MTMR4
entrez
9110
canonical
uniprot
Q9NYA4
canonical
ensembl
ENSG00000108389
resolver
ensp
ENSP00000325285
resolver
ensp
ENSP00000507664
resolver
enst
ENST00000323456
resolver
enst
ENST00000682306
resolver
genesymbol
MTMR4
resolver
genesymbol_syn
KIAA0647
resolver
genesymbol_syn
ZFYVE11
resolver
hgnc
HGNC:7452
resolver
uniprot
A0A804HJV7
resolver
uniprot
D3DTZ6
resolver
uniprot
Q8IV27
resolver
uniprot
Q9Y4D5
resolver
uniprot_entry
A0A804HJV7_HUMAN
resolver
uniprot_entry
MTMR4_HUMAN
resolver
uniprot_sec
D3DTZ6
resolver
uniprot_sec
Q8IV27
resolver
uniprot_sec
Q9Y4D5
resolver
activity_regulation
ACTIVITY REGULATION: The phosphatidylinositol-3-phosphate phosphatase activity is inhibited by vanadate. {ECO:0000269|PubMed:11302699}.
uniprot
proteins
amino_acid_sequence
MGEEGPPSLEYIQAKDLFPPKELVKEEENLQVPFTVLQGEGVEFLGRAADALIAISNYRLHIKFKDSVINVPLRMIDSVESRDMFQLHISCKDSKVVRCHFSTFKQCQEWLSRLSRATARPAKPEDLFAFAYHAWCLGLTEEDQHTHLCQPGEHIRCRQEAELARMGFDLQNVWRVSHINSNYKLCPSYPQKLLVPVWITDKELENVASFRSWKRIPVVVYRHLRNGAAIARCSQPEISWWGWRNADDEYLVTSIAKACALDPGTRATGGSLSTGNNDTSEACDADFDSSLTACSGVESTAAPQKLLILDARSYTAAVANRAKGGGCECEEYYPNCEVVFMGMANIHAIRNSFQYLRAVCSQMPDPSNWLSALESTKWLQHLSVMLKAAVLVANTVDREGRPVLVHCSDGWDRTPQIVALAKILLDPYYRTLEGFQVLVESDWLDFGHKFGDRCGHQENVEDQNEQCPVFLQWLDSVHQLLKQFPCLFEFNEAFLVKLVQHTYSCLYGTFLANNPCEREKRNIYKRTCSVWALLRAGNKNFHNFLYTPSSDMVLHPVCHVRALHLWTAVYLPASSPCTLGEENMDLYLSPVAQSQEFSGRSLDRLPKTRSMDDLLSACDTSSPLTRTSSDPNLNNHCQEVRVGLEPWHSNPEGSETSFVDSGVGGPQQTVGEVGLPPPLPSSQKDYLSNKPFKSHKSCSPSYKLLNTAVPREMKSNTSDPEIKVLEETKGPAPDPSAQDELGRTLDGIGEPPEHCPETEAVSALSKVISNKCDGVCNFPESSQNSPTGTPQQAQPDSMLGVPSKCVLDHSLSTVCNPPSAACQTPLDPSTDFLNQDPSGSVASISHQEQLSSVPDLTHGEEDIGKRGNNRNGQLLENPRFGKMPLELVRKPISQSQISEFSFLGSNWDSFQGMVTSFPSGEATPRRLLSYGCCSKRPNSKQMRATGPCFGGQWAQREGVKSPVCSSHSNGHCTGPGGKNQMWLSSHPKQVSSTKPVPLNCPSPVPPLYLDDDGLPFPTDVIQHRLRQIEAGYKQEVEQLRRQVRELQMRLDIRHCCAPPAEPPMDYEDDFTCLKESDGSDTEDFGSDHSEDCLSEASWEPVDKKETEVTRWVPDHMASHCYNCDCEFWLAKRRHHCRNCGNVFCAGCCHLKLPIPDQQLYDPVLVCNSCYEHIQVSRARELMSQQLKKPIATASS
uniprot
proteins
ec_number
3.1.3.95
uniprot
proteins
function
FUNCTION: Lipid phosphatase that specifically dephosphorylates the D-3 position of phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate, generating phosphatidylinositol and phosphatidylinositol 5-phosphate (PubMed:11302699, PubMed:16787938, PubMed:20736309, PubMed:27625994, PubMed:29962048, PubMed:30944173). Decreases the levels of phosphatidylinositol 3-phosphate, a phospholipid found in cell membranes where it acts as key regulator of both cell signaling and intracellular membrane traffic, in a subset of endosomal membranes to negatively regulate both endocytic recycling and trafficking and/or maturation of endosomes toward lysosomes (PubMed:16787938, PubMed:20736309, PubMed:29962048). Through phosphatidylinositol 3-phosphate turnover in phagosome membranes regulates phagocytosis and phagosome maturation (PubMed:31543504). By decreasing phosphatidylinositol 3-monophosphate (PI3P) levels in immune cells it can also regulate the innate immune response (PubMed:30944173). Beside its lipid phosphatase activity, can also function as a molecular adapter to regulate midbody abscission during mitotic cytokinesis (PubMed:25659891). Can also negatively regulate TGF-beta and BMP signaling through Smad proteins dephosphorylation and retention in endosomes (PubMed:20061380, PubMed:23150675). {ECO:0000269|PubMed:11302699, ECO:0000269|PubMed:16787938, ECO:0000269|PubMed:20061380, ECO:0000269|PubMed:20736309, ECO:0000269|PubMed:23150675, ECO:0000269|PubMed:25659891, ECO:0000269|PubMed:27625994, ECO:0000269|PubMed:29962048, ECO:0000269|PubMed:30944173, ECO:0000269|PubMed:31543504}.
uniprot
proteins
mass_dalton
133353
uniprot
proteins
mutagenesis
MUTAGEN 11; /note="Y->A: Loss of function in mitotic abscission. Decreased interaction with CEP55."; /evidence="ECO:0000269|PubMed:25659891"; MUTAGEN 407; /note="C->A: Loss of phosphatase activity. Dominant negative."; /evidence="ECO:0000269|PubMed:20736309"; MUTAGEN 407; /note="C->S: No effect on function in mitotic abscission."; /evidence="ECO:0000269|PubMed:25659891"; MUTAGEN 1006; /note="P->A: Loss of interaction with NEDD4. Loss of ubiquitination."; /evidence="ECO:0000269|PubMed:19125695"; MUTAGEN 1169; /note="C->S: Loss of localization to early endosome membranes. No effect on function in mitotic abscission."; /evidence="ECO:0000269|PubMed:16787938, ECO:0000269|PubMed:25659891
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated. Ubiquitination by NEDD4 probably leads to proteasomal degradation. {ECO:0000269|PubMed:19125695}.; PTM: Phosphorylated by CDK1 during mitosis. {ECO:0000269|PubMed:25659891}.
uniprot
proteins
protein_family
Non-receptor class myotubularin subfamily
uniprot
proteins
protein_family
Protein-tyrosine phosphatase family
uniprot
proteins
pubmed
11302699
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
16787938
uniprot
proteins
pubmed
19125695
uniprot
proteins
pubmed
20061380
uniprot
proteins
pubmed
20736309
uniprot
proteins
pubmed
23150675
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25659891
uniprot
proteins
pubmed
27625994
uniprot
proteins
pubmed
29962048
uniprot
proteins
pubmed
30944173
uniprot
proteins
pubmed
31543504
uniprot
proteins
pubmed
9734811
uniprot
proteins
sequence_length
1195
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:11302699, ECO:0000269|PubMed:16787938, ECO:0000269|PubMed:20736309}; Peripheral membrane protein {ECO:0000269|PubMed:11302699}. Recycling endosome membrane {ECO:0000269|PubMed:20736309}; Peripheral membrane protein {ECO:0000269|PubMed:11302699}. Late endosome membrane {ECO:0000269|PubMed:29962048}; Peripheral membrane protein {ECO:0000269|PubMed:11302699}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:31543504}; Peripheral membrane protein {ECO:0000269|PubMed:11302699}.
uniprot
proteins