Synj2
entrez
84018
canonical
uniprot
O55207
canonical
ensembl
ENSRNOG00000017114
resolver
ensp
ENSRNOP00000059744
resolver
ensp
ENSRNOP00000062564
resolver
ensp
ENSRNOP00000063385
resolver
ensp
ENSRNOP00000104494
resolver
ensp
ENSRNOP00000112432
resolver
enst
ENSRNOT00000066798
resolver
enst
ENSRNOT00000067661
resolver
enst
ENSRNOT00000068476
resolver
enst
ENSRNOT00000129353
resolver
genesymbol
Synj2
resolver
uniprot
A0ABK0LNE2
resolver
uniprot
F1LPP1
resolver
uniprot
F1M0S5
resolver
uniprot
F1M2D6
resolver
uniprot
Q91ZD8
resolver
uniprot
Q91ZD9
resolver
uniprot_entry
A0ABK0LNE2_RAT
resolver
uniprot_entry
F1LPP1_RAT
resolver
uniprot_entry
F1M0S5_RAT
resolver
uniprot_entry
F1M2D6_RAT
resolver
uniprot_entry
SYNJ2_RAT
resolver
uniprot_sec
Q91ZD8
resolver
uniprot_sec
Q91ZD9
resolver
activity_regulation
ACTIVITY REGULATION: The phosphatidylinositol-4-phosphate phosphatase activity is inhibited by hydrogen peroxide (H2O2) without affecting phosphatidylinositol phosphate 5-phosphatase activity (PubMed:38442648). The dual phosphatidylinositol-4,5-bisphosphate phosphatase activity is inhibited through cysteine oxidation of the 4- phosphatase domain by H2O2 molecules in the plasma membrane in cells that are activated with growth factors (PubMed:38442648). {ECO:0000269|PubMed:38442648}.
uniprot
proteins
amino_acid_sequence
MALSKGLRLLARLDPTGPSSVLLEARGRGDCLLFEAGAVATLAPEEKEVIKGLYGKPTDAYGCLGELSLKSGGVPLSFLVLVTGCTSVGRIPDAEIYKITGTEFYPLQEEAKEEDRLPALKKILSSGVFYFAWPNDGACFDLTIRAQKQGDDCSEWGTSFFWNQLLHVPLRQHQVNCHDWLLKVICGVVTIRTVYASHKQAKACLISRISCERAGARFLTRGVNDDGHVSNFVETEQAIYMDDGVSSFVQIRGSVPLFWEQPGLQVGSHHLRLHRGLEANAPAFERHMVLLKEQYGQQVVVNLLGSRGGEEVLNRAFKKLLWASCHAGDTPMINFDFHQFAKGRKLEKLENLLRPQLKLHWDDFGVFAKGENVSPRFQKGTLRMNCLDCLDRTNTVQCFIALEVLHLQLESLGLNSKPITDRFVESFKAMWSLNGHGLSKVFTGSRALEGKAKVGKLKDGARSMSRTIQSNFFDGVKQEAIKLLLVGDVYNEESTDKGRMLLDNTALLGLGSNKQNSLSGMLDGKATPRILKAMTERQSEFTNFKRIQIAMGTWNVNGGKQFRSNLLGTTELTDWLLDAPQLSGAVDSQDDGGPADIFAVGFEEMVELSAGNIVNASTTNRKMWGEQLQKAISRSHRYILLTSAQLVGVCLYIFVRPYHVPFIRDVAIDTVKTGMGGKAGNKGAVGIRFQFHSTSFCFICSHLTAGQSQVKERNEDYREITHKLSFPSGRNIFSHDYVFWCGDFNYRIDLTYEEVFYFVKRQDWKKLMEFDQLQLQKSSGKIFKDFHEGTINFGPTYKYDVGSAAYDTSDKCRTPAWTDRVLWWRKKHPYDKTAGELNLLDSDLDGDANIRHTWSPGTLKYYGRAELQASDHRPVLAIVEVEVQEVDVGARERVFQEVSSVQGPLDATVIVNLQSPTLEERNEFPEDLRTELMQTLGNYGTIILVRINQGQMLVTFADSHSALSVLDVDGMKVKGRAVKIRPKTKDWLEGLREELIRKRDSMAPVSPTANSCLLEENFDFTSLDYESEGDVLEDDEDYLADEFGQPVVSDSELGGDDSSDTMSASTPASKSPALAKKKQHPTYKDDADLMTLKLELEVAGNFRHRSPSRSLSVPNRPRPPHPPQRPPPPTGLMVKKSASDASISSGTHGQYSILQTAKLLPGAPQQPPKARTGISKPYNVKQIKTTNAQEAEAAIRCLLEAGGGVPESAPGATPLRNQGSSKPEASLGPPVLPRRPVPRVPTMKKPTLRRTGKPMLPEEQCEQQPVHFTMASQEMNLETPPPITAPIPPVPKPRTFQPGRGVERRPSGGKPEPDDAPPVTGAVELSSPEAPEAPSLAPKVPPRRKKSAPAAFHLQVLQSNSQLLQGLTCSSSSPSPPKPDTPLLYPQMALGTSSAISPETDGPRVTEPEAASFHGDYPDPFWSLLHHPKLLNNNTWLSKSSEPLDLGSRTPERTHTDSAQVNASVVERGLPPDHGGKDFSHWMAASNKDKRTTLGV
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:11498538, PubMed:38442648, PubMed:9388224). 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:38442648, PubMed:9388224). 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) (PubMed:11498538, PubMed:38442648). 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 (PubMed:38442648). May play a role in tumor cell invadopodia formation (By similarity). {ECO:0000250|UniProtKB:O15056, ECO:0000269|PubMed:11498538, ECO:0000269|PubMed:38442648, ECO:0000269|PubMed:9388224}.
uniprot
proteins
mass_dalton
165264
uniprot
proteins
mutagenesis
MUTAGEN 386; /note="C->S: Loss of oxidation after exposure to hydrogen peroxide."; /evidence="ECO:0000269|PubMed:38442648"; MUTAGEN 388; /note="D->N: Abolishes phosphatase activity."; /evidence="ECO:0000269|PubMed:11498538"; MUTAGEN 435; /note="G->V: Reduced phosphatase activity."; /evidence="ECO:0000269|PubMed:11498538"; MUTAGEN 466; /note="R->H: No effect."; /evidence="ECO:0000269|PubMed:11498538"; MUTAGEN O55207-3:1246; /note="P->A: Abolishes SYNJ2BP/OMP25 binding."; /evidence="ECO:0000269|PubMed:9388224"; MUTAGEN O55207-3:1248; /note="L->A: Abolishes SYNJ2BP/OMP25 binding."; /evidence="ECO:0000269|PubMed:9388224
uniprot
proteins
post_translational_modification
PTM: Oxidized at Cys-386 (Probable). 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 (PubMed:38442648). {ECO:0000269|PubMed:38442648, ECO:0000305|PubMed:38442648}.; PTM: The SRC-mediated phosphorylation of Tyr-490 contributes to invadopodia formation by stimulating SYNJ2 5'-phosphatase activity. {ECO:0000250|UniProtKB:O15056}.
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
10357812
uniprot
proteins
pubmed
11498538
uniprot
proteins
pubmed
38442648
uniprot
proteins
pubmed
9388224
uniprot
proteins
sequence_length
1496
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11498538}. Cell membrane {ECO:0000269|PubMed:11498538}. Presynapse {ECO:0000269|PubMed:11498538}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11498538}. Note=Localizes at presynapse terminals in brain and at bundles of microtubules surrounding the nucleus in the elongating spermatids corresponding to the manchette (PubMed:11498538). Translocates from the cytoplasm to membrane ruffles in a RAC1-dependent manner (PubMed:11498538). {ECO:0000269|PubMed:11498538}.; SUBCELLULAR LOCATION: [Isoform 2A]: Mitochondrion {ECO:0000269|PubMed:10357812}. Note=Interaction of isoform 2A with SYNJ2BP/OMP25 results in localization to the mitochondrion (PubMed:10357812). {ECO:0000269|PubMed:10357812}.
uniprot
proteins