CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
184RISNINEKYKLCGSYubiquitination[1]
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. 
Interpro
 IPR010569; Myotub-related.
 IPR017906; Myotubularin_phosphatase_dom.
 IPR016130; Tyr_Pase_AS.
 IPR000306; Znf_FYVE.
 IPR017455; Znf_FYVE-rel.
 IPR011011; Znf_FYVE_PHD.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF01363; FYVE
 PF06602; Myotub-related 
SMART
 SM00064; FYVE 
PROSITE
 PS51339; PPASE_MYOTUBULARIN
 PS00383; TYR_PHOSPHATASE_1
 PS50056; TYR_PHOSPHATASE_2
 PS50178; ZF_FYVE 
PRINTS