Synj2
entrez
20975
canonical
uniprot
Q9D2G5
canonical
ensembl
ENSMUSG00000023805
resolver
ensp
ENSMUSP00000060382
resolver
ensp
ENSMUSP00000079164
resolver
ensp
ENSMUSP00000111451
resolver
ensp
ENSMUSP00000111456
resolver
ensp
ENSMUSP00000111457
resolver
ensp
ENSMUSP00000286480
resolver
ensp
ENSMUSP00000286481
resolver
enst
ENSMUST00000115785
resolver
enst
ENSMUST00000115790
resolver
enst
ENSMUST00000115791
resolver
genesymbol
Synj2
resolver
genesymbol_syn
Kiaa0348
resolver
uniprot
D3YZB2
resolver
uniprot
E9Q4P5
resolver
uniprot
F8WHD8
resolver
uniprot
O35404
resolver
uniprot
O88399
resolver
uniprot
O88400
resolver
uniprot
O88401
resolver
uniprot
O88402
resolver
uniprot
O88403
resolver
uniprot
O88404
resolver
uniprot
Q3TTB3
resolver
uniprot_entry
D3YZB2_MOUSE
resolver
uniprot_entry
E9Q4P5_MOUSE
resolver
uniprot_entry
F8WHD8_MOUSE
resolver
uniprot_entry
Q3TTB3_MOUSE
resolver
uniprot_entry
SYNJ2_MOUSE
resolver
uniprot_sec
O35404
resolver
uniprot_sec
O88399
resolver
uniprot_sec
O88400
resolver
uniprot_sec
O88401
resolver
uniprot_sec
O88402
resolver
uniprot_sec
O88403
resolver
uniprot_sec
O88404
resolver
amino_acid_sequence
MALSKGLRLLARLDPTGPSSVLLEARGRGDCLLFEAGAVATLAPEEKEVIKGLYSKLTDAYGCLGELRLQSGGVPLSFLVLVTGCMSVGRIPDAEIYKITATELYPLQEEAKEEDRLPTLKKILSSGVFYFAWPNDGACFDLTIRAQKQGDDGSEWGTSFFWNQLLHVPLRQHQVNCHNWLLKVICGVVTIRTVYASHKQAKACLISRISCERAGARFLTRGVNDDGHVSNFVETEQTIYMDDGVSSFVQIRGSVPLFWEQPGLQVGSHHLRLHRGLEANAPAFERHMVLLKEQYGKQVVVNLLGSRGGEEVLNRAFKKLLWASCHAGDTPMINFDFHQFAKGRKLEKLENLLRPQLQLHWEDFGVFAKGENVSPRFQKGTLRMNCLDCLDRTNTVQCFIALEVLHLQLESLGLNSKPIIDRFVESFKAMWSLNGHSLSKVFTGSRALEGKAKVGKLKDGARSMSRTIQSNFFDGVKQEAIKLLLVGDVYNEESTDKGRMLLDNTALLATPRILKAMTERQSEFTNFKRIQIAVGTWNVNGGKQFRSNLLGTAELTDWLLDAPQLSGAVDSQDDGSPADVFAIGFEEMVELSAGNIVNASTTNRKMWGEQLQKAISRSHRYILLTSAQLVGVCLYIFVRPYHVPFIRDVAIDTVKTGMGGKAGNKGAVGIRFQLHSTSFCFVCSHLTAGQSQVKERNEDYREITHKLSFPSGRNIFSHDYVFWCGDFNYRIDLTYEEVFYFVKRQDWKKLMEFDQLQLQKSSGKIFKDFHEGAVNFGPTYKYDVGSAAYDTSDKCRTPAWTDRVLWWRKKHPYDKTAGELNLLDSDLDGDPQIRHTWSPGTLKYYGRAELQASDHRPVLAIVEVEVQEVDVGARERVFQEVSSVQGPLDATVVVNLQSPTLEEKNEFPEDLRTELMQTLGNYGTIILVRINQGQMLVTFADSHSALSVLDVDGMKVKGRAVKIRPKTKDWLEGLREELLRKRDSMAPVSPTANSCLLEENFDFSSLDYESEGDVLEEDEDYLVDGFGQPVVSDSELGGDNSSDTMSSLTPASKSPALAKKKQHPTYKAGLMVKKSASDASISSGTHGQYSILQTAKLLPGAPQQPPKARTGISKPYNVKQIKTTNAQEAEAAIRCLLEASGGVPESAPGAIPLRNQGSSKPEATLGPPALPRRPAPRVPTMKKPTLRRTGKPMLPEENFEPQPVHFTMASQEMNLETPPPITATPIPPVPKPRTLQPGKGVEGRPSSGKPEPDEAPSVTGTVESPPPEAQEAPSLAPKVPPRRKKSAPAAFHLQVLQNNSQVLQGLTCSSSSPPSLKPDTHPLCLQVALGTSSARSPETHGPRVTEPEAASFHGNYPDPFWSLLHHPKLLNNTWLSKSSEPLDVGSRNPERTHTEPAQVNASLAERGLPPDHGGKDLSHWVTASNKDKRTTLGV
uniprot
proteins
ec_number
3.1.3.-
uniprot
proteins
ec_number
3.1.3.36
uniprot
proteins
ec_number
3.1.3.95
uniprot
proteins
function
FUNCTION: Phosphatase that hydrolyzes phosphate groups from the inositol ring of phosphoinositides and inositol phosphates, in a domain-specific manner (PubMed:9442075). The 5-PPase domain catalyzes removal of the 5-phosphate from substrates such as phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2), phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3), inositol-1,4,5-trisphosphate (Ins(1,4,5)P3) and inositol-1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4) (PubMed:9442075). The SAC domain hydrolyzes phosphates at the 3- and 4-positions of the inositol ring, targeting phosphatidylinositol-3-phosphate (PI(3)P), phosphatidylinositol-4-phosphate (PI(4)P), and phosphatidylinositol-3,5-bisphosphate (PI(3,5)P2) (By similarity). Plays a role in the phosphatidylinositol metabolic process during the early stage of clathrin-coated-pit formation (By similarity). During EGF activation, plays a role in receptor-mediated endocytosis (RME) by converting PtdIns(4,5)P2 to PtdIns(4)P through the H2O2-dependent oxidation of the 4-phosphatase domain (By similarity). May play a role in tumor cell invadopodia formation (By similarity). {ECO:0000250|UniProtKB:O15056, ECO:0000250|UniProtKB:O55207, ECO:0000269|PubMed:9442075}.
uniprot
proteins
mass_dalton
158480
uniprot
proteins
post_translational_modification
PTM: The SRC-mediated phosphorylation of Tyr-490 contributes to invadopodia formation by stimulating SYNJ2 5'-phosphatase activity. {ECO:0000250|UniProtKB:O15056}.; PTM: Oxidized at Cys-386. Oxidation at Cys-386 mediates conversion of PtdIns(4,5)P2 to PtdIns(4)P that is achieved through the H2O2-dependent oxidation of the 4-phosphatase domain of the dual phosphatidylinositol-4,5-bisphosphate phosphatase activity and is required for receptor-mediated endocytosis (RME) during EGF activation. {ECO:0000250|UniProtKB:O55207}.
uniprot
proteins
protein_family
4
uniprot
proteins
protein_family
5-trisphosphate 5-phosphatase family
uniprot
proteins
protein_family
Synaptojanin family; Inositol 1
uniprot
proteins
pubmed
14621295
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15722415
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
9442075
uniprot
proteins
pubmed
9636665
uniprot
proteins
sequence_length
1434
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15056}. Cell membrane {ECO:0000250|UniProtKB:O15056}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:O15056}. Presynapse {ECO:0000250|UniProtKB:O55207}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O55207}. Note=Localizes at presynapse terminals in brain and at bundles of microtubules surrounding the nucleus in the elongating spermatids corresponding to the manchette (By similarity). Translocates from the cytoplasm to membrane ruffles in a RAC1-dependent manner (By similarity). {ECO:0000250|UniProtKB:O15056}.
uniprot
proteins