CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022375
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Myotubularin-related protein 4 
Protein Synonyms/Alias
 FYVE domain-containing dual specificity protein phosphatase 2; FYVE-DSP2; Zinc finger FYVE domain-containing protein 11 
Gene Name
 MTMR4 
Gene Synonyms/Alias
 KIAA0647; ZFYVE11 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
184SHINSNYKLCPSYPQubiquitination[1]
202VPVWITDKELENVASubiquitination[1]
257YLVTSIAKACALDPGubiquitination[1]
882LENPRFGKMPLELVRubiquitination[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
 Dephosphorylates proteins phosphorylated on Ser, Thr, and Tyr residues and low molecular weight phosphatase substrate para-nitrophenylphosphate. Phosphorylates phosphatidylinositol 3,4,5-trisphosphate (PIP3). 
Sequence Annotation
 DOMAIN 153 570 Myotubularin phosphatase.
 ZN_FING 1114 1174 FYVE-type.
 REGION 320 323 Substrate binding (By similarity).
 REGION 345 346 Substrate binding (By similarity).
 REGION 407 413 Substrate binding (By similarity).
 ACT_SITE 407 407 Phosphocysteine intermediate (By
 BINDING 453 453 Substrate (By similarity).  
Keyword
 Coiled coil; Complete proteome; Cytoplasm; Hydrolase; Membrane; Metal-binding; Polymorphism; Protein phosphatase; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1195 AA 
Protein Sequence
MGEEGPPSLE YIQAKDLFPP KELVKEEENL QVPFTVLQGE GVEFLGRAAD ALIAISNYRL 60
HIKFKDSVIN VPLRMIDSVE SRDMFQLHIS CKDSKVVRCH FSTFKQCQEW LSRLSRATAR 120
PAKPEDLFAF AYHAWCLGLT EEDQHTHLCQ PGEHIRCRQE AELARMGFDL QNVWRVSHIN 180
SNYKLCPSYP QKLLVPVWIT DKELENVASF RSWKRIPVVV YRHLRNGAAI ARCSQPEISW 240
WGWRNADDEY LVTSIAKACA LDPGTRATGG SLSTGNNDTS EACDADFDSS LTACSGVEST 300
AAPQKLLILD ARSYTAAVAN RAKGGGCECE EYYPNCEVVF MGMANIHAIR NSFQYLRAVC 360
SQMPDPSNWL SALESTKWLQ HLSVMLKAAV LVANTVDREG RPVLVHCSDG WDRTPQIVAL 420
AKILLDPYYR TLEGFQVLVE SDWLDFGHKF GDRCGHQENV EDQNEQCPVF LQWLDSVHQL 480
LKQFPCLFEF NEAFLVKLVQ HTYSCLYGTF LANNPCEREK RNIYKRTCSV WALLRAGNKN 540
FHNFLYTPSS DMVLHPVCHV RALHLWTAVY LPASSPCTLG EENMDLYLSP VAQSQEFSGR 600
SLDRLPKTRS MDDLLSACDT SSPLTRTSSD PNLNNHCQEV RVGLEPWHSN PEGSETSFVD 660
SGVGGPQQTV GEVGLPPPLP SSQKDYLSNK PFKSHKSCSP SYKLLNTAVP REMKSNTSDP 720
EIKVLEETKG PAPDPSAQDE LGRTLDGIGE PPEHCPETEA VSALSKVISN KCDGVCNFPE 780
SSQNSPTGTP QQAQPDSMLG VPSKCVLDHS LSTVCNPPSA ACQTPLDPST DFLNQDPSGS 840
VASISHQEQL SSVPDLTHGE EDIGKRGNNR NGQLLENPRF GKMPLELVRK PISQSQISEF 900
SFLGSNWDSF QGMVTSFPSG EATPRRLLSY GCCSKRPNSK QMRATGPCFG GQWAQREGVK 960
SPVCSSHSNG HCTGPGGKNQ MWLSSHPKQV SSTKPVPLNC PSPVPPLYLD DDGLPFPTDV 1020
IQHRLRQIEA GYKQEVEQLR RQVRELQMRL DIRHCCAPPA EPPMDYEDDF TCLKESDGSD 1080
TEDFGSDHSE DCLSEASWEP VDKKETEVTR WVPDHMASHC YNCDCEFWLA KRRHHCRNCG 1140
NVFCAGCCHL KLPIPDQQLY DPVLVCNSCY EHIQVSRARE LMSQQLKKPI ATASS 1195 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0031901; C:early endosome membrane; TAS:Reactome.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004722; F:protein serine/threonine phosphatase activity; TAS:Reactome.
 GO:0004725; F:protein tyrosine phosphatase activity; TAS:ProtInc.
 GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
 GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome. 
Interpro
 IPR010569; Myotub-related.
 IPR017906; Myotubularin_phosphatase_dom.
 IPR000387; Tyr/Dual-sp_Pase.
 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