATCAACCACTCCTGTGAGCCCAACTGCTTC
TCTCGGGTCATCCACGTGGAGGGCCAGAAACACATTGTTATCTTCGCCCTGCGCCGCATC
CTGCGTGGTGAGGAGCTCACCTACGACTACAAGTTCCCCATCGAGGATGCCAGCAACAAG
CTGCCCTGCAACTGTGGCGCCAAGCGCTGCCGTCGGTTCCTTAACTGA
|
| Enzyme 19 GenBank Gene ID |
NM_014727.1  |
| Enzyme 19 GeneCard ID |
WBP7  |
| Enzyme 19 GenAtlas ID |
Not Available |
| Enzyme 19 HGNC ID |
Not Available |
| Enzyme 19 Chromosome Location |
Not Available |
| Enzyme 19 Locus |
Not Available |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed
]
- Huntsman DG, Chin SF, Muleris M, Batley SJ, Collins VP, Wiedemann LM, Aparicio S, Caldas C: MLL2, the second human homolog of the Drosophila trithorax gene, maps to 19q13.1 and is amplified in solid tumor cell lines. Oncogene. 1999 Dec 23;18(56):7975-84. [PubMed
]
- Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- FitzGerald KT, Diaz MO: MLL2: A new mammalian member of the trx/MLL family of genes. Genomics. 1999 Jul 15;59(2):187-92. [PubMed
]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- De Santa F, Totaro MG, Prosperini E, Notarbartolo S, Testa G, Natoli G: The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing. Cell. 2007 Sep 21;130(6):1083-94. Epub 2007 Sep 6. [PubMed
]
- Cho YW, Hong T, Hong S, Guo H, Yu H, Kim D, Guszczynski T, Dressler GR, Copeland TD, Kalkum M, Ge K: PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex. J Biol Chem. 2007 Jul 13;282(28):20395-406. Epub 2007 May 11. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
14764 |
| Enzyme 20 Name |
Probable histone-lysine N-methyltransferase NSD2 |
| Enzyme 20 Synonyms |
- Multiple myeloma SET domain-containing protein
- Nuclear SET domain-containing protein 2
- Protein trithorax-5
- Wolf-Hirschhorn syndrome candidate 1 protein
|
| Enzyme 20 Gene Name |
WHSC1 |
| Enzyme 20 Protein Sequence |
>Probable histone-lysine N-methyltransferase NSD2
MEFSIKQSPLSVQSVVKCIKMKQAPEILGSANGKTPSCEVNRECSVFLSKAQLSSSLQEG
VMQKFNGHDALPFIPADKLKDLTSRVFNGEPGAHDAKLRFESQEMKGIGTPPNTTPIKNG
SPEIKLKITKTYMNGKPLFESSICGDSAADVSQSEENGQKPENKARRNRKRSIKYDSLLE
QGLVEAALVSKISSPSDKKIPAKKESCPNTGRDKDHLLKYNVGDLVWSKVSGYPWWPCMV
SADPLLHSYTKLKGQKKSARQYHVQFFGDAPERAWIFEKSLVAFEGEGQFEKLCQESAKQ
APTKAEKIKLLKPISGKLRAQWEMGIVQAEEAASMSVEERKAKFTFLYVGDQLHLNPQVA
KEAGIAAESLGEMAESSGVSEEAAENPKSVREECIPMKRRRRAKLCSSAETLESHPDIGK
STPQKTAEADPRRGVGSPPGRKKTTVSMPRSRKGDAASQFLVFCQKHRDEVVAEHPDASG
EEIEELLRSQWSLLSEKQRARYNTKFALVAPVQAEEDSGNVNGKKRNHTKRIQDPTEDAE
AEDTPRKRLRTDKHSLRKRDTITDKTARTSSYKAMEAASSLKSQAATKNLSDACKPLKKR
NRASTAASSALGFSKSSSPSASLTENEVSDSPGDEPSESPYESADETQTEVSVSSKKSER
GVTAKKEYVCQLCEKPGSLLLCEGPCCGAFHLACLGLSRRPEGRFTCSECASGIHSCFVC
KESKTDVKRCVVTQCGKFYHEACVKKYPLTVFESRGFRCPLHSCVSCHASNPSNPRPSKG
KMMRCVRCPVAYHSGDACLAAGCSVIASNSIICTAHFTARKGKRHHAHVNVSWCFVCSKG
GSLLCCESCPAAFHPDCLNIEMPDGSWFCNDCRAGKKLHFQDIIWVKLGNYRWWPAEVCH
PKNVPPNIQKMKHEIGEFPVFFFGSKDYYWTHQARVFPYMEGDRGSRYQGVRGIGRVFKN
ALQEAEARFREIKLQREARETQESERKPPPYKHIKVNKPYGKVQIYTADISEIPKCNCKP
TDENPCGFDSECLNRMLMFECHPQVCPAGEFCQNQCFTKRQYPETKIIKTDGKGWGLVAK
RDIRKGEFVNEYVGELIDEEECMARIKHAHENDITHFYMLTIDKDRIIDAGPKGNYSRFM
NHSCQPNCETLKWTVNGDTRVGLFAVCDIPAGTELTFNYNLDCLGNEKTVCRCGASNCSG
FLGDRPKTSTTLSSEEKGKKTKKKTRRRRAKGEGKRQSEDECFRCGDGGQLVLCDRKFCT
KAYHLSCLGLGKRPFGKWECPWHHCDVCGKPSTSFCHLCPNSFCKEHQDGTAFSCTPDGR
SYCCEHDLGAASVRSTKTEKPPPEPGKPKGKRRRRRGWRRVTEGK
|
| Enzyme 20 Number of Residues |
1365 |
| Enzyme 20 Molecular Weight |
152257.0 |
| Enzyme 20 Theoretical pI |
8.81 |
| Enzyme 20 GO Classification |
| Function |
- DNA binding
- binding
- catalytic activity
- cation binding
- histone-lysine N-methyltransferase activity
- ion binding
- metal ion binding
- methyltransferase activity
- nucleic acid binding
- protein binding
- protein methyltransferase activity
- protein-lysine N-methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
- transition metal ion binding
- zinc ion binding
|
| Process |
| — |
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 20 General Function |
Involved in histone-lysine N-methyltransferase activity |
| Enzyme 20 Specific Function |
Probable histone methyltransferase. May act as a transcription regulator that binds DNA and suppresses IL5 transcription |
| Enzyme 20 Pathways |
|
| Enzyme 20 Reactions |
- S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
|
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
109633019  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
O96028  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
NSD2_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>4098 bp
ATGGAATTTAGCATCAAGCAGAGTCCCCTTTCTGTTCAGAGTGTTGTAAAGTGCATAAAG
ATGAAGCAGGCACCAGAAATCCTCGGCAGTGCCAACGGGAAGACTCCGAGCTGCGAGGTG
AACCGCGAGTGTTCTGTGTTCCTCAGCAAAGCCCAGCTCTCCAGTAGCCTGCAGGAGGGG
GTCATGCAGAAGTTTAACGGCCACGACGCCCTGCCCTTTATTCCAGCCGACAAGCTGAAA
GATCTTACTTCCCGGGTGTTTAATGGAGAACCCGGCGCACACGATGCCAAACTGCGTTTT
GAGTCCCAGGAAATGAAAGGGATTGGGACACCCCCTAACACTACCCCTATCAAAAATGGC
TCTCCAGAAATTAAGCTGAAAATCACCAAAACATACATGAATGGGAAGCCTCTCTTTGAA
TCTTCCATTTGTGGTGACAGTGCTGCTGATGTGTCTCAGTCAGAAGAAAATGGACAAAAA
CCAGAAAACAAGGCGAGAAGGAACAGGAAGAGGAGCATAAAATATGACTCCTTGCTGGAG
CAGGGCCTTGTCGAAGCAGCTCTTGTGTCTAAGATCTCAAGTCCTTCAGATAAAAAGATT
CCAGCTAAGAAAGAGTCTTGTCCAAACACTGGAAGAGACAAAGACCACCTGTTGAAATAC
AACGTTGGTGATTTGGTGTGGTCCAAAGTGTCGGGTTACCCTTGGTGGCCTTGCATGGTT
TCTGCAGATCCACTCCTTCACAGCTATACCAAACTTAAAGGTCAGAAAAAGAGTGCACGC
CAGTATCACGTACAGTTCTTTGGTGACGCCCCAGAAAGAGCTTGGATATTTGAGAAGAGC
CTCGTAGCTTTTGAAGGAGAAGGACAGTTTGAAAAATTATGCCAGGAAAGTGCCAAGCAG
GCACCCACGAAAGCTGAGAAAATTAAGCTATTGAAACCAATTTCAGGGAAATTGAGGGCC
CAGTGGGAAATGGGCATTGTTCAAGCAGAAGAAGCTGCAAGCATGTCAGTGGAGGAGCGG
AAAGCCAAGTTCACCTTTCTCTATGTGGGGGACCAGCTTCATCTCAACCCTCAAGTAGCC
AAGGAGGCTGGCATTGCTGCAGAGTCTTTGGGAGAAATGGCAGAATCCTCAGGAGTCAGT
GAAGAAGCTGCTGAAAACCCCAAGTCTGTGAGAGAAGAGTGCATTCCCATGAAGAGAAGG
CGGAGGGCCAAACTGTGTAGCTCTGCAGAGACCCTGGAGAGTCACCCCGACATAGGGAAG
AGTACTCCTCAAAAGACGGCAGAGGCTGACCCCAGAAGAGGAGTAGGGTCTCCTCCTGGG
AGGAAGAAGACCACAGTCTCCATGCCACGAAGCAGGAAGGGAGATGCAGCATCCCAGTTT
TTGGTCTTCTGTCAAAAACACAGGGATGAGGTGGTAGCTGAGCACCCAGATGCTTCAGGT
GAGGAGATTGAAGAGCTGCTCAGGTCACAGTGGAGTCTGCTGAGTGAGAAGCAGAGAGCA
CGCTACAACACCAAGTTTGCCCTGGTGGCCCCTGTCCAGGCTGAAGAAGACTCTGGTAAT
GTAAATGGGAAAAAAAGAAACCACACAAAGAGGATACAGGACCCTACAGAAGATGCTGAA
GCTGAGGACACACCCAGGAAAAGACTCAGGACGGACAAGCACAGTCTTCGGAAGAGAGAC
ACAATCACTGACAAAACGGCCAGAACAAGCTCTTACAAGGCCATGGAGGCAGCCTCCTCG
CTCAAGAGCCAGGCAGCAACGAAAAATCTGTCTGATGCATGTAAACCACTGAAGAAGCGA
AATCGGGCTTCCACGGCAGCATCTTCAGCTCTTGGGTTTAGCAAAAGTTCATCTCCTTCT
GCATCCTTAACTGAGAATGAGGTCTCGGACAGCCCGGGAGACGAGCCCTCGGAGTCCCCA
TACGAAAGTGCAGACGAAACACAAACTGAAGTATCTGTCTCATCCAAAAAGTCTGAGCGA
GGAGTGACTGCCAAAAAGGAGTATGTGTGCCAGCTGTGTGAGAAGCCGGGCAGCCTCCTG
CTCTGTGAAGGACCCTGCTGCGGAGCTTTCCACCTCGCCTGCCTTGGGCTTTCCCGGAGG
CCAGAAGGGAGGTTCACCTGCAGCGAGTGTGCCTCAGGGATTCACTCATGTTTCGTGTGT
AAAGAGAGCAAGACAGATGTTAAGCGCTGTGTGGTAACTCAGTGTGGAAAATTTTACCAT
GAGGCTTGTGTGAAAAAATACCCTCTGACTGTATTTGAGAGCCGAGGTTTCCGCTGCCCC
CTCCACAGCTGTGTGAGCTGCCATGCTTCCAACCCTTCAAACCCAAGGCCGTCAAAAGGT
AAAATGATGCGGTGTGTCCGCTGCCCCGTTGCCTATCACAGCGGGGATGCTTGTCTGGCA
GCAGGATGCTCAGTGATCGCCTCCAACAGCATCATCTGCACTGCCCACTTCACTGCTCGG
AAGGGGAAGCGACACCACGCCCACGTCAACGTGAGCTGGTGCTTCGTGTGCTCCAAAGGG
GGGAGCCTTCTGTGCTGTGAGTCCTGCCCAGCGGCCTTCCACCCTGACTGCCTGAACATC
GAGATGCCTGACGGCAGCTGGTTCTGCAATGACTGCAGGGCTGGGAAGAAGCTGCACTTC
CAGGATATCATTTGGGTGAAACTTGGGAACTACAGATGGTGGCCGGCAGAAGTTTGCCAT
CCCAAAAATGTTCCCCCAAATATTCAGAAAATGAAGCACGAGATTGGAGAATTCCCTGTG
TTTTTCTTTGGGTCTAAAGATTATTACTGGACGCATCAGGCGCGAGTGTTCCCGTACATG
GAGGGGGACCGGGGCAGCCGCTACCAGGGGGTCAGAGGGATCGGAAGAGTCTTCAAAAAC
GCACTGCAAGAAGCTGAAGCTCGTTTTCGTGAAATTAAGCTTCAGAGGGAAGCCCGAGAA
ACACAGGAGAGCGAGCGCAAGCCCCCACCATACAAGCACATCAAGGTGAATAAGCCTTAC
GGGAAAGTCCAGATCTACACAGCGGATATTTCAGAAATCCCTAAGTGCAACTGCAAGCCC
ACAGATGAGAATCCTTGTGGCTTTGATTCGGAGTGTCTGAACAGGATGCTGATGTTTGAG
TGCCACCCGCAGGTGTGTCCCGCGGGCGAGTTCTGCCAGAACCAGTGCTTCACCAAGCGC
CAGTACCCAGAGACCAAGATCATCAAGACAGATGGCAAAGGGTGGGGCCTGGTCGCCAAG
AGGGACATCAGAAAGGGAGAATTTGTTAACGAGTACGTTGGGGAGCTGATCGACGAGGAG
GAGTGCATGGCGAGAATCAAGCACGCACACGAGAACGACATCACCCACTTCTACATGCTC
ACTATAGACAAGGACCGTATAATAGACGCTGGCCCCAAAGGAAACTACTCTCGATTTATG
AATCACAGCTGCCAGCCCAACTGTGAGACCCTCAAGTGGACAGTGAATGGGGACACTCGT
GTGGGCCTGTTTGCCGTCTGTGACATTCCTGCAGGGACGGAGCTGACTTTTAACTACAAC
CTCGATTGTCTGGGCAATGAAAAAACGGTCTGCCGGTGTGGAGCCTCCAATTGCAGTGGA
TTCCTCGGGGATAGACCAAAGACCTCGACGACCCTTTCATCAGAGGAAAAGGGCAAAAAG
ACCAAGAAGAAAACGAGGCGGCGCAGAGCAAAAGGGGAAGGGAAGAGGCAGTCAGAGGAC
GAGTGCTTCCGCTGCGGTGATGGCGGGCAGCTGGTGCTGTGTGACCGCAAGTTCTGCACC
AAGGCCTACCACCTGTCCTGCCTGGGCCTTGGCAAGCGGCCCTTCGGGAAGTGGGAATGT
CCTTGGCATCATTGTGACGTGTGTGGCAAACCTTCGACTTCATTTTGCCACCTCTGCCCC
AATTCGTTCTGTAAGGAGCACCAGGACGGGACAGCCTTCAGCTGCACCCCGGACGGGCGG
TCCTACTGCTGTGAGCATGACTTAGGGGCGGCATCGGTCAGAAGCACCAAGACTGAGAAG
CCCCCCCCAGAGCCAGGGAAGCCGAAGGGGAAGAGGCGGCGGCGGAGGGGCTGGCGGAGA
GTCACAGAGGGCAAATAG
|
| Enzyme 20 GenBank Gene ID |
NM_001042424.2  |
| Enzyme 20 GeneCard ID |
WHSC1  |
| Enzyme 20 GenAtlas ID |
WHSC1  |
| Enzyme 20 HGNC ID |
HGNC:12766  |
| Enzyme 20 Chromosome Location |
4 |
| Enzyme 20 Locus |
4p16.3 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Chesi M, Nardini E, Lim RS, Smith KD, Kuehl WM, Bergsagel PL: The t(4;14) translocation in myeloma dysregulates both FGFR3 and a novel gene, MMSET, resulting in IgH/MMSET hybrid transcripts. Blood. 1998 Nov 1;92(9):3025-34. [PubMed
]
- Stec I, Wright TJ, van Ommen GJ, de Boer PA, van Haeringen A, Moorman AF, Altherr MR, den Dunnen JT: WHSC1, a 90 kb SET domain-containing gene, expressed in early development and homologous to a Drosophila dysmorphy gene maps in the Wolf-Hirschhorn syndrome critical region and is fused to IgH in t(4;14) multiple myeloma. Hum Mol Genet. 1998 Jul;7(7):1071-82. [PubMed
]
- Garlisi CG, Uss AS, Xiao H, Tian F, Sheridan KE, Wang L, Motasim Billah M, Egan RW, Stranick KS, Umland SP: A unique mRNA initiated within a middle intron of WHSC1/MMSET encodes a DNA binding protein that suppresses human IL-5 transcription. Am J Respir Cell Mol Biol. 2001 Jan;24(1):90-98. [PubMed
]
- Keats JJ, Maxwell CA, Taylor BJ, Hendzel MJ, Chesi M, Bergsagel PL, Larratt LM, Mant MJ, Reiman T, Belch AR, Pilarski LM: Overexpression of transcripts originating from the MMSET locus characterizes all t(4;14)(p16;q32)-positive multiple myeloma patients. Blood. 2005 May 15;105(10):4060-9. Epub 2005 Jan 27. [PubMed
]
- Kikuno R, Nagase T, Ishikawa K, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Jun 30;6(3):197-205. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
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- Malgeri U, Baldini L, Perfetti V, Fabris S, Vignarelli MC, Colombo G, Lotti V, Compasso S, Bogni S, Lombardi L, Maiolo AT, Neri A: Detection of t(4;14)(p16.3;q32) chromosomal translocation in multiple myeloma by reverse transcription-polymerase chain reaction analysis of IGH-MMSET fusion transcripts. Cancer Res. 2000 Aug 1;60(15):4058-61. [PubMed
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- Perfetti V, Coluccia AM, Intini D, Malgeri U, Vignarelli MC, Casarini S, Merlini G, Neri A: Translocation T(4;14)(p16.3;q32) is a recurrent genetic lesion in primary amyloidosis. Am J Pathol. 2001 May;158(5):1599-603. [PubMed
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- Santra M, Zhan F, Tian E, Barlogie B, Shaughnessy J Jr: A subset of multiple myeloma harboring the t(4;14)(p16;q32) translocation lacks FGFR3 expression but maintains an IGH/MMSET fusion transcript. Blood. 2003 Mar 15;101(6):2374-6. Epub 2002 Nov 14. [PubMed
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- Intini D, Fabris S, Storlazzi T, Otsuki T, Ciceri G, Verdelli D, Lombardi L, Rocchi M, Neri A: Identification of a novel IGH-MMSET fusion transcript in a human myeloma cell line with the t(4;14)(p16.3;q32) chromosomal translocation. Br J Haematol. 2004 Aug;126(3):437-9. [PubMed
]
- Hudlebusch HR, Theilgaard-Monch K, Lodahl M, Johnsen HE, Rasmussen T: Identification of ID-1 as a potential target gene of MMSET in multiple myeloma. Br J Haematol. 2005 Sep;130(5):700-8. [PubMed
]
- Todoerti K, Ronchetti D, Agnelli L, Castellani S, Marelli S, Deliliers GL, Zanella A, Lombardi L, Neri A: Transcription repression activity is associated with the type I isoform of the MMSET gene involved in t(4;14) in multiple myeloma. Br J Haematol. 2005 Oct;131(2):214-8. [PubMed
]
- Bergemann AD, Cole F, Hirschhorn K: The etiology of Wolf-Hirschhorn syndrome. Trends Genet. 2005 Mar;21(3):188-95. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed
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- Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed
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- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
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- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
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- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
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- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
14765 |
| Enzyme 21 Name |
Histone-lysine N-methyltransferase NSD3 |
| Enzyme 21 Synonyms |
- Nuclear SET domain-containing protein 3
- Protein whistle
- WHSC1-like 1 isoform 9 with methyltransferase activity to lysine
- Wolf-Hirschhorn syndrome candidate 1-like protein 1
- WHSC1-like protein 1
|
| Enzyme 21 Gene Name |
WHSC1L1 |
| Enzyme 21 Protein Sequence |
>Histone-lysine N-methyltransferase NSD3
MDFSFSFMQGIMGNTIQQPPQLIDSANIRQEDAFDNNSDIAEDGGQTPYEATLQQGFQYP
ATTEDLPPLTNGYPSSISVYETQTKYQSYNQYPNGSANGFGAVRNFSPTDYYHSEIPNTR
PHEILEKPSPPQPPPPPSVPQTVIPKKTGSPEIKLKITKTIQNGRELFESSLCGDLLNEV
QASEHTKSKHESRKEKRKKSNKHDSSRSEERKSHKIPKLEPEEQNRPNERVDTVSEKPRE
EPVLKEEAPVQPILSSVPTTEVSTGVKFQVGDLVWSKVGTYPWWPCMVSSDPQLEVHTKI
NTRGAREYHVQFFSNQPERAWVHEKRVREYKGHKQYEELLAEATKQASNHSEKQKIRKPR
PQRERAQWDIGIAHAEKALKMTREERIEQYTFIYIDKQPEEALSQAKKSVASKTEVKKTR
RPRSVLNTQPEQTNAGEVASSLSSTEIRRHSQRRHTSAEEEEPPPVKIAWKTAAARKSLP
ASITMHKGSLDLQKCNMSPVVKIEQVFALQNATGDGKFIDQFVYSTKGIGNKTEISVRGQ
DRLIISTPNQRNEKPTQSVSSPEATSGSTGSVEKKQQRRSIRTRSESEKSTEVVPKKKIK
KEQVETVPQATVKTGLQKGASEISDSCKPLKKRSRASTDVEMTSSAYRDTSDSDSRGLSD
LQVGFGKQVDSPSATADADVSDVQSMDSSLSRRGTGMSKKDTVCQICESSGDSLIPCEGE
CCKHFHLECLGLASLPDSKFICMECKTGQHPCFSCKVSGKDVKRCSVGACGKFYHEACVR
KFPTAIFESKGFRCPQHCCSACSMEKDIHKASKGRMMRCLRCPVAYHSGDACIAAGSMLV
SSYILICSNHSKRSSNSSAVNVGFCFVCARGLIVQDHSDPMFSSYAYKSHYLLNESNRAE
LMKLPMIPSSSASKKKCEKGGRLLCCESCPASFHPECLSIEMPEGCWNCNDCKAGKKLHY
KQIVWVKLGNYRWWPAEICNPRSVPLNIQGLKHDLGDFPVFFFGSHDYYWVHQGRVFPYV
EGDKSFAEGQTSINKTFKKALEEAAKRFQELKAQRESKEALEIEKNSRKPPPYKHIKANK
VIGKVQIQVADLSEIPRCNCKPADENPCGLESECLNRMLQYECHPQVCPAGDRCQNQCFT
KRLYPDAEIIKTERRGWGLRTKRSIKKGEFVNEYVGELIDEEECRLRIKRAHENSVTNFY
MLTVTKDRIIDAGPKGNYSRFMNHSCNPNCETQKWTVNGDVRVGLFALCDIPAGMELTFN
YNLDCLGNGRTECHCGADNCSGFLGVRPKSACASTNEEKAKNAKLKQKRRKIKTEPKQMH
EDYCFQCGDGGELVMCDKKDCPKAYHLLCLNLTQPPYGKWECPWHQCDECSSAAVSFCEF
CPHSFCKDHEKGALVPSALEGRLCCSEHDPMAPVSPEYWSKIKCKWESQDHGEEVKE
|
| Enzyme 21 Number of Residues |
1437 |
| Enzyme 21 Molecular Weight |
161611.8 |
| Enzyme 21 Theoretical pI |
8.26 |
| Enzyme 21 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- histone-lysine N-methyltransferase activity
- ion binding
- metal ion binding
- methyltransferase activity
- protein binding
- protein methyltransferase activity
- protein-lysine N-methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
- transition metal ion binding
- zinc ion binding
|
| Process |
| — |
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 21 General Function |
Involved in histone-lysine N-methyltransferase activity |
| Enzyme 21 Specific Function |
Histone methyltransferase. Preferentially methylates 'Lys-4' and 'Lys-27' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation, while 'Lys-27' is a mark for transcriptional repression |
| Enzyme 21 Pathways |
|
| Enzyme 21 Reactions |
- S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
|
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
13699811  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q9BZ95  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
NSD3_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>4314 bp
ATGGATTTCTCTTTCTCTTTCATGCAAGGGATCATGGGAAACACAATTCAGCAACCACCT
CAACTCATTGACTCCGCCAACATCCGTCAGGAGGATGCCTTTGATAACAACAGTGACATT
GCTGAAGATGGTGGCCAGACACCATATGAAGCTACTTTGCAGCAAGGCTTTCAGTACCCA
GCTACAACAGAAGATCTTCCTCCACTCACAAATGGGTATCCATCATCAATCAGTGTGTAT
GAAACTCAAACCAAATACCAGTCATATAATCAGTATCCTAATGGGTCAGCCAATGGCTTT
GGTGCAGTTAGAAACTTTAGCCCCACTGACTATTATCATTCAGAAATTCCAAACACAAGA
CCACATGAAATTCTGGAAAAACCTTCCCCTCCACAGCCACCACCTCCTCCTTCGGTACCA
CAAACTGTGATTCCAAAGAAGACTGGCTCACCTGAAATTAAACTAAAAATAACCAAAACT
ATCCAGAATGGCAGGGAATTGTTTGAGTCTTCCCTTTGTGGAGACCTTTTAAATGAAGTA
CAGGCAAGTGAGCACACGAAATCAAAGCATGAAAGCAGAAAAGAAAAGAGGAAAAAAAGC
AACAAGCATGACTCATCAAGATCTGAAGAGCGCAAGTCACACAAAATCCCCAAATTAGAA
CCAGAGGAACAAAATAGACCAAATGAGAGGGTTGACACTGTATCAGAAAAACCAAGGGAA
GAACCAGTACTAAAAGAGGAAGCCCCAGTTCAGCCAATACTATCTTCTGTTCCAACAACG
GAAGTGTCCACTGGTGTTAAGTTTCAGGTTGGCGATCTTGTGTGGTCCAAGGTGGGAACC
TATCCTTGGTGGCCTTGTATGGTTTCAAGTGATCCCCAGCTTGAGGTTCATACTAAAATT
AACACAAGAGGTGCCCGAGAATATCATGTCCAGTTTTTTAGCAACCAGCCAGAGAGGGCG
TGGGTTCATGAAAAACGGGTACGAGAGTATAAAGGTCATAAACAGTATGAAGAATTACTG
GCTGAGGCAACCAAACAAGCCAGCAATCACTCTGAGAAACAAAAGATTCGGAAACCCCGA
CCTCAGAGAGAACGTGCTCAGTGGGATATTGGCATTGCCCATGCAGAGAAAGCATTGAAA
ATGACTCGAGAAGAAAGAATAGAACAGTATACTTTTATTTACATTGATAAACAGCCTGAA
GAGGCTTTATCCCAAGCAAAAAAGAGTGTTGCCTCCAAAACCGAAGTTAAAAAAACCCGA
CGACCAAGATCTGTGCTGAATACTCAGCCAGAACAGACCAATGCAGGGGAGGTGGCCTCC
TCACTCTCAAGTACTGAAATTCGGAGACATAGCCAGAGGCGGCACACAAGTGCGGAAGAG
GAAGAGCCACCGCCTGTTAAAATAGCCTGGAAAACTGCGGCAGCAAGGAAATCCTTACCA
GCTTCCATTACGATGCACAAAGGGAGCCTGGATTTGCAGAAGTGTAACATGTCTCCAGTT
GTGAAAATTGAACAAGTGTTTGCTCTTCAGAATGCTACAGGGGATGGGAAATTTATCGAT
CAATTTGTTTATTCAACAAAGGGAATTGGTAACAAAACAGAAATAAGTGTCAGGGGGCAA
GACAGGCTTATAATTTCTACACCAAACCAGAGAAATGAAAAGCCAACGCAGAGTGTATCA
TCTCCTGAAGCAACATCTGGTTCTACAGGCTCAGTAGAAAAGAAGCAACAGAGAAGATCA
ATTAGAACTCGTTCTGAATCAGAGAAATCCACTGAGGTTGTGCCAAAGAAGAAGATCAAA
AAGGAGCAGGTTGAAACAGTTCCTCAGGCTACAGTGAAGACTGGATTACAGAAAGGTGCC
AGCGAGATTTCAGATTCCTGTAAACCTCTAAAGAAAAGGAGTCGCGCCTCAACTGATGTA
GAAATGACTAGTTCAGCATACAGAGACACATCTGACTCCGATTCTAGAGGACTGAGTGAC
CTGCAGGTAGGCTTTGGAAAGCAAGTAGATAGCCCTTCAGCTACTGCAGATGCAGACGTT
TCTGATGTGCAGTCCATGGATTCAAGTTTGTCGAGAAGAGGCACTGGAATGAGTAAGAAG
GACACTGTATGTCAGATTTGTGAAAGCTCTGGTGACTCTCTGATTCCTTGTGAGGGAGAG
TGCTGCAAACACTTTCACCTGGAGTGCCTGGGATTGGCATCACTTCCTGATAGCAAGTTC
ATCTGCATGGAATGTAAAACTGGGCAGCACCCATGTTTTTCGTGTAAAGTGTCTGGTAAA
GATGTGAAGCGTTGTTCTGTTGGTGCTTGTGGGAAATTTTATCATGAAGCCTGTGTCCGC
AAATTCCCCACTGCCATCTTTGAATCAAAAGGATTCCGCTGTCCTCAGCACTGCTGCTCT
GCCTGCTCTATGGAGAAAGATATCCACAAAGCAAGTAAAGGCCGCATGATGAGATGTTTA
AGATGTCCAGTTGCCTATCACTCTGGAGATGCTTGCATTGCGGCCGGAAGCATGTTAGTA
TCCTCCTACATTCTCATCTGTAGTAATCATTCCAAACGGAGCAGTAATTCTTCTGCTGTA
AATGTAGGCTTTTGTTTCGTTTGTGCCAGAGGGCTGATAGTTCAGGACCATTCAGACCCC
ATGTTCAGTTCATATGCCTATAAGTCCCACTACCTACTGAATGAATCAAATCGTGCTGAG
TTGATGAAATTACCTATGATTCCTTCTTCGTCAGCTTCCAAAAAGAAATGTGAGAAAGGT
GGAAGATTGCTCTGCTGTGAATCGTGCCCAGCTTCCTTCCACCCGGAATGCCTAAGCATA
GAAATGCCAGAAGGCTGCTGGAATTGTAATGACTGTAAAGCTGGCAAGAAACTACATTAC
AAGCAGATTGTTTGGGTCAAATTGGGAAATTACAGATGGTGGCCAGCAGAGATCTGCAAC
CCCAGGTCTGTGCCACTGAACATCCAGGGCCTTAAACATGACTTGGGGGACTTCCCTGTA
TTCTTCTTTGGTTCTCATGACTACTACTGGGTACACCAGGGCAGAGTGTTCCCTTATGTT
GAAGGAGACAAAAGCTTTGCTGAAGGGCAGACTAGTATTAACAAGACCTTCAAAAAGGCA
CTGGAAGAAGCTGCAAAACGTTTCCAGGAATTGAAAGCACAAAGAGAAAGTAAAGAAGCC
CTAGAGATTGAAAAAAACTCAAGAAAACCCCCTCCCTACAAACACATCAAAGCTAACAAA
GTAATAGGAAAGGTGCAGATCCAGGTTGCTGACCTGTCAGAGATTCCCCGCTGTAACTGC
AAGCCAGCTGATGAAAACCCTTGTGGCTTGGAATCGGAGTGCCTGAACAGAATGTTGCAG
TATGAATGCCACCCGCAGGTGTGCCCAGCTGGAGATCGTTGTCAGAACCAGTGCTTTACA
AAGAGACTATACCCTGATGCAGAGATCATCAAAACGGAGCGGAGAGGCTGGGGCCTCAGG
ACCAAAAGGAGCATTAAGAAGGGTGAATTTGTAAATGAATACGTCGGTGAATTAATTGAT
GAAGAAGAATGCAGATTGCGAATCAAGCGAGCCCACGAGAACAGTGTAACTAATTTTTAT
ATGTTAACTGTTACCAAGGACCGTATAATTGATGCCGGCCCAAAAGGAAATTATTCTCGC
TTCATGAACCACAGTTGTAATCCCAACTGTGAAACACAAAAGTGGACAGTGAATGGAGAT
GTTCGAGTGGGACTATTTGCTCTCTGTGATATTCCTGCAGGGATGGAGTTAACATTTAAT
TATAACCTAGATTGTCTGGGCAACGGCAGAACGGAGTGCCACTGTGGAGCAGATAACTGC
AGTGGTTTTCTAGGAGTGCGGCCAAAGTCGGCATGTGCGTCAACAAATGAAGAGAAGGCA
AAAAATGCTAAGTTAAAACAGAAGAGACGAAAGATCAAAACAGAACCAAAGCAGATGCAT
GAAGATTACTGTTTTCAATGTGGAGATGGTGGAGAGCTGGTCATGTGTGACAAAAAAGAC
TGTCCCAAAGCATACCACCTCCTATGCCTTAACCTGACTCAGCCACCATATGGAAAGTGG
GAGTGTCCGTGGCATCAGTGCGATGAGTGCAGCAGTGCAGCTGTTTCCTTCTGTGAATTC
TGTCCACATTCATTTTGTAAAGATCATGAAAAGGGGGCCCTGGTTCCCTCTGCACTGGAA
GGCCGCCTCTGCTGCTCGGAACATGACCCCATGGCTCCTGTGTCACCAGAATACTGGAGC
AAGATAAAATGTAAATGGGAATCACAAGATCATGGAGAAGAAGTAAAAGAATAA
|
| Enzyme 21 GenBank Gene ID |
NM_023034.1  |
| Enzyme 21 GeneCard ID |
WHSC1L1  |
| Enzyme 21 GenAtlas ID |
WHSC1L1  |
| Enzyme 21 HGNC ID |
HGNC:12767  |
| Enzyme 21 Chromosome Location |
8 |
| Enzyme 21 Locus |
8p11.2 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
- Stec I, van Ommen GJ, den Dunnen JT: WHSC1L1, on human chromosome 8p11.2, closely resembles WHSC1 and maps to a duplicated region shared with 4p16.3. Genomics. 2001 Aug;76(1-3):5-8. [PubMed
]
- Angrand PO, Apiou F, Stewart AF, Dutrillaux B, Losson R, Chambon P: NSD3, a new SET domain-containing gene, maps to 8p12 and is amplified in human breast cancer cell lines. Genomics. 2001 May 15;74(1):79-88. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Rosati R, La Starza R, Veronese A, Aventin A, Schwienbacher C, Vallespi T, Negrini M, Martelli MF, Mecucci C: NUP98 is fused to the NSD3 gene in acute myeloid leukemia associated with t(8;11)(p11.2;p15). Blood. 2002 May 15;99(10):3857-60. [PubMed
]
- Tonon G, Wong KK, Maulik G, Brennan C, Feng B, Zhang Y, Khatry DB, Protopopov A, You MJ, Aguirre AJ, Martin ES, Yang Z, Ji H, Chin L, Depinho RA: High-resolution genomic profiles of human lung cancer. Proc Natl Acad Sci U S A. 2005 Jul 5;102(27):9625-30. Epub 2005 Jun 27. [PubMed
]
- Kim SM, Kee HJ, Eom GH, Choe NW, Kim JY, Kim YS, Kim SK, Kook H, Kook H, Seo SB: Characterization of a novel WHSC1-associated SET domain protein with H3K4 and H3K27 methyltransferase activity. Biochem Biophys Res Commun. 2006 Jun 23;345(1):318-23. Epub 2006 Apr 27. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
14777 |
| Enzyme 22 Name |
Histone-lysine N-methyltransferase SETD2 |
| Enzyme 22 Synonyms |
- HIF-1
- Huntingtin yeast partner B
- Huntingtin-interacting protein 1
- HIP-1
- Huntingtin-interacting protein B
- Lysine N-methyltransferase 3A
- SET domain-containing protein 2
- hSET2
- p231HBP
|
| Enzyme 22 Gene Name |
SETD2 |
| Enzyme 22 Protein Sequence |
>Histone-lysine N-methyltransferase SETD2
MKQLQPQPPPKMGDFYDPEHPTPEEEENEAKIENVQKTGFIKGPMFKGVASSRFLPKGTK
TKVNLEEQGRQKVSFSFSLTKKTLQNRFLTALGNEKQSDTPNPPAVPLQVDSTPKMKMEI
GDTLSTAEESSPPKSRVELGKIHFKKHLLHVTSRPLLATTTAVASPPTHAAPLPAVIAES
TTVDSPPSSPPPPPPPAQATTLSSPAPVTEPVALPHTPITVLMAAPVPLPVDVAVRSLKE
PPIIIVPESLEADTKQDTISNSLEEHVTQILNEQADISSKKEDSHIGKDEEIPDSSKISL
SCKKTGSKKKSSQSEGIFLGSESDEDSVRTSSSQRSHDLKFSASIEKERDFKKSSAPLKS
EDLGKPSRSKTDRDDKYFSYSKLERDTRYVSSRCRSERERRRSRSHSRSERGSRTNLSYS
RSERSHYYDSDRRYHRSSPYRERTRYSRPYTDNRARESSDSEEEYKKTYSRRTSSHSSSY
RDLRTSSYSKSDRDCKTETSYLEMERRGKYSSKLERESKRTSENEAIKRCCSPPNELGFR
RGSSYSKHDSSASRYKSTLSKPIPKSDKFKNSFCCTELNEEIKQSHSFSLQTPCSKGSEL
RMINKNPEREKAGSPAPSNRLNDSPTLKKLDELPIFKSEFITHDSHDSIKELDSLSKVKN
DQLRSFCPIELNINGSPGAESDLATFCTSKTDAVLMTSDDSVTGSELSPLVKACMLSSNG
FQNISRCKEKDLDDTCMLHKKSESPFRETEPLVSPHQDKLMSMPVMTVDYSKTVVKEPVD
TRVSCCKTKDSDIYCTLNDSNPSLCNSEAENIEPSVMKISSNSFMNVHLESKPVICDSRN
LTDHSKFACEEYKQSIGSTSSASVNHFDDLYQPIGSSGIASSLQSLPPGIKVDSLTLLKC
GENTSPVLDAVLKSKKSSEFLKHAGKETIVEVGSDLPDSGKGFASRENRRNNGLSGKCLQ
EAQEEGNSILPERRGRPEISLDERGEGGHVHTSDDSEVVFSSCDLNLTMEDSDGVTYALK
CDSSGHAPEIVSTVHEDYSGSSESSNDESDSEDTDSDDSSIPRNRLQSVVVVPKNSTLPM
EETSPCSSRSSQSYRHYSDHWEDERLESRRHLYEEKFESIASKACPQTDKFFLHKGTEKN
PEISFTQSSRKQIDNRLPELSHPQSDGVDSTSHTDVKSDPLGHPNSEETVKAKIPSRQQE
ELPIYSSDFEDVPNKSWQQTTFQNRPDSRLGKTELSFSSSCEIPHVDGLHSSEELRNLGW
DFSQEKPSTTYQQPDSSYGACGGHKYQQNAEQYGGTRDYWQGNGYWDPRSGRPPGTGVVY
DRTQGQVPDSLTDDREEEENWDQQDGSHFSDQSDKFLLSLQKDKGSVQAPEISSNSIKDT
LAVNEKKDFSKNLEKNDIKDRGPLKKRRQEIESDSESDGELQDRKKVRVEVEQGETSVPP
GSALVGPSCVMDDFRDPQRWKECAKQGKMPCYFDLIEENVYLTERKKNKSHRDIKRMQCE
CTPLSKDERAQGEIACGEDCLNRLLMIECSSRCPNGDYCSNRRFQRKQHADVEVILTEKK
GWGLRAAKDLPSNTFVLEYCGEVLDHKEFKARVKEYARNKNIHYYFMALKNDEIIDATQK
GNCSRFMNHSCEPNCETQKWTVNGQLRVGFFTTKLVPSGSELTFDYQFQRYGKEAQKCFC
GSANCRGYLGGENRVSIRAAGGKMKKERSRKKDSVDGELEALMENGEGLSDKNQVLSLSR
LMVRIETLEQKLTCLELIQNTHSQSCLKSFLERHGLSLLWIWMAELGDGRESNQKLQEEI
IKTLEHLPIPTKNMLEESKVLPIIQRWSQTKTAVPPLSEGDGYSSENTSRAHTPLNTPDP
STKLSTEADTDTPKKLMFRRLKIISENSMDSAISDATSELEGKDGKEDLDQLENVPVEEE
EELQSQQLLPQQLPECKVDSETNIEASKLPTSEPEADAEIEPKESNGTKLEEPINEETPS
QDEEEGVSDVESERSQEQPDKTVDISDLATKLLDSWKDLKEVYRIPKKSQTEKENTTTER
GRDAVGFRDQTPAPKTPNRSRERDPDKQTQNKEKRKRRSSLSPPSSAYERGTKRPDDRYD
TPTSKKKVRIKDRNKLSTEERRKLFEQEVAQREAQKQQQQMQNLGMTSPLPYDSLGYNAP
HHPFAGYPPGYPMQAYVDPSNPNAGKVLLPTPSMDPVCSPAPYDHAQPLVGHSTEPLSAP
PPVPVVPHVAAPVEVSSSQYVAQSDGVVHQDSSVAVLPVPAPGPVQGQNYSVWDSNQQSV
SVQQQYSPAQSQATIYYQGQTCPTVYGVTSPYSQTTPPIVQSYAQPSLQYIQGQQIFTAH
PQGVVVQPAAAVTTIVAPGQPQPLQPSEMVVTNNLLDLPPPSPPKPKTIVLPPNWKTARD
PEGKIYYYHVITRQTQWDPPTWESPGDDASLEHEAEMDLGTPTYDENPMKASKKPKTAEA
DTSSELAKKSKEVFRKEMSQFIVQCLNPYRKPDCKVGRITTTEDFKHLARKLTHGVMNKE
LKYCKNPEDLECNENVKHKTKEYIKKYMQKFGAVYKPKEDTELE
|
| Enzyme 22 Number of Residues |
2564 |
| Enzyme 22 Molecular Weight |
287594.2 |
| Enzyme 22 Theoretical pI |
6.02 |
| Enzyme 22 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- histone-lysine N-methyltransferase activity
- ion binding
- metal ion binding
- methyltransferase activity
- oxidoreductase activity
- protein binding
- protein methyltransferase activity
- protein-lysine N-methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
- transition metal ion binding
|
| Process |
- biological regulation
- metabolic process
- oxidation reduction
- regulation of biological process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
- regulation of transcription, DNA-dependent
|
| Component |
- chromosome
- intracellular membrane-bounded organelle
- intracellular non-membrane-bounded organelle
- membrane-bounded organelle
- non-membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 22 General Function |
Involved in histone-lysine N-methyltransferase activity |
| Enzyme 22 Specific Function |
Histone methyltransferase that methylates 'Lys-36' of histone H3. H3 'Lys-36' methylation represents a specific tag for epigenetic transcriptional activation. Probably plays a role in chromatin structure modulation during elongation via its interaction with hyperphosphorylated POLR2A. Binds DNA at promoters. May also act as a transcription activator that binds to promoters. Binds to the promoters of adenovirus 12 E1A gene in case of infection, possibly leading to regulate its expression |
| Enzyme 22 Pathways |
|
| Enzyme 22 Reactions |
- S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine [RN:R03938]
|
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
197313748  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
Q9BYW2  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
SETD2_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>7695 bp
ATGAAGCAGCTGCAGCCGCAGCCGCCTCCGAAGATGGGGGATTTCTACGACCCGGAGCAC
CCGACCCCTGAAGAAGAAGAAAATGAGGCAAAGATTGAAAATGTGCAGAAAACAGGTTTC
ATCAAAGGACCAATGTTCAAAGGTGTTGCTTCTAGTCGATTTTTGCCCAAAGGCACCAAA
ACAAAAGTTAATTTGGAAGAACAGGGACGACAGAAGGTGTCATTCAGCTTCAGCCTTACA
AAGAAAACTTTGCAGAATAGGTTTCTCACTGCACTTGGCAATGAAAAGCAAAGTGATACT
CCAAACCCTCCAGCTGTACCTCTTCAGGTAGACTCGACTCCTAAAATGAAAATGGAAATT
GGTGATACCTTATCTACTGCAGAAGAATCTTCCCCACCAAAGTCAAGGGTGGAATTGGGC
AAAATTCATTTTAAGAAACATCTGCTTCATGTAACATCCAGGCCACTGCTGGCTACTACC
ACAGCAGTAGCATCTCCACCTACTCATGCAGCACCATTACCAGCAGTGATAGCAGAATCA
ACAACTGTAGACTCACCGCCCTCATCTCCGCCTCCACCGCCTCCACCTGCCCAAGCCACA
ACACTCTCATCACCAGCACCAGTAACAGAGCCAGTGGCCTTGCCACATACACCAATAACA
GTTCTAATGGCAGCACCAGTACCCTTACCAGTAGATGTAGCAGTTAGATCTCTGAAAGAA
CCACCAATTATAATTGTACCAGAATCTTTAGAAGCAGATACTAAGCAGGACACTATATCT
AATAGTTTAGAAGAACACGTAACTCAAATATTGAATGAGCAAGCAGATATTTCCTCAAAA
AAAGAAGATTCCCATATTGGGAAGGATGAAGAAATTCCAGATAGTTCTAAGATTAGTCTG
AGCTGTAAAAAAACAGGTTCTAAGAAGAAATCCTCACAATCTGAAGGCATCTTTCTTGGT
TCAGAATCTGATGAAGATTCTGTACGGACTTCTTCAAGTCAAAGATCACATGATTTAAAA
TTTTCAGCAAGCATTGAAAAGGAAAGAGATTTTAAAAAGAGCTCAGCACCTTTAAAAAGT
GAGGATCTAGGGAAACCTTCACGATCTAAAACAGACAGAGATGATAAATATTTTAGCTAT
TCAAAACTTGAAAGAGATACTCGGTATGTATCTTCCCGATGTAGATCAGAAAGAGAGCGA
CGGCGGAGCAGATCTCACTCTAGGTCTGAGAGAGGCTCTAGAACTAATTTATCCTATTCC
AGGTCAGAACGATCTCATTATTATGACTCTGATCGTCGCTACCATAGGAGCTCCCCTTAT
CGAGAGAGGACGCGCTATTCTCGGCCATACACAGATAACAGAGCACGAGAGAGTTCTGAC
TCAGAAGAAGAGTATAAGAAGACATACTCAAGGCGTACCTCATCTCATTCCTCTTCTTAC
AGAGACCTAAGGACATCATCCTATTCTAAATCTGATCGGGACTGTAAAACTGAGACCTCT
TACTTAGAGATGGAAAGAAGAGGCAAGTATTCTTCAAAACTAGAAAGAGAATCTAAAAGG
ACTTCAGAAAATGAAGCAATTAAAAGATGTTGTTCTCCCCCTAATGAACTGGGATTCCGA
CGAGGGTCATCATATTCTAAGCATGACAGTAGTGCTTCCCGTTATAAATCTACCCTTTCA
AAACCTATACCCAAGTCTGATAAATTTAAAAATTCTTTCTGTTGTACAGAATTAAATGAA
GAAATCAAACAGTCTCATTCTTTTAGTTTACAGACACCTTGTTCAAAAGGTAGTGAATTA
AGAATGATTAATAAAAATCCTGAAAGAGAAAAGGCTGGGTCTCCAGCTCCATCAAATCGA
TTAAATGATTCACCTACTTTAAAAAAGCTAGATGAATTGCCTATTTTTAAGTCCGAATTT
ATAACACATGATAGCCATGATAGTATTAAGGAATTAGACTCTTTATCTAAAGTGAAGAAT
GATCAATTAAGAAGTTTTTGTCCCATAGAATTAAATATAAATGGATCTCCTGGGGCAGAA
TCTGATTTGGCAACATTTTGCACTTCTAAAACTGATGCTGTTTTAATGACTTCTGATGAT
AGTGTGACTGGATCGGAATTATCCCCTTTGGTCAAAGCATGCATGCTTTCATCAAATGGA
TTTCAGAATATTAGTAGGTGCAAAGAAAAAGACTTGGATGATACCTGCATGCTGCATAAG
AAGTCAGAAAGCCCATTTAGAGAAACAGAACCTCTGGTGTCACCACACCAAGATAAACTC
ATGTCTATGCCAGTTATGACTGTGGATTATTCCAAAACAGTAGTTAAAGAACCAGTTGAT
ACGAGGGTTTCTTGCTGCAAAACCAAAGATTCAGACATATACTGTACTTTGAACGATAGC
AACCCTTCTTTGTGTAACTCTGAAGCTGAAAATATTGAGCCTTCAGTTATGAAGATTTCT
TCAAATAGCTTTATGAATGTGCATTTGGAATCAAAACCAGTTATATGTGATAGTAGAAAT
TTGACAGATCACTCAAAATTTGCATGTGAAGAATATAAGCAGAGCATCGGTAGCACTAGT
TCAGCTTCTGTTAATCATTTTGATGATTTATATCAACCTATTGGGAGTTCAGGTATTGCT
TCATCTCTTCAGAGTCTTCCACCAGGAATAAAGGTGGACAGTCTAACTCTCTTGAAATGC
GGAGAGAACACATCTCCAGTTCTGGATGCAGTGCTAAAGAGTAAAAAAAGTTCAGAGTTT
TTAAAGCATGCAGGGAAAGAAACAATAGTAGAAGTAGGTAGTGACCTTCCTGATTCAGGA
AAGGGATTTGCTTCCAGGGAGAACAGGCGTAATAATGGGTTATCTGGGAAATGTTTGCAA
GAGGCTCAAGAAGAAGGGAATTCCATATTGCCTGAAAGAAGAGGAAGACCAGAAATCTCT
TTAGATGAAAGAGGAGAAGGAGGACATGTGCATACTTCTGATGACTCAGAAGTTGTATTT
TCTTCTTGTGATTTGAATTTAACCATGGAAGACAGTGATGGTGTAACTTATGCATTAAAG
TGTGACAGTAGTGGTCATGCCCCAGAAATTGTGTCTACAGTTCATGAAGATTATTCTGGC
TCTTCTGAAAGTTCAAATGATGAAAGTGATTCAGAAGATACAGATTCGGATGATAGCAGT
ATTCCAAGAAACCGTCTCCAGTCTGTTGTGGTTGTGCCAAAGAATTCTACTTTGCCCATG
GAAGAAACAAGTCCTTGTTCTTCTCGGAGCAGTCAAAGTTATAGACACTATTCTGACCAT
TGGGAAGATGAGAGATTGGAGTCAAGGAGACATTTGTATGAGGAAAAATTTGAAAGTATA
GCAAGTAAAGCCTGTCCTCAAACTGATAAGTTTTTCCTTCATAAAGGAACAGAGAAGAAT
CCGGAAATTTCTTTTACACAGTCCAGTAGAAAACAAATAGATAATCGCCTGCCTGAACTT
TCTCATCCTCAGAGTGATGGGGTTGATAGTACAAGTCATACAGATGTGAAATCTGACCCT
CTGGGTCACCCAAATTCAGAGGAAACCGTGAAAGCCAAAATACCTTCTAGGCAGCAAGAA
GAGCTGCCAATTTATTCTTCTGATTTTGAAGATGTCCCAAATAAGTCTTGGCAACAGACC
ACTTTCCAAAACAGGCCAGATAGTAGACTGGGAAAAACAGAATTGAGTTTTTCTTCCTCT
TGTGAGATACCACATGTGGATGGCTTGCACTCATCAGAAGAGCTCAGAAACTTAGGTTGG
GACTTCTCTCAAGAAAAGCCTTCTACCACGTATCAGCAACCTGACAGTAGCTATGGAGCT
TGTGGTGGACACAAGTATCAGCAAAATGCAGAACAGTATGGTGGGACACGTGATTACTGG
CAAGGCAATGGTTACTGGGATCCAAGATCAGGTAGACCTCCTGGAACTGGGGTTGTGTAT
GATCGAACTCAAGGACAAGTACCAGATTCCCTAACAGATGATCGTGAAGAAGAGGAGAAT
TGGGATCAACAGGATGGATCCCATTTTTCAGACCAGTCCGATAAATTTCTTCTATCCCTT
CAGAAAGACAAGGGGTCAGTGCAAGCACCTGAAATAAGCAGCAATTCCATTAAGGACACT
TTAGCTGTGAATGAAAAGAAAGATTTTTCAAAAAACTTAGAAAAAAATGATATCAAAGAT
AGAGGGCCTCTTAAAAAAAGGAGGCAGGAAATAGAGAGTGATTCTGAAAGTGATGGTGAG
CTTCAGGACAGAAAGAAAGTTAGAGTGGAGGTAGAGCAGGGAGAGACATCAGTGCCCCCA
GGTTCAGCACTGGTTGGGCCCTCCTGTGTCATGGATGACTTCAGGGACCCACAGCGATGG
AAGGAATGTGCCAAGCAAGGGAAAATGCCATGTTACTTTGATCTTATTGAAGAAAATGTT
TATTTAACAGAAAGAAAGAAGAATAAATCTCATCGAGATATTAAGCGAATGCAGTGTGAG
TGTACACCTCTTTCTAAAGATGAAAGAGCTCAAGGTGAAATAGCATGTGGGGAAGATTGT
CTTAATCGTCTTCTCATGATTGAATGTTCTTCTCGGTGTCCAAATGGGGATTATTGTTCC
AATAGACGGTTTCAGAGAAAACAGCATGCAGATGTGGAAGTCATACTCACAGAAAAGAAA
GGCTGGGGCTTGAGAGCTGCCAAAGACCTTCCTTCGAACACCTTTGTCCTAGAATATTGT
GGAGAGGTACTCGATCATAAAGAGTTTAAAGCTCGAGTGAAGGAGTATGCACGAAACAAA
AACATCCATTACTATTTCATGGCCCTGAAGAATGATGAGATAATAGATGCCACTCAAAAA
GGAAATTGCTCTCGTTTCATGAATCACAGCTGTGAACCAAATTGTGAAACCCAAAAATGG
ACTGTGAACGGACAACTGAGGGTTGGGTTTTTTACCACCAAACTGGTTCCTTCAGGCTCA
GAGTTAACGTTTGACTATCAGTTCCAGAGATATGGAAAAGAAGCCCAGAAATGTTTCTGC
GGATCAGCCAATTGCCGGGGTTACCTGGGAGGAGAAAACAGAGTCAGCATCAGAGCAGCA
GGAGGGAAAATGAAGAAGGAACGATCTCGTAAGAAGGATTCAGTGGATGGAGAGCTAGAA
GCTCTGATGGAAAATGGTGAGGGTCTCTCTGATAAAAACCAGGTGCTCAGCTTATCCCGG
CTAATGGTTAGAATTGAAACTTTGGAGCAGAAACTTACCTGTCTGGAACTCATACAGAAC
ACACACTCACAGTCCTGCCTGAAGTCCTTTCTGGAACGTCATGGGCTGTCTTTGTTGTGG
ATCTGGATGGCAGAGCTAGGTGACGGCCGGGAAAGTAACCAGAAGCTTCAGGAAGAGATT
ATAAAGACTTTGGAACACTTGCCCATTCCTACTAAAAATATGTTGGAGGAAAGCAAAGTA
CTTCCAATTATTCAACGCTGGTCTCAGACTAAGACTGCTGTCCCTCCGTTGAGTGAAGGA
GATGGGTATTCTAGTGAGAATACATCGCGTGCTCATACACCACTCAACACACCTGATCCT
TCCACCAAGCTGAGCACAGAAGCTGACACAGACACTCCCAAGAAACTAATGTTTCGCAGA
CTGAAAATTATAAGTGAAAATAGCATGGACAGTGCAATCTCTGATGCAACCAGTGAGCTA
GAAGGCAAGGATGGCAAAGAGGATCTTGATCAATTAGAAAATGTCCCTGTAGAGGAAGAG
GAAGAATTGCAGTCACAACAGCTACTCCCACAACAGCTGCCTGAATGCAAAGTTGATAGT
GAAACCAACATAGAAGCTAGTAAGCTACCTACATCTGAACCAGAAGCTGACGCTGAAATA
GAGCCCAAAGAGAGCAACGGCACAAAACTAGAAGAACCTATTAATGAAGAAACACCATCC
CAAGATGAAGAGGAGGGTGTGTCTGATGTGGAGAGTGAAAGGAGCCAAGAACAGCCAGAT
AAAACAGTGGATATAAGTGATTTGGCCACCAAACTCCTGGACAGTTGGAAAGACCTAAAG
GAGGTATATCGAATTCCAAAGAAAAGTCAAACTGAAAAGGAAAACACAACAACTGAACGA
GGAAGGGATGCTGTTGGCTTCAGAGATCAAACACCTGCCCCGAAGACTCCTAATAGGTCA
AGAGAGAGAGACCCAGACAAGCAAACTCAAAATAAAGAGAAAAGGAAACGAAGAAGCTCC
CTCTCACCACCCTCTTCTGCCTATGAGCGGGGAACAAAAAGGCCAGATGACAGATATGAT
ACACCAACTTCTAAAAAGAAAGTACGAATTAAAGACCGCAATAAACTTTCTACAGAGGAA
CGCCGGAAGTTGTTTGAGCAAGAGGTGGCTCAACGGGAGGCTCAGAAACAACAGCAACAG
ATGCAGAACCTGGGAATGACATCACCACTGCCCTATGACTCTCTTGGTTATAATGCCCCG
CATCATCCCTTTGCTGGTTACCCACCAGGTTATCCCATGCAGGCCTATGTGGATCCCAGC
AACCCTAATGCTGGAAAGGTGCTCCTGCCCACACCCAGCATGGACCCAGTGTGTTCTCCT
GCTCCTTATGATCATGCTCAGCCCTTGGTGGGACATTCTACAGAACCCCTTTCTGCCCCT
CCACCAGTACCAGTGGTGCCACATGTGGCAGCTCCTGTGGAAGTTTCCAGTTCCCAGTAT
GTGGCCCAGAGTGATGGTGTAGTACACCAAGACTCCAGCGTTGCTGTCTTGCCAGTGCCG
GCCCCCGGCCCAGTTCAGGGACAGAATTATAGTGTTTGGGATTCAAACCAACAGTCTGTC
AGTGTACAGCAGCAGTACTCTCCTGCACAGTCTCAAGCAACCATATATTATCAAGGACAG
ACATGTCCAACAGTCTATGGTGTGACATCACCTTATTCACAGACAACTCCACCAATTGTA
CAGAGTTATGCCCAGCCAAGTCTTCAGTATATCCAGGGGCAACAGATTTTCACAGCTCAT
CCACAAGGAGTGGTGGTACAGCCAGCCGCAGCAGTGACTACAATAGTTGCACCAGGGCAG
CCTCAGCCCTTGCAGCCATCTGAAATGGTTGTGACAAATAATCTCTTGGATCTGCCGCCC
CCCTCTCCTCCCAAACCAAAAACCATTGTCTTACCTCCCAACTGGAAGACAGCTCGAGAT
CCAGAAGGGAAGATTTATTACTACCATGTGATCACAAGGCAGACTCAGTGGGATCCTCCT
ACTTGGGAAAGCCCAGGAGATGATGCCAGCCTTGAGCATGAAGCTGAGATGGACCTGGGA
ACTCCAACATATGATGAAAACCCCATGAAGGCCTCGAAAAAGCCCAAGACAGCAGAAGCA
GACACCTCCAGTGAACTAGCAAAGAAAAGCAAAGAAGTATTCAGAAAAGAGATGTCCCAG
TTCATCGTCCAGTGCCTGAACCCTTACCGGAAACCTGACTGCAAAGTGGGAAGAATTACC
ACAACTGAAGACTTTAAACATCTGGCTCGCAAGCTGACTCACGGTGTTATGAATAAGGAG
CTGAAGTACTGTAAGAATCCTGAGGACCTGGAGTGCAATGAGAATGTGAAACACAAAACC
AAGGAGTACATTAAGAAGTACATGCAGAAGTTTGGGGCTGTTTACAAACCCAAAGAGGAC
ACTGAATTAGAGTGA
|
| Enzyme 22 GenBank Gene ID |
NM_014159.6  |
| Enzyme 22 GeneCard ID |
SETD2  |
| Enzyme 22 GenAtlas ID |
SETD2  |
| Enzyme 22 HGNC ID |
HGNC:18420  |
| Enzyme 22 Chromosome Location |
3 |
| Enzyme 22 Locus |
3p21.31 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
- Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Rega S, Stiewe T, Chang DI, Pollmeier B, Esche H, Bardenheuer W, Marquitan G, Putzer BM: Identification of the full-length huntingtin- interacting protein p231HBP/HYPB as a DNA-binding factor. Mol Cell Neurosci. 2001 Jul;18(1):68-79. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Sun XJ, Wei J, Wu XY, Hu M, Wang L, Wang HH, Zhang QH, Chen SJ, Huang QH, Chen Z: Identification and characterization of a novel human histone H3 lysine 36-specific methyltransferase. J Biol Chem. 2005 Oct 21;280(42):35261-71. Epub 2005 Aug 22. [PubMed
]
- Nagase T, Kikuno R, Hattori A, Kondo Y, Okumura K, Ohara O: Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Dec 31;7(6):347-55. [PubMed
]
- Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed
]
- Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed
]
- Faber PW, Barnes GT, Srinidhi J, Chen J, Gusella JF, MacDonald ME: Huntingtin interacts with a family of WW domain proteins. Hum Mol Genet. 1998 Sep;7(9):1463-74. [PubMed
]
- Passani LA, Bedford MT, Faber PW, McGinnis KM, Sharp AH, Gusella JF, Vonsattel JP, MacDonald ME: Huntingtin's WW domain partners in Huntington's disease post-mortem brain fulfill genetic criteria for direct involvement in Huntington's disease pathogenesis. Hum Mol Genet. 2000 Sep 1;9(14):2175-82. [PubMed
]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
- Li M, Phatnani HP, Guan Z, Sage H, Greenleaf AL, Zhou P: Solution structure of the Set2-Rpb1 interacting domain of human Set2 and its interaction with the hyperphosphorylated C-terminal domain of Rpb1. Proc Natl Acad Sci U S A. 2005 Dec 6;102(49):17636-41. Epub 2005 Nov 28. [PubMed
]
|
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
14942 |
| Enzyme 23 Name |
Lysine-specific demethylase 2A |
| Enzyme 23 Synonyms |
- CXXC-type zinc finger protein 8
- F-box and leucine-rich repeat protein 11
- F-box protein FBL7
- F-box protein Lilina
- F-box/LRR-repeat protein 11
- JmjC domain-containing histone demethylation protein 1A
- [Histone-H3]-lysine-36 demethylase 1A
|
| Enzyme 23 Gene Name |
KDM2A |
| Enzyme 23 Protein Sequence |
>Lysine-specific demethylase 2A
MEPEEERIRYSQRLRGTMRRRYEDDGISDDEIEGKRTFDLEEKLHTNKYNANFVTFMEGK
DFNVEYIQRGGLRDPLIFKNSDGLGIKMPDPDFTVNDVKMCVGSRRMVDVMDVNTQKGIE
MTMAQWTRYYETPEEEREKLYNVISLEFSHTRLENMVQRPSTVDFIDWVDNMWPRHLKES
QTESTNAILEMQYPKVQKYCLMSVRGCYTDFHVDFGGTSVWYHIHQGGKVFWLIPPTAHN
LELYENWLLSGKQGDIFLGDRVSDCQRIELKQGYTFVIPSGWIHAVYTPTDTLVFGGNFL
HSFNIPMQLKIYNIEDRTRVPNKFRYPFYYEMCWYVLERYVYCITNRSHLTKEFQKESLS
MDLELNGLESGNGDEEAVDREPRRLSSRRSVLTSPVANGVNLDYDGLGKTCRSLPSLKKT
LAGDSSSDCSRGSHNGQVWDPQCAPRKDRQVHLTHFELEGLRCLVDKLESLPLHKKCVPT
GIEDEDALIADVKILLEELANSDPKLALTGVPIVQWPKRDKLKFPTRPKVRVPTIPITKP
HTMKPAPRLTPVRPAAASPIVSGARRRRVRCRKCKACVQGECGVCHYCRDMKKFGGPGRM
KQSCVLRQCLAPRLPHSVTCSLCGEVDQNEETQDFEKKLMECCICNEIVHPGCLQMDGEG
LLNEELPNCWECPKCYQEDSSEKAQKRKMEESDEEAVQAKVLRPLRSCDEPLTPPPHSPT
SMLQLIHDPVSPRGMVTRSSPGAGPSDHHSASRDERFKRRQLLRLQATERTMVREKENNP
SGKKELSEVEKAKIRGSYLTVTLQRPTKELHGTSIVPKLQAITASSANLRHSPRVLVQHC
PARTPQRGDEEGLGGEEEEEEEEEEEDDSAEEGGAARLNGRGSWAQDGDESWMQREVWMS
VFRYLSRRELCECMRVCKTWYKWCCDKRLWTKIDLSRCKAIVPQALSGIIKRQPVSLDLS
WTNISKKQLTWLVNRLPGLKDLLLAGCSWSAVSALSTSSCPLLRTLDLRWAVGIKDPQIR
DLLTPPADKPGQDNRSKLRNMTDFRLAGLDITDATLRLIIRHMPLLSRLDLSHCSHLTDQ
SSNLLTAVGSSTRYSLTELNMAGCNKLTDQTLIYLRRIANVTLIDLRGCKQITRKACEHF
ISDLSINSLYCLSDEKLIQKIS
|
| Enzyme 23 Number of Residues |
1162 |
| Enzyme 23 Molecular Weight |
132791.6 |
| Enzyme 23 Theoretical pI |
7.61 |
| Enzyme 23 GO Classification |
| Function |
- DNA binding
- binding
- cation binding
- ion binding
- metal ion binding
- nucleic acid binding
- protein binding
- transition metal ion binding
- zinc ion binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 23 General Function |
Involved in DNA binding |
| Enzyme 23 Specific Function |
Histone demethylase that specifically demethylates 'Lys- 36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys- 36'. May also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. Required to maintain the heterochromatic state. Associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. Required to sustain centromeric integrity and genomic stability, particularly during mitosis |
| Enzyme 23 Pathways |
Not Available |
| Enzyme 23 Reactions |
- (1) protein N6,N6-dimethyl-L-lysine + 2-oxoglutarate + O2 = protein N6-methyl-L-lysine + succinate + formaldehyde + CO2
- (2) protein N6-methyl-L-lysine + 2-oxoglutarate + O2 = protein L-lysine + succinate + formaldehyde + CO2
|
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
16306580  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
Q9Y2K7  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
KDM2A_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>3489 bp
ATGGAACCCGAAGAAGAAAGGATTCGTTACAGCCAGAGATTGCGTGGTACCATGCGACGA
CGCTATGAAGATGATGGCATTTCAGATGATGAAATTGAAGGAAAAAGAACTTTTGACTTG
GAAGAGAAACTGCACACCAACAAATATAATGCCAATTTTGTTACTTTTATGGAAGGAAAA
GATTTTAATGTAGAGTATATTCAGCGGGGTGGCTTGAGAGATCCTCTGATTTTCAAGAAT
TCTGATGGACTCGGAATAAAAATGCCGGATCCAGACTTCACTGTGAATGATGTCAAAATG
TGTGTGGGGAGTCGTCGCATGGTGGATGTCATGGACGTGAACACACAGAAAGGCATTGAA
ATGACCATGGCTCAGTGGACACGCTACTATGAGACCCCAGAGGAGGAGCGAGAGAAACTC
TATAATGTCATCAGCCTCGAGTTTAGCCACACCAGGCTGGAGAATATGGTGCAGAGGCCC
TCCACGGTGGATTTCATTGACTGGGTAGACAACATGTGGCCAAGGCACTTGAAGGAAAGC
CAGACTGAATCAACAAATGCCATCTTGGAGATGCAGTACCCTAAAGTGCAGAAGTACTGT
CTAATGAGTGTTCGAGGCTGCTATACTGACTTCCATGTGGACTTTGGTGGTACCTCTGTT
TGGTATCACATCCATCAAGGGGGAAAGGTCTTCTGGCTCATCCCCCCTACAGCCCACAAC
CTGGAGCTGTACGAGAATTGGCTGCTGTCAGGGAAACAGGGAGACATCTTTCTGGGTGAC
CGGGTATCAGATTGTCAGCGCATTGAGCTCAAGCAGGGCTATACCTTCGTCATTCCCTCA
GGCTGGATTCATGCTGTGTATACTCCTACAGACACATTAGTGTTTGGGGGCAATTTTTTG
CATAGCTTCAACATCCCTATGCAGTTAAAAATATACAACATTGAAGATCGGACACGGGTT
CCAAATAAGTTTCGCTATCCATTCTACTATGAGATGTGTTGGTATGTGTTGGAGCGCTAT
GTGTACTGCATAACCAACCGTTCCCACCTAACTAAGGAATTTCAGAAAGAGTCCCTCAGC
ATGGATTTGGAGTTAAATGGGTTGGAGTCTGGGAATGGGGATGAGGAAGCAGTGGATCGA
GAACCCCGACGCTTGAGCAGCAGGCGTTCTGTCCTCACTAGCCCTGTAGCGAATGGAGTC
AACCTGGATTATGATGGACTGGGCAAAACCTGCCGAAGTCTTCCAAGTCTGAAGAAAACT
TTGGCTGGGGACTCATCTTCTGACTGTAGCCGGGGCTCCCACAATGGACAAGTGTGGGAT
CCCCAGTGTGCTCCCCGAAAGGACAGGCAAGTGCATCTGACCCATTTTGAGCTTGAAGGC
CTTCGCTGCCTTGTAGATAAGTTGGAGTCTCTGCCACTGCACAAGAAATGTGTCCCCACA
GGGATAGAAGATGAAGATGCTCTCATTGCTGATGTAAAGATTTTGCTGGAGGAGCTTGCC
AACAGCGATCCCAAGTTAGCCCTCACTGGAGTTCCTATAGTACAGTGGCCAAAAAGGGAT
AAGCTTAAATTCCCCACTCGGCCAAAGGTGCGGGTTCCTACCATCCCCATTACGAAGCCT
CACACTATGAAACCAGCTCCACGGTTAACACCTGTGAGGCCAGCTGCTGCCTCCCCGATT
GTGTCAGGAGCCAGACGGAGACGAGTGCGATGTCGAAAATGCAAAGCCTGTGTGCAAGGA
GAGTGTGGTGTTTGCCACTACTGCAGAGACATGAAGAAGTTTGGGGGGCCTGGACGCATG
AAGCAGTCCTGTGTCCTCCGACAGTGCTTGGCACCCAGACTGCCTCACTCAGTCACATGT
TCCCTCTGTGGAGAGGTGGATCAGAATGAAGAGACACAAGACTTTGAGAAGAAACTCATG
GAATGCTGTATCTGCAATGAGATTGTTCATCCTGGCTGCCTCCAGATGGACGGAGAGGGG
TTGCTTAACGAAGAATTGCCAAATTGCTGGGAATGTCCAAAGTGCTACCAGGAGGACAGC
TCGGAGAAAGCCCAGAAGCGGAAAATGGAAGAGAGTGACGAAGAAGCTGTGCAAGCCAAA
GTCCTGCGGCCCCTGCGGAGCTGCGATGAGCCTCTCACGCCCCCGCCTCATTCACCCACT
TCCATGCTGCAGCTCATCCATGACCCGGTTTCCCCCCGGGGTATGGTGACTCGGTCATCC
CCTGGGGCTGGCCCCAGCGACCACCACAGTGCCAGCCGCGATGAGCGCTTCAAACGGCGG
CAGTTGCTGCGGCTGCAGGCCACAGAGCGCACCATGGTACGGGAAAAGGAGAACAATCCC
AGCGGCAAAAAGGAGCTGTCTGAAGTTGAGAAAGCCAAGATCCGGGGATCGTACCTCACT
GTCACGCTACAGAGGCCCACCAAAGAGCTCCACGGGACATCCATTGTGCCCAAGCTGCAG
GCCATCACGGCCTCCTCTGCCAACCTTCGCCATTCCCCCCGTGTGCTAGTGCAGCACTGC
CCAGCCCGAACCCCCCAGCGTGGGGATGAGGAGGGGCTGGGGGGAGAGGAGGAGGAAGAG
GAGGAGGAGGAGGAGGAAGATGACAGTGCAGAGGAGGGGGGTGCAGCCAGGCTGAATGGC
CGGGGCAGTTGGGCTCAGGATGGAGACGAAAGCTGGATGCAGCGGGAGGTCTGGATGTCT
GTCTTCCGCTACCTCAGCCGCAGAGAACTTTGTGAATGTATGCGAGTGTGCAAGACGTGG
TATAAATGGTGCTGCGACAAGAGACTTTGGACAAAAATTGACTTGAGTAGGTGTAAGGCC
ATTGTGCCCCAGGCCCTCAGTGGCATCATCAAGAGGCAGCCAGTCAGCCTTGACCTCAGT
TGGACCAACATCTCTAAAAAGCAACTGACATGGCTCGTCAATAGGCTGCCAGGACTGAAA
GACCTCCTCCTAGCAGGCTGCTCCTGGTCTGCAGTCTCTGCCCTCAGCACCTCCAGCTGC
CCCCTTCTCAGGACCCTTGATCTTCGGTGGGCAGTAGGAATCAAGGACCCTCAAATTCGG
GACTTGCTTACTCCACCGGCTGATAAACCAGGTCAGGACAATCGCAGCAAGCTCCGGAAC
ATGACCGACTTCCGGCTGGCAGGCCTTGACATCACAGATGCCACGCTTCGCCTCATAATT
CGCCACATGCCCCTCCTGTCTCGACTCGACCTCAGTCACTGCAGCCACCTTACAGATCAG
TCCTCCAATCTACTCACTGCTGTCGGGTCTTCCACTCGCTACTCTCTCACAGAGCTCAAT
ATGGCAGGTTGCAATAAATTGACAGACCAGACCCTGATCTACCTACGGCGCATTGCCAAC
GTCACCTTGATCGACCTTCGAGGATGCAAGCAGATCACTCGAAAAGCCTGCGAGCACTTC
ATCTCAGACTTGTCCATCAACAGCCTCTACTGCCTGTCTGACGAGAAGCTGATACAGAAG
ATCAGCTAA
|
| Enzyme 23 GenBank Gene ID |
NM_012308.2  |
| Enzyme 23 GeneCard ID |
KDM2A  |
| Enzyme 23 GenAtlas ID |
KDM2A  |
| Enzyme 23 HGNC ID |
HGNC:13606  |
| Enzyme 23 Chromosome Location |
1 |
| Enzyme 23 Locus |
11q13.2 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
- Ilyin GP, Rialland M, Pigeon C, Guguen-Guillouzo C: cDNA cloning and expression analysis of new members of the mammalian F-box protein family. Genomics. 2000 Jul 1;67(1):40-7. [PubMed
]
- Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Feb 26;6(1):63-70. [PubMed
]
- Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed
]
- Hattori A, Okumura K, Nagase T, Kikuno R, Hirosawa M, Ohara O: Characterization of long cDNA clones from human adult spleen. DNA Res. 2000 Dec 31;7(6):357-66. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Tsukada Y, Fang J, Erdjument-Bromage H, Warren ME, Borchers CH, Tempst P, Zhang Y: Histone demethylation by a family of JmjC domain-containing proteins. Nature. 2006 Feb 16;439(7078):811-6. Epub 2005 Dec 18. [PubMed
]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed
]
- Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed
]
- Frescas D, Guardavaccaro D, Kuchay SM, Kato H, Poleshko A, Basrur V, Elenitoba-Johnson KS, Katz RA, Pagano M: KDM2A represses transcription of centromeric satellite repeats and maintains the heterochromatic state. Cell Cycle. 2008 Nov 15;7(22):3539-47. Epub 2008 Nov 24. [PubMed
]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed
]
- Carrascal M, Ovelleiro D, Casas V, Gay M, Abian J: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment. J Proteome Res. 2008 Dec;7(12):5167-76. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
- Blackledge NP, Zhou JC, Tolstorukov MY, Farcas AM, Park PJ, Klose RJ: CpG islands recruit a histone H3 lysine 36 demethylase. Mol Cell. 2010 Apr 23;38(2):179-90. [PubMed
]
|
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
14943 |
| Enzyme 24 Name |
Lysine-specific demethylase 2B |
| Enzyme 24 Synonyms |
- CXXC-type zinc finger protein 2
- F-box and leucine-rich repeat protein 10
- F-box protein FBL10
- F-box/LRR-repeat protein 10
- JmjC domain-containing histone demethylation protein 1B
- Jumonji domain-containing EMSY-interactor methyltransferase motif protein
- Protein JEMMA
- Protein-containing CXXC domain 2
- [Histone-H3]-lysine-36 demethylase 1B
|
| Enzyme 24 Gene Name |
KDM2B |
| Enzyme 24 Protein Sequence |
>Lysine-specific demethylase 2B
MAGPQMGGSAEDHPPRKRHAAEKQKKKTVIYTKCFEFESATQRPIDRQRYDENEDLSDVE
EIVSVRGFSLEEKLRSQLYQGDFVHAMEGKDFNYEYVQREALRVPLIFREKDGLGIKMPD
PDFTVRDVKLLVGSRRLVDVMDVNTQKGTEMSMSQFVRYYETPEAQRDKLYNVISLEFSH
TKLEHLVKRPTVVDLVDWVDNMWPQHLKEKQTEATNAIAEMKYPKVKKYCLMSVKGCFTD
FHIDFGGTSVWYHVFRGGKIFWLIPPTLHNLALYEEWVLSGKQSDIFLGDRVERCQRIEL
KQGYTFFIPSGWIHAVYTPVDSLVFGGNILHSFNVPMQLRIYEIEDRTRVQPKFRYPFYY
EMCWYVLERYVYCVTQRSHLTQEYQRESMLIDAPRKPSIDGFSSDSWLEMEEEACDQQPQ
EEEEKDEEGEGRDRAPKPPTDGSTSPTSTPSEDQEALGKKPKAPALRFLKRTLSNESEES
VKSTTLAVDYPKTPTGSPATEVSAKWTHLTEFELKGLKALVEKLESLPENKKCVPEGIED
PQALLEGVKNVLKEHADDDPSLAITGVPVVTWPKKTPKNRAVGRPKGKLGPASAVKLAAN
RTTAGARRRRTRCRKCEACLRTECGECHFCKDMKKFGGPGRMKQSCIMRQCIAPVLPHTA
VCLVCGEAGKEDTVEEEEGKFNLMLMECSICNEIIHPGCLKIKESEGVVNDELPNCWECP
KCNHAGKTGKQKRGPGFKYASNLPGSLLKEQKMNRDNKEGQEPAKRRSECEEAPRRRSDE
HSKKVPPDGLLRRKSDDVHLRKKRKYEKPQELSGRKRASSLQTSPGSSSHLSPRPPLGSS
LSPWWRSSLTYFQQQLKPGKEDKLFRKKRRSWKNAEDRMALANKPLRRFKQEPEDELPEA
PPKTRESDHSRSSSPTAGPSTEGAEGPEEKKKVKMRRKRRLPNKELSRELSKELNHEIQR
TENSLANENQQPIKSEPESEGEEPKRPPGICERPHRFSKGLNGTPRELRHQLGPSLRSPP
RVISRPPPSVSPPKCIQMERHVIRPPPISPPPDSLPLDDGAAHVMHREVWMAVFSYLSHQ
DLCVCMRVCRTWNRWCCDKRLWTRIDLNHCKSITPLMLSGIIRRQPVSLDLSWTNISKKQ
LSWLINRLPGLRDLVLSGCSWIAVSALCSSSCPLLRTLDVQWVEGLKDAQMRDLLSPPTD
NRPGQMDNRSKLRNIVELRLAGLDITDASLRLIIRHMPLLSKLHLSYCNHVTDQSINLLT
AVGTTTRDSLTEINLSDCNKVTDQCLSFFKRCGNICHIDLRYCKQVTKEGCEQFIAEMSV
SVQFGQVEEKLLQKLS
|
| Enzyme 24 Number of Residues |
1336 |
| Enzyme 24 Molecular Weight |
152613.4 |
| Enzyme 24 Theoretical pI |
8.68 |
| Enzyme 24 GO Classification |
| Function |
- DNA binding
- binding
- cation binding
- ion binding
- metal ion binding
- nucleic acid binding
- protein binding
- transition metal ion binding
- zinc ion binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 24 General Function |
Involved in DNA binding |
| Enzyme 24 Specific Function |
Histone demethylase that demethylates 'Lys-4' and 'Lys- 36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' and dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. Preferentially binds the transcribed region of ribosomal RNA and represses the transcription of ribosomal RNA genes which inhibits cell growth and proliferation. May also serve as a substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex |
| Enzyme 24 Pathways |
Not Available |
| Enzyme 24 Reactions |
- (1) protein N6,N6-dimethyl-L-lysine + 2-oxoglutarate + O2 = protein N6-methyl-L-lysine + succinate + formaldehyde + CO2
- (2) protein N6-methyl-L-lysine + 2-oxoglutarate + O2 = protein L-lysine + succinate + formaldehyde + CO2
|
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
54112382  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
Q8NHM5  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
KDM2B_HUMAN  |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>4011 bp
ATGGCGGGTCCGCAAATGGGGGGATCTGCAGAGGATCACCCCCCACGAAAAAGACATGCA
GCAGAAAAGCAAAAAAAGAAAACAGTTATATATACAAAATGCTTTGAATTTGAGTCGGCC
ACACAGCGCCCGATTGACCGCCAGCGATACGACGAGAACGAGGACTTGTCGGACGTGGAG
GAGATCGTCAGCGTCCGCGGCTTCAGCCTGGAGGAGAAGCTTCGCAGCCAGCTGTACCAG
GGGGACTTCGTGCACGCCATGGAGGGCAAAGATTTCAACTATGAGTACGTACAGAGAGAA
GCTCTCAGGGTTCCCCTGATATTTCGAGAAAAGGATGGACTGGGAATTAAGATGCCTGAC
CCTGATTTCACAGTCCGAGACGTCAAACTCCTAGTGGGGAGCCGGCGGCTTGTGGACGTG
ATGGATGTGAACACCCAGAAGGGCACGGAGATGAGCATGTCCCAGTTTGTGCGTTACTAC
GAGACGCCCGAGGCCCAGCGGGACAAGCTGTACAACGTCATCAGCCTAGAGTTCAGCCAC
ACCAAGCTGGAGCACTTGGTCAAGCGTCCGACTGTGGTAGACCTGGTGGACTGGGTGGAC
AACATGTGGCCCCAGCATCTGAAGGAGAAGCAGACAGAAGCCACGAACGCCATTGCAGAG
ATGAAGTACCCGAAAGTGAAAAAGTACTGTCTGATGAGCGTGAAAGGTTGTTTCACCGAC
TTCCACATCGACTTTGGAGGCACTTCCGTTTGGTACCATGTTTTCCGGGGTGGGAAGATT
TTTTGGCTGATTCCTCCAACGCTGCACAATTTGGCGCTGTACGAGGAGTGGGTGCTGTCA
GGCAAACAGAGTGACATCTTTCTGGGAGACCGTGTGGAACGATGCCAAAGAATTGAGCTG
AAGCAGGGCTACACATTTTTCATCCCTTCCGGTTGGATCCATGCCGTCTACACCCCTGTA
GACTCTTTGGTGTTCGGCGGAAACATCCTGCACAGCTTTAACGTGCCCATGCAGCTGCGG
ATCTACGAGATCGAGGACAGGACGCGGGTGCAGCCCAAATTCCGTTACCCCTTCTACTAT
GAGATGTGCTGGTATGTCCTGGAGAGATACGTGTACTGTGTGACCCAGCGCTCCCACCTC
ACTCAGGAATACCAGAGGGAGTCGATGCTTATTGATGCCCCGAGGAAGCCCAGCATAGAC
GGCTTCTCTTCGGATTCCTGGCTGGAGATGGAGGAGGAGGCCTGTGATCAGCAGCCTCAG
GAGGAGGAGGAGAAGGACGAGGAGGGCGAGGGCAGGGACAGGGCACCCAAACCGCCCACC
GATGGCTCCACTTCACCCACCAGCACGCCCTCTGAGGACCAGGAGGCCCTCGGGAAGAAG
CCCAAAGCACCTGCCCTGCGATTCCTCAAAAGGACTTTGTCTAATGAGTCGGAGGAAAGT
GTGAAGTCCACCACATTGGCCGTAGACTACCCCAAGACCCCCACCGGCTCTCCCGCCACG
GAGGTCTCTGCCAAATGGACCCATCTCACTGAGTTTGAACTGAAGGGCCTGAAAGCTCTG
GTGGAGAAACTGGAATCCCTCCCGGAGAACAAGAAGTGTGTCCCCGAGGGCATCGAGGAC
CCCCAGGCACTCCTGGAGGGTGTGAAGAACGTCCTGAAGGAGCACGCAGATGATGACCCT
AGTCTGGCCATCACTGGGGTCCCTGTGGTGACTTGGCCAAAGAAGACTCCAAAGAACCGG
GCTGTGGGTCGGCCCAAGGGGAAGCTGGGCCCGGCCTCCGCGGTGAAGTTGGCCGCCAAC
CGGACAACGGCAGGAGCTCGGCGGCGCCGGACGCGATGCCGCAAGTGCGAGGCCTGCCTG
CGGACCGAGTGCGGAGAGTGCCACTTCTGCAAGGACATGAAGAAGTTCGGGGGCCCCGGG
CGCATGAAGCAGAGCTGCATCATGCGGCAGTGCATCGCGCCAGTGCTGCCCCACACCGCC
GTGTGCCTTGTGTGTGGCGAGGCGGGGAAGGAAGACACGGTGGAAGAGGAGGAAGGCAAG
TTTAACCTCATGCTCATGGAGTGCTCCATCTGCAATGAAATCATCCACCCTGGATGCCTT
AAGATTAAGGAGTCAGAGGGTGTGGTCAACGACGAGCTTCCAAACTGCTGGGAGTGTCCG
AAGTGTAACCACGCCGGCAAGACCGGGAAACAAAAGCGTGGCCCTGGCTTTAAGTACGCC
TCCAACCTGCCCGGCTCCCTGCTCAAGGAGCAGAAGATGAACCGGGACAACAAGGAAGGG
CAGGAACCTGCCAAGCGGAGGAGTGAGTGTGAGGAGGCGCCCCGGCGCAGGTCGGATGAG
CACTCGAAGAAGGTGCCGCCGGACGGCCTTCTGCGCAGAAAGTCTGACGACGTGCACCTG
AGGAAGAAGCGGAAATACGAGAAGCCCCAGGAGCTGAGTGGACGCAAGCGGGCCTCATCG
CTTCAAACGTCCCCCGGTTCCTCCTCTCACCTCTCGCCGAGGCCCCCTCTAGGCAGCAGC
CTCAGCCCCTGGTGGAGATCCAGTCTCACTTACTTCCAGCAGCAGCTCAAACCTGGCAAA
GAAGATAAGCTTTTCAGGAAAAAGCGGCGGTCCTGGAAGAACGCCGAGGACCGCATGGCG
CTGGCCAACAAGCCCCTCCGGCGCTTCAAGCAGGAACCCGAGGACGAACTGCCCGAGGCG
CCCCCCAAGACCAGGGAGAGCGACCACTCCCGCTCCAGCTCCCCCACCGCGGGACCCAGC
ACCGAAGGGGCCGAGGGCCCGGAGGAGAAGAAGAAGGTGAAGATGCGCCGGAAGCGGCGG
CTTCCCAACAAGGAGCTGAGCAGGGAGCTGAGCAAGGAGCTCAACCACGAGATCCAGAGG
ACGGAGAACAGCCTGGCCAACGAGAACCAGCAGCCCATCAAGTCGGAGCCTGAGAGCGAG
GGCGAGGAGCCCAAGCGGCCCCCGGGCATCTGCGAGCGTCCCCACCGCTTCAGCAAGGGG
CTCAACGGCACCCCCCGGGAGCTGCGGCACCAGCTGGGGCCCAGCCTGCGCAGCCCGCCC
CGTGTCATCTCCCGGCCCCCACCCTCCGTGTCCCCGCCCAAGTGTATCCAGATGGAGCGC
CATGTGATCCGGCCACCCCCCATCAGCCCCCCGCCTGACTCGCTACCCCTGGACGATGGG
GCAGCCCACGTCATGCACAGGGAGGTGTGGATGGCCGTCTTCAGCTACCTCAGCCACCAA
GACCTGTGTGTGTGCATGCGGGTCTGCAGGACCTGGAACCGCTGGTGCTGCGATAAGCGG
TTGTGGACCCGCATTGACCTGAACCACTGCAAGTCTATCACACCCCTGATGCTGAGTGGC
ATCATCCGGCGACAGCCCGTCTCCCTCGACCTCAGCTGGACCAATATCTCCAAGAAGCAG
CTGAGCTGGCTCATCAACCGGCTGCCTGGGCTCCGGGACTTGGTGCTGTCAGGCTGCTCA
TGGATCGCGGTCTCGGCCCTTTGCAGCTCCAGTTGTCCGCTGCTCCGGACCCTGGATGTC
CAGTGGGTGGAGGGACTAAAGGATGCCCAGATGCGGGATCTCCTGTCCCCGCCCACAGAC
AACAGGCCAGGTCAGATGGACAATCGGAGCAAGCTCCGGAACATCGTGGAGCTGCGCCTG
GCAGGCCTGGACATCACAGATGCCTCCCTGCGGCTCATCATCCGCCACATGCCCCTGCTC
TCCAAGCTCCACCTCAGTTACTGTAACCACGTCACCGACCAGTCTATCAACCTGCTCACT
GCTGTTGGCACCACCACCCGAGACTCCTTAACCGAGATCAACCTGTCTGACTGCAATAAG
GTCACTGATCAGTGCCTGTCCTTCTTCAAACGCTGTGGAAACATCTGTCATATTGACCTG
AGGTACTGCAAGCAAGTCACCAAGGAAGGCTGTGAGCAGTTCATAGCCGAGATGTCTGTG
AGTGTCCAGTTTGGGCAAGTAGAAGAAAAACTCCTGCAAAAACTGAGTTAG
|
| Enzyme 24 GenBank Gene ID |
NM_032590.4  |
| Enzyme 24 GeneCard ID |
KDM2B  |
| Enzyme 24 GenAtlas ID |
KDM2B  |
| Enzyme 24 HGNC ID |
HGNC:13610  |
| Enzyme 24 Chromosome Location |
1 |
| Enzyme 24 Locus |
12q24.31 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed
]
- Tsukada Y, Fang J, Erdjument-Bromage H, Warren ME, Borchers CH, Tempst P, Zhang Y: Histone demethylation by a family of JmjC domain-containing proteins. Nature. 2006 Feb 16;439(7078):811-6. Epub 2005 Dec 18. [PubMed
]
- Frescas D, Guardavaccaro D, Bassermann F, Koyama-Nasu R, Pagano M: JHDM1B/FBXL10 is a nucleolar protein that represses transcription of ribosomal RNA genes. Nature. 2007 Nov 8;450(7167):309-13. [PubMed
]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
|
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
15077 |
| Enzyme 25 Name |
Uncharacterized protein KARS (Lysyl-tRNA synthetase, isoform CRA_d) |
| Enzyme 25 Synonyms |
Not Available |
| Enzyme 25 Gene Name |
KARS |
| Enzyme 25 Protein Sequence |
>Uncharacterized protein KARS (Lysyl-tRNA synthetase, isoform CRA_d)
MLTQAAVRLVRGSLRKTSWAEWGHRELRLGQLAPFTAPHKDKSFSDQRSELKRRLKAEKK
VAEKEAKQKELSEKQLSQATAAATNHTTDNGVGPEEESVDPNQYYKIRSQAIHQLKVNGE
DPYPHKFHVDISLTDFIQKYSHLQPGDHLTDITLKVAGRIHAKRASGGKLIFYDLRGEGV
KLQVMANSRNYKSEEEFIHINNKLRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHM
LPHLHFGLKDKETRYRQRYLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMN
IIPGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHN
PEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYHPDGPEGQAYDVDFTPPFR
RINMVEELEKALGMKLPETNLFETEETRKILDDICVAKAVECPPPRTTARLLDKLVGEFL
EVTCINPTFICDHPQIMSPLAKWHRSKEGLTERFELFVMKKEICNAYTELNDPMRQRQLF
EEQAKAKAAGDDEAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFPA
MKPEDKKENVATTDTLESTTVGTSV
|
| Enzyme 25 Number of Residues |
625 |
| Enzyme 25 Molecular Weight |
71498 |
| Enzyme 25 Theoretical pI |
6.80 |
| Enzyme 25 GO Classification |
Not Available |
| Enzyme 25 General Function |
Translation, ribosomal structure and biogenesis |
| Enzyme 25 Specific Function |
Not Available |
| Enzyme 25 Pathways |
Not Available |
| Enzyme 25 Reactions |
Not Available |
| Enzyme 25 Pfam Domain Function |
Not Available |
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
Not Available |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
A8MSK1  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
A8MSK1_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
Not Available |
| Enzyme 25 GenBank Gene ID |
AC025287  |
| Enzyme 25 GeneCard ID |
A8MSK1  |
| Enzyme 25 GenAtlas ID |
KARS  |
| Enzyme 25 HGNC ID |
HGNC:6215  |
| Enzyme 25 Chromosome Location |
16 |
| Enzyme 25 Locus |
16q23-q24 |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
Not Available |
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
16426 |
| Enzyme 26 Name |
cDNA, FLJ93758, Homo sapiens biotinidase (BTD), mRNA (Biotinidase, isoform CRA_a) |
| Enzyme 26 Synonyms |
Not Available |
| Enzyme 26 Gene Name |
BTD |
| Enzyme 26 Protein Sequence |
>cDNA, FLJ93758, Homo sapiens biotinidase (BTD), mRNA (Biotinidase, isoform CRA_a)
MAHAHIQGGRRAKSRFVVCIMSGARSKLALFLCGCYVVALGAHTGEESVADHHEAEYYVA
AVYEHPSILSLNPLALISRQEALELMNQNLDIYEQQVMTAAQKDVQIIVFPEDGIHGFNF
TRTSIYPFLDFMPSPQVVRWNPCLEPHRFNDTEVLQRLSCMAIRGDMFLVANLGTKEPCH
SSDPRCPKDGRYQFNTNVVFSNNGTLVDRYRKHNLYFEAAFDVPLKVDLITFDTPFAGRF
GIFTCFDILFFDPAIRVLRDYKVKHVVYPTAWMNQLPLLAAIEIQKAFAVAFGINVLAAN
VHHPVLGMTGSGIHTPLESFWYHDMENPKSHLIIAQVAKNPVGLIGAENATGETDPSHSK
FLKILSGDPYCEKDAQEVHCDEATKWNVNAPPTFHSEMMYDNFTLVPVWGKEGYLHVCSN
GLCCYLLYERPTLSKELYALGVFDGLHTVHGTYYIQVCALVRCGGLGFDTCGQEITEATG
IFEFHLWGNFSTSYIFPLFLTSGMTLEVPDQLGWENDHYFLRKSRLSSGLVTAALYGRLY
ERD
|
| Enzyme 26 Number of Residues |
543 |
| Enzyme 26 Molecular Weight |
61134 |
| Enzyme 26 Theoretical pI |
6.22 |
| Enzyme 26 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
|
| Process |
- metabolism
- nitrogen compound metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 26 General Function |
Not Available |
| Enzyme 26 Specific Function |
Not Available |
| Enzyme 26 Pathways |
Not Available |
| Enzyme 26 Reactions |
Not Available |
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
Not Available |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
B2R865  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
B2R865_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
Not Available |
| Enzyme 26 GenBank Gene ID |
AK313252  |
| Enzyme 26 GeneCard ID |
B2R865  |
| Enzyme 26 GenAtlas ID |
Not Available |
| Enzyme 26 HGNC ID |
Not Available |
| Enzyme 26 Chromosome Location |
Not Available |
| Enzyme 26 Locus |
Not Available |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
Not Available |
| Enzyme 26 Metabolite References |
Not Available |