Q13615 · MTMR3_HUMAN
- ProteinPhosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR3
- GeneMTMR3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1198 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 (PubMed:11302699, PubMed:11676921, PubMed:12646134).
Could also have a molecular sequestering/adapter activity and regulate biological processes independently of its phosphatase activity. It includes the regulation of midbody abscission during mitotic cytokinesis (PubMed:25659891).
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphate
- a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate
- 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate
- 1,2-dioctanoyl-sn-glycero-3-phospho-(1-D-myo-inositol-3-phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate
- 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-phosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + phosphate
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 326 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 326 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 351 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 351 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 352 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 352 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Active site | 413 | Phosphocysteine intermediate | ||||
Sequence: C | ||||||
Binding site | 414 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 414 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 415 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 415 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 416 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 416 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 417 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 417 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 418 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 418 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 419 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 419 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 455 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 459 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-bisphosphate) (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 459 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 1125 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1128 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1141 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1144 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1149 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1152 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1171 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1174 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended namePhosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR3
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ13615
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_035656 | 221 | in a breast cancer sample; somatic mutation | |||
Sequence: V → L | ||||||
Mutagenesis | 413 | Loss of lipid phosphatase activity. No effect on function in mitotic abscission. | ||||
Sequence: C → S | ||||||
Mutagenesis | 1174 | Loss of function in mitotic abscission. Decreased interaction with PLK1. | ||||
Sequence: C → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,128 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000094936 | 1-1198 | UniProt | Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR3 | |||
Sequence: MDEETRHSLECIQANQIFPRKQLIREDENLQVPFLELHGESTEFVGRAEDAIIALSNYRLHIKFKESLVNVPLQLIESVECRDIFQLHLTCKDCKVIRCQFSTFEQCQEWLKRLNNAIRPPAKIEDLFSFAYHAWCMEVYASEKEQHGDLCRPGEHVTSRFKNEVERMGFDMNNAWRISNINEKYKLCGSYPQELIVPAWITDKELESVSSFRSWKRIPAVIYRHQSNGAVIARCGQPEVSWWGWRNADDEHLVQSVAKACASDSRSSGSKLSTRNTSRDFPNGGDLSDVEFDSSLSNASGAESLAIQPQKLLILDARSYAAAVANRAKGGGCECPEYYPNCEVVFMGMANIHSIRRSFQSLRLLCTQMPDPGNWLSALESTKWLHHLSVLLKSALLVVHAVDQDQRPVLVHCSDGWDRTPQIVALAKLLLDPYYRTIEGFQVLVEMEWLDFGHKFADRCGHGENSDDLNERCPVFLQWLDCVHQLQRQFPCSFEFNEAFLVKLVQHTYSCLFGTFLCNNAKERGEKHTQERTCSVWSLLRAGNKAFKNLLYSSQSEAVLYPVCHVRNLMLWSAVYLPCPSPTTPVDDSCAPYPAPGTSPDDPPLSRLPKTRSYDNLTTACDNTVPLASRRCSDPSLNEKWQEHRRSLELSSLAGPGEDPLSADSLGKPTRVPGGAELSVAAGVAEGQMENILQEATKEESGVEEPAHRAGIEIQEGKEDPLLEKESRRKTPEASAIGLHQDPELGDAALRSHLDMSWPLFSQGISEQQSGLSVLLSSLQVPPRGEDSLEVPVEQFRIEEIAEGREEAVLPIPVDAKVGYGTSQSCSLLPSQVPFETRGPNVDSSTDMLVEDKVKSVSGPQGHHRSCLVNSGKDRLPQTMEPSPSETSLVERPQVGSVVHRTSLGSTLSLTRSPCALPLAECKEGLVCNGAPETENRASEQPPGLSTLQMYPTPNGHCANGEAGRSKDSLSRQLSAMSCSSAHLHSRNLHHKWLHSHSGRPSATSSPDQPSRSHLDDDGMSVYTDTIQQRLRQIESGHQQEVETLKKQVQELKSRLESQYLTSSLHFNGDFGDEVTSIPDSESNLDQNCLSRCSTEIFSEASWEQVDKQDTEMTRWLPDHLAAHCYACDSAFWLASRKHHCRNCGNVFCSSCCNQKVPVPSQQLFEPSRVCKSCYSSLHPTSSSIDLELDKPIAATSN | |||||||
Modified residue (large scale data) | 5 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 8 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 8 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 611 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 613 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 613 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 614 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 618 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 633 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 633 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 647 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 647 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 651 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 651 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 701 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 731 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 731 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 788 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 883 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 903 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 906 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 909 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 909 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 913 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1006 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1064 | UniProt | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q13615 | EXOSC5 Q9NQT4 | 3 | EBI-371938, EBI-371876 | |
BINARY | Q13615 | LONRF1 Q17RB8 | 3 | EBI-371938, EBI-2341787 | |
BINARY | Q13615 | MTOR P42345 | 3 | EBI-371938, EBI-359260 | |
BINARY | Q13615 | RPTOR Q8N122 | 3 | EBI-371938, EBI-1567928 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region, coiled coil, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 155-576 | Myotubularin phosphatase | ||||
Sequence: EHVTSRFKNEVERMGFDMNNAWRISNINEKYKLCGSYPQELIVPAWITDKELESVSSFRSWKRIPAVIYRHQSNGAVIARCGQPEVSWWGWRNADDEHLVQSVAKACASDSRSSGSKLSTRNTSRDFPNGGDLSDVEFDSSLSNASGAESLAIQPQKLLILDARSYAAAVANRAKGGGCECPEYYPNCEVVFMGMANIHSIRRSFQSLRLLCTQMPDPGNWLSALESTKWLHHLSVLLKSALLVVHAVDQDQRPVLVHCSDGWDRTPQIVALAKLLLDPYYRTIEGFQVLVEMEWLDFGHKFADRCGHGENSDDLNERCPVFLQWLDCVHQLQRQFPCSFEFNEAFLVKLVQHTYSCLFGTFLCNNAKERGEKHTQERTCSVWSLLRAGNKAFKNLLYSSQSEAVLYPVCHVRNLMLWSAVY | ||||||
Compositional bias | 265-283 | Polar residues | ||||
Sequence: SRSSGSKLSTRNTSRDFPN | ||||||
Region | 265-285 | Disordered | ||||
Sequence: SRSSGSKLSTRNTSRDFPNGG | ||||||
Region | 590-612 | Disordered | ||||
Sequence: CAPYPAPGTSPDDPPLSRLPKTR | ||||||
Region | 650-669 | Disordered | ||||
Sequence: LSSLAGPGEDPLSADSLGKP | ||||||
Region | 716-735 | Disordered | ||||
Sequence: EGKEDPLLEKESRRKTPEAS | ||||||
Region | 855-891 | Disordered | ||||
Sequence: KSVSGPQGHHRSCLVNSGKDRLPQTMEPSPSETSLVE | ||||||
Compositional bias | 872-891 | Polar residues | ||||
Sequence: GKDRLPQTMEPSPSETSLVE | ||||||
Region | 933-974 | Disordered | ||||
Sequence: ETENRASEQPPGLSTLQMYPTPNGHCANGEAGRSKDSLSRQL | ||||||
Compositional bias | 934-954 | Polar residues | ||||
Sequence: TENRASEQPPGLSTLQMYPTP | ||||||
Region | 993-1019 | Disordered | ||||
Sequence: WLHSHSGRPSATSSPDQPSRSHLDDDG | ||||||
Coiled coil | 1029-1062 | |||||
Sequence: QRLRQIESGHQQEVETLKKQVQELKSRLESQYLT | ||||||
Zinc finger | 1119-1179 | FYVE-type | ||||
Sequence: DHLAAHCYACDSAFWLASRKHHCRNCGNVFCSSCCNQKVPVPSQQLFEPSRVCKSCYSSLH |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q13615-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameB
- SynonymsFYVE-DSP1b
- Length1,198
- Mass (Da)133,619
- Last updated2003-07-19 v3
- ChecksumFE6F4B165074D5F8
Q13615-2
- NameA
- SynonymsFYVE-DSP1a
- Differences from canonical
- 1076-1112: Missing
- 1142-1142: R → RDTDRVDQTW
Q13615-3
- NameC
- SynonymsFYVE-DSP1c
- Differences from canonical
- 1076-1112: Missing
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 265-283 | Polar residues | ||||
Sequence: SRSSGSKLSTRNTSRDFPN | ||||||
Sequence conflict | 560-578 | in Ref. 7 | ||||
Sequence: LYPVCHVRNLMLWSAVYLP → CILQPFHCGQQKEFGVGYI | ||||||
Compositional bias | 872-891 | Polar residues | ||||
Sequence: GKDRLPQTMEPSPSETSLVE | ||||||
Compositional bias | 934-954 | Polar residues | ||||
Sequence: TENRASEQPPGLSTLQMYPTP | ||||||
Alternative sequence | VSP_007781 | 1076-1112 | in isoform A and isoform C | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_007782 | 1142 | in isoform A | |||
Sequence: R → RDTDRVDQTW |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF233436 EMBL· GenBank· DDBJ | AAF40203.2 EMBL· GenBank· DDBJ | mRNA | ||
AF233437 EMBL· GenBank· DDBJ | AAF40204.1 EMBL· GenBank· DDBJ | mRNA | ||
AF233438 EMBL· GenBank· DDBJ | AAF40205.1 EMBL· GenBank· DDBJ | mRNA | ||
AB002369 EMBL· GenBank· DDBJ | BAA20826.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
CR456525 EMBL· GenBank· DDBJ | CAG30411.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471095 EMBL· GenBank· DDBJ | EAW59852.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471095 EMBL· GenBank· DDBJ | EAW59855.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC142713 EMBL· GenBank· DDBJ | AAI42714.1 EMBL· GenBank· DDBJ | mRNA | ||
BC148216 EMBL· GenBank· DDBJ | AAI48217.1 EMBL· GenBank· DDBJ | mRNA | ||
BC152455 EMBL· GenBank· DDBJ | AAI52456.1 EMBL· GenBank· DDBJ | mRNA | ||
AC003071 EMBL· GenBank· DDBJ | AAB83949.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U58034 EMBL· GenBank· DDBJ | AAC79119.1 EMBL· GenBank· DDBJ | Genomic DNA |