Tag | Content |
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CPLM ID | CPLM-012167 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Myotubularin-related protein 3 |
Protein Synonyms/Alias | FYVE domain-containing dual specificity protein phosphatase 1; FYVE-DSP1; Zinc finger FYVE domain-containing protein 10 |
Gene Name | MTMR3 |
Gene Synonyms/Alias | KIAA0371; ZFYVE10 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
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184 | RISNINEKYKLCGSY | ubiquitination | [1] |
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Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] |
Functional Description | Phosphatase that acts on lipids with a phosphoinositol headgroup. Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate. May also dephosphorylate proteins phosphorylated on Ser, Thr, and Tyr residues. |
Sequence Annotation | DOMAIN 155 576 Myotubularin phosphatase. ZN_FING 1119 1179 FYVE-type. REGION 326 329 Substrate binding (By similarity). REGION 351 352 Substrate binding (By similarity). REGION 413 419 Substrate binding (By similarity). ACT_SITE 413 413 Phosphocysteine intermediate (By BINDING 459 459 Substrate (By similarity). MOD_RES 613 613 Phosphoserine (By similarity). MOD_RES 633 633 Phosphoserine. MOD_RES 647 647 Phosphoserine. MOD_RES 731 731 Phosphothreonine. MOD_RES 1181 1181 Phosphothreonine (By similarity). |
Keyword | Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Hydrolase; Membrane; Metal-binding; Phosphoprotein; Polymorphism; Protein phosphatase; Reference proteome; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1198 AA |
Protein Sequence | MDEETRHSLE CIQANQIFPR KQLIREDENL QVPFLELHGE STEFVGRAED AIIALSNYRL 60 HIKFKESLVN VPLQLIESVE CRDIFQLHLT CKDCKVIRCQ FSTFEQCQEW LKRLNNAIRP 120 PAKIEDLFSF AYHAWCMEVY ASEKEQHGDL CRPGEHVTSR FKNEVERMGF DMNNAWRISN 180 INEKYKLCGS YPQELIVPAW ITDKELESVS SFRSWKRIPA VIYRHQSNGA VIARCGQPEV 240 SWWGWRNADD EHLVQSVAKA CASDSRSSGS KLSTRNTSRD FPNGGDLSDV EFDSSLSNAS 300 GAESLAIQPQ KLLILDARSY AAAVANRAKG GGCECPEYYP NCEVVFMGMA NIHSIRRSFQ 360 SLRLLCTQMP DPGNWLSALE STKWLHHLSV LLKSALLVVH AVDQDQRPVL VHCSDGWDRT 420 PQIVALAKLL LDPYYRTIEG FQVLVEMEWL DFGHKFADRC GHGENSDDLN ERCPVFLQWL 480 DCVHQLQRQF PCSFEFNEAF LVKLVQHTYS CLFGTFLCNN AKERGEKHTQ ERTCSVWSLL 540 RAGNKAFKNL LYSSQSEAVL YPVCHVRNLM LWSAVYLPCP SPTTPVDDSC APYPAPGTSP 600 DDPPLSRLPK TRSYDNLTTA CDNTVPLASR RCSDPSLNEK WQEHRRSLEL SSLAGPGEDP 660 LSADSLGKPT RVPGGAELSV AAGVAEGQME NILQEATKEE SGVEEPAHRA GIEIQEGKED 720 PLLEKESRRK TPEASAIGLH QDPELGDAAL RSHLDMSWPL FSQGISEQQS GLSVLLSSLQ 780 VPPRGEDSLE VPVEQFRIEE IAEGREEAVL PIPVDAKVGY GTSQSCSLLP SQVPFETRGP 840 NVDSSTDMLV EDKVKSVSGP QGHHRSCLVN SGKDRLPQTM EPSPSETSLV ERPQVGSVVH 900 RTSLGSTLSL TRSPCALPLA ECKEGLVCNG APETENRASE QPPGLSTLQM YPTPNGHCAN 960 GEAGRSKDSL SRQLSAMSCS SAHLHSRNLH HKWLHSHSGR PSATSSPDQP SRSHLDDDGM 1020 SVYTDTIQQR LRQIESGHQQ EVETLKKQVQ ELKSRLESQY LTSSLHFNGD FGDEVTSIPD 1080 SESNLDQNCL SRCSTEIFSE ASWEQVDKQD TEMTRWLPDH LAAHCYACDS AFWLASRKHH 1140 CRNCGNVFCS SCCNQKVPVP SQQLFEPSRV CKSCYSSLHP TSSSIDLELD KPIAATSN 1198 |
Gene Ontology | GO:0005829; C:cytosol; TAS:Reactome. GO:0016020; C:membrane; IDA:UniProtKB. GO:0005634; C:nucleus; IDA:HPA. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IDA:UniProtKB. GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB. GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB. GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome. GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB. GO:0044281; P:small molecule metabolic process; TAS:Reactome. |
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