|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5597 |
| Enzyme 1 Name |
Type I inositol-1,4,5-trisphosphate 5-phosphatase |
| Enzyme 1 Synonyms |
- 5PTase
|
| Enzyme 1 Gene Name |
INPP5A |
| Enzyme 1 Protein Sequence |
>Type I inositol-1,4,5-trisphosphate 5-phosphatase
MAGKAAAPGTAVLLVTANVGSLFDDPENLQKNWLREFYQVVHTHKPHFMALHCQEFGGKN
YEASMSHVDKFVKELLSSDAMKEYNRARVYLDENYKSQEHFTALGSFYFLHESLKNIYQF
DFKAKKYRKVAGKEIYSDTLESTPMLEKEKFPQDYFPECKWSRKGFIRTRWCIADCAFDL
VNIHLFHDASNLVAWETSPSVYSGIRHKALGYVLDRIIDQRFEKVSYFVFGDFNFRLDSK
SVVETLCTKATMQTVRAADTNEVVKLIFRESDNDRKVMLQLEKKLFDYFNQEVFRDNNGT
ALLEFDKELSVFKDRLYELDISFPPSYPYSEDARQGEQYMNTRCPAWCDRILMSPSAKEL
VLRSESEEKVVTYDHIGPNVCMGDHKPVFLAFRIMPGAGKPHAHVHKCCVVQ
|
| Enzyme 1 Number of Residues |
412 |
| Enzyme 1 Molecular Weight |
47819.2 |
| Enzyme 1 Theoretical pI |
7.04 |
| Enzyme 1 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphatase activity
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in inositol or phosphatidylinositol phosphatase activity |
| Enzyme 1 Specific Function |
Major isoenzyme hydrolyzing the calcium-mobilizing second messenger Ins(1,4,5)P3, this is a signal-terminating reaction |
| Enzyme 1 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 1 Reactions |
- (1) D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate [RN:R03394]
- (2) 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate [RN:R03430]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
57209040  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q14642  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
I5P1_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1239 bp
ATGGCGGGGAAGGCGGCCGCCCCGGGCACCGCGGTGCTGCTGGTCACGGCCAACGTGGGC
TCGCTCTTCGACGACCCAGAAAACCTGCAGAAGAACTGGCTTCGGGAATTTTACCAGGTC
GTGCACACACACAAGCCGCACTTCATGGCCTTGCACTGTCAGGAGTTTGGAGGGAAGAAC
TACGAGGCCTCCATGTCCCACGTGGACAAGTTCGTCAAAGAACTATTGTCGAGTGATGCG
ATGAAAGAATATAACAGGGCTCGAGTCTACCTGGATGAAAACTACAAATCCCAGGAGCAC
TTCACGGCACTAGGAAGCTTTTATTTTCTTCATGAGTCCTTAAAAAACATCTACCAGTTT
GACTTTAAAGCTAAGAAGTATAGAAAGGTCGCTGGCAAAGAGATCTACTCGGATACCTTA
GAGAGCACGCCCATGCTGGAGAAGGAGAAGTTTCCGCAGGACTACTTCCCCGAGTGCAAA
TGGTCAAGAAAAGGCTTCATCCGGACGAGGTGGTGCATTGCAGACTGTGCCTTTGACTTG
GTGAATATCCATCTTTTCCATGATGCTTCCAATCTGGTCGCCTGGGAAACAAGCCCTTCC
GTGTACTCGGGAATCCGGCACAAGGCACTGGGCTACGTGCTGGACAGAATCATTGATCAG
CGATTCGAGAAGGTTTCCTACTTTGTATTTGGTGATTTCAACTTCCGGCTGGATTCCAAG
TCCGTCGTGGAGACGCTCTGCACAAAAGCCACCATGCAGACGGTCCGGGCCGCCGACACC
AATGAAGTGGTGAAGCTCATATTTCGTGAGTCGGACAACGACCGGAAGGTTATGCTCCAG
TTAGAAAAGAAACTCTTCGACTACTTCAACCAGGAGGTTTTCCGAGACAACAACGGCACC
GCGCTCTTGGAGTTTGACAAGGAGTTGTCTGTCTTTAAGGACAGACTGTATGAACTGGAC
ATCTCGTTCCCTCCCAGCTACCCGTACAGTGAGGACGCCCGCCAGGGTGAGCAGTACATG
AACACCCGGTGCCCAGCCTGGTGTGACCGCATCCTCATGTCCCCGTCTGCCAAGGAGCTG
GTGCTGCGGTCGGAGAGCGAGGAGAAGGTTGTCACCTATGACCACATTGGGCCCAACGTC
TGCATGGGAGACCACAAGCCCGTGTTCCTGGCCTTCCGAATCATGCCCGGGGCAGGTAAA
CCTCATGCCCATGTGCACAAGTGTTGTGTCGTGCAGTGA
|
| Enzyme 1 GenBank Gene ID |
AL356603  |
| Enzyme 1 GeneCard ID |
INPP5A  |
| Enzyme 1 GenAtlas ID |
INPP5A  |
| Enzyme 1 HGNC ID |
HGNC:6076  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
10q26.3 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- De Smedt F, Verjans B, Mailleux P, Erneux C: Cloning and expression of human brain type I inositol 1,4,5-trisphosphate 5-phosphatase. High levels of mRNA in cerebellar Purkinje cells. FEBS Lett. 1994 Jun 20;347(1):69-72. [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
]
- Laxminarayan KM, Chan BK, Tetaz T, Bird PI, Mitchell CA: Characterization of a cDNA encoding the 43-kDa membrane-associated inositol-polyphosphate 5-phosphatase. J Biol Chem. 1994 Jun 24;269(25):17305-10. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5598 |
| Enzyme 2 Name |
Inositol polyphosphate 1-phosphatase |
| Enzyme 2 Synonyms |
- IPP
- IPPase
|
| Enzyme 2 Gene Name |
INPP1 |
| Enzyme 2 Protein Sequence |
>Inositol polyphosphate 1-phosphatase
MSDILRELLCVSEKAANIARACRQQEALFQLLIEEKKEGEKNKKFAVDFKTLADVLVQEV
IKQNMENKFPGLEKNIFGEESNEFTNDWGEKITLRLCSTEEETAELLSKVLNGNKVASEA
LARVVHQDVAFTDPTLDSTEINVPQDILGIWVDPIDSTYQYIKGSADIKSNQGIFPCGLQ
CVTILIGVYDIQTGVPLMGVINQPFVSRDPNTLRWKGQCYWGLSYMGTNMHSLQLTISRR
NGSETHTGNTGSEAAFSPSFSAVISTSEKETIKAALSRVCGDRIFGAAGAGYKSLCVVQG
LVDIYIFSEDTTFKWDSCAAHAILRAMGGGIVDLKECLERNPETGLDLPQLVYHVENEGA
AGVDRWANKGGLIAYRSRKRLETFLSLLVQNLAPAETHT
|
| Enzyme 2 Number of Residues |
399 |
| Enzyme 2 Molecular Weight |
43997.6 |
| Enzyme 2 Theoretical pI |
4.91 |
| Enzyme 2 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphatase activity
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in inositol or phosphatidylinositol phosphatase activity |
| Enzyme 2 Specific Function |
1D-myo-inositol 1,4-bisphosphate + H(2)O = 1D- myo-inositol 4-phosphate + phosphate |
| Enzyme 2 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 2 Reactions |
- 1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate [RN:R03393]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
Not Available |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P49441  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
INPP_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1200 bp
ATGTCAGATATCCTCCGGGAGCTGCTCTGTGTCTCTGAGAAGGCTGCTAACATTGCCCGG
GCGTGCAGACAGCAGGAAGCCCTCTTCCAGCTGCTGATCGAAGAAAAGAAAGAGGGAGAA
AAGAACAAGAAGTTTGCAGTTGACTTCAAGACTCTGGCTGATGTACTGGTACAGGAAGTT
ATAAAACAGAATATGGAGAACAAGTTTCCAGGCTTGGAAAAAAATATTTTTGGAGAAGAA
TCCAATGAGTTTACTAATGACTGGGGGGAAAAGATTACCTTGAGGTTGTGTTCAACAGAG
GAAGAAACAGCAGAGCTTCTTAGCAAAGTCCTCAATGGTAACAAGGTAGCATCTGAAGCA
TTAGCCAGGGTTGTTCATCAGGATGTTGCCTTTACTGACCCAACTCTGGATTCCACAGAG
ATCAATGTTCCACAGGACATTTTGGGAATTTGGGTGGACCCCATAGATTCAACTTATCAG
TATATAAAAGGTTCTGCTGACATTAAATCCAACCAGGGAATCTTCCCCTGTGGACTTCAG
TGTGTCACCATTTTAATTGGTGTCTATGACATACAGACAGGGGTTCCCCTGATGGGAGTC
ATCAATCAACCTTTTGTGTCACGAGATCCAAACACCCTCAGGTGGAAAGGACAGTGCTAT
TGGGGCCTTTCTTACATGGGGACCAACATGCATTCACTACAGCTCACCATCTCTAGAAGA
AACGGCAGTGAAACACACACTGGAAACACCGGCTCTGAGGCAGCATTCTCCCCCAGTTTT
TCAGCCGTAATTAGTACAAGTGAAAAGGAGACTATCAAAGCTGCATTGTCACGTGTGTGT
GGAGATCGCATATTTGGGGCAGCTGGGGCTGGTTATAAGAGCCTATGTGTTGTCCAAGGC
CTCGTTGACATTTACATCTTTTCAGAAGATACCACATTCAAATGGGACTCTTGTGCTGCT
CATGCCATACTGCGGGCCATGGGTGGGGGAATAGTAGACTTGAAAGAATGCTTAGAAAGA
AATCCAGAAACAGGGCTTGATTTGCCACAGTTGGTGTACCACGTGGAAAATGAGGGTGCT
GCTGGGGTGGATCGGTGGGCCAACAAGGGAGGACTCATTGCATACAGATCCAGGAAGCGG
CTGGAGACATTCCTGAGCCTCCTGGTCCAAAACCTGGCACCTGCAGAGACGCATACCTAG
|
| Enzyme 2 GenBank Gene ID |
L08488  |
| Enzyme 2 GeneCard ID |
INPP1  |
| Enzyme 2 GenAtlas ID |
INPP1  |
| Enzyme 2 HGNC ID |
HGNC:6071  |
| Enzyme 2 Chromosome Location |
2 |
| Enzyme 2 Locus |
2q32 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- York JD, Veile RA, Donis-Keller H, Majerus PW: Cloning, heterologous expression, and chromosomal localization of human inositol polyphosphate 1-phosphatase. Proc Natl Acad Sci U S A. 1993 Jun 15;90(12):5833-7. [PubMed
]
- Lovlie R, Gulbrandsen AK, Molven A, Steen VM: Genomic structure and sequence analysis of a human inositol polyphosphate 1-phosphatase gene (INPP1). Pharmacogenetics. 1999 Aug;9(4):517-28. [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
]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed
]
- Steen VM, Lovlie R, Osher Y, Belmaker RH, Berle JO, Gulbrandsen AK: The polymorphic inositol polyphosphate 1-phosphatase gene as a candidate for pharmacogenetic prediction of lithium-responsive manic-depressive illness. Pharmacogenetics. 1998 Jun;8(3):259-68. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5599 |
| Enzyme 3 Name |
Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A |
| Enzyme 3 Synonyms |
- Inositol polyphosphate 5-phosphatase J
|
| Enzyme 3 Gene Name |
INPP5J |
| Enzyme 3 Protein Sequence |
>Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A
MEGQSSRGSRRPGTRAGLGSLPMPQGVAQTGAPSKVDSSFQLPAKKNAALGPSEPRLALA
PVGPRAAMSASSEGPRLALASPRPILAPLCTPEGQKTATAHRSSSLAPTSVGQLVMSASA
GPKPPPATTGSVLAPTSLGLVMPASAGPRSPPVTLGPNLAPTSRDQKQEPPASVGPKPTL
AASGLSLALASEEQPPELPSTPSPVPSPVLSPTQEQALAPASTASGAASVGQTSARKRDA
PAPRPLPASEGHLQPPAQTSGPTGSPPCIQTSPDPRLSPSFRARPEALHSSPEDPVLPRP
PQTLPLDVGQGPSEPGTHSPGLLSPTFRPGAPSGQTVPPPLPKPPRSPSRSPSHSPNRSP
CVPPAPDMALPRLGTQSTGPGRCLSPNLQAQEAPAPVTTSSSTSTLSSSPWSAQPTWKSD
PGFRITVVTWNVGTAMPPDDVTSLLHLGGGDDSDGADMIAIGLQEVNSMLNKRLKDALFT
DQWSELFMDALGPFNFVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNK
GGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTILSLQQFQGPGAQGILDHDLVFW
FGDLNFRIESYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKF
DVGTNKYDTSAKKRKPAWTDRILWKVKAPGGGPSPSGRKSHRLQVTQHSYRSHMEYTVSD
HKPVAAQFLLQFAFRDDMPLVRLEVADEWVRPEQAVVRYRMETVFARSSWDWIGLYRVGF
RHCKDYVAYVWAKHEDVDGNTYQVTFSEESLPKGHGDFILGYYSHNHSILIGITEPFQIS
LPSSELASSSTDSSGTSSEGEDDSTLELLAPKSRSPSPGKSKRHRSRSPGLARFPGLALR
PSSRERRGASRSPSPQSRRLSRVAPDRSSNGSSRGSSEEGPSGLPGPWAFPPAVPRSLGL
LPALRLETVDPGGGGSWGPDREALAPNSLSPSPQGHRGLEEGGLGP
|
| Enzyme 3 Number of Residues |
1006 |
| Enzyme 3 Molecular Weight |
107195.7 |
| Enzyme 3 Theoretical pI |
9.53 |
| Enzyme 3 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphatase activity
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in inositol or phosphatidylinositol phosphatase activity |
| Enzyme 3 Specific Function |
Inositol 5-phosphatase, which converts inositol 1,4,5- trisphosphate to inositol 1,4-bisphosphate. Also converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4- phosphate and inositol 1,3,4,5-tetrakisphosphate to inositol 1,3,4-trisphosphate in vitro. May be involved in modulation of the function of inositol and phosphatidylinositol polyphosphate- binding proteins that are present at membranes ruffles |
| Enzyme 3 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 3 Reactions |
- (1) D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate [RN:R03394]
- (2) 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate [RN:R03430]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
50726960  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q15735  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
PI5PA_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
Not Available |
| Enzyme 3 GenBank Gene ID |
Not Available |
| Enzyme 3 GeneCard ID |
INPP5J  |
| Enzyme 3 GenAtlas ID |
INPP5J  |
| Enzyme 3 HGNC ID |
HGNC:8956  |
| Enzyme 3 Chromosome Location |
2 |
| Enzyme 3 Locus |
22q12.2 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 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
]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [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
]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5600 |
| Enzyme 4 Name |
Inositol polyphosphate 5-phosphatase K |
| Enzyme 4 Synonyms |
- Skeletal muscle and kidney-enriched inositol phosphatase
|
| Enzyme 4 Gene Name |
INPP5K |
| Enzyme 4 Protein Sequence |
>Inositol polyphosphate 5-phosphatase K
MSSRKLSGPKGRRLSIHVVTWNVASAAPPLDLSDLLQLNNRNLNLDIYVIGLQELNSGII
SLLSDAAFNDSWSSFLMDVLSPLSFIKVSHVRMQGILLLVFAKYQHLPYIQILSTKSTPT
GLFGYWGNKGGVNICLKLYGYYVSIINCHLPPHISNNYQRLEHFDRILEMQNCEGRDIPN
ILDHDLIIWFGDMNFRIEDFGLHFVRESIKNRCYGGLWEKDQLSIAKKHDPLLREFQEGR
LLFPPTYKFDRNSNDYDTSEKKRKPAWTDRILWRLKRQPCAGPDTPIPPASHFSLSLRGY
SSHMTYGISDHKPVSGTFDLELKPLVSAPLIVLMPEDLWTVENDMMVSYSSTSDFPSSPW
DWIGLYKVGLRDVNDYVSYAWVGDSKVSCSDNLNQVYIDISNIPTTEDEFLLCYYSNSLR
SVVGISRPFQIPPGSLREDPLGEAQPQI
|
| Enzyme 4 Number of Residues |
448 |
| Enzyme 4 Molecular Weight |
51089.8 |
| Enzyme 4 Theoretical pI |
6.51 |
| Enzyme 4 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphatase activity
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 4 General Function |
Involved in inositol or phosphatidylinositol phosphatase activity |
| Enzyme 4 Specific Function |
Inositol 5-phosphatase which acts on inositol 1,4,5- trisphosphate, inositol 1,3,4,5-tetrakisphosphate, phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-triphosphate. Has 6-fold higher affinity for phosphatidylinositol 4,5-bisphosphate than for inositol 1,4,5- trisphosphate. May negatively regulate assembly of the actin cytoskeleton |
| Enzyme 4 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 4 Reactions |
- (1) D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate [RN:R03394]
- (2) 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate [RN:R03430]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
7209855  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q9BT40  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
INP5K_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1347 bp
ATGAGCTCGCGGAAGCTGAGCGGGCCGAAAGGCAGGAGGCTCAGCATACACGTCGTGACT
TGGAACGTGGCTTCGGCAGCGCCCCCTCTAGATCTCAGTGACCTGCTTCAGCTGAACAAC
CGGAACCTCAATCTTGACATATATGTTATTGGTTTGCAGGAATTGAACTCTGGGATCATA
AGCCTCCTTTCCGATGCTGCCTTTAATGACTCGTGGAGCAGTTTCCTCATGGATGTGCTT
TCCCCTCTGAGCTTCATCAAGGTCTCCCATGTCCGTATGCAGGGGATCCTCTTACTGGTC
TTTGCCAAGTATCAGCATTTGCCCTATATCCAGATTCTGTCTACTAAATCCACCCCCACT
GGCCTGTTTGGGTACTGGGGGAACAAAGGTGGAGTCAACATCTGCCTGAAGCTTTATGGC
TACTATGTCAGCATCATCAACTGCCACCTGCCTCCCCACATTTCCAACAATTACCAGCGG
CTGGAGCACTTTGACCGGATCCTGGAGATGCAGAATTGTGAGGGGCGAGACATCCCAAAC
ATCCTGGACCACGACCTCATTATCTGGTTTGGAGACATGAACTTTCGGATCGAGGACTTT
GGGTTGCACTTTGTTCGGGAATCCATTAAAAATCGGTGCTACGGTGGCCTGTGGGAGAAG
GACCAGCTCAGCATTGCCAAGAAACATGACCCGCTGCTCCGGGAGTTCCAGGAGGGCCGC
CTACTCTTCCCGCCCACCTACAAGTTTGATAGGAACTCCAACGACTATGACACCAGTGAG
AAAAAACGCAAGCCTGCATGGACCGATCGCATCCTGTGGAGGCTGAAGCGGCAGCCCTGT
GCTGGCCCCGACACTCCCATACCGCCGGCGTCACACTTCTCCTTGTCTCTGAGGGGCTAC
AGCAGCCACATGACGTACGGCATCAGCGACCACAAGCCTGTCTCCGGCACGTTCGACTTG
GAGCTGAAGCCATTGGTGTCTGCTCCGCTGATCGTCCTGATGCCCGAGGACCTGTGGACC
GTGGAAAATGACATGATGGTCAGCTACTCTTCAACCTCGGACTTCCCCAGCAGCCCGTGG
GACTGGATTGGACTGTACAAGGTGGGGCTGCGGGACGTTAATGACTACGTGTCCTATGCC
TGGGTCGGGGACAGCAAGGTCTCCTGCAGCGACAACCTGAACCAGGTTTACATCGACATC
AGCAATATCCCTACCACTGAAGATGAGTTTCTCCTCTGTTACTACAGAAACAGTCTGCGT
TCTGTGGTGGGGATAAGAAGACCCTTCCAGATCCCGCCTGGCTCCTTGAGGGAGGACCCA
CTGGGTGAAGCACAGCCACAGATCTGA
|
| Enzyme 4 GenBank Gene ID |
AB036829  |
| Enzyme 4 GeneCard ID |
INPP5K  |
| Enzyme 4 GenAtlas ID |
INPP5K  |
| Enzyme 4 HGNC ID |
HGNC:33882  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
17p13.3 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Ijuin T, Mochizuki Y, Fukami K, Funaki M, Asano T, Takenawa T: Identification and characterization of a novel inositol polyphosphate 5-phosphatase. J Biol Chem. 2000 Apr 14;275(15):10870-5. [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
]
- Gurung R, Tan A, Ooms LM, McGrath MJ, Huysmans RD, Munday AD, Prescott M, Whisstock JC, Mitchell CA: Identification of a novel domain in two mammalian inositol-polyphosphate 5-phosphatases that mediates membrane ruffle localization. The inositol 5-phosphatase skip localizes to the endoplasmic reticulum and translocates to membrane ruffles following epidermal growth factor stimulation. J Biol Chem. 2003 Mar 28;278(13):11376-85. Epub 2003 Jan 20. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
8839 |
| Enzyme 5 Name |
Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2 |
| Enzyme 5 Synonyms |
- Inositol polyphosphate phosphatase-like protein 1
- INPPL-1
- Protein 51C
- SH2 domain-containing inositol-5'-phosphatase 2
- SH2 domain-containing inositol phosphatase 2
- SHIP-2
|
| Enzyme 5 Gene Name |
INPPL1 |
| Enzyme 5 Protein Sequence |
>Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2
MASACGAPGPGGALGSQAPSWYHRDLSRAAAEELLARAGRDGSFLVRDSESVAGAFALCV
LYQKHVHTYRILPDGEDFLAVQTSQGVPVRRFQTLGELIGLYAQPNQGLVCALLLPVEGE
REPDPPDDRDASDGEDEKPPLPPRSGSTSISAPTGPSSPLPAPETPTAPAAESAPNGLST
VSHDYLKGSYGLDLEAVRGGASHLPHLTRTLATSCRRLHSEVDKVLSGLEILSKVFDQQS
SPMVTRLLQQQNLPQTGEQELESLVLKLSVLKDFLSGIQKKALKALQDMSSTAPPAPQPS
TRKAKTIPVQAFEVKLDVTLGDLTKIGKSQKFTLSVDVEGGRLVLLRRQRDSQEDWTTFT
HDRIRQLIKSQRVQNKLGVVFEKEKDRTQRKDFIFVSARKREAFCQLLQLMKNKHSKQDE
PDMISVFIGTWNMGSVPPPKNVTSWFTSKGLGKTLDEVTVTIPHDIYVFGTQENSVGDRE
WLDLLRGGLKELTDLDYRPIAMQSLWNIKVAVLVKPEHENRISHVSTSSVKTGIANTLGN
KGAVGVSFMFNGTSFGFVNCHLTSGNEKTARRNQNYLDILRLLSLGDRQLNAFDISLRFT
HLFWFGDLNYRLDMDIQEILNYISRKEFEPLLRVDQLNLEREKHKVFLRFSEEEISFPPT
YRYERGSRDTYAWHKQKPTGVRTNVPSWCDRILWKSYPETHIICNSYGCTDDIVTSDHSP
VFGTFEVGVTSQFISKKGLSKTSDQAYIEFESIEAIVKTASRTKFFIEFYSTCLEEYKKS
FENDAQSSDNINFLKVQWSSRQLPTLKPILADIEYLQDQHLLLTVKSMDGYESYGECVVA
LKSMIGSTAQQFLTFLSHRGEETGNIRGSMKVRVPTERLGTRERLYEWISIDKDEAGAKS
KAPSVSRGSQEPRSGSRKPAFTEASCPLSRLFEEPEKPPPTGRPPAPPRAAPREEPLTPR
LKPEGAPEPEGVAAPPPKNSFNNPAYYVLEGVPHQLLPPEPPSPARAPVPSATKNKVAIT
VPAPQLGHHRHPRVGEGSSSDEESGGTLPPPDFPPPPLPDSAIFLPPSLDPLPGPVVRGR
GGAEARGPPPPKAHPRPPLPPGPSPASTFLGEVASGDDRSCSVLQMAKTLSEVDYAPAGP
ARSALLPGPLELQPPRGLPSDYGRPLSFPPPRIRESIQEDLAEEAPCLQGGRASGLGEAG
MSAWLRAIGLERYEEGLVHNGWDDLEFLSDITEEDLEEAGVQDPAHKRLLLDTLQLSK
|
| Enzyme 5 Number of Residues |
1258 |
| Enzyme 5 Molecular Weight |
138597.5 |
| Enzyme 5 Theoretical pI |
6.49 |
| Enzyme 5 GO Classification |
| Function |
- binding
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphatase activity
- phosphatase activity
- phosphoric ester hydrolase activity
- protein binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 5 General Function |
Involved in inositol or phosphatidylinositol phosphatase activity |
| Enzyme 5 Specific Function |
Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol- 3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling. Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6 |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
Not Available |
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
222136583  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
O15357  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
SHIP2_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>3777 bp
ATGGCCTCGGCCTGCGGGGCGCCGGGCCCGGGGGGCGCCCTGGGCAGCCAGGCCCCCTCC
TGGTACCACCGCGACCTGAGCCGGGCGGCCGCGGAGGAGCTGCTGGCCCGGGCGGGCCGC
GATGGCAGCTTCCTGGTCCGAGACAGCGAGAGCGTGGCGGGGGCCTTCGCGCTCTGCGTC
CTGTATCAGAAGCATGTGCACACGTATCGCATTCTGCCTGATGGAGAAGATTTCTTGGCT
GTGCAGACCTCGCAGGGTGTGCCTGTGCGCCGCTTCCAGACCCTGGGTGAGCTCATCGGC
CTGTACGCCCAGCCCAACCAGGGCCTTGTGTGCGCCCTGCTTCTTCCTGTAGAGGGTGAG
CGAGAGCCGGACCCACCGGATGACCGGGATGCCTCAGATGGGGAGGATGAGAAGCCCCCG
CTGCCCCCGCGCTCTGGCTCCACCAGCATTTCTGCCCCCACTGGGCCCAGCAGTCCCCTG
CCAGCTCCTGAGACTCCCACAGCTCCAGCTGCTGAGAGTGCTCCCAATGGGCTGAGCACC
GTCTCGCACGACTACCTGAAAGGCAGCTATGGGCTGGACCTGGAAGCTGTGAGGGGTGGA
GCCAGCCACCTGCCCCACCTCACCCGTACCCTCGCTACCTCATGCCGGAGGCTGCACAGT
GAGGTGGACAAGGTCCTGTCAGGCCTGGAGATCCTGTCCAAGGTGTTTGACCAGCAGAGC
TCGCCCATGGTGACCCGCCTTTTGCAGCAGCAGAACCTGCCACAGACAGGGGAGCAGGAA
CTAGAGAGCCTGGTGCTGAAGCTGTCAGTGCTAAAGGACTTCCTGTCAGGCATCCAGAAG
AAGGCCCTGAAGGCCCTACAGGACATGAGCTCCACAGCACCCCCAGCTCCGCAGCCATCC
ACACGTAAGGCCAAGACCATCCCCGTGCAGGCCTTTGAGGTGAAGCTAGATGTGACCCTG
GGTGACCTGACCAAGATTGGGAAGTCACAGAAGTTCACGCTGAGCGTGGATGTGGAGGGT
GGGCGGCTGGTGCTGCTGCGGAGACAGCGGGACTCCCAGGAGGACTGGACCACCTTCACG
CACGACCGCATCCGCCAGCTCATTAAGTCCCAGCGTGTCCAGAACAAGCTGGGTGTTGTG
TTTGAGAAGGAGAAGGACCGGACTCAGCGCAAGGACTTCATCTTTGTCAGTGCCCGGAAG
CGGGAGGCCTTCTGCCAGCTGTTGCAGCTCATGAAGAACAAGCACTCCAAGCAGGACGAG
CCCGACATGATCTCAGTCTTCATAGGCACCTGGAACATGGGAAGTGTACCACCTCCAAAA
AACGTGACATCCTGGTTCACATCGAAGGGTCTGGGGAAGACCCTGGACGAGGTCACAGTG
ACCATACCCCATGACATCTATGTCTTTGGGACCCAGGAGAACTCAGTGGGCGACCGCGAG
TGGCTGGACCTACTGCGCGGGGGCCTCAAGGAGCTTACGGATCTGGATTACCGCCCGATT
GCCATGCAATCACTGTGGAATATCAAGGTGGCAGTGCTGGTCAAGCCAGAGCACGAGAAC
CGTATCAGCCATGTCAGTACGTCCAGTGTGAAGACTGGCATCGCCAACACCCTGGGGAAC
AAGGGGGCTGTGGGCGTCTCCTTCATGTTTAATGGCACCTCATTTGGCTTTGTGAATTGT
CACCTCACCTCGGGAAATGAGAAGACGGCTCGGAGGAACCAAAACTACTTGGACATCCTG
CGGCTGCTCTCGCTGGGCGACCGGCAGCTCAATGCCTTTGACATCTCTCTGCGTTTCACA
CACCTCTTCTGGTTTGGGGACCTCAACTACCGCCTGGACATGGATATCCAGGAGATCCTG
AACTACATCAGCAGGAAAGAGTTTGAGCCCCTCCTCAGGGTGGACCAGCTCAACCTGGAG
CGGGAGAAGCACAAGGTCTTCCTTCGATTCAGTGAGGAGGAGATCTCCTTCCCACCCACC
TACCGCTATGAGCGGGGTTCCCGGGACACATATGCCTGGCACAAGCAGAAGCCAACTGGG
GTCCGGACCAATGTGCCCTCATGGTGTGACCGGATTCTGTGGAAATCCTACCCTGAAACT
CACATCATCTGCAATTCTTATGGTTGCACTGATGACATCGTCACCAGCGACCATTCCCCC
GTGTTTGGGACATTTGAGGTTGGAGTTACCTCCCAGTTCATCTCCAAGAAAGGGCTCTCA
AAGACTTCAGACCAGGCCTACATTGAGTTTGAGAGCATCGAGGCCATTGTGAAGACAGCC
AGCCGCACCAAGTTCTTCATCGAGTTCTACTCTACCTGCCTGGAGGAATACAAGAAGAGC
TTTGAGAATGATGCCCAGAGCAGTGACAACATCAACTTCCTCAAAGTGCAGTGGTCTTCA
CGCCAGCTGCCCACGCTCAAACCAATTCTGGCTGATATCGAGTACCTGCAGGACCAGCAC
CTCCTGCTCACAGTCAAGTCCATGGATGGCTATGAATCCTATGGGGAGTGTGTGGTTGCA
CTCAAATCCATGATCGGCAGCACGGCCCAACAGTTCCTGACCTTCCTATCCCACCGTGGC
GAGGAGACAGGCAATATCAGAGGCTCCATGAAGGTGCGGGTGCCCACGGAGCGCCTGGGC
ACCCGTGAGCGGCTCTACGAGTGGATCAGCATTGATAAGGATGAGGCAGGAGCAAAGAGC
AAAGCCCCCTCTGTGTCCCGAGGGAGCCAGGAGCCCAGGTCAGGGAGCCGCAAGCCAGCC
TTCACAGAGGCCTCCTGCCCGCTCTCCAGGTTATTTGAAGAACCAGAGAAACCGCCACCA
ACGGGGAGGCCCCCAGCCCCACCCCGAGCAGCTCCCCGGGAGGAGCCCTTGACCCCCAGG
TTGAAGCCAGAGGGAGCTCCTGAACCAGAAGGGGTGGCGGCCCCCCCACCCAAGAACAGC
TTCAATAACCCTGCCTACTACGTCCTTGAAGGGGTCCCGCACCAGCTGCTGCCCCCGGAG
CCACCCTCGCCTGCCAGGGCCCCTGTCCCATCTGCCACCAAGAACAAAGTGGCCATTACA
GTGCCTGCTCCACAGCTTGGGCACCACCGGCACCCTCGTGTGGGAGAGGGGAGTTCTTCA
GATGAGGAGTCTGGAGGCACACTGCCCCCTCCAGACTTTCCACCTCCACCACTGCCGGAC
TCAGCCATCTTCCTGCCCCCCAGCCTGGATCCTTTACCAGGGCCAGTGGTCCGGGGCCGT
GGTGGGGCTGAGGCCCGTGGCCCACCACCTCCCAAGGCCCATCCAAGGCCTCCACTGCCC
CCAGGCCCCTCACCAGCCAGCACTTTCCTGGGGGAAGTGGCCAGTGGGGATGACCGGTCC
TGCTCGGTGCTGCAGATGGCCAAGACGCTGAGCGAGGTGGACTATGCCCCTGCTGGGCCT
GCACGCTCAGCGCTCCTCCCAGGCCCCCTGGAGCTGCAGCCCCCCCGGGGACTGCCCTCG
GACTATGGCCGGCCCCTCAGCTTCCCTCCACCCCGCATCCGGGAGAGCATCCAGGAAGAC
CTGGCAGAGGAGGCTCCGTGCCTGCAGGGCGGGCGGGCCAGCGGGCTGGGCGAGGCAGGC
ATGAGTGCCTGGCTGCGGGCCATCGGCTTGGAGCGCTATGAGGAGGGCCTGGTGCATAAT
GGCTGGGACGACCTGGAGTTTCTCAGTGACATCACCGAGGAGGACTTGGAGGAGGCTGGG
GTGCAGGACCCGGCTCACAAGCGCCTCCTTCTGGACACCCTGCAGCTCAGCAAGTGA
|
| Enzyme 5 GenBank Gene ID |
NM_001567.3  |
| Enzyme 5 GeneCard ID |
INPPL1  |
| Enzyme 5 GenAtlas ID |
INPPL1  |
| Enzyme 5 HGNC ID |
HGNC:6080  |
| Enzyme 5 Chromosome Location |
1 |
| Enzyme 5 Locus |
11q23 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Hejna JA, Saito H, Merkens LS, Tittle TV, Jakobs PM, Whitney MA, Grompe M, Friedberg AS, Moses RE: Cloning and characterization of a human cDNA (INPPL1) sharing homology with inositol polyphosphate phosphatases. Genomics. 1995 Sep 1;29(1):285-7. [PubMed
]
- Pesesse X, Deleu S, De Smedt F, Drayer L, Erneux C: Identification of a second SH2-domain-containing protein closely related to the phosphatidylinositol polyphosphate 5-phosphatase SHIP. Biochem Biophys Res Commun. 1997 Oct 29;239(3):697-700. [PubMed
]
- Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [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
]
- Habib T, Hejna JA, Moses RE, Decker SJ: Growth factors and insulin stimulate tyrosine phosphorylation of the 51C/SHIP2 protein. J Biol Chem. 1998 Jul 17;273(29):18605-9. [PubMed
]
- Wisniewski D, Strife A, Swendeman S, Erdjument-Bromage H, Geromanos S, Kavanaugh WM, Tempst P, Clarkson B: A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase (SHIP2) is constitutively tyrosine phosphorylated and associated with src homologous and collagen gene (SHC) in chronic myelogenous leukemia progenitor cells. Blood. 1999 Apr 15;93(8):2707-20. [PubMed
]
- Bruhns P, Vely F, Malbec O, Fridman WH, Vivier E, Daeron M: Molecular basis of the recruitment of the SH2 domain-containing inositol 5-phosphatases SHIP1 and SHIP2 by fcgamma RIIB. J Biol Chem. 2000 Dec 1;275(48):37357-64. [PubMed
]
- Pesesse X, Dewaste V, De Smedt F, Laffargue M, Giuriato S, Moreau C, Payrastre B, Erneux C: The Src homology 2 domain containing inositol 5-phosphatase SHIP2 is recruited to the epidermal growth factor (EGF) receptor and dephosphorylates phosphatidylinositol 3,4,5-trisphosphate in EGF-stimulated COS-7 cells. J Biol Chem. 2001 Jul 27;276(30):28348-55. Epub 2001 May 10. [PubMed
]
- Dyson JM, O'Malley CJ, Becanovic J, Munday AD, Berndt MC, Coghill ID, Nandurkar HH, Ooms LM, Mitchell CA: The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin. J Cell Biol. 2001 Dec 10;155(6):1065-79. Epub 2001 Dec 10. [PubMed
]
- Prasad N, Topping RS, Decker SJ: SH2-containing inositol 5'-phosphatase SHIP2 associates with the p130(Cas) adapter protein and regulates cellular adhesion and spreading. Mol Cell Biol. 2001 Feb;21(4):1416-28. [PubMed
]
- Steen H, Kuster B, Fernandez M, Pandey A, Mann M: Tyrosine phosphorylation mapping of the epidermal growth factor receptor signaling pathway. J Biol Chem. 2002 Jan 11;277(2):1031-9. Epub 2001 Oct 30. [PubMed
]
- Prasad N, Topping RS, Decker SJ: Src family tyrosine kinases regulate adhesion-dependent tyrosine phosphorylation of 5'-inositol phosphatase SHIP2 during cell attachment and spreading on collagen I. J Cell Sci. 2002 Oct 1;115(Pt 19):3807-15. [PubMed
]
- Vandenbroere I, Paternotte N, Dumont JE, Erneux C, Pirson I: The c-Cbl-associated protein and c-Cbl are two new partners of the SH2-containing inositol polyphosphate 5-phosphatase SHIP2. Biochem Biophys Res Commun. 2003 Jan 10;300(2):494-500. [PubMed
]
- Dyson JM, Munday AD, Kong AM, Huysmans RD, Matzaris M, Layton MJ, Nandurkar HH, Berndt MC, Mitchell CA: SHIP-2 forms a tetrameric complex with filamin, actin, and GPIb-IX-V: localization of SHIP-2 to the activated platelet actin cytoskeleton. Blood. 2003 Aug 1;102(3):940-8. Epub 2003 Apr 3. [PubMed
]
- Pengal RA, Ganesan LP, Fang H, Marsh CB, Anderson CL, Tridandapani S: SHIP-2 inositol phosphatase is inducibly expressed in human monocytes and serves to regulate Fcgamma receptor-mediated signaling. J Biol Chem. 2003 Jun 20;278(25):22657-63. Epub 2003 Apr 10. [PubMed
]
- Salomon AR, Ficarro SB, Brill LM, Brinker A, Phung QT, Ericson C, Sauer K, Brock A, Horn DM, Schultz PG, Peters EC: Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry. Proc Natl Acad Sci U S A. 2003 Jan 21;100(2):443-8. Epub 2003 Jan 9. [PubMed
]
- Vandeput F, Backers K, Villeret V, Pesesse X, Erneux C: The influence of anionic lipids on SHIP2 phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase activity. Cell Signal. 2006 Dec;18(12):2193-9. Epub 2006 May 23. [PubMed
]
- Paternotte N, Zhang J, Vandenbroere I, Backers K, Blero D, Kioka N, Vanderwinden JM, Pirson I, Erneux C: SHIP2 interaction with the cytoskeletal protein Vinexin. FEBS J. 2005 Dec;272(23):6052-66. [PubMed
]
- Prasad NK, Decker SJ: SH2-containing 5'-inositol phosphatase, SHIP2, regulates cytoskeleton organization and ligand-dependent down-regulation of the epidermal growth factor receptor. J Biol Chem. 2005 Apr 1;280(13):13129-36. Epub 2005 Jan 24. [PubMed
]
- Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed
]
- Zhang Y, Wolf-Yadlin A, Ross PL, Pappin DJ, Rush J, Lauffenburger DA, White FM: Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol Cell Proteomics. 2005 Sep;4(9):1240-50. Epub 2005 Jun 11. [PubMed
]
- Koch A, Mancini A, El Bounkari O, Tamura T: The SH2-domian-containing inositol 5-phosphatase (SHIP)-2 binds to c-Met directly via tyrosine residue 1356 and involves hepatocyte growth factor (HGF)-induced lamellipodium formation, cell scattering and cell spreading. Oncogene. 2005 May 12;24(21):3436-47. [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
]
- Raaijmakers JH, Deneubourg L, Rehmann H, de Koning J, Zhang Z, Krugmann S, Erneux C, Bos JL: The PI3K effector Arap3 interacts with the PI(3,4,5)P3 phosphatase SHIP2 in a SAM domain-dependent manner. Cell Signal. 2007 Jun;19(6):1249-57. Epub 2007 Jan 20. [PubMed
]
- Zhuang G, Hunter S, Hwang Y, Chen J: Regulation of EphA2 receptor endocytosis by SHIP2 lipid phosphatase via phosphatidylinositol 3-Kinase-dependent Rac1 activation. J Biol Chem. 2007 Jan 26;282(4):2683-94. Epub 2006 Nov 29. [PubMed
]
- Artemenko Y, Gagnon A, Ibrahim S, Sorisky A: Regulation of PDGF-stimulated SHIP2 tyrosine phosphorylation and association with Shc in 3T3-L1 preadipocytes. J Cell Physiol. 2007 Jun;211(3):598-607. [PubMed
]
- Marion E, Kaisaki PJ, Pouillon V, Gueydan C, Levy JC, Bodson A, Krzentowski G, Daubresse JC, Mockel J, Behrends J, Servais G, Szpirer C, Kruys V, Gauguier D, Schurmans S: The gene INPPL1, encoding the lipid phosphatase SHIP2, is a candidate for type 2 diabetes in rat and man. Diabetes. 2002 Jul;51(7):2012-7. [PubMed
]
- Kaisaki PJ, Delepine M, Woon PY, Sebag-Montefiore L, Wilder SP, Menzel S, Vionnet N, Marion E, Riveline JP, Charpentier G, Schurmans S, Levy JC, Lathrop M, Farrall M, Gauguier D: Polymorphisms in type II SH2 domain-containing inositol 5-phosphatase (INPPL1, SHIP2) are associated with physiological abnormalities of the metabolic syndrome. Diabetes. 2004 Jul;53(7):1900-4. [PubMed
]
- Kagawa S, Sasaoka T, Yaguchi S, Ishihara H, Tsuneki H, Murakami S, Fukui K, Wada T, Kobayashi S, Kimura I, Kobayashi M: Impact of SRC homology 2-containing inositol 5'-phosphatase 2 gene polymorphisms detected in a Japanese population on insulin signaling. J Clin Endocrinol Metab. 2005 May;90(5):2911-9. Epub 2005 Feb 1. [PubMed
]
- Marcano AC, Burke B, Gungadoo J, Wallace C, Kaisaki PJ, Woon PY, Farrall M, Clayton D, Brown M, Dominiczak A, Connell JM, Webster J, Lathrop M, Caulfield M, Samani N, Gauguier D, Munroe PB: Genetic association analysis of inositol polyphosphate phosphatase-like 1 (INPPL1, SHIP2) variants with essential hypertension. J Med Genet. 2007 Sep;44(9):603-5. Epub 2007 Jun 8. [PubMed
]
- Wolf-Yadlin A, Hautaniemi S, Lauffenburger DA, White FM: Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks. Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5860-5. Epub 2007 Mar 26. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- 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
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
13063 |
| Enzyme 6 Name |
Inositol-tetrakisphosphate 1-kinase |
| Enzyme 6 Synonyms |
- Inositol 1,3,4-trisphosphate 5/6-kinase
- Inositol-triphosphate 5/6-kinase
- Ins(1,3,4)P(3) 5/6-kinase
|
| Enzyme 6 Gene Name |
ITPK1 |
| Enzyme 6 Protein Sequence |
>Inositol-tetrakisphosphate 1-kinase
MQTFLKGKRVGYWLSEKKIKKLNFQAFAELCRKRGMEVVQLNLSRPIEEQGPLDVIIHKL
TDVILEADQNDSQSLELVHRFQEYIDAHPETIVLDPLPAIRTLLDRSKSYELIRKIEAYM
EDDRICSPPFMELTSLCGDDTMRLLEKNGLTFPFICKTRVAHGTNSHEMAIVFNQEGLNA
IQPPCVVQNFINHNAVLYKVFVVGESYTVVQRPSLKNFSAGTSDRESIFFNSHNVSKPES
SSVLTELDKIEGVFERPSDEVIRELSRALRQALGVSLFGIDIIINNQTGQHAVIDINAFP
GYEGVSEFFTDLLNHIATVLQGQSTAMAATGDVALLRHSKLLAEPAGGLVGERTCSASPG
CCGSMMGQDAPWKAEADAGGTAKLPHQRLGCNAGVSPSFQQHCVASLATKASSQ
|
| Enzyme 6 Number of Residues |
414 |
| Enzyme 6 Molecular Weight |
45620.6 |
| Enzyme 6 Theoretical pI |
6.09 |
| Enzyme 6 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- inositol or phosphatidylinositol kinase activity
- inositol tetrakisphosphate 1-kinase activity
- inositol tetrakisphosphate kinase activity
- inositol trisphosphate kinase activity
- inositol-1,3,4-trisphosphate 5/6-kinase activity
- ion binding
- kinase activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- alcohol metabolic process
- inositol metabolic process
- inositol phosphate metabolic process
- inositol trisphosphate metabolic process
- metabolic process
- polyol metabolic process
- small molecule metabolic process
|
| Component |
|
|
| Enzyme 6 General Function |
Involved in catalytic activity |
| Enzyme 6 Specific Function |
Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3. Phosphorylates Ins(3,4,5,6)P4 at position 1 to form Ins(1,3,4,5,6)P5. This reaction is thought to have regulatory importance, since Ins(3,4,5,6)P4 is an inhibitor of plasma membrane Ca(2+)-activated Cl(-) channels, while Ins(1,3,4,5,6)P5 is not. Also phosphorylates Ins(1,3,4)P3 on O-5 and O-6 to form Ins(1,3,4,6)P4, an essential molecule in the hexakisphosphate (InsP6) pathway. Also acts as an inositol polyphosphate phosphatase that dephosphorylate Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4 to Ins(1,3,4)P3, and Ins(1,3,4,5,6)P5 to Ins(3,4,5,6)P4. May also act as an isomerase that interconverts the inositol tetraphosphate isomers Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4 in the presence of ADP and magnesium. Probably acts as the rate-limiting enzyme of the InsP6 pathway. Modifies TNF-alpha-induced apoptosis by interfering with the activation of TNFRSF1A-associated death domain |
| Enzyme 6 Pathways |
- Inositol Metabolism (map00562
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 6 Reactions |
- (1) ATP + 1D-myo-inositol 1,3,4-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate [RN:R03428]
- (2) ATP + 1D-myo-inositol 1,3,4-trisphosphate = ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate [RN:R03429]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
12006346  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q13572  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
ITPK1_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1245 bp
ATGCAGACCTTTCTGAAAGGGAAGAGAGTTGGCTACTGGCTGAGCGAGAAGAAAATCAAG
AAGCTGAATTTCCAGGCCTTCGCCGAGCTGTGCAGGAAGCGAGGGATGGAGGTTGTGCAG
CTGAACCTTAGCCGGCCGATCGAGGAGCAGGGCCCCCTGGACGTCATCATCCACAAGCTG
ACTGACGTCATCCTTGAAGCCGACCAGAATGATAGCCAGTCCCTGGAGCTGGTGCACAGG
TTCCAGGAGTACATCGATGCCCACCCTGAGACCATCGTCCTGGACCCGCTCCCTGCCATC
AGAACCCTGCTTGACCGCTCCAAGTCCTATGAGCTCATCCGGAAGATTGAGGCCTACATG
GAAGACGACAGGATCTGCTCGCCACCCTTCATGGAGCTCACGAGCCTGTGCGGGGATGAC
ACCATGCGGCTGCTGGAGAAGAACGGCTTGACTTTCCCATTCATTTGCAAAACCAGAGTG
GCTCATGGCACCAACTCTCACGAGATGGCTATCGTGTTCAACCAGGAGGGCCTGAACGCC
ATCCAGCCACCCTGCGTGGTCCAGAATTTCATCAACCACAACGCCGTCCTGTACAAGGTG
TTCGTGGTTGGCGAGTCCTACACCGTGGTCCAGAGGCCCTCACTCAAGAACTTCTCCGCA
GGCACATCAGACCGTGAGTCCATCTTCTTCAACAGCCACAACGTGTCAAAGCCGGAGTCG
TCATCGGTCCTGACGGAGCTGGACAAGATCGAGGGCGTGTTCGAGCGGCCGAGCGACGAG
GTCATCCGGGAGCTCTCCCGGGCCCTGCGGCAGGCACTGGGCGTGTCACTCTTTGGCATC
GACATCATCATCAACAACCAGACAGGGCAGCACGCCGTCATTGACATCAATGCCTTCCCA
GGCTACGAGGGCGTGAGCGAGTTCTTCACAGACCTCCTGAACCACATCGCCACTGTCCTG
CAGGGCCAGAGCACAGCCATGGCAGCCACAGGGGACGTGGCCCTGCTGAGGCACAGCAAG
CTTCTGGCCGAGCCGGCGGGCGGCCTGGTGGGCGAGCGGACATGCAGCGCCAGCCCCGGC
TGCTGCGGCAGCATGATGGGCCAGGACGCGCCCTGGAAGGCTGAGGCCGACGCGGGCGGC
ACCGCCAAGCTGCCGCACCAGAGACTCGGCTGCAACGCCGGCGTGTCGCCCAGCTTCCAG
CAGCATTGTGTGGCCTCCCTGGCCACCAAGGCCTCCTCCCAGTAG
|
| Enzyme 6 GenBank Gene ID |
AF279372  |
| Enzyme 6 GeneCard ID |
ITPK1  |
| Enzyme 6 GenAtlas ID |
ITPK1  |
| Enzyme 6 HGNC ID |
HGNC:6177  |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
14q31 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Wilson MP, Majerus PW: Isolation of inositol 1,3,4-trisphosphate 5/6-kinase, cDNA cloning and expression of the recombinant enzyme. J Biol Chem. 1996 May 17;271(20):11904-10. [PubMed
]
- Yang X, Shears SB: Multitasking in signal transduction by a promiscuous human Ins(3,4,5,6)P(4) 1-kinase/Ins(1,3,4)P(3) 5/6-kinase. Biochem J. 2000 Nov 1;351 Pt 3:551-5. [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
]
- Wilson MP, Sun Y, Cao L, Majerus PW: Inositol 1,3,4-trisphosphate 5/6-kinase is a protein kinase that phosphorylates the transcription factors c-Jun and ATF-2. J Biol Chem. 2001 Nov 2;276(44):40998-1004. Epub 2001 Aug 31. [PubMed
]
- Ho MW, Yang X, Carew MA, Zhang T, Hua L, Kwon YU, Chung SK, Adelt S, Vogel G, Riley AM, Potter BV, Shears SB: Regulation of Ins(3,4,5,6)P(4) signaling by a reversible kinase/phosphatase. Curr Biol. 2002 Mar 19;12(6):477-82. [PubMed
]
- Sun Y, Wilson MP, Majerus PW: Inositol 1,3,4-trisphosphate 5/6-kinase associates with the COP9 signalosome by binding to CSN1. J Biol Chem. 2002 Nov 29;277(48):45759-64. Epub 2002 Sep 24. [PubMed
]
- Sun Y, Mochizuki Y, Majerus PW: Inositol 1,3,4-trisphosphate 5/6-kinase inhibits tumor necrosis factor-induced apoptosis. J Biol Chem. 2003 Oct 31;278(44):43645-53. Epub 2003 Aug 18. [PubMed
]
- Qian X, Mitchell J, Wei SJ, Williams J, Petrovich RM, Shears SB: The Ins(1,3,4)P3 5/6-kinase/Ins(3,4,5,6)P4 1-kinase is not a protein kinase. Biochem J. 2005 Jul 15;389(Pt 2):389-95. [PubMed
]
- Miller GJ, Wilson MP, Majerus PW, Hurley JH: Specificity determinants in inositol polyphosphate synthesis: crystal structure of inositol 1,3,4-trisphosphate 5/6-kinase. Mol Cell. 2005 Apr 15;18(2):201-12. [PubMed
]
- Chamberlain PP, Qian X, Stiles AR, Cho J, Jones DH, Lesley SA, Grabau EA, Shears SB, Spraggon G: Integration of inositol phosphate signaling pathways via human ITPK1. J Biol Chem. 2007 Sep 21;282(38):28117-25. Epub 2007 Jul 6. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
16706 |
| Enzyme 7 Name |
cDNA FLJ35540 fis, clone SPLEN2002493, highly similar to Phosphatidylinositol 4,5-bisphosphate5-phosphatase A (EC 3.1.3.56) |
| Enzyme 7 Synonyms |
- SubName: Phosphatidylinositol (4,5) bisphosphate 5-phosphatase, A, isoform CRA_a
|
| Enzyme 7 Gene Name |
PIB5PA |
| Enzyme 7 Protein Sequence |
>cDNA FLJ35540 fis, clone SPLEN2002493, highly similar to Phosphatidylinositol 4,5-bisphosphate5-phosphatase A (EC 3.1.3.56)
MALPRLGTQSTGPGRCLSPNLQAQEAPAPVTTSSSTSTLSSSPWSAQPTWKSDPGFRITV
VTWNVGTAMPPDDVTSLLHLGGGDDSDGADMIAIGLQEVNSMLNKRLKDALFTDQWSELF
MDALGPFNFVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRL
AAFGHMLCFLNCHLPAHMDKAEQRKDNFQTILSLQQFQGPGAQGILDHDLVFWFGDLNFR
IESYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDVGTNKY
DTSAKKRKPAWTDRILWKVKAPGGGPSPSGRKSHRLQVTQHSYRSHMEYTVSDHKPVAAQ
FLLQFAFRDDMPLVRLEVADEWVRPEQAVVRYRMETVFARSSWDWIGLYRVGFRHCKDYV
AYVWAKHEDVDGNTYQVTFSEESLPKGHGDFILGYYSHNHSILIGITEPFQISLPSSELA
SSSTDSSGTSSEGEDDSTLELLAPKSRSPSPGKSKRHRSRSPGLARFPGLALRPSSRERR
GASRSPSPQSRRLSRVAPDRSSNGSSRGSSEEGPSGLPGPWAFPPAVPRSLGLLPALRLE
TVDPGGGGSWGPDREALAPNSLSPSPQGHRGLEEGGLGP
|
| Enzyme 7 Number of Residues |
639 |
| Enzyme 7 Molecular Weight |
70465 |
| Enzyme 7 Theoretical pI |
8.24 |
| Enzyme 7 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphatase activity
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 7 General Function |
Not Available |
| Enzyme 7 Specific Function |
Not Available |
| Enzyme 7 Pathways |
Not Available |
| Enzyme 7 Reactions |
- (1) D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate [RN:R03394]
- (2) 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate [RN:R03430] ALL_REAC R03394 R03430
|
| 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 |
B3KS54  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
B3KS54_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
Not Available |
| Enzyme 7 GenBank Gene ID |
AK092859  |
| Enzyme 7 GeneCard ID |
B3KS54  |
| Enzyme 7 GenAtlas ID |
Not Available |
| Enzyme 7 HGNC ID |
Not Available |
| Enzyme 7 Chromosome Location |
22 |
| Enzyme 7 Locus |
22q11.2-q13.2 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
Not Available |
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
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|
| Enzyme 8 ID |
16707 |
| Enzyme 8 Name |
cDNA, FLJ92960, Homo sapiens skeletal muscle and kidney enriched inositolphosphatase (SKIP), transcript variant 2, mRNA (Skeletal muscle and kidney enriched inositol phosphatase, isoform CRA_a) |
| Enzyme 8 Synonyms |
Not Available |
| Enzyme 8 Gene Name |
SKIP |
| Enzyme 8 Protein Sequence |
>cDNA, FLJ92960, Homo sapiens skeletal muscle and kidney enriched inositolphosphatase (SKIP), transcript variant 2, mRNA (Skeletal muscle and kidney enriched inositol phosphatase, isoform CRA_a)
MDVLSPLSFIKVSHVRMQGILLLVFAKYQHLPYIQILSTKSTPTGLFGYWGNKGGVNICL
KLYGYYVSIINCHLPPHISNNYQRLEHFDRILEMQNCEGRDIPNILDHDLIIWFGDMNFR
IEDFGLHFVRESIKNRCYGGLWEKDQLSIAKKHDPLLREFQEGRLLFPPTYKFDRNSNDY
DTSEKKRKPAWTDRILWRLKRQPCAGPDTPIPPASHFSLSLRGYSSHMTYGISDHKPVSG
TFDLELKPLVSAPLIVLMPEDLWTVENDMMVSYSSTSDFPSSPWDWIGLYKVGLRDVNDY
VSYAWVGDSKVSCSDNLNQVYIDISNIPTTEDEFLLCYYSNSLRSVVGISRPFQIPPGSL
REDPLGEAQPQI
|
| Enzyme 8 Number of Residues |
372 |
| Enzyme 8 Molecular Weight |
42784 |
| Enzyme 8 Theoretical pI |
6.43 |
| Enzyme 8 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphatase activity
- phosphoric ester hydrolase activity
- phosphoric monoester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 8 General Function |
Not Available |
| Enzyme 8 Specific Function |
Not Available |
| Enzyme 8 Pathways |
Not Available |
| Enzyme 8 Reactions |
Not Available |
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
Not Available |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
B2R6I2  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
B2R6I2_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
Not Available |
| Enzyme 8 GenBank Gene ID |
AK312585  |
| Enzyme 8 GeneCard ID |
B2R6I2  |
| Enzyme 8 GenAtlas ID |
Not Available |
| Enzyme 8 HGNC ID |
Not Available |
| Enzyme 8 Chromosome Location |
17 |
| Enzyme 8 Locus |
17p13.3 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
Not Available |
| Enzyme 8 Metabolite References |
Not Available |