|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5603 |
| Enzyme 1 Name |
Glycogen debranching enzyme |
| Enzyme 1 Synonyms |
- Glycogen debrancher
- 4-alpha-glucanotransferase
- Oligo-1,4-1,4-glucantransferase
- Amylo-alpha-1,6-glucosidase
- Amylo-1,6-glucosidase
- Dextrin 6-alpha-D-glucosidase
|
| Enzyme 1 Gene Name |
AGL |
| Enzyme 1 Protein Sequence |
>Glycogen debranching enzyme
MGHSKQIRILLLNEMEKLEKTLFRLEQGYELQFRLGPTLQGKAVTVYTNYPFPGETFNRE
KFRSLDWENPTEREDDSDKYCKLNLQQSGSFQYYFLQGNEKSGGGYIVVDPILRVGADNH
VLPLDCVTLQTFLAKCLGPFDEWESRLRVAKESGYNMIHFTPLQTLGLSRSCYSLANQLE
LNPDFSRPNRKYTWNDVGQLVEKLKKEWNVICITDVVYNHTAANSKWIQEHPECAYNLVN
SPHLKPAWVLDRALWRFSCDVAEGKYKEKGIPALIENDHHMNSIRKIIWEDIFPKLKLWE
FFQVDVNKAVEQFRRLLTQENRRVTKSDPNQHLTIIQDPEYRRFGCTVDMNIALTTFIPH
DKGPAAIEECCNWFHKRMEELNSEKHRLINYHQEQAVNCLLGNVFYERLAGHGPKLGPVT
RKHPLVTRYFTFPFEEIDFSMEESMIHLPNKACFLMAHNGWVMGDDPLRNFAEPGSEVYL
RRELICWGDSVKLRYGNKPEDCPYLWAHMKKYTEITATYFQGVRLDNCHSTPLHVAEYML
DAARNLQPNLYVVAELFTGSEDLDNVFVTRLGISSLIREAMSAYNSHEEGRLVYRYGGEP
VGSFVQPCLRPLMPAIAHALFMDITHDNECPIVHRSAYDALPSTTIVSMACCASGSTRGY
DELVPHQISVVSEERFYTKWNPEALPSNTGEVNFQSGIIAARCAISKLHQELGAKGFIQV
YVDQVDEDIVAVTRHSPSIHQSVVAVSRTAFRNPKTSFYSKEVPQMCIPGKIEEVVLEAR
TIERNTKPYRKDENSINGTPDITVEIREHIQLNESKIVKQAGVATKGPNEYIQEIEFENL
SPGSVIIFRVSLDPHAQVAVGILRNHLTQFSPHFKSGSLAVDNADPILKIPFASLASRLT
LAELNQILYRCESEEKEDGGGCYDIPNWSALKYAGLQGLMSVLAEIRPKNDLGHPFCNNL
RSGDWMIDYVSNRLISRSGTIAEVGKWLQAMFFYLKQIPRYLIPCYFDAILIGAYTTLLD
TAWKQMSSFVQNGSTFVKHLSLGSVQLCGVGKFPSLPILSPALMDVPYRLNEITKEKEQC
CVSLAAGLPHFSSGIFRCWGRDTFIALRGILLITGRYVEARNIILAFAGTLRHGLIPNLL
GEGIYARYNCRDAVWWWLQCIQDYCKMVPNGLDILKCPVSRMYPTDDSAPLPAGTLDQPL
FEVIQEAMQKHMQGIQFRERNAGPQIDRNMKDEGFNITAGVDEETGFVYGGNRFNCGTWM
DKMGESDRARNRGIPATPRDGSAVEIVGLSKSAVRWLLELSKKNIFPYHEVTVKRHGKAI
KVSYDEWNRKIQDNFEKLFHVSEDPSDLNEKHPNLVHKRGIYKDSYGASSPWCDYQLRPN
FTIAMVVAPELFTTEKAWKALEIAEKKLLGPLGMKTLDPDDMVYCGIYDNALDNDNYNLA
KGFNYHQGPEWLWPIGYFLRAKLYFSRLMGPETTAKTIVLVKNVLSRHYVHLERSPWKGL
PELTNENAQYCPFSCETQAWSIATILETLYDL
|
| Enzyme 1 Number of Residues |
1532 |
| Enzyme 1 Molecular Weight |
174762.3 |
| Enzyme 1 Theoretical pI |
6.74 |
| Enzyme 1 GO Classification |
| Function |
- 4-alpha-glucanotransferase activity
- amylo-alpha-1,6-glucosidase activity
- binding
- catalytic activity
- cation binding
- glycogen debranching enzyme activity
- ion binding
|
| Process |
- alcohol metabolic process
- carbohydrate metabolic process
- glucose metabolic process
- glycogen biosynthetic process
- glycogen metabolic process
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- primary metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in catalytic activity |
| Enzyme 1 Specific Function |
Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4- alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6- glucosidase in glycogen degradation |
| Enzyme 1 Pathways |
- Starch and Sucrose Metabolism (map00500
)
|
| Enzyme 1 Reactions |
- Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin ALL_REAC (other) R02109 R06158(G)
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
6580116  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P35573  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
GDE_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>4599 bp
ATGGGACACAGTAAACAGATTCGAATTTTACTTCTGAACGAAATGGAGAAACTGGAAAAG
ACCCTCTTCAGACTTGAACAAGGGTATGAGCTACAGTTCCGATTAGGCCCAACTTTACAG
GGAAAAGCAGTTACCGTGTATACAAATTACCCATTTCCTGGAGAAACATTTAATAGAGAA
AAATTCCGTTCTCTGGATTGGGAAAATCCAACAGAAAGAGAAGATGATTCTGATAAATAC
TGTAAACTTAATCTGCAACAATCTGGTTCATTTCAGTATTATTTCCTTCAAGGAAATGAG
AAAAGTGGTGGAGGTTACATAGTTGTGGACCCCATTTTACGTGTTGGTGCTGATAATCAT
GTGCTACCCTTGGACTGTGTTACTCTTCAGACATTTTTAGCTAAGTGTTTGGGACCTTTT
GATGAATGGGAAAGCAGACTTAGGGTTGCAAAAGAATCAGGCTACAACATGATTCATTTT
ACCCCATTGCAGACTCTTGGACTATCTAGGTCATGCTACTCCCTTGCCAATCAGTTAGAA
TTAAATCCTGACTTTTCAAGACCTAATAGAAAGTATACCTGGAATGATGTTGGACAGCTA
GTGGAAAAATTAAAAAAGGAATGGAATGTTATTTGTATTACTGATGTTGTCTACAATCAT
ACTGCTGCTAATAGTAAATGGATCCAGGAACATCCAGAATGTGCCTATAATCTTGTGAAT
TCTCCACACTTAAAACCTGCCTGGGTCTTAGACAGAGCACTTTGGCGTTTCTCCTGTGAT
GTTGCAGAAGGGAAATACAAAGAAAAGGGAATACCTGCTTTGATTGAAAATGATCACCAT
ATGAATTCCATCCGAAAAATAATTTGGGAGGATATTTTTCCAAAGCTTAAACTTTGGGAA
TTTTTCCAAGTAGATGTCAACAAAGCGGTTGAGCAATTTAGAAGACTTCTTACACAAGAA
AATAGGCGAGTAACCAAGTCTGATCCAAACCAACACCTTACGATTATTCAAGATCCTGAA
TACAGACGGTTTGGCTGTACTGTAGATATGAACATTGCACTAACGACTTTCATACCACAT
GACAAGGGGCCAGCAGCAATTGAAGAATGCTGTAATTGGTTTCATAAAAGAATGGAGGAA
TTAAATTCAGAGAAGCATCGACTCATTAACTATCATCAGGAACAGGCAGTTAATTGCCTT
TTGGGAAATGTGTTTTATGAACGACTGGCTGGCCATGGTCCAAAACTAGGACCTGTCACT
AGAAAGCATCCTTTAGTTACCAGGTATTTTACTTTCCCATTTGAAGAGATAGACTTCTCC
ATGGAAGAATCTATGATTCATCTGCCAAATAAAGCTTGTTTTCTGATGGCACACAATGGA
TGGGTAATGGGAGATGATCCTCTTCGAAACTTTGCTGAACCGGGTTCAGAAGTTTACCTA
AGGAGAGAACTTATTTGCTGGGGAGACAGTGTTAAATTACGCTATGGGAATAAACCAGAG
GACTGTCCTTATCTCTGGGCACACATGAAAAAATACACTGAAATAACTGCAACTTATTTC
CAGGGAGTACGTCTTGATAACTGCCACTCAACACCTCTTCACGTAGCTGAGTACATGTTG
GATGCTGCTAGGAATTTGCAACCCAATTTATATGTAGTAGCTGAACTGTTCACAGGAAGT
GAAGATCTGGACAATGTCTTTGTTACTAGACTGGGCATTAGTTCCTTAATAAGAGAGGCA
ATGAGTGCATATAATAGTCATGAAGAGGGCAGATTAGTTTACCGATATGGAGGAGAACCT
GTTGGATCCTTTGTTCAGCCCTGTTTGAGGCCTTTAATGCCAGCTATTGCACATGCCCTG
TTTATGGATATTACGCATGATAATGAGTGTCCTATTGTGCATAGATCAGCGTATGATGCT
CTTCCAAGTACTACAATTGTTTCTATGGCATGTTGTGCTAGTGGAAGTACAAGAGGCTAT
GATGAATTAGTGCCTCATCAGATTTCAGTGGTTTCTGAAGAACGGTTTTACACTAAGTGG
AATCCTGAAGCATTGCCTTCAAACACAGGTGAAGTTAATTTCCAAAGCGGCATTATTGCA
GCCAGGTGTGCTATCAGTAAACTTCATCAGGAGCTTGGAGCCAAGGGTTTTATTCAGGTG
TATGTGGATCAAGTTGATGAAGACATAGTGGCAGTAACAAGACACTCACCTAGCATCCAT
CAGTCTGTTGTGGCTGTATCTAGAACTGCTTTCAGGAATCCCAAGACTTCATTTTACAGC
AAGGAAGTGCCTCAAATGTGCATCCCTGGCAAAATTGAAGAAGTAGTTCTTGAAGCTAGA
ACTATTGAGAGAAACACGAAACCTTATAGGAAGGATGAGAATTCAATCAATGGAACACCA
GATATCACAGTAGAAATTAGAGAACATATTCAGCTTAATGAAAGTAAAATTGTTAAACAA
GCTGGAGTTGCCACAAAAGGGCCCAATGAATATATTCAAGAAATAGAATTTGAAAACTTG
TCTCCAGGAAGTGTTATTATATTCAGAGTTAGTCTTGATCCACATGCACAAGTCGCTGTT
GGAATTCTTCGAAATCATCTGACACAATTCAGTCCTCACTTTAAATCTGGCAGCCTAGCT
GTTGACAATGCAGATCCTATATTAAAAATTCCTTTTGCTTCTCTTGCCTCCAGATTAACT
TTGGCTGAGCTAAATCAGATCCTTTACCGATGTGAATCAGAAGAAAAGGAAGATGGTGGA
GGGTGCTATGACATACCAAACTGGTCAGCCCTTAAATATGCAGGTCTTCAAGGTTTAATG
TCTGTATTGGCAGAAATAAGACCAAAGAATGACTTGGGGCATCCTTTTTGTAATAATTTG
AGATCTGGAGATTGGATGATTGACTATGTCAGTAACCGGCTTATTTCACGATCAGGAACT
ATTGCTGAAGTTGGTAAATGGTTGCAGGCTATGTTCTTCTACCTGAAGCAGATCCCACGT
TACCTTATCCCATGTTACTTTGATGCTATATTAATTGGTGCATATACCACTCTTCTGGAT
ACAGCATGGAAGCAGATGTCAAGCTTTGTTCAGAATGGTTCAACCTTTGTGAAACACCTT
TCATTGGGTTCAGTTCAACTGTGTGGAGTAGGAAAATTCCCTTCCCTGCCAATTCTTTCA
CCTGCCCTAATGGATGTACCTTATAGGTTAAATGAGATCACAAAAGAAAAGGAGCAATGT
TGTGTTTCTCTAGCTGCAGGCTTACCTCATTTTTCTTCTGGTATTTTCCGCTGCTGGGGA
AGGGATACTTTTATTGCACTTAGAGGTATACTGCTGATTACTGGACGCTATGTAGAAGCC
AGGAATATTATTTTAGCATTTGCGGGTACCCTGAGGCATGGTCTCATTCCTAATCTACTG
GGTGAAGGAATTTATGCCAGATACAATTGTCGGGATGCTGTGTGGTGGTGGCTGCAGTGT
ATCCAGGATTACTGTAAAATGGTTCCAAATGGTCTAGACATTCTCAAGTGCCCAGTTTCC
AGAATGTATCCTACAGATGATTCTGCTCCTTTGCCTGCTGGCACACTGGATCAGCCATTG
TTTGAAGTCATACAGGAAGCAATGCAAAAACACATGCAGGGCATACAGTTCCGAGAAAGG
AATGCTGGTCCCCAGATAGATCGAAACATGAAGGACGAAGGTTTTAATATAACTGCAGGA
GTTGATGAAGAAACAGGATTTGTTTATGGAGGAAATCGTTTCAATTGTGGCACATGGATG
GATAAAATGGGAGAAAGTGACAGAGCTAGAAACAGAGGAATCCCAGCCACACCAAGAGAT
GGGTCTGCTGTGGAAATTGTGGGCCTGAGTAAATCTGCTGTTCGCTGGTTGCTGGAATTA
TCCAAAAAAAATATTTTCCCTTATCATGAAGTCACAGTAAAAAGACATGGAAAGGCTATA
AAGGTCTCATATGATGAGTGGAACAGAAAAATACAAGACAACTTTGAAAAGCTATTTCAT
GTTTCCGAAGACCCTTCAGATTTAAATGAAAAGCATCCAAATCTGGTTCACAAACGTGGC
ATATACAAAGATAGTTATGGAGCTTCAAGTCCTTGGTGTGACTATCAGCTCAGGCCTAAT
TTTACCATAGCAATGGTTGTGGCCCCTGAGCTCTTTACTACAGAAAAAGCATGGAAAGCT
TTGGAGATTGCAGAAAAAAAATTGCTTGGTCCCCTTGGCATGAAAACTTTAGATCCAGAT
GATATGGTTTACTGTGGAATTTATGACAATGCATTAGACAATGACAACTACAATCTTGCT
AAAGGTTTCAATTATCACCAAGGACCTGAGTGGCTGTGGCCTATTGGGTATTTTCTTCGT
GCAAAATTATATTTTTCCAGATTGATGGGCCCGGAGACTACTGCAAAGACTATAGTTTTG
GTTAAAAATGTTCTTTCCCGACATTATGTTCATCTTGAGAGATCCCCTTGGAAAGGACTT
CCAGAACTGACCAATGAGAATGCCCAGTACTGTCCTTTCAGCTGTGAAACACAAGCCTGG
TCAATTGCTACTATTCTTGAGACACTTTATGATTTATAG
|
| Enzyme 1 GenBank Gene ID |
AB035443  |
| Enzyme 1 GeneCard ID |
AGL  |
| Enzyme 1 GenAtlas ID |
AGL  |
| Enzyme 1 HGNC ID |
HGNC:321  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
1p21 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Yang BZ, Ding JH, Enghild JJ, Bao Y, Chen YT: Molecular cloning and nucleotide sequence of cDNA encoding human muscle glycogen debranching enzyme. J Biol Chem. 1992 May 5;267(13):9294-9. [PubMed
]
- Bao Y, Dawson TL Jr, Chen YT: Human glycogen debranching enzyme gene (AGL): complete structural organization and characterization of the 5' flanking region. Genomics. 1996 Dec 1;38(2):155-65. [PubMed
]
- Bao Y, Yang BZ, Dawson TL Jr, Chen YT: Isolation and nucleotide sequence of human liver glycogen debranching enzyme mRNA: identification of multiple tissue-specific isoforms. Gene. 1997 Sep 15;197(1-2):389-98. [PubMed
]
- Okubo M, Horinishi A, Takeuchi M, Suzuki Y, Sakura N, Hasegawa Y, Igarashi T, Goto K, Tahara H, Uchimoto S, Omichi K, Kanno H, Hayasaka K, Murase T: Heterogeneous mutations in the glycogen-debranching enzyme gene are responsible for glycogen storage disease type IIIa in Japan. Hum Genet. 2000 Jan;106(1):108-15. [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
]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed
]
- Cheng A, Zhang M, Gentry MS, Worby CA, Dixon JE, Saltiel AR: A role for AGL ubiquitination in the glycogen storage disorders of Lafora and Cori's disease. Genes Dev. 2007 Oct 1;21(19):2399-409. [PubMed
]
- Okubo M, Kanda F, Horinishi A, Takahashi K, Okuda S, Chihara K, Murase T: Glycogen storage disease type IIIa: first report of a causative missense mutation (G1448R) of the glycogen debranching enzyme gene found in a homozygous patient. Hum Mutat. 1999 Dec;14(6):542-3. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5612 |
| Enzyme 2 Name |
Glycogen phosphorylase, brain form |
| Enzyme 2 Synonyms |
Not Available |
| Enzyme 2 Gene Name |
PYGB |
| Enzyme 2 Protein Sequence |
>Glycogen phosphorylase, brain form
MAKPLTDSEKRKQISVRGLAGLGDVAEVRKSFNRHLHFTLVKDRNVATPRDYFFALAHTV
RDHLVGRWIRTQQHYYERDPKRIYYLSLEFYMGRTLQNTMVNLGLQNACDEAIYQLGLDL
EELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEFGIFNQKIVNGWQVEEA
DDWLRYGNPWEKARPEYMLPVHFYGRVEHTPDGVKWLDTQVVLAMPYDTPVPGYKNNTVN
TMRLWSAKAPNDFKLQDFNVGDYIEAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFV
VAATLQDIIRRFKSSKFGCRDPVRTCFETFPDKVAIQLNDTHPALSIPELMRILVDVEKV
DWDKAWEITKKTCAYTNHTVLPEALERWPVSMFEKLLPRHLEIIYAINQRHLDHVAALFP
GDVDRLRRMSVIEEGDCKRINMAHLCVIGSHAVNGVARIHSEIVKQSVFKDFYELEPEKF
QNKTNGITPRRWLLLCNPGLADTIVEKIGEEFLTDLSQLKKLLPLVSDEVFIRDVAKVKQ
ENKLKFSAFLEKEYKVKINPSSMFDVHVKRIHEYKRQLLNCLHVVTLYNRIKRDPAKAFV
PRTVMIGGKAAPGYHMAKLIIKLVTSIGDVVNHDPVVGDRLKVIFLENYRVSLAEKVIPA
ADLSQQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGAENLFIFGLRVEDVE
ALDRKGYNAREYYDHLPELKQAVDQISSGFFSPKEPDCFKDIVNMLMHHDRFKVFADYEA
YMQCQAQVDQLYRNPKEWTKKVIRNIACSGKFSSDRTITEYAREIWGVEPSDLQIPPPNI
PRD
|
| Enzyme 2 Number of Residues |
843 |
| Enzyme 2 Molecular Weight |
96695.2 |
| Enzyme 2 Theoretical pI |
6.85 |
| Enzyme 2 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- phosphorylase activity
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in phosphorylase activity |
| Enzyme 2 Specific Function |
Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties |
| Enzyme 2 Pathways |
- Starch and Sucrose Metabolism (map00500
)
|
| Enzyme 2 Reactions |
- [(1->4)-alpha-D-glucosyl]n + phosphate = [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate [RN:R01821 R06050]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
9650807  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P11216  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
PYGB_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>2532 bp
ATGGCGAAGCCGCTGACGGACAGCGAGAAGCGGAAGCAGATCAGCGTGCGCGGCCTGGCG
GGGCTAGGCGACGTGGCCGAGGTGCGGAAGAGCTTCAACCGGCACTTGCACTTCACGCTG
GTCAAGGACCGCAATGTGGCCACGCCCCGCGACTACTTCTTCGCGCTGGCGCACACGGTG
CGCGACCACCTCGTGGGCCGCTGGATCCGCACGCAGCAGCACTACTACGAGCGCGACCCC
AAGCGCATTTATTATCTTTCCCTGGAATTCTACATGGGTCGCACGCTGCAGAACACGATG
GTGAACCTGGGCCTTCAGAATGCCTGCGATGAAGCCATCTATCAGTTGGGGTTAGACTTG
GAGGAACTCGAGGAGATAGAAGAAGATGCTGGCCTTGGGAATGGAGGCCTGGGGAGGCTG
GCAGCGTGTTTCCTTGACTCAATGGCTACCTTGGGCCTGGCAGCATACGGCTATGGAATC
CGCTATGAATTTGGGATTTTTAACCAGAAGATTGTCAATGGCTGGCAGGTAGAGGAGGCC
GATGACTGGCTGCGCTACGGCAACCCCTGGGAGAAAGCGCGGCCTGAGTATATGCTTCCC
GTGCACTTCTACGGACGCGTGGAGCACACCCCCGACGGCGTGAAGTGGCTGGACACACAG
GTGGTGCTGGCCATGCCCTACGACACCCCAGTGCCCGGCTACAAGAACAACACCGTCAAC
ACCATGCGGCTGTGGTCCGCCAAGGCTCCCAACGACTTCAAGCTGCAGGACTTCAACGTG
GGAGACTACATCGAGGCGGTCCTGGACCGGAACTTGGCTGAGAACATCTCCAGGGTCCTG
TATCCAAATGATAACTTCTTTGAGGGGAAGGAGCTGCGGCTGAAGCAGGAGTACTTCGTG
GTGGCCGCCACGCTCCAGGACATCATCCGCCGCTTCAAGTCGTCCAAGTTCGGCTGCCGG
GACCCTGTGAGAACCTGTTTCGAGACGTTCCCAGACAAGGTGGCCATCCAGCTGAACGAC
ACCCACCCCGCCCTCTCCATCCCTGAGCTCATGCGGATCCTGGTGGACGTGGAGAAGGTG
GACTGGGACAAGGCCTGGGAAATCACGAAGAAGACCTGTGCATACACCAACCACACTGTG
CTGCCTGAGGCCTTGGAGCGCTGGCCCGTGTCCATGTTTGAGAAGCTGCTGCCGCGGCAC
CTGGAGATAATCTATGCCATCAACCAGCGGCACCTGGACCACGTGGCCGCGCTGTTTCCC
GGCGATGTGGACCGCCTGCGCAGGATGTCTGTGATCGAGGAGGGGGACTGCAAGCGGATC
AACATGGCCCACCTGTGTGTGATTGGGTCCCATGCTGTCAATGGTGTGGCGAGGATCCAC
TCGGAGATCGTGAAACAGTCGGTCTTTAAGGATTTTTATGAACTGGAGCCAGAGAAGTTC
CAGAATAAGACCAATGGCATCACCCCCCGCCGGTGGCTGCTGCTGTGCAACCCGGGGCTG
GCCGATACCATCGTGGAGAAAATTGGGGAGGAGTTCCTGACTGACCTGAGCCAGCTGAAG
AAGCTGCTGCCGCTGGTCAGTGACGAGGTGTTCATCAGGGACGTGGCCAAGGTCAAACAG
GAGAACAAGCTCAAGTTCTCGGCCTTCCTGGAGAAGGAGTACAAGGTGAAGATCAACCCC
TCCTCCATGTTCGATGTGCATGTGAAGAGGATCCACGAGTACAAGCGGCAGCTGCTCAAC
TGCCTGCACGTCGTCACCCTGTACAATCGAATCAAGAGAGACCCGGCCAAGGCTTTTGTG
CCCAGGACTGTTATGATTGGGGGCAAGGCAGCGCCCGGTTACCACATGGCCAAGCTGATC
ATCAAGTTGGTCACCTCCATCGGCGACGTCGTCAATCATGACCCAGTTGTGGGTGACAGG
TTGAAAGTGATCTTCCTGGAGAACTACCGTGTGTCCTTGGCTGAGAAAGTGATCCCGGCC
GCTGATCTGTCGCAGCAGATCTCCACTGCAGGCACCGAGGCCTCAGGCACAGGCAACATG
AAGTTCATGCTCAACGGGGCCCTCACCATCGGCACCATGGACGGCGCCAACGTGGAGATG
GCCGAGGAGGCCGGGGCCGAGAACCTCTTCATCTTCGGCCTGCGGGTGGAGGATGTCGAG
GCCTTGGACCGGAAAGGGTACAATGCCAGGGAGTACTACGACCACCTGCCCGAGCTGAAG
CAGGCCGTGGACCAGATCAGCAGTGGCTTTTTTTCTCCCAAGGAGCCAGACTGCTTCAAG
GACATCGTGAACATGCTGATGCACCATGACAGGTTCAAGGTGTTTGCAGACTATGAAGCC
TACATGCAGTGCCAGGCACAGGTGGACCAGCTGTACCGGAACCCCAAGGAGTGGACCAAG
AAGGTCATCAGGAACATCGCCTGCTCGGGCAAGTTCTCCAGTGACCGGACCATCACGGAG
TATGCACGGGAGATCTGGGGTGTGGAGCCCTCCGACCTGCAGATCCCGCCCCCCAACATC
CCCCGGGACTAG
|
| Enzyme 2 GenBank Gene ID |
AL121772  |
| Enzyme 2 GeneCard ID |
PYGB  |
| Enzyme 2 GenAtlas ID |
PYGB  |
| Enzyme 2 HGNC ID |
HGNC:9723  |
| Enzyme 2 Chromosome Location |
2 |
| Enzyme 2 Locus |
20p11.2-p11.1 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Newgard CB, Littman DR, van Genderen C, Smith M, Fletterick RJ: Human brain glycogen phosphorylase. Cloning, sequence analysis, chromosomal mapping, tissue expression, and comparison with the human liver and muscle isozymes. J Biol Chem. 1988 Mar 15;263(8):3850-7. [PubMed
]
- Gelinas RP, Froman BE, McElroy F, Tait RC, Gorin FA: Human brain glycogen phosphorylase: characterization of fetal cDNA and genomic sequences. Brain Res Mol Brain Res. 1989 Nov;6(2-3):177-85. [PubMed
]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [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
]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [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
]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [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
]
- Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [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
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
6384 |
| Enzyme 3 Name |
Glycogenin-2 |
| Enzyme 3 Synonyms |
- GN-2
- GN2
|
| Enzyme 3 Gene Name |
GYG2 |
| Enzyme 3 Protein Sequence |
>Glycogenin-2
MSETEFHHGAQAGLELLRSSNSPTSASQSAGMTVTDQAFVTLATNDIYCQGALVLGQSLR
RHRLTRKLVVLITPQVSSLLRVILSKVFDEVIEVNLIDSADYIHLAFLKRPELGLTLTKL
HCWTLTHYSKCVFLDADTLVLSNVDELFDRGEFSAAPDPGWPDCFNSGVFVFQPSLHTHK
LLLQHAMEHGSFDGADQGLLNSFFRNWSTTDIHKHLPFIYNLSSNTMYTYSPAFKQFGSS
AKVVHFLGSMKPWNYKYNPQSGSVLEQGSASSSQHQAAFLHLWWTVYQNNVLPLYKSVQA
GEARASPGHTLCHSDVGGPCADSASGVGEPCENSTPSAGVPCANSPLGSNQPAQGLPEPT
QIVDETLSLPEGRRSEDMIACPETETPAVITCDPLSQPSPQPADFTETETILQPANKVES
VSSEETFEPSQELPAEALRDPSLQDALEVDLAVSVSQISIEEKVKELSPEEERRKWEEGR
IDYMGKDAFARIQEKLDRFLQ
|
| Enzyme 3 Number of Residues |
501 |
| Enzyme 3 Molecular Weight |
55183.3 |
| Enzyme 3 Theoretical pI |
4.74 |
| Enzyme 3 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in transferase activity, transferring glycosyl groups |
| Enzyme 3 Specific Function |
Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
- UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin [RN:R03681]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
119964690  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
O15488  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
GLYG2_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1506 bp
ATGTCGGAGACAGAGTTTCACCATGGTGCCCAGGCTGGTCTCGAACTCCTGAGGTCAAGC
AATTCACCCACCTCAGCCTCCCAAAGTGCTGGAATGACAGTGACTGATCAGGCTTTTGTC
ACACTAGCCACCAATGACATCTACTGCCAGGGCGCCCTGGTCCTGGGGCAGTCACTGAGG
AGACACAGGCTGACGAGGAAGCTGGTGGTGTTGATCACTCCTCAGGTGTCCAGCCTGCTC
AGGGTCATCCTCTCGAAGGTGTTCGATGAAGTCATTGAAGTGAATCTAATCGATAGTGCC
GACTACATCCACCTGGCCTTTCTGAAGAGACCTGAGCTCGGGCTCACCCTCACCAAGCTT
CACTGTTGGACTCTCACTCACTACAGCAAGTGTGTCTTCCTGGATGCAGACACTCTGGTG
CTGTCCAATGTCGATGAGCTGTTTGACAGGGGAGAGTTTTCTGCGGCCCCGGACCCCGGA
TGGCCGGATTGCTTCAATAGCGGGGTGTTTGTCTTCCAGCCTTCTCTCCACACGCATAAA
CTCCTGCTACAGCACGCCATGGAACACGGCAGCTTTGACGGGGCAGACCAAGGCTTACTG
AATAGTTTCTTCAGGAACTGGTCGACCACAGACATCCACAAGCACCTGCCGTTCATCTAT
AACTTGAGTAGTAACACGATGTACACTTACAGCCCTGCCTTCAAGCAATTCGGTTCCAGT
GCAAAGGTCGTCCACTTTTTGGGGTCCATGAAACCTTGGAACTACAAGTACAATCCACAG
AGTGGCTCGGTGTTGGAGCAAGGCTCAGCGTCCAGCAGCCAGCACCAGGCGGCATTCCTT
CATCTCTGGTGGACGGTCTACCAGAACAACGTGCTGCCCCTTTATAAAAGCGTCCAAGCG
GGGGAAGCACGCGCGTCTCCTGGTCACACACTTTGCCACAGTGATGTGGGGGGGCCGTGT
GCGGATTCAGCCTCTGGTGTTGGAGAGCCGTGTGAAAATTCAACACCCAGTGCGGGCGTG
CCGTGTGCAAATTCACCACTGGGTTCTAACCAGCCTGCTCAGGGCCTTCCGGAGCCGACC
CAGATAGTGGATGAGACCCTGTCCCTACCTGAAGGACGCCGTTCAGAAGATATGATAGCT
TGTCCTGAAACTGAGACTCCTGCCGTGATAACGTGTGACCCACTGTCCCAGCCTTCCCCT
CAGCCTGCAGACTTCACAGAGACTGAAACCATCTTGCAGCCAGCAAATAAAGTCGAAAGT
GTCTCATCCGAGGAAACCTTCGAACCAAGCCAGGAACTCCCTGCTGAGGCTCTCAGGGAC
CCCAGTCTGCAGGATGCACTGGAGGTCGACCTGGCCGTCTCTGTTTCCCAGATCTCCATC
GAAGAGAAGGTGAAGGAATTGAGCCCCGAGGAAGAGAGGAGGAAGTGGGAGGAAGGCCGT
ATCGACTACATGGGGAAGGACGCGTTTGCTCGCATCCAGGAGAAGCTGGACCGGTTCCTG
CAGTAA
|
| Enzyme 3 GenBank Gene ID |
NM_003918.2  |
| Enzyme 3 GeneCard ID |
GYG2  |
| Enzyme 3 GenAtlas ID |
GYG2  |
| Enzyme 3 HGNC ID |
HGNC:4700  |
| Enzyme 3 Chromosome Location |
Not Available |
| Enzyme 3 Locus |
Not Available |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Mu J, Skurat AV, Roach PJ: Glycogenin-2, a novel self-glucosylating protein involved in liver glycogen biosynthesis. J Biol Chem. 1997 Oct 31;272(44):27589-97. [PubMed
]
- Zhai L, Mu J, Zong H, DePaoli-Roach AA, Roach PJ: Structure and chromosomal localization of the human glycogenin-2 gene GYG2. Gene. 2000 Jan 25;242(1-2):229-35. [PubMed
]
- Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [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
]
- Mu J, Roach PJ: Characterization of human glycogenin-2, a self-glucosylating initiator of liver glycogen metabolism. J Biol Chem. 1998 Dec 25;273(52):34850-6. [PubMed
]
- Harris RA, Yang A, Stein RC, Lucy K, Brusten L, Herath A, Parekh R, Waterfield MD, O'Hare MJ, Neville MA, Page MJ, Zvelebil MJ: Cluster analysis of an extensive human breast cancer cell line protein expression map database. Proteomics. 2002 Feb;2(2):212-23. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
7128 |
| Enzyme 4 Name |
Serine/threonine-protein phosphatase PP1-beta catalytic subunit |
| Enzyme 4 Synonyms |
- PP-1B
|
| Enzyme 4 Gene Name |
PPP1CB |
| Enzyme 4 Protein Sequence |
>Serine/threonine-protein phosphatase PP1-beta catalytic subunit
MADGELNVDSLITRLLEVRGCRPGKIVQMTEAEVRGLCIKSREIFLSQPILLELEAPLKI
CGDIHGQYTDLLRLFEYGGFPPEANYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLL
RGNHECASINRIYGFYDECKRRFNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQ
SMEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVSKFLNRHDL
DLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGGMMSVDETLMCSFQILKPSEK
KAKYQYGGLNSGRPVTPPRTANPPKKR
|
| Enzyme 4 Number of Residues |
327 |
| Enzyme 4 Molecular Weight |
37186.5 |
| Enzyme 4 Theoretical pI |
6.06 |
| Enzyme 4 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 4 General Function |
Involved in hydrolase activity |
| Enzyme 4 Specific Function |
Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
- a phosphoprotein + H2O = a protein + phosphate [RN:R00164]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
531476  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P62140  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
PP1B_HUMAN  |
| Enzyme 4 PDB ID |
1S70  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>984 bp
ATGGCGGACGGGGAGCTGAACGTGGACAGCCTCATCACCCGGCTGCTGGAGGTACGAGGA
TGTCGTCCAGGAAAGATTGTGCAGATGACTGAAGCAGAAGTTCGAGGCTTATGTATCAAG
TCTCGGGAGATCTTTCTCAGCCAGCCTATTCTTTTGGAATTGGAAGCACCGCTGAAAATT
TGTGGAGATATTCATGGACAATATACAGATTTACTGAGATTATTTGAATATGGAGGTTTC
CCACCAGAAGCCAACTATCTTTTCTTAGGAGATTATGTGGACAGAGGAAAGCAGTCTTTG
GAAACCATTTGTTTGCTATTGGCTTATAAAATCAAATATCCAGAGAACTTCTTTCTCTTA
AGAGGAAACCATGAGTGTGCTAGCATCAATCGCATTTATGGATTCTATGATGAATGCAAA
CGAAGATTTAATATTAAATTGTGGAAGACCTTCACTGATTGTTTTAACTGTCTGCCTATA
GCAGCCATTGTGGATGAGAAGATCTTCTGTTGTCATGGAGGATTGTCACCAGACCTGCAA
TCTATGGAGCAGATTCGGAGAATTATGAGACCTACTGATGTCCCTGATACAGGTTTGCTC
TGTGATTTGCTATGGTCTGATCCAGATAAGGATGTGCAAGGCTGGGGAGAAAATGATCGT
GGTGTTTCCTTTACTTTTGGAGCTGATGTAGTCAGTAAATTTCTGAATCGTCATGATTTA
GATTTGATTTGTCGAGCTCATCAGGTGGTGGAAGATGGATATGAATTTTTTGCTAAACGA
CAGTTGGTAACCTTATTTTCAGCCCCAAATTACTGTGGCGAGTTTGATAATGCTGGTGGA
ATGATGAGTGTGGATGAAACTTTGATGTGTTCATTTCAGATATTGAAACCATCTGAAAAG
AAAGCTAAATACCAGTATGGTGGACTGAATTCTGGACGTCCTGTCACTCCACCTCGAACA
GCTAATCCGCCGAAGAAAAGGTGA
|
| Enzyme 4 GenBank Gene ID |
X80910  |
| Enzyme 4 GeneCard ID |
PPP1CB  |
| Enzyme 4 GenAtlas ID |
PPP1CB  |
| Enzyme 4 HGNC ID |
HGNC:9282  |
| Enzyme 4 Chromosome Location |
2 |
| Enzyme 4 Locus |
2p23 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Barker HM, Brewis ND, Street AJ, Spurr NK, Cohen PT: Three genes for protein phosphatase 1 map to different human chromosomes: sequence, expression and gene localisation of protein serine/threonine phosphatase 1 beta (PPP1CB). Biochim Biophys Acta. 1994 Jan 13;1220(2):212-8. [PubMed
]
- Prochazka M, Mochizuki H, Baier LJ, Cohen PT, Bogardus C: Molecular and linkage analysis of type-1 protein phosphatase catalytic beta-subunit gene: lack of evidence for its major role in insulin resistance in Pima Indians. Diabetologia. 1995 Apr;38(4):461-6. [PubMed
]
- Verin AD, Csortos C, Durbin SD, Aydanyan A, Wang P, Patterson CE, Garcia JG: Characterization of the protein phosphatase 1 catalytic subunit in endothelium: involvement in contractile responses. J Cell Biochem. 2000 Jul 19;79(1):113-25. [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
]
- 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
]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed
]
- Tan I, Ng CH, Lim L, Leung T: Phosphorylation of a novel myosin binding subunit of protein phosphatase 1 reveals a conserved mechanism in the regulation of actin cytoskeleton. J Biol Chem. 2001 Jun 15;276(24):21209-16. Epub 2001 Apr 3. [PubMed
]
- Trinkle-Mulcahy L, Sleeman JE, Lamond AI: Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells. J Cell Sci. 2001 Dec;114(Pt 23):4219-28. [PubMed
]
- Connor JH, Weiser DC, Li S, Hallenbeck JM, Shenolikar S: Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1. Mol Cell Biol. 2001 Oct;21(20):6841-50. [PubMed
]
- Ceulemans H, Vulsteke V, De Maeyer M, Tatchell K, Stalmans W, Bollen M: Binding of the concave surface of the Sds22 superhelix to the alpha 4/alpha 5/alpha 6-triangle of protein phosphatase-1. J Biol Chem. 2002 Dec 6;277(49):47331-7. Epub 2002 Sep 10. [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
]
- Boyce M, Bryant KF, Jousse C, Long K, Harding HP, Scheuner D, Kaufman RJ, Ma D, Coen DM, Ron D, Yuan J: A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress. Science. 2005 Feb 11;307(5711):935-9. [PubMed
]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [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
]
- Fujiki R, Chikanishi T, Hashiba W, Ito H, Takada I, Roeder RG, Kitagawa H, Kato S: GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis. Nature. 2009 May 21;459(7245):455-9. Epub 2009 Apr 19. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
7291 |
| Enzyme 5 Name |
Laforin |
| Enzyme 5 Synonyms |
- Lafora PTPase
- LAFPTPase
|
| Enzyme 5 Gene Name |
EPM2A |
| Enzyme 5 Protein Sequence |
>Laforin
MRFRFGVVVPPAVAGARPELLVVGSRPELGRWEPRGAVRLRPAGTAAGDGALALQEPGLW
LGEVELAAEEAAQDGAEPGRVDTFWYKFLKREPGGELSWEGNGPHHDRCCTYNENNLVDG
VYCLPIGHWIEATGHTNEMKHTTDFYFNIAGHQAMHYSRILPNIWLGSCPRQVEHVTIKL
KHELGITAVMNFQTEWDIVQNSSGCNRYPEPMTPDTMIKLYREEGLAYIWMPTPDMSTEG
RVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKR
PAVYIDEEALARAQEDFFQKFGKVRSSVCSL
|
| Enzyme 5 Number of Residues |
331 |
| Enzyme 5 Molecular Weight |
37157.3 |
| Enzyme 5 Theoretical pI |
6.64 |
| Enzyme 5 GO Classification |
| Function |
- binding
- carbohydrate binding
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphatase activity
- phosphoprotein phosphatase activity
- phosphoric ester hydrolase activity
- protein tyrosine phosphatase activity
- protein tyrosine/serine/threonine phosphatase activity
|
| Process |
- carbohydrate metabolic process
- cellular metabolic process
- dephosphorylation
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- primary metabolic process
- protein amino acid dephosphorylation
|
| Component |
| — |
|
| Enzyme 5 General Function |
Involved in carbohydrate binding |
| Enzyme 5 Specific Function |
Dual specificity protein phosphatase. May be involved in the control of glycogen metabolism, particularly in monitoring for and preventing the formation of poorly branched glycogen molecules (polyglucosans). Acts as a scaffold protein to facilitate PPP1R3C/PTG ubiquitination by NHLRC1/malin. Forms a complex with NHLRC1/malin and HSP70 and this complex suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS) |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
- protein tyrosine phosphate + H2O = protein tyrosine + phosphate [RN:R02585]
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
6005986  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
O95278  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
EPM2A_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>996 bp
ATGCGCTTCCGCTTTGGGGTGGTGGTGCCACCCGCCGTGGCCGGCGCCCGGCCGGAGCTG
CTGGTGGTGGGGTCGCGGCCCGAGCTGGGGCGTTGGGAGCCGCGCGGTGCCGTCCGCCTG
AGGCCGGCCGGCACCGCGGCGGGCGACGGGGCCCTGGCGCTGCAGGAGCCGGGCCTGTGG
CTCGGGGAGGTGGAGCTGGCGGCCGAGGAGGCGGCGCAGGACGGGGCGGAGCCGGGCCGC
GTGGACACGTTCTGGTACAAGTTCCTGAAGCGGGAGCCGGGAGGAGAGCTCTCCTGGGAA
GGCAATGGACCTCATCATGACCGTTGCTGTACTTACAATGAAAACAACTTGGTGGATGGT
GTGTATTGTCTCCCAATAGGACACTGGATTGAGGCCACTGGGCACACCAATGAAATGAAG
CACACAACAGACTTCTATTTTAATATTGCAGGCCACCAAGCCATGCATTATTCAAGAATT
CTACCAAATATCTGGCTGGGTAGCTGCCCTCGTCAGGTGGAACATGTAACCATCAAACTG
AAGCATGAATTGGGGATTACAGCTGTAATGAATTTCCAGACTGAATGGGATATTGTACAG
AATTCCTCAGGCTGTAACCGCTACCCAGAGCCCATGACTCCAGACACTATGATTAAACTA
TATAGGGAAGAAGGCTTGGCCTACATCTGGATGCCAACACCAGATATGAGCACCGAAGGC
CGAGTACAGATGCTGCCCCAGGCGGTGTGCCTGCTGCATGCGCTGCTGGAGAAGGGACAC
ATCGTGTACGTGCACTGCAACGCTGGGGTGGGCCGCTCCACCGCGGCTGTCTGCGGCTGG
CTCCAGTATGTGATGGGCTGGAATCTGAGGAAGGTGCAGTATTTCCTCATGGCCAAGAGG
CCGGCTGTCTACATTGACGAAGAGGCCTTGGCCCGGGCACAAGAAGATTTTTTCCAGAAA
TTTGGGAAGGTTCGTTCTTCTGTGTGTAGCCTGTAG
|
| Enzyme 5 GenBank Gene ID |
AF084535  |
| Enzyme 5 GeneCard ID |
EPM2A  |
| Enzyme 5 GenAtlas ID |
EPM2A  |
| Enzyme 5 HGNC ID |
HGNC:3413  |
| Enzyme 5 Chromosome Location |
6 |
| Enzyme 5 Locus |
6q24 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Minassian BA, Lee JR, Herbrick JA, Huizenga J, Soder S, Mungall AJ, Dunham I, Gardner R, Fong CY, Carpenter S, Jardim L, Satishchandra P, Andermann E, Snead OC 3rd, Lopes-Cendes I, Tsui LC, Delgado-Escueta AV, Rouleau GA, Scherer SW: Mutations in a gene encoding a novel protein tyrosine phosphatase cause progressive myoclonus epilepsy. Nat Genet. 1998 Oct;20(2):171-4. [PubMed
]
- Ganesh S, Agarwala KL, Ueda K, Akagi T, Shoda K, Usui T, Hashikawa T, Osada H, Delgado-Escueta AV, Yamakawa K: Laforin, defective in the progressive myoclonus epilepsy of Lafora type, is a dual-specificity phosphatase associated with polyribosomes. Hum Mol Genet. 2000 Sep 22;9(15):2251-61. [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
]
- Serratosa JM, Gomez-Garre P, Gallardo ME, Anta B, de Bernabe DB, Lindhout D, Augustijn PB, Tassinari CA, Malafosse RM, Topcu M, Grid D, Dravet C, Berkovic SF, de Cordoba SR: A novel protein tyrosine phosphatase gene is mutated in progressive myoclonus epilepsy of the Lafora type (EPM2). Hum Mol Genet. 1999 Feb;8(2):345-52. [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
]
- Minassian BA, Andrade DM, Ianzano L, Young EJ, Chan E, Ackerley CA, Scherer SW: Laforin is a cell membrane and endoplasmic reticulum-associated protein tyrosine phosphatase. Ann Neurol. 2001 Feb;49(2):271-5. [PubMed
]
- Ganesh S, Suzuki T, Yamakawa K: Alternative splicing modulates subcellular localization of laforin. Biochem Biophys Res Commun. 2002 Mar 15;291(5):1134-7. [PubMed
]
- Wang J, Stuckey JA, Wishart MJ, Dixon JE: A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen. J Biol Chem. 2002 Jan 25;277(4):2377-80. Epub 2001 Dec 5. [PubMed
]
- Ianzano L, Zhao XC, Minassian BA, Scherer SW: Identification of a novel protein interacting with laforin, the EPM2a progressive myoclonus epilepsy gene product. Genomics. 2003 Jun;81(6):579-87. [PubMed
]
- Ganesh S, Tsurutani N, Suzuki T, Ueda K, Agarwala KL, Osada H, Delgado-Escueta AV, Yamakawa K: The Lafora disease gene product laforin interacts with HIRIP5, a phylogenetically conserved protein containing a NifU-like domain. Hum Mol Genet. 2003 Sep 15;12(18):2359-68. Epub 2003 Jul 29. [PubMed
]
- Fernandez-Sanchez ME, Criado-Garcia O, Heath KE, Garcia-Fojeda B, Medrano-Fernandez I, Gomez-Garre P, Sanz P, Serratosa JM, Rodriguez de Cordoba S: Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation. Hum Mol Genet. 2003 Dec 1;12(23):3161-71. Epub 2003 Oct 7. [PubMed
]
- Ganesh S, Tsurutani N, Suzuki T, Hoshii Y, Ishihara T, Delgado-Escueta AV, Yamakawa K: The carbohydrate-binding domain of Lafora disease protein targets Lafora polyglucosan bodies. Biochem Biophys Res Commun. 2004 Jan 23;313(4):1101-9. [PubMed
]
- Gentry MS, Worby CA, Dixon JE: Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin. Proc Natl Acad Sci U S A. 2005 Jun 14;102(24):8501-6. Epub 2005 Jun 1. [PubMed
]
- Cheng A, Zhang M, Gentry MS, Worby CA, Dixon JE, Saltiel AR: A role for AGL ubiquitination in the glycogen storage disorders of Lafora and Cori's disease. Genes Dev. 2007 Oct 1;21(19):2399-409. [PubMed
]
- Worby CA, Gentry MS, Dixon JE: Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG). J Biol Chem. 2008 Feb 15;283(7):4069-76. Epub 2007 Dec 10. [PubMed
]
- Garyali P, Siwach P, Singh PK, Puri R, Mittal S, Sengupta S, Parihar R, Ganesh S: The malin-laforin complex suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system. Hum Mol Genet. 2009 Feb 15;18(4):688-700. Epub 2008 Nov 25. [PubMed
]
- Gomez-Garre P, Sanz Y, Rodriguez De Cordoba SR, Serratosa JM: Mutational spectrum of the EPM2A gene in progressive myoclonus epilepsy of Lafora: high degree of allelic heterogeneity and prevalence of deletions. Eur J Hum Genet. 2000 Dec;8(12):946-54. [PubMed
]
- Ganesh S, Shoda K, Amano K, Uchiyama A, Kumada S, Moriyama N, Hirose S, Yamakawa K: Mutation screening for Japanese Lafora's disease patients: identification of novel sequence variants in the coding and upstream regulatory regions of EPM2A gene. Mol Cell Probes. 2001 Oct;15(5):281-9. [PubMed
]
- Ganesh S, Delgado-Escueta AV, Suzuki T, Francheschetti S, Riggio C, Avanzini G, Rabinowicz A, Bohlega S, Bailey J, Alonso ME, Rasmussen A, Thomson AE, Ochoa A, Prado AJ, Medina MT, Yamakawa K: Genotype-phenotype correlations for EPM2A mutations in Lafora's progressive myoclonus epilepsy: exon 1 mutations associate with an early-onset cognitive deficit subphenotype. Hum Mol Genet. 2002 May 15;11(11):1263-71. [PubMed
]
- Ki CS, Kong SY, Seo DW, Hong SB, Kim HJ, Kim JW: Two novel mutations in the EPM2A gene in a Korean patient with Lafora's progressive myoclonus epilepsy. J Hum Genet. 2003;48(1):51-4. [PubMed
]
- Annesi G, Sofia V, Gambardella A, Candiano IC, Spadafora P, Annesi F, Cutuli N, De Marco EV, Civitelli D, Carrideo S, Tarantino P, Barone R, Zappia M, Quattrone A: A novel exon 1 mutation in a patient with atypical lafora progressive myoclonus epilepsy seen as childhood-onset cognitive deficit. Epilepsia. 2004 Mar;45(3):294-5. [PubMed
]
- Ianzano L, Young EJ, Zhao XC, Chan EM, Rodriguez MT, Torrado MV, Scherer SW, Minassian BA: Loss of function of the cytoplasmic isoform of the protein laforin (EPM2A) causes Lafora progressive myoclonus epilepsy. Hum Mutat. 2004 Feb;23(2):170-6. [PubMed
]
- Singh S, Suzuki T, Uchiyama A, Kumada S, Moriyama N, Hirose S, Takahashi Y, Sugie H, Mizoguchi K, Inoue Y, Kimura K, Sawaishi Y, Yamakawa K, Ganesh S: Mutations in the NHLRC1 gene are the common cause for Lafora disease in the Japanese population. J Hum Genet. 2005;50(7):347-52. Epub 2005 Jul 15. [PubMed
]
- Singh S, Satishchandra P, Shankar SK, Ganesh S: Lafora disease in the Indian population: EPM2A and NHLRC1 gene mutations and their impact on subcellular localization of laforin and malin. Hum Mutat. 2008 Jun;29(6):E1-12. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
7293 |
| Enzyme 6 Name |
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit |
| Enzyme 6 Synonyms |
- PP-1G
- Protein phosphatase 1C catalytic subunit
|
| Enzyme 6 Gene Name |
PPP1CC |
| Enzyme 6 Protein Sequence |
>Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
MADLDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAPLK
ICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFL
LRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDL
QSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHKHD
LDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAE
KKKPNATRPVTPPRGMITKQAKK
|
| Enzyme 6 Number of Residues |
323 |
| Enzyme 6 Molecular Weight |
36983.4 |
| Enzyme 6 Theoretical pI |
6.50 |
| Enzyme 6 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 6 General Function |
Involved in hydrolase activity |
| Enzyme 6 Specific Function |
Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II |
| Enzyme 6 Pathways |
Not Available |
| Enzyme 6 Reactions |
- a phosphoprotein + H2O = a protein + phosphate [RN:R00164]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
402778  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P36873  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
PP1G_HUMAN  |
| Enzyme 6 PDB ID |
1IT6  |
| Enzyme 6 PDB File |
Show |
| Enzyme 6 3D Structure |
|
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>972 bp
ATGGCGGATTTAGATAAACTCAACATCGACAGCATTATCCAACGGCTGCTGGAAGTGAGA
GGGTCCAAGCCTGGTAAGAATGTCCAGCTTCAGGAGAATGAAATCAGAGGACTGTGCTTA
AAGTCTCGTGAAATCTTTCTCAGTCAGCCTATCCTACTAGAACTTGAAGCACCACTCAAA
ATATGTGGTGACATCCATGGACAATACTATGATTTGCTGCGACTTTTTGAGTACGGTGGT
TTCCCACCAGAAAGCAACTACCTGTTTCTTGGGGACTATGTGGACAGGGGAAAGCAGTCA
TTGGAGACGATCTGCCTCTTACTGGCCTACAAAATAAAATATCCTGAGAATTTTTTTCTT
CTCAGAGGGAACCATGAATGTGCCAGCATCAACAGAATTTATGGATTTTATGATGAATGT
AAAAGAAGATACAACATTAAACTATGGAAAACTTTCACAGACTGTTTTAACTGTTTACCG
ATAGCAGCCATCGTGGATGAGAAGATATTCTGCTGTCATGGAGGTTTATCACCAGATCTT
CAATCTATGGAGCAGATTCGGCGAATTATGCGACCAACTGATGTACCAGATCAAGGTCTT
CTTTGTGATCTTTTGTGGTCTGACCCCGATAAAGATGTCTTAGGCTGGGGTGAAAATGAC
AGAGGAGTGTCCTTCACATTTGGTGCAGAAGTGGTTGCAAAATTTCTCCATAAGCATGAT
TTGGATCTTATATGTAGAGCCCATCAGGTGGTTGAAGATGGATATGAATTTTTTGCAAAG
AGGCAGTTGGTCACTCTGTTTTCTGCGCCCAATTATTGCGGAGAGTTTGACAATGCAGGT
GCCATGATGAGTGTGGATGAAACACTAATGTGTTCTTTTCAGATTTTAAAGCCTGCAGAG
AAAAAGAAGCCAAATGCCACGAGACCTGTAACGCCTCCAAGGGGTATGATCACAAAGCAA
GCAAAGAAATAG
|
| Enzyme 6 GenBank Gene ID |
X74008  |
| Enzyme 6 GeneCard ID |
PPP1CC  |
| Enzyme 6 GenAtlas ID |
PPP1CC  |
| Enzyme 6 HGNC ID |
HGNC:9283  |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
12q24.1-q24.2 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Barker HM, Craig SP, Spurr NK, Cohen PT: Sequence of human protein serine/threonine phosphatase 1 gamma and localization of the gene (PPP1CC) encoding it to chromosome bands 12q24.1-q24.2. Biochim Biophys Acta. 1993 Aug 18;1178(2):228-33. [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
]
- Norman SA, Mott DM: Molecular cloning and chromosomal localization of a human skeletal muscle PP-1 gamma 1 cDNA. Mamm Genome. 1994 Jan;5(1):41-5. [PubMed
]
- MacKintosh RW, Dalby KN, Campbell DG, Cohen PT, Cohen P, MacKintosh C: The cyanobacterial toxin microcystin binds covalently to cysteine-273 on protein phosphatase 1. FEBS Lett. 1995 Sep 11;371(3):236-40. [PubMed
]
- Armstrong CG, Browne GJ, Cohen P, Cohen PT: PPP1R6, a novel member of the family of glycogen-targetting subunits of protein phosphatase 1. FEBS Lett. 1997 Nov 24;418(1-2):210-4. [PubMed
]
- Trinkle-Mulcahy L, Sleeman JE, Lamond AI: Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells. J Cell Sci. 2001 Dec;114(Pt 23):4219-28. [PubMed
]
- Connor JH, Weiser DC, Li S, Hallenbeck JM, Shenolikar S: Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1. Mol Cell Biol. 2001 Oct;21(20):6841-50. [PubMed
]
- Ceulemans H, Vulsteke V, De Maeyer M, Tatchell K, Stalmans W, Bollen M: Binding of the concave surface of the Sds22 superhelix to the alpha 4/alpha 5/alpha 6-triangle of protein phosphatase-1. J Biol Chem. 2002 Dec 6;277(49):47331-7. Epub 2002 Sep 10. [PubMed
]
- Trinkle-Mulcahy L, Andrews PD, Wickramasinghe S, Sleeman J, Prescott A, Lam YW, Lyon C, Swedlow JR, Lamond AI: Time-lapse imaging reveals dynamic relocalization of PP1gamma throughout the mammalian cell cycle. Mol Biol Cell. 2003 Jan;14(1):107-17. [PubMed
]
- Boyce M, Bryant KF, Jousse C, Long K, Harding HP, Scheuner D, Kaufman RJ, Ma D, Coen DM, Ron D, Yuan J: A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress. Science. 2005 Feb 11;307(5711):935-9. [PubMed
]
- Trinkle-Mulcahy L, Andersen J, Lam YW, Moorhead G, Mann M, Lamond AI: Repo-Man recruits PP1 gamma to chromatin and is essential for cell viability. J Cell Biol. 2006 Feb 27;172(5):679-92. Epub 2006 Feb 21. [PubMed
]
- Gunawardena SR, Ruis BL, Meyer JA, Kapoor M, Conklin KF: NOM1 targets protein phosphatase I to the nucleolus. J Biol Chem. 2008 Jan 4;283(1):398-404. Epub 2007 Oct 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
]
- Fujiki R, Chikanishi T, Hashiba W, Ito H, Takada I, Roeder RG, Kitagawa H, Kato S: GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis. Nature. 2009 May 21;459(7245):455-9. Epub 2009 Apr 19. [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
]
- Egloff MP, Cohen PT, Reinemer P, Barford D: Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate. J Mol Biol. 1995 Dec 15;254(5):942-59. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
7564 |
| Enzyme 7 Name |
Alpha-amylase 1 |
| Enzyme 7 Synonyms |
- 1,4-alpha-D-glucan glucanohydrolase 1
- Salivary alpha-amylase
|
| Enzyme 7 Gene Name |
AMY1A |
| Enzyme 7 Protein Sequence |
>Alpha-amylase 1
MKLFWLLFTIGFCWAQYSSNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPP
NENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGN
AVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLSGL
LDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNWFPEG
SKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWG
FMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWP
RYFENGKDVNDWVGPPNDNGVTKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVVDGQP
FTNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISGDKINGNCTGI
KIYVSDDGKAHFSISNSAEDPFIAIHAESKL
|
| Enzyme 7 Number of Residues |
511 |
| Enzyme 7 Molecular Weight |
57767.5 |
| Enzyme 7 Theoretical pI |
6.92 |
| Enzyme 7 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- ion binding
|
| Process |
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 7 General Function |
Involved in catalytic activity |
| Enzyme 7 Specific Function |
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides |
| Enzyme 7 Pathways |
- Starch and Sucrose Metabolism (map00500
)
|
| Enzyme 7 Reactions |
- Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units ALL_REAC (other) R02108 R06209(G)
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
Not Available |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P04745  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
AMY1_HUMAN  |
| Enzyme 7 PDB ID |
1MFV  |
| Enzyme 7 PDB File |
Show |
| Enzyme 7 3D Structure |
|
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>1536 bp
ATGAAGCTCTTTTGGTTGCTTTTCACCATTGGGTTCTGCTGGGCTCAGTATTCCTCAAAT
ACACAACAAGGACGAACATCTATTGTTCATCTGTTTGAATGGCGATGGGTTGATATTGCT
CTTGAATGTGAGCGATATTTAGCTCCCAAGGGATTTGGAGGGGTTCAGGTCTCTCCACCA
AATGAAAATGTTGCCATTCACAACCCTTTCAGACCTTGGTGGGAAAGATACCAACCAGTT
AGCTATAAATTATGCACAAGATCTGGAAATGAAGATGAATTTAGAAACATGGTGACTAGA
TGCAACAATGTTGGGGTTCGTATTTATGTGGATGCTGTAATTAATCATATGTGTGGTAAT
GCTGTGAGTGCAGGAACAAGCAGTACCTGTGGAAGTTACTTCAACCCTGGAAGTAGGGAC
TTTCCAGCAGTCCCATATTCTGGATGGGATTTTAATGATGGTAAATGTAAAACTGGAAGT
GGAGATATCGAGAACTATAATGATGCTACTCAGGTCAGAGATTGTCGTCTGTCTGGTCTT
CTCGATCTTGCACTGGGGAAGGATTATGTGCGTTCTAAGATTGCCGAATATATGAACCAT
CTCATTGACATTGGTGTTGCAGGGTTCAGAATTGATGCTTCCAAGCACATGTGGCCTGGA
GACATAAAGGCAATTTTGGACAAACTGCATAATCTAAACAGTAACTGGTTCCCGGAAGGT
AGTAAACCTTTCATTTACCAGGAGGTAATTGATCTGGGTGGTGAGCCAATTAAAAGCAGT
GACTACTTTGGTAATGGCCGGGTGACAGAATTCAAGTATGGTGCAAAACTCGGCACAGTT
ATTCGCAAGTGGAATGGAGAGAAGATGTCTTACTTAAAGAACTGGGGAGAAGGTTGGGGT
TTCATGCCTTCTGACAGAGCGCTTGTCTTTGTGGATAACCATGACAATCAACGAGGACAT
GGCGCTGGAGGAGCCTCTATACTTACCTTCTGGGATGCTAGGCTGTACAAAATGGCAGTT
GGATTTATGCTTGCTCATCCTTATGGATTTACACGAGTAATGTCAAGCTACCGTTGGCCA
AGATATTTTGAAAATGGAAAAGATGTTAATGATTGGGTTGGGCCACCAAATGATAATGGA
GTAACTAAAGAAGTTACTATTAATCCAGACACTACTTGTGGCAATGACTGGGTCTGTGAA
CATCGATGGCGCCAAATAAGGAACATGGTTAATTTCCGCAATGTAGTGGATGGCCAGCCT
TTTACAAACTGGTATGATAATGGGAGCAACCAAGTGGCTTTTGGGAGAGGAAACAGAGGA
TTCATTGTTTTCAACAATGATGACTGGACATTTTCTTTAACTTTGCAAACTGGTCTTCCT
GCTGGCACATACTGTGATGTCATTTCTGGAGATAAAATTAATGGCAACTGCACAGGCATT
AAAATCTACGTTTCTGATGATGGCAAAGCTCATTTTTCTATTAGTAACTCTGCTGAAGAT
CCATTTATTGCAATTCATGCTGAATCTAAATTGTAA
|
| Enzyme 7 GenBank Gene ID |
AK292341  |
| Enzyme 7 GeneCard ID |
AMY1A  |
| Enzyme 7 GenAtlas ID |
AMY1A  |
| Enzyme 7 HGNC ID |
HGNC:474  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
1p21 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Nishide T, Nakamura Y, Emi M, Yamamoto T, Ogawa M, Mori T, Matsubara K: Primary structure of human salivary alpha-amylase gene. Gene. 1986;41(2-3):299-304. [PubMed
]
- Nishide T, Emi M, Nakamura Y, Matsubara K: Corrected sequences of cDNAs for human salivary and pancreatic alpha-amylases [corrected] Gene. 1984 May;28(2):263-70. [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
]
- 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
]
- Gumucio DL, Wiebauer K, Caldwell RM, Samuelson LC, Meisler MH: Concerted evolution of human amylase genes. Mol Cell Biol. 1988 Mar;8(3):1197-205. [PubMed
]
- Handy DE, Larsen SH, Karn RC, Hodes ME: Identification of a human salivary amylase gene. Partial sequence of genomic DNA suggests a mode of regulation different from that of mouse, Amy1. Mol Biol Med. 1987 Jun;4(3):145-55. [PubMed
]
- Bank RA, Hettema EH, Arwert F, Amerongen AV, Pronk JC: Electrophoretic characterization of posttranslational modifications of human parotid salivary alpha-amylase. Electrophoresis. 1991 Jan;12(1):74-9. [PubMed
]
- Ramachandran P, Boontheung P, Xie Y, Sondej M, Wong DT, Loo JA: Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry. J Proteome Res. 2006 Jun;5(6):1493-503. [PubMed
]
- Ramasubbu N, Paloth V, Luo Y, Brayer GD, Levine MJ: Structure of human salivary alpha-amylase at 1.6 A resolution: implications for its role in the oral cavity. Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):435-46. [PubMed
]
- Ramasubbu N, Ragunath C, Mishra PJ: Probing the role of a mobile loop in substrate binding and enzyme activity of human salivary amylase. J Mol Biol. 2003 Jan 31;325(5):1061-76. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
8603 |
| Enzyme 8 Name |
Maltase-glucoamylase, intestinal |
| Enzyme 8 Synonyms |
- Maltase
- Alpha-glucosidase
- Glucoamylase
- Glucan 1,4-alpha-glucosidase
|
| Enzyme 8 Gene Name |
MGAM |
| Enzyme 8 Protein Sequence |
>Maltase-glucoamylase, intestinal
MARKKLKKFTTLEIVLSVLLLVLFIISIVLIVLLAKESLKSTAPDPGTTGTPDPGTTGTP
DPGTTGTTHARTTGPPDPGTTGTTPVSAECPVVNELERINCIPDQPPTKATCDQRGCCWN
PQGAVSVPWCYYSKNHSYHVEGNLVNTNAGFTARLKNLPSSPVFGSNVDNVLLTAEYQTS
NRFHFKLTDQTNNRFEVPHEHVQSFSGNAAASLTYQVEISRQPFSIKVTRRSNNRVLFDS
SIGPLLFADQFLQLSTRLPSTNVYGLGEHVHQQYRHDMNWKTWPIFNRDTTPNGNGTNLY
GAQTFFLCLEDASGLSFGVFLMNSNAMEVVLQPAPAITYRTIGGILDFYVFLGNTPEQVV
QEYLELIGRPALPSYWALGFHLSRYEYGTLDNMREVVERNRAAQLPYDVQHADIDYMDER
RDFTYDSVDFKGFPEFVNELHNNGQKLVIIVDPAISNNSSSSKPYGPYDRGSDMKIWVNS
SDGVTPLIGEVWPGQTVFPDYTNPNCAVWWTKEFELFHNQVEFDGIWIDMNEVSNFVDGS
VSGCSTNNLNNPPFTPRILDGYLFCKTLCMDAVQHWGKQYDIHNLYGYSMAVATAEAAKT
VFPNKRSFILTRSTFAGSGKFAAHWLGDNTATWDDLRWSIPGVLEFNLFGIPMVGPDICG
FALDTPEELCRRWMQLGAFYPFSRNHNGQGYKDQDPASFGADSLLLNSSRHYLNIRYTLL
PYLYTLFFRAHSRGDTVARPLLHEFYEDNSTWDVHQQFLWGPGLLITPVLDEGAEKVMAY
VPDAVWYDYETGSQVRWRKQKVEMELPGDKIGLHLRGGYIFPTQQPNTTTLASRKNPLGL
IIALDENKEAKGELFWDNGETKDTVANKVYLLCEFSVTQNRLEVNISQSTYKDPNNLAFN
EIKILGTEEPSNVTVKHNGVPSQTSPTVTYDSNLKVAIITDIDLLLGEAYTVEWSIKIRD
EEKIDCYPDENGASAENCTARGCIWEASNSSGVPFCYFVNDLYSVSDVQYNSHGATADIS
LKSSVYANAFPSTPVNPLRLDVTYHKNEMLQFKIYDPNKNRYEVPVPLNIPSMPSSTPEG
QLYDVLIKKNPFGIEIRRKSTGTIIWDSQLLGFTFSDMFIRISTRLPSKYLYGFGETEHR
SYRRDLEWHTWGMFSRDQPPGYKKNSYGVHPYYMGLEEDGSAHGVLLLNSNAMDVTFQPL
PALTYRTTGGVLDFYVFLGPTPELVTQQYTELIGRPVMVPYWSLGFQLCRYGYQNDSEIA
SLYDEMVAAQIPYDVQYSDIDYMERQLDFTLSPKFAGFPALINRMKADGMRVILILDPAI
SGNETQPYPAFTRGVEDDVFIKYPNDGDIVWGKVWPDFPDVVVNGSLDWDSQVELYRAYV
AFPDFFRNSTAKWWKREIEELYNNPQNPERSLKFDGMWIDMNEPSSFVNGAVSPGCRDAS
LNHPPYMPHLESRDRGLSSKTLCMESQQILPDGSLVQHYNVHNLYGWSQTRPTYEAVQEV
TGQRGVVITRSTFPSSGRWAGHWLGDNTAAWDQLKKSIIGMMEFSLFGISYTGADICGFF
QDAEYEMCVRWMQLGAFYPFSRNHNTIGTRRQDPVSWDVAFVNISRTVLQTRYTLLPYLY
TLMHKAHTEGVTVVRPLLHEFVSDQVTWDIDSQFLLGPAFLVSPVLERNARNVTAYFPRA
RWYDYYTGVDINARGEWKTLPAPLDHINLHVRGGYILPWQEPALNTHLSRQKFMGFKIAL
DDEGTAGGWLFWDDGQSIDTYGKGLYYLASFSASQNTMQSHIIFNNYITGTNPLKLGYIE
IWGVGSVPVTSVSISVSGMVITPSFNNDPTTQVLSIDVTDRNISLHNFTSLTWISTL
|
| Enzyme 8 Number of Residues |
1857 |
| Enzyme 8 Molecular Weight |
209850.8 |
| Enzyme 8 Theoretical pI |
5.17 |
| Enzyme 8 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
|
| Process |
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 8 General Function |
Involved in catalytic activity |
| Enzyme 8 Specific Function |
May serve as an alternate pathway for starch digestion when luminal alpha-amylase activity is reduced because of immaturity or malnutrition. May play a unique role in the digestion of malted dietary oligosaccharides used in food manufacturing |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of D-glucose ALL_REAC (other) R00028 R00801 R00802 R06084(G) R06087(G) R06088(G) INHIBITOR Castanospermine [CPD:C02256]
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
221316699  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
O43451  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
MGA_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>5574 bp
ATGGCAAGAAAGAAGCTGAAAAAATTTACTACTTTGGAGATTGTGCTCAGTGTTCTTCTG
CTTGTGTTGTTTATCATCAGTATTGTTCTAATTGTGCTTTTAGCCAAAGAGTCACTGAAA
TCAACAGCCCCAGATCCTGGGACAACTGGTACCCCAGATCCTGGGACAACTGGTACCCCA
GATCCTGGAACAACTGGTACCACACATGCTAGGACAACGGGTCCCCCAGATCCTGGAACA
ACTGGTACCACTCCTGTTTCTGCTGAATGTCCAGTGGTAAATGAATTGGAACGAATTAAT
TGCATCCCTGACCAGCCGCCAACAAAGGCCACATGTGACCAACGTGGCTGTTGCTGGAAT
CCCCAGGGAGCTGTAAGTGTTCCCTGGTGCTACTATTCCAAGAATCATAGCTACCATGTA
GAGGGCAACCTTGTCAACACAAATGCAGGATTCACAGCCCGGTTGAAAAATCTGCCTTCT
TCACCAGTGTTTGGAAGCAATGTTGACAATGTTCTTCTCACAGCAGAATATCAGACATCT
AATCGTTTCCACTTTAAGTTGACTGACCAAACCAATAACAGGTTTGAAGTGCCCCACGAA
CACGTGCAGTCCTTCAGTGGAAATGCTGCTGCTTCTTTGACCTACCAAGTTGAAATCTCC
AGACAGCCATTTAGCATCAAAGTGACCAGAAGAAGCAACAATCGTGTTTTGTTTGACTCG
AGCATTGGGCCCCTACTGTTTGCTGACCAGTTCTTGCAGCTCTCCACTCGACTGCCTAGC
ACTAACGTGTATGGCCTGGGAGAGCATGTGCACCAGCAGTATCGGCATGATATGAATTGG
AAGACCTGGCCCATATTTAACAGAGACACAACTCCCAATGGAAACGGAACTAATTTGTAT
GGTGCGCAGACATTCTTCTTGTGCCTTGAAGATGCTAGTGGATTGTCCTTTGGGGTGTTT
CTGATGAACAGCAATGCCATGGAGGTTGTCCTTCAGCCTGCGCCAGCCATCACTTACCGC
ACCATTGGGGGCATTCTCGACTTCTATGTGTTCTTGGGAAACACTCCAGAGCAAGTTGTT
CAAGAATATCTAGAGCTCATTGGGCGGCCAGCCCTTCCCTCCTACTGGGCGCTTGGATTT
CACCTCAGTCGTTACGAATATGGAACCTTAGACAACATGAGGGAAGTCGTGGAGAGAAAT
CGCGCAGCACAGCTCCCTTATGATGTTCAGCATGCTGATATTGATTATATGGATGAGAGA
AGGGACTTCACTTATGATTCAGTGGATTTTAAAGGCTTCCCTGAATTTGTCAACGAGTTA
CACAATAATGGACAGAAGCTTGTCATCATTGTGGATCCAGCCATCTCCAACAACTCTTCC
TCAAGTAAACCCTATGGCCCATATGACAGGGGTTCAGATATGAAGATATGGGTGAATAGT
TCAGATGGAGTGACTCCACTCATTGGGGAGGTCTGGCCTGGACAAACTGTGTTTCCTGAT
TATACCAATCCCAACTGTGCTGTTTGGTGGACAAAGGAATTTGAGCTTTTTCACAATCAA
GTAGAGTTTGATGGAATCTGGATTGATATGAATGAAGTCTCCAACTTTGTTGATGGTTCG
GTCTCAGGATGTTCCACAAACAACCTAAATAATCCCCCATTCACTCCCAGAATCCTGGAT
GGGTACCTGTTCTGCAAGACTCTCTGTATGGATGCAGTGCAGCACTGGGGCAAGCAGTAT
GACATTCACAATCTGTATGGCTACTCCATGGCGGTCGCCACAGCAGAAGCTGCCAAGACT
GTGTTCCCTAATAAGAGAAGCTTCATTCTGACCCGTTCTACCTTTGCGGGCTCTGGCAAG
TTTGCAGCACATTGGTTAGGAGACAACACTGCCACCTGGGATGACCTGAGATGGTCCATC
CCTGGCGTGCTTGAGTTCAACCTTTTTGGCATCCCAATGGTGGGTCCTGACATATGTGGC
TTTGCTTTGGACACCCCTGAGGAGCTCTGTAGGCGGTGGATGCAGTTGGGTGCATTTTAT
CCGTTTTCTAGAAATCACAATGGCCAAGGCTACAAGGACCAGGATCCTGCCTCCTTTGGA
GCTGACTCCCTGCTGTTGAATTCCTCCAGGCACTACCTTAACATCCGCTATACTCTATTG
CCCTACCTATACACCCTCTTCTTCCGTGCTCACAGCCGAGGGGACACGGTGGCCAGGCCC
CTTTTGCATGAGTTCTACGAGGACAACAGCACTTGGGATGTGCACCAACAGTTCTTATGG
GGGCCCGGCCTCCTCATCACTCCAGTTCTGGATGAAGGTGCAGAGAAAGTGATGGCATAT
GTGCCTGATGCTGTCTGGTATGACTACGAGACTGGGAGCCAAGTGAGATGGAGGAAGCAA
AAAGTCGAGATGGAACTTCCTGGAGACAAAATTGGACTTCACCTTCGAGGAGGCTACATC
TTCCCCACACAGCAGCCAAATACAACCACTCTGGCCAGTCGAAAGAACCCTCTTGGTCTT
ATCATTGCCCTAGATGAGAACAAAGAAGCAAAAGGAGAACTTTTCTGGGATAATGGGGAA
ACGAAGGATACTGTGGCCAATAAAGTGTATCTTTTATGTGAGTTTTCTGTCACTCAAAAC
CGCTTGGAGGTGAATATTTCACAATCAACCTACAAGGACCCCAATAATTTAGCATTTAAT
GAGATTAAAATTCTTGGGACGGAGGAACCTAGCAATGTTACAGTGAAACACAATGGTGTC
CCAAGTCAGACTTCTCCTACAGTCACTTATGATTCTAACCTGAAGGTTGCCATTATCACA
GATATTGATCTTCTCCTGGGAGAAGCATACACAGTGGAATGGAGCATAAAGATAAGGGAT
GAAGAAAAAATAGACTGTTACCCTGATGAGAATGGTGCTTCTGCCGAAAACTGCACTGCC
CGTGGCTGTATCTGGGAGGCATCCAATTCTTCTGGAGTCCCTTTTTGCTATTTTGTCAAC
GACCTATACTCTGTCAGTGATGTTCAGTATAATTCCCATGGGGCCACAGCTGACATCTCC
TTAAAGTCTTCCGTTTATGCCAATGCCTTCCCCTCCACACCCGTGAACCCCCTTCGCCTG
GATGTCACTTACCATAAGAATGAAATGCTGCAGTTCAAGATTTATGATCCCAACAAGAAT
CGGTATGAAGTTCCAGTCCCTCTGAACATACCCAGCATGCCATCCAGCACCCCTGAGGGT
CAACTCTATGATGTGCTCATTAAGAAGAATCCATTTGGGATTGAAATTCGCCGGAAGAGT
ACAGGCACTATAATTTGGGACTCTCAGCTCCTTGGCTTTACCTTCAGTGACATGTTTATC
CGCATCTCCACCCGCCTTCCCTCCAAGTACCTCTATGGCTTTGGGGAAACTGAGCACAGG
TCCTATAGGAGAGACTTGGAGTGGCACACTTGGGGGATGTTCTCCCGAGACCAGCCCCCA
GGGTACAAGAAGAATTCCTATGGTGTCCACCCCTACTACATGGGGCTGGAGGAGGACGGC
AGTGCCCATGGAGTGCTCCTGCTGAACAGCAATGCCATGGATGTGACGTTCCAGCCCCTG
CCTGCCTTGACATACCGCACCACAGGGGGAGTTCTGGACTTTTATGTGTTCTTGGGGCCG
ACTCCAGAGCTTGTCACCCAGCAGTACACTGAGTTGATTGGCCGGCCTGTGATGGTACCT
TACTGGTCTTTGGGGTTCCAGCTGTGTCGCTATGGCTACCAGAATGACTCTGAGATCGCC
AGCTTGTATGATGAGATGGTGGCTGCCCAGATCCCTTATGATGTGCAGTACTCAGACATC
GACTACATGGAGCGGCAGCTGGACTTCACCCTCAGCCCCAAGTTTGCTGGGTTTCCAGCT
CTGATCAATCGCATGAAGGCTGATGGGATGCGGGTCATCCTCATTCTGGATCCAGCCATT
TCTGGCAATGAGACACAGCCTTATCCTGCCTTCACTCGGGGCGTGGAGGATGACGTCTTC
ATCAAATACCCAAATGATGGAGACATTGTCTGGGGAAAGGTCTGGCCTGATTTTCCTGAT
GTTGTTGTGAATGGGTCTCTAGACTGGGACAGCCAAGTGGAGCTATATCGAGCTTATGTG
GCCTTCCCAGACTTTTTCCGTAATTCAACTGCCAAGTGGTGGAAGAGGGAAATAGAAGAA
CTATACAACAATCCACAGAATCCAGAGAGGAGCTTGAAGTTTGATGGCATGTGGATTGAT
ATGAATGAACCATCAAGCTTCGTGAATGGGGCAGTTTCTCCAGGCTGCAGGGACGCCTCT
CTGAACCACCCTCCCTACATGCCACATTTGGAGTCCAGGGACAGGGGCCTGAGCAGCAAG
ACCCTTTGTATGGAGAGTCAGCAGATCCTCCCAGACGGCTCCCTGGTGCAGCACTACAAC
GTGCACAACCTGTATGGGTGGTCCCAGACCAGACCCACATACGAAGCCGTGCAGGAGGTG
ACGGGACAGCGAGGGGTCGTCATCACCCGCTCCACATTTCCCTCTTCTGGCCGCTGGGCA
GGACATTGGCTGGGAGACAACACGGCCGCATGGGATCAGCTGAAGAAGTCTATCATTGGC
ATGATGGAGTTCAGCCTCTTCGGCATATCCTATACGGGAGCAGATATCTGTGGGTTCTTT
CAAGATGCTGAATATGAGATGTGTGTTCGCTGGATGCAGCTGGGGGCCTTTTACCCCTTC
TCAAGAAACCACAACACCATTGGGACCAGGAGACAAGACCCTGTGTCCTGGGATGTTGCT
TTTGTGAATATTTCCAGAACTGTCCTGCAGACCAGATACACCCTGTTGCCATATCTGTAT
ACCTTGATGCATAAGGCCCACACGGAGGGCGTCACTGTTGTGCGGCCTCTGCTCCATGAG
TTTGTGTCAGACCAGGTGACATGGGACATAGACAGTCAGTTCCTGCTGGGCCCAGCCTTC
CTGGTCAGCCCTGTCCTGGAGCGTAATGCCAGAAATGTCACTGCATATTTCCCTAGAGCC
CGCTGGTATGATTACTACACGGGTGTGGATATTAATGCAAGAGGAGAGTGGAAGACCTTG
CCAGCCCCTCTTGACCACATTAATCTTCATGTCCGTGGGGGCTACATCCTGCCCTGGCAA
GAGCCTGCACTGAACACCCACTTAAGCCGCCAGAAATTCATGGGCTTCAAAATTGCCTTG
GATGATGAAGGAACTGCTGGGGGCTGGCTCTTCTGGGATGATGGGCAAAGCATTGATACC
TATGGGAAAGGACTCTATTACTTGGCCAGCTTTTCTGCCAGCCAGAATACGATGCAAAGC
CATATAATTTTCAACAATTACATCACTGGTACAAATCCTTTGAAACTGGGCTACATTGAA
ATCTGGGGAGTGGGCAGTGTCCCCGTTACCAGTGTCAGCATCTCTGTGAGTGGCATGGTC
ATAACACCCTCCTTCAACAATGACCCCACGACACAGGTATTAAGCATCGATGTGACTGAC
AGAAACATCAGCCTACATAATTTTACTTCATTGACGTGGATAAGCACTCTGTGA
|
| Enzyme 8 GenBank Gene ID |
NM_004668.2  |
| Enzyme 8 GeneCard ID |
MGAM  |
| Enzyme 8 GenAtlas ID |
MGAM  |
| Enzyme 8 HGNC ID |
HGNC:7043  |
| Enzyme 8 Chromosome Location |
7 |
| Enzyme 8 Locus |
7q34 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Nichols BL, Eldering J, Avery S, Hahn D, Quaroni A, Sterchi E: Human small intestinal maltase-glucoamylase cDNA cloning. Homology to sucrase-isomaltase. J Biol Chem. 1998 Jan 30;273(5):3076-81. [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
]
- Naim HY, Sterchi EE, Lentze MJ: Structure, biosynthesis, and glycosylation of human small intestinal maltase-glucoamylase. J Biol Chem. 1988 Dec 25;263(36):19709-17. [PubMed
]
- Danielsen EM: Tyrosine sulfation, a post-translational modification of microvillar enzymes in the small intestinal enterocyte. EMBO J. 1987 Oct;6(10):2891-6. [PubMed
]
- Sim L, Quezada-Calvillo R, Sterchi EE, Nichols BL, Rose DR: Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity. J Mol Biol. 2008 Jan 18;375(3):782-92. Epub 2007 Nov 1. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
13111 |
| Enzyme 9 Name |
Glucan , branching enzyme 1 variant |
| Enzyme 9 Synonyms |
Not Available |
| Enzyme 9 Gene Name |
Not Available |
| Enzyme 9 Protein Sequence |
>Glucan , branching enzyme 1 variant
RAPDRRGSPRLASTRLGALRLRPSRRVPARAPAPAQAPLDPLGPRLLGLRRNMAAPMTPA
ARPEDYEAALNAALADVPELARLLEIDPYLKPYAVDFQRRYKQFSQILKNIGENEGGIDK
FSRGYESFGVHRCADGGLYCKEWAPGAEGVFLTGDFNGWNPFSYPYKKLDYGKWELYIPP
KQNKSVLVPHGSKLKVVITSKSGEILYRISPWAKYVVREGDNVNYDWIHWDPEHSYEFKH
SRPKKPRSLRIYESHVGISSHEGKVASYKHFTCNVLPRIKGLGYNCIQLMAIMEHAYYAS
FGYQITSFFAASSRYGTPEELQELVDTAHSMGIIVLLDVVHSHASKNSADGLNMFDGTDS
CYFHSGPRGTHDLWDSRLFAYSSWEVLRFLLSNIRWWLEEYRFDGFRFDGVTSMLYHHHG
VGQGFSGDYSEYFGLQVDEDALTYLMLANHLVHTLCPDSITIAEDVSGMPALCSPISQGG
GGFDYRLAMAIPDKWIQLLKEFKDEDWNMGDIVYTLTNRRYLEKCIAYAESHDQALVGDK
SLAFWLMDAEMYTNMSVLTPFTPVIDRGIQLHKMIRLITHGLGGEGYLNFMGNEFGHPEW
LDFPRKGNNESYHYARRQFHLTDDDLLRYKFLNNFDRDMNRLEERYGWLAAPQAYVSEKH
EGNKIIAFERAGLLFIFNFHPSKSYTDYRVGTALPGKFKIVLDSDAAEYGGHQRLDHSTD
FFSEAFEHNGRPYSLLVYIPSRVALILQNVDLPN
|
| Enzyme 9 Number of Residues |
754 |
| Enzyme 9 Molecular Weight |
86112.7 |
| Enzyme 9 Theoretical pI |
6.93 |
| Enzyme 9 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
- ion binding
|
| Process |
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 9 General Function |
Involved in catalytic activity |
| Enzyme 9 Specific Function |
Not Available |
| Enzyme 9 Pathways |
Not Available |
| Enzyme 9 Reactions |
Not Available |
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
62089042  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q59ET0  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
Q59ET0_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>2265 bp
AGGGCCCCGGACCGCCGCGGCTCGCCTCGGCTTGCCTCGACACGCCTAGGCGCCCTCCGG
CTCCGCCCTAGCCGCCGCGTCCCAGCTAGAGCTCCAGCGCCCGCTCAGGCCCCACTCGAC
CCTCTCGGGCCTCGGCTACTTGGACTGCGGCGGAATATGGCGGCTCCGATGACTCCCGCG
GCTCGGCCCGAGGACTACGAGGCGGCGCTCAATGCCGCCCTGGCTGACGTGCCCGAACTG
GCCAGACTCCTGGAGATCGACCCGTACTTGAAGCCCTACGCCGTGGACTTCCAGCGCAGG
TATAAGCAGTTTAGCCAAATTTTGAAGAACATTGGAGAAAATGAAGGTGGTATTGATAAG
TTTTCCAGAGGCTATGAATCATTTGGCGTCCACAGATGTGCTGATGGTGGTTTATACTGC
AAAGAATGGGCCCCGGGAGCAGAAGGAGTTTTTCTTACTGGAGATTTTAATGGTTGGAAT
CCATTTTCGTACCCATACAAAAAACTGGATTATGGAAAATGGGAGCTGTATATCCCACCA
AAGCAGAATAAATCTGTACTCGTGCCTCATGGATCCAAATTAAAGGTAGTTATTACTAGT
AAAAGCGGAGAGATCTTGTATCGTATTTCACCGTGGGCAAAGTATGTGGTTCGTGAAGGT
GATAATGTGAATTATGATTGGATACACTGGGATCCAGAACACTCATATGAGTTTAAGCAT
TCCAGACCAAAGAAGCCACGGAGTCTAAGAATTTATGAATCTCATGTGGGAATTTCTTCC
CATGAAGGAAAAGTAGCTTCTTATAAACATTTTACATGCAATGTACTACCAAGAATCAAA
GGCCTTGGATACAACTGCATTCAGTTGATGGCAATCATGGAGCATGCTTACTATGCCAGC
TTTGGTTACCAAATCACAAGCTTCTTTGCAGCTTCCAGCCGTTATGGAACACCTGAAGAG
CTACAAGAACTGGTAGACACAGCTCATTCCATGGGTATCATAGTCCTCTTAGATGTGGTA
CACAGCCATGCTTCAAAAAATTCAGCAGATGGATTGAATATGTTTGATGGGACAGATTCC
TGTTATTTTCATTCTGGACCTAGAGGGACTCATGATCTTTGGGATAGCAGATTGTTTGCC
TACTCCAGCTGGGAAGTTTTAAGATTCCTTCTGTCAAACATAAGATGGTGGTTGGAAGAA
TATCGCTTTGATGGATTTCGTTTTGATGGTGTTACGTCCATGCTTTATCATCACCATGGA
GTGGGTCAAGGTTTCTCAGGTGATTACAGTGAATATTTCGGACTACAAGTAGATGAAGAT
GCCTTGACTTACCTCATGTTGGCAAATCATTTGGTTCACACGCTGTGTCCCGATTCTATA
ACAATAGCTGAGGATGTATCAGGAATGCCAGCTCTGTGCTCTCCAATTTCCCAGGGAGGG
GGTGGTTTTGACTATCGACTAGCCATGGCAATTCCAGATAAGTGGATTCAGCTACTTAAA
GAGTTTAAAGATGAAGACTGGAACATGGGCGATATAGTATACACGCTCACAAACAGGCGC
TACCTTGAAAAGTGCATTGCTTATGCAGAGAGCCATGATCAGGCATTGGTTGGGGATAAG
TCGCTGGCATTTTGGTTGATGGATGCCGAAATGTATACAAACATGAGTGTCCTGACTCCT
TTTACTCCAGTTATTGATCGTGGAATACAGCTTCATAAAATGATTCGACTCATTACGCAT
GGGCTTGGTGGAGAAGGCTATCTCAATTTCATGGGTAATGAATTTGGGCATCCTGAATGG
TTAGACTTCCCAAGAAAAGGAAATAATGAGAGTTACCATTATGCCAGGCGGCAGTTTCAT
TTAACTGACGACGACCTTCTTCGCTACAAGTTCCTAAATAATTTTGACAGGGATATGAAT
AGATTGGAAGAAAGATATGGTTGGCTTGCAGCTCCACAGGCCTACGTGAGTGAAAAACAT
GAAGGCAATAAGATCATTGCTTTTGAAAGAGCAGGTCTTCTTTTCATTTTCAACTTCCAT
CCAAGCAAGAGCTACACTGACTACCGAGTTGGAACAGCATTGCCAGGGAAATTCAAAATT
GTGCTAGATTCAGATGCAGCGGAATATGGAGGGCATCAGAGACTGGACCACAGCACTGAC
TTTTTTTCTGAGGCTTTTGAACATAATGGGCGTCCCTATTCTCTTTTGGTGTACATTCCA
AGCAGAGTGGCCCTCATCCTTCAGAATGTGGATCTGCCGAATTGA
|
| Enzyme 9 GenBank Gene ID |
AB209731  |
| Enzyme 9 GeneCard ID |
Not Available |
| Enzyme 9 GenAtlas ID |
Not Available |
| Enzyme 9 HGNC ID |
HGNC:4180  |
| Enzyme 9 Chromosome Location |
Not Available |
| Enzyme 9 Locus |
Not Available |
| Enzyme 9 SNPs |
Not Available |
| Enzyme 9 General References |
Not Available |
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
14405 |
| Enzyme 10 Name |
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit |
| Enzyme 10 Synonyms |
- PP-1A
|
| Enzyme 10 Gene Name |
PPP1CA |
| Enzyme 10 Protein Sequence |
>Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
MSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLK
ICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFL
LRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDL
QSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHD
LDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAD
KNKGKYGQFSGLNPGGRPITPPRNSAKAKK
|
| Enzyme 10 Number of Residues |
330 |
| Enzyme 10 Molecular Weight |
37511.7 |
| Enzyme 10 Theoretical pI |
6.25 |
| Enzyme 10 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 10 General Function |
Involved in hydrolase activity |
| Enzyme 10 Specific Function |
Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- a phosphoprotein + H2O = a protein + phosphate [RN:R00164]
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
35451  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P62136  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
PP1A_HUMAN  |
| Enzyme 10 PDB ID |
1FJM  |
| Enzyme 10 PDB File |
Show |
| Enzyme 10 3D Structure |
|
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>993 bp
ATGTCCGACAGCGAGAAGCTCAACCTGGACTCGATCATCGGGCGCCTGCTGGAAGTGCAG
GGCTCGCGGCCTGGCAAGAATGTACAGCTGACAGAGAACGAGATCCGCGGTCTGTGCCTG
AAATCCCGGGAGATTTTTCTGAGCCAGCCCATTCTTCTGGAGCTGGAGGCACCCCTCAAG
ATCTGCGGTGACATACACGGCCAGTACTACGACCTTCTGCGACTATTTGAGTATGGCGGT
TTCCCTCCCGAGAGCAACTACCTCTTTCTGGGGGACTATGTGGACAGGGGCAAGCAGTCC
TTGGAGACCATCTGCCTGCTGCTGGCCTATAAGATCAAGTACCCCGAGAACTTCTTCCTG
CTCCGTGGGAACCACGAGTGTGCCAGCATCAACCGCATCTATGGTTTCTACGATGAGTGC
AAGAGACGCTACAACATCAAACTGTGGAAAACCTTCACTGACTGCTTCAACTGCCTGCCC
ATCGCGGCCATAGTGGACGAAAAGATCTTCTGCTGCCACGGAGGCCTGTCCCCGGACCTG
CAGTCTATGGAGCAGATTCGGCGGATCATGCGGCCCACAGATGTGCCTGACCAGGGCCTG
CTGTGTGACCTGCTGTGGTCTGACCCTGACAAGGACGTGCAGGGCTGGGGCGAGAACGAC
CGTGGCGTCTCTTTTACCTTTGGAGCCGAGGTGGTGGCCAAGTTCCTCCACAAGCACGAC
TTGGACCTCATCTGCCGAGCACACCAGGTGGTAGAAGACGGCTACGAGTTCTTTGCCAAG
CGGCAGCTGGTGACACTTTTCTCAGCTCCCAACTACTGTGGCGAGTTTGACAATGCTGGC
GCCATGATGAGTGTGGACGAGACCCTCATGTGCTCTTTCCAGATCCTCAAGCCCGCCGAC
AAGAACAAGGGGAAGTACGGGCAGTTCAGTGGCCTGAACCCTGGAGGCCGACCCATCACC
CCACCCCGCAATTCCGCCAAAGCCAAGAAATAG
|
| Enzyme 10 GenBank Gene ID |
X70848  |
| Enzyme 10 GeneCard ID |
PPP1CA  |
| Enzyme 10 GenAtlas ID |
PPP1CA  |
| Enzyme 10 HGNC ID |
HGNC:9281  |
| Enzyme 10 Chromosome Location |
1 |
| Enzyme 10 Locus |
11q13 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Song Q, Khanna KK, Lu H, Lavin MF: Cloning and characterization of a human protein phosphatase 1-encoding cDNA. Gene. 1993 Jul 30;129(2):291-5. [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
]
- Barker HM, Jones TA, da Cruz e Silva EF, Spurr NK, Sheer D, Cohen PT: Localization of the gene encoding a type I protein phosphatase catalytic subunit to human chromosome band 11q13. Genomics. 1990 Jun;7(2):159-66. [PubMed
]
- He B, Gross M, Roizman B: The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase. Proc Natl Acad Sci U S A. 1997 Feb 4;94(3):843-8. [PubMed
]
- Trinkle-Mulcahy L, Sleeman JE, Lamond AI: Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells. J Cell Sci. 2001 Dec;114(Pt 23):4219-28. [PubMed
]
- Connor JH, Weiser DC, Li S, Hallenbeck JM, Shenolikar S: Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1. Mol Cell Biol. 2001 Oct;21(20):6841-50. [PubMed
]
- Ceulemans H, Vulsteke V, De Maeyer M, Tatchell K, Stalmans W, Bollen M: Binding of the concave surface of the Sds22 superhelix to the alpha 4/alpha 5/alpha 6-triangle of protein phosphatase-1. J Biol Chem. 2002 Dec 6;277(49):47331-7. Epub 2002 Sep 10. [PubMed
]
- Cohen PT: Protein phosphatase 1--targeted in many directions. J Cell Sci. 2002 Jan 15;115(Pt 2):241-56. [PubMed
]
- Boyce M, Bryant KF, Jousse C, Long K, Harding HP, Scheuner D, Kaufman RJ, Ma D, Coen DM, Ron D, Yuan J: A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress. Science. 2005 Feb 11;307(5711):935-9. [PubMed
]
- Ulke-Lemee A, Trinkle-Mulcahy L, Chaulk S, Bernstein NK, Morrice N, Glover M, Lamond AI, Moorhead GB: The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G. Biochim Biophys Acta. 2007 Oct;1774(10):1339-50. Epub 2007 Aug 15. [PubMed
]
- Gunawardena SR, Ruis BL, Meyer JA, Kapoor M, Conklin KF: NOM1 targets protein phosphatase I to the nucleolus. J Biol Chem. 2008 Jan 4;283(1):398-404. Epub 2007 Oct 26. [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
]
- 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
]
- Fujiki R, Chikanishi T, Hashiba W, Ito H, Takada I, Roeder RG, Kitagawa H, Kato S: GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis. Nature. 2009 May 21;459(7245):455-9. Epub 2009 Apr 19. [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 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
16936 |
| Enzyme 11 Name |
Protein phosphatase 1 regulatory subunit 3C |
| Enzyme 11 Synonyms |
- Protein phosphatase 1 regulatory subunit 5
- PP1 subunit R5
- Protein targeting to glycogen
- PTG
|
| Enzyme 11 Gene Name |
PPP1R3C |
| Enzyme 11 Protein Sequence |
>Protein phosphatase 1 regulatory subunit 3C
MSCTRMIQVLDPRPLTSSVMPVDVAMRLCLAHSPPVKSFLGPYDEFQRRHFVNKLKPLKS
CLNIKHKAKSQNDWKCSHNQAKKRVVFADSKGLSLTAIHVFSDLPEEPAWDLQFDLLDLN
DISSALKHHEEKNLILDFPQPSTDYLSFRSHFQKNFVCLENCSLQERTVTGTVKVKNVSF
EKKVQIRITFDSWKNYTDVDCVYMKNVYGGTDSDTFSFAIDLPPVIPTEQKIEFCISYHA
NGQVFWDNNDGQNYRIVHVQWKPDGVQTQMAPQDCAFHQTSPKTELESTIFGSPRLASGL
FPEWQSWGRMENLASYR
|
| Enzyme 11 Number of Residues |
317 |
| Enzyme 11 Molecular Weight |
36445.2 |
| Enzyme 11 Theoretical pI |
7.52 |
| Enzyme 11 GO Classification |
Not Available |
| Enzyme 11 General Function |
Involved in protein serine/threonine phosphatase activity |
| Enzyme 11 Specific Function |
Acts as a glycogen-targeting subunit for PP1 and regulates its activity. Activates glycogen synthase, reduces glycogen phosphorylase activity and limits glycogen breakdown. Dramatically increases basal and insulin-stimulated glycogen synthesis upon overexpression in a variety of cell types |
| Enzyme 11 Pathways |
Not Available |
| Enzyme 11 Reactions |
Not Available |
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
189053715  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q9UQK1  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
PPR3C_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>954 bp
ATGAGCTGCACCAGAATGATCCAGGTTTTAGATCCACGTCCTTTGACAAGTTCGGTCATG
CCCGTGGATGTGGCCATGAGGCTTTGCTTGGCACATTCACCACCTGTGAAGAGTTTCCTG
GGCCCGTACGATGAATTTCAACGACGACATTTTGTGAATAAATTAAAGCCCCTGAAATCA
TGTCTCAATATAAAACACAAAGCCAAATCACAGAATGACTGGAAGTGCTCACACAACCAA
GCCAAGAAGCGCGTTGTGTTTGCTGACTCCAAGGGCCTCTCTCTCACTGCGATCCATGTC
TTCTCCGACCTCCCAGAAGAACCAGCGTGGGATCTGCAGTTTGATCTCTTGGACCTTAAT
GATATCTCCTCTGCCTTAAAACACCACGAGGAGAAAAACTTGATTTTAGATTTCCCTCAG
CCTTCAACCGATTACTTAAGTTTCCGGAGCCACTTTCAGAAGAACTTTGTCTGTCTGGAG
AACTGCTCGTTGCAAGAGCGAACAGTGACAGGGACTGTTAAAGTCAAAAATGTGAGTTTT
GAGAAGAAAGTTCAGATCCGTATCACTTTCGATTCTTGGAAAAACTACACTGACGTAGAC
TGTGTCTATATGAAAAATGTGTATGGTGGCACAGATAGTGATACCTTCTCATTTGCCATT
GACTTACCCCCTGTCATTCCAACTGAGCAGAAAATTGAGTTCTGCATTTCTTACCATGCT
AATGGGCAAGTCTTTTGGGACAACAATGATGGTCAGAATTATAGAATTGTTCATGTTCAA
TGGAAGCCTGATGGGGTGCAGACACAGATGGCACCCCAGGACTGTGCATTCCACCAGACG
TCTCCTAAGACAGAGTTAGAGTCAACAATCTTTGGCAGTCCGAGGCTGGCTAGTGGGCTC
TTCCCAGAGTGGCAGAGCTGGGGGAGAATGGAGAACTTGGCCTCTTATCGATGA
|
| Enzyme 11 GenBank Gene ID |
AK313149  |
| Enzyme 11 GeneCard ID |
PPP1R3C  |
| Enzyme 11 GenAtlas ID |
PPP1R3C  |
| Enzyme 11 HGNC ID |
HGNC:9293  |
| Enzyme 11 Chromosome Location |
1 |
| Enzyme 11 Locus |
10q23-q24 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Doherty MJ, Young PR, Cohen PT: Amino acid sequence of a novel protein phosphatase 1 binding protein (R5) which is related to the liver- and muscle-specific glycogen binding subunits of protein phosphatase 1. FEBS Lett. 1996 Dec 16;399(3):339-43. [PubMed
]
- Permana PA, Luczy-Bachman G, Bogardus C: Protein targeting to glycogen/PPP1R5: screening of coding and flanking genomic regions for polymorphisms and association analysis with insulin action in Pima Indians. Biochem Biophys Res Commun. 1999 Apr 29;258(1):184-6. [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
]
- 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
]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [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
]
- Fernandez-Sanchez ME, Criado-Garcia O, Heath KE, Garcia-Fojeda B, Medrano-Fernandez I, Gomez-Garre P, Sanz P, Serratosa JM, Rodriguez de Cordoba S: Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation. Hum Mol Genet. 2003 Dec 1;12(23):3161-71. Epub 2003 Oct 7. [PubMed
]
- Worby CA, Gentry MS, Dixon JE: Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG). J Biol Chem. 2008 Feb 15;283(7):4069-76. Epub 2007 Dec 10. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
16937 |
| Enzyme 12 Name |
Protein phosphatase 1 regulatory subunit 3B |
| Enzyme 12 Synonyms |
- Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL
- Protein phosphatase 1 regulatory subunit 4
- PP1 subunit R4
- Protein phosphatase 1 subunit GL
|
| Enzyme 12 Gene Name |
PPP1R3B |
| Enzyme 12 Protein Sequence |
>Protein phosphatase 1 regulatory subunit 3B
MMAVDIEYRYNCMAPSLRQERFAFKISPKPSKPLRPCIQLSSKNEASGMVAPAVQEKKVK
KRVSFADNQGLALTMVKVFSEFDDPLDMPFNITELLDNIVSLTTAESESFVLDFSQPSAD
YLDFRNRLQADHVCLENCVLKDKAIAGTVKVQNLAFEKTVKIRMTFDTWKSYTDFPCQYV
KDTYAGSDRDTFSFDISLPEKIQSYERMEFAVYYECNGQTYWDSNRGKNYRIIRAELKST
QGMTKPHSGPDLGISFDQFGSPRCSYGLFPEWPSYLGYEKLGPYY
|
| Enzyme 12 Number of Residues |
285 |
| Enzyme 12 Molecular Weight |
32694.9 |
| Enzyme 12 Theoretical pI |
5.92 |
| Enzyme 12 GO Classification |
Not Available |
| Enzyme 12 General Function |
Involved in glycogen metabolic process |
| Enzyme 12 Specific Function |
Acts as a glycogen-targeting subunit for phosphatase PP1. Facilitates interaction of the PP1 with enzymes of the glycogen metabolism and regulates its activity. Suppresses the rate at which PP1 dephosphorylates (inactivates) glycogen phosphorylase and enhances the rate at which it activates glycogen synthase and therefore limits glycogen breakdown. Its activity is inhibited by PYGL, resulting in inhibition of the glycogen synthase and glycogen phosphorylase phosphatase activities of PP1. Dramatically increases basal and insulin-stimulated glycogen synthesis upon overexpression in hepatocytes |
| Enzyme 12 Pathways |
Not Available |
| Enzyme 12 Reactions |
Not Available |
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
10436349  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q86XI6  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
PPR3B_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>858 bp
ATGATGGCTGTGGACATCGAGTACAGATACAACTGCATGGCTCCTTCCTTGCGCCAAGAG
AGGTTTGCCTTTAAGATCTCACCAAAGCCCAGCAAACCACTGAGGCCTTGTATTCAGCTG
AGCAGCAAGAATGAAGCCAGTGGAATGGTGGCCCCGGCTGTCCAGGAGAAGAAGGTGAAA
AAGCGGGTGTCCTTCGCAGACAACCAGGGGCTGGCCCTGACAATGGTCAAAGTGTTCTCG
GAATTCGATGACCCGCTAGATATGCCATTCAACATCACCGAGCTCCTAGACAACATTGTG
AGCTTGACGACAGCAGAGAGCGAGAGCTTTGTTCTGGATTTTTCCCAGCCCTCTGCAGAT
TACTTAGACTTTAGAAATCGACTTCAGGCCGACCACGTCTGCCTTGAGAACTGTGTGCTC
AAGGACAAGGCCATTGCAGGCACTGCGAAGGTTCAGAACCTCGCATTTGAGAAGACCGTG
AAAATAAGGATGACGTTCGACACCTGGAAGAGCTACACAGACTTTCCTTGTCAGTACGTG
AAGGACACTTATGCCGGTTCAGACAGGGACACGTTCTCCTTCGACATCAGTTTGCCCGAG
AAGATTCAGTCTTATGAAAGAATGGAGTTTGCTGTGTACTACGAGTGCAATGGACAGACG
TACTGGGACAGCAACAGAGGCAAGAACTATAGGATCATCCGGGCTGAGTTAAAATCTACC
CAGGGAATGACCAAGCCCCACAGTGGACCGGATTTGGGAATATCCTTTGACCAGTTCGGA
AGCCCTCGGTGTTCCTATGGTCTGTTTCCAGAGTGGCCAAGTTACTTAGGATATGAAAAG
CTAGGGCCCTACTACTAG
|
| Enzyme 12 GenBank Gene ID |
AK024067  |
| Enzyme 12 GeneCard ID |
PPP1R3B  |
| Enzyme 12 GenAtlas ID |
PPP1R3B  |
| Enzyme 12 HGNC ID |
HGNC:14942  |
| Enzyme 12 Chromosome Location |
8 |
| Enzyme 12 Locus |
8p23.1 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- 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
]
- Munro S, Cuthbertson DJ, Cunningham J, Sales M, Cohen PT: Human skeletal muscle expresses a glycogen-targeting subunit of PP1 that is identical to the insulin-sensitive glycogen-targeting subunit G(L) of liver. Diabetes. 2002 Mar;51(3):591-8. [PubMed
]
- Montori-Grau M, Guitart M, Lerin C, Andreu AL, Newgard CB, Garcia-Martinez C, Gomez-Foix AM: Expression and glycogenic effect of glycogen-targeting protein phosphatase 1 regulatory subunit GL in cultured human muscle. Biochem J. 2007 Jul 1;405(1):107-13. [PubMed
]
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| Enzyme 12 Metabolite References |
Not Available |