SYNJ1
entrez
8867
canonical
uniprot
O43426
canonical
ensembl
ENSG00000159082
resolver
ensp
ENSP00000349903
resolver
ensp
ENSP00000371931
resolver
ensp
ENSP00000487560
resolver
ensp
ENSP00000501426
resolver
ensp
ENSP00000501530
resolver
ensp
ENSP00000572304
resolver
ensp
ENSP00000704104
resolver
enst
ENST00000630077
resolver
genesymbol
SYNJ1
resolver
genesymbol_syn
INPP5G
resolver
genesymbol_syn
KIAA0910
resolver
hgnc
HGNC:11503
resolver
uniprot
A0A0D9SGJ6
resolver
uniprot
B9EGN3
resolver
uniprot
O43425
resolver
uniprot
O94984
resolver
uniprot
Q05CZ1
resolver
uniprot
Q4KMR1
resolver
uniprot_entry
A0A0D9SGJ6_HUMAN
resolver
uniprot_entry
B9EGN3_HUMAN
resolver
uniprot_entry
Q05CZ1_HUMAN
resolver
uniprot_entry
SYNJ1_HUMAN
resolver
uniprot_sec
O43425
resolver
uniprot_sec
O94984
resolver
uniprot_sec
Q4KMR1
resolver
activity_regulation
ACTIVITY REGULATION: Inositol 1,4,5-trisphosphate 5-phosphatase is inhibited by epigallocatechin with an IC(50) of 0.51 uM for gambogic acid (GA) and epigallocatechin monogallate (EGCG) wih an IC(50) of 94 uM (PubMed:40969890). Gambogic acid is the more selective inhibitor and acts through a non competitive inhibition mechanism, (PubMed:40969890). {ECO:0000269|PubMed:40969890}.
uniprot
proteins
amino_acid_sequence
MAFSKGFRIYHKLDPPPFSLIVETRHKEECLMFESGAVAVLSSAEKEAIKGTYSKVLDAYGLLGVLRLNLGDTMLHYLVLVTGCMSVGKIQESEVFRVTSTEFISLRIDSSDEDRISEVRKVLNSGNFYFAWSASGISLDLSLNAHRSMQEQTTDNRFFWNQSLHLHLKHYGVNCDDWLLRLMCGGVEIRTIYAAHKQAKACLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVVYLDDSVSSFIQIRGSVPLFWEQPGLQVGSHRVRMSRGFEANAPAFDRHFRTLKNLYGKQIIVNLLGSKEGEHMLSKAFQSHLKASEHAADIQMVNFDYHQMVKGGKAEKLHSVLKPQVQKFLDYGFFYFNGSEVQRCQSGTVRTNCLDCLDRTNSVQAFLGLEMLAKQLEALGLAEKPQLVTRFQEVFRSMWSVNGDSISKIYAGTGALEGKAKLKDGARSVTRTIQNNFFDSSKQEAIDVLLLGNTLNSDLADKARALLTTGSLRVSEQTLQSASSKVLKSMCENFYKYSKPKKIRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQEFQDKRSKPTDIFAIGFEEMVELNAGNIVSASTTNQKLWAVELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKERNEDFIEIARKLSFPMGRMLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQVFRGFLEGKVTFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRAELKTSDHRPVVALIDIDIFEVEAEERQNIYKEVIAVQGPPDGTVLVSIKSSLPENNFFDDALIDELLQQFASFGEVILIRFVEDKMWVTFLEGSSALNVLSLNGKELLNRTITIALKSPDWIKNLEEEMSLEKISIALPSSTSSTLLGEDAEVAADFDMEGDVDDYSAEVEELLPQHLQPSSSSGLGTSPSSSPRTSPCQSPTISEGPVPSLPIRPSRAPSRTPGPPSAQSSPIDAQPATPLPQKDPAQPLEPKRPPPPRPVAPPTRPAPPQRPPPPSGARSPAPTRKEFGGIGAPPSPGVARREMEAPKSPGTTRKDNIGRSQPSPQAGLAGPGPAGYSTARPTIPPRAGVISAPQSHARASAGRLTPESQSKTSETSKGSTFLPEPLKPQAAFPPQSSLPPPAQRLQEPLVPVAAPMPQSGPQPNLETPPQPPPRSRSSHSLPSEASSQPQVKTNGISDGKRESPLKIDPFEDLSFNLLAVSKAQLSVQTSPVPTPDPKRLIQLPSATQSNVLSSVSCMPTMPPIPARSQSQENMRSSPNPFITGLTRTNPFSDRTAAPGNPFRAKSEESEATSWFSKEEPVTISPFPSLQPLGHNKSRASSSLDGFKDSFDLQGQSTLKISNPKGWVTFEEEEDFGVKGKSKSACSDLLGNQPSSFSGSNLTLNDDWNKGTNVSFCVLPSRRPPPPPVPLLPPGTSPPVDPFTTLASKASPTLDFTER
uniprot
proteins
disease_involvement
DISEASE: Parkinson disease 20, early-onset (PARK20) [MIM:615530]: An early-onset form of Parkinson disease, a complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. PARK20 is characterized by young adult-onset of parkinsonism. Additional features may include seizures, cognitive decline, abnormal eye movements, and dystonia. {ECO:0000269|PubMed:23804563, ECO:0000269|PubMed:23804577, ECO:0000269|PubMed:27496670, ECO:0000269|PubMed:28502045, ECO:0000269|PubMed:31751865, ECO:0000269|PubMed:33349335}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Developmental and epileptic encephalopathy 53 (DEE53) [MIM:617389]: A form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. DEE53 inheritance is autosomal recessive. {ECO:0000269|PubMed:27435091}. Note=The disease is caused by variants affecting the gene represented in this entry.
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:10224048, PubMed:18093523, PubMed:23804563, PubMed:27435091, PubMed:33349335, PubMed:40969890). 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:18093523, PubMed:23804563, PubMed:27435091, PubMed:33349335, PubMed:40969890). 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:10224048, PubMed:18093523, PubMed:23804563, PubMed:27435091). Plays a role in the phosphatidylinositol metabolic process during an unconventional endocytic mechanism, the ultrafast endocytosis where it participates in the rapide neck formation of the newly generated synaptic vesicle through its phosphoinositide 5-phosphatase activity (By similarity). Also, participates in the clathrin uncoating of synaptc vesicle formed via budding from synaptic endosomes after ultrafast endocytosis through combined activity of its phosphatase domains (By similarity). Additionally, regulates actin filament rearrangement by hydrolyzing PIP2 bound to actin regulatory proteins (By similarity). {ECO:0000250|UniProtKB:O18964, ECO:0000250|UniProtKB:Q8CHC4, ECO:0000269|PubMed:10224048, ECO:0000269|PubMed:18093523, ECO:0000269|PubMed:23804563, ECO:0000269|PubMed:27435091, ECO:0000269|PubMed:33349335, ECO:0000269|PubMed:40969890}.
uniprot
proteins
mass_dalton
173103
uniprot
proteins
mutagenesis
MUTAGEN 383; /note="C->S: Almost complete loss of phosphatidylinositol-3-phosphate phosphatase activity. Almost complete loss of phosphatidylinositol-4-phosphate phosphatase activity. Does not affect the 5-phosphatase activity. Does not affect localization at presynapse. Does not affect exocytosis. Does not restore endocytosis. Does not restore vesicle re-availability."; /evidence="ECO:0000269|PubMed:18093523"; MUTAGEN 730; /note="D->A: Complete loss of 5-phosphatase activity. Does not affect phosphatidylinositol-3-phosphate phosphatase activity. Does not affect phosphatidylinositol-4-phosphate phosphatase activity. Does not affect presynapse localization. Does not restore vesicle re-availability."; /evidence="ECO:0000269|PubMed:18093523"; MUTAGEN 1106..1107; /note="KR->AA: Reduces interaction with SH3GL2; when associated with A-1112; A-1119 and A-1125. Does not affect phosphoinosite 5 phoaphatase activity; when associated with A-1112; A-1119 and A-1125. Does not affect Does not affect phosphatidylinositol-3-phosphate phosphatase activity; when associated with A-1112; A-1119 and A-1125. Does not affect phosphatidylinositol-4-phosphate phosphatase; when associated with A-1112; A-1119 and A-1125. Does not affect AMPH interaction; when associated with A-1112; A-1119 and A-1125. Restores the endocytic defect after short stimuli without perturbing the rate ofexocytosis; when associated with A-1112; A-1119 and A-1125. Does not restore the endocytic defect during persistent activity; when associated with A-1112; A-1119 and A-1125. Partially restores vesicle re-availability; when associated with A-1112; A-1119 and A-1125."; /evidence="ECO:0000269|PubMed:18093523"; MUTAGEN 1112; /note="R->A: Reduces interaction with SH3GL2; when associated with 1106-AA-1107; A-1119 and A-1125. Does not affect phosphoinosite 5 phoaphatase activity; when associated with 1106-AA-1107; A-1119 and A-1125. Does not affect phosphatidylinositol-3-phosphate phosphatase; when associated with 1106-AA-1107; A-1119 and A-1125. Does not affect phosphatidylinositol-4-phosphate phosphatase; when associated with 1106-AA-1107; A-1119 and A-1125. Does not affect AMPH interaction; when associated with 1106-AA-1107; A-1119 and A-1125. Restores the endocytic defect after short stimuli without perturbing the rate ofexocytosis; when associated with 1106-AA-1107; A-1119 and A-1125. Does not restore the endocytic defect during persistent activity; when associated with 1106-AA-1107; A-1119 and A-1125. Partially restores vesicle re-availability; when associated with 1106-AA-1107; A-1119 and A-1125."; /evidence="ECO:0000269|PubMed:18093523"; MUTAGEN 1119; /note="R->A: Reduces interaction with SH3GL2; when associated with 1106-AA-1107; A-1112 and A-1125. Does not affect phosphoinosite 5 phoaphatase activity; when associated with 1106-AA-1107; A-1112 and A-1125. Does not affect phosphatidylinositol-3-phosphate phosphatase; when associated with 1106-AA-1107; A-1112 and A-1125. Does not affect phosphatidylinositol-4-phosphate phosphatase; when associated with 1106-AA-1107; A-1112 and A-1125. Does not affect AMPH interaction; when associated with 1106-AA-1107; A-1112 and A-1125. Restores the endocytic defect after short stimuli without perturbing the rate ofexocytosis; when associated with 1106-AA-1107; A-1112 and A-1125. Does not restore the endocytic defect during persistent activity; when associated with 1106-AA-1107; A-1112 and A-1125. Partially restores vesicle re-availability; when associated with 1106-AA-1107; A-1112 and A-1125."; /evidence="ECO:0000269|PubMed:18093523"; MUTAGEN 1125; /note="R->A: Reduces interaction with SH3GL2; when associated with 106-AA-1107; A-1112 and A-1119. Does not affect phosphoinosite 5 phoaphatase activity; when associated with 106-AA-1107; A-1112 and A-1119. Does not affect phosphatidylinositol-3-phosphate phosphatase; when associated with 106-AA-1107; A-1112 and A-1119. Does not affect phosphatidylinositol-4-phosphate phosphatase; when associated with 106-AA-1107; A-1112 and A-1119. Does not affect AMPH interaction; when associated with 106-AA-1107; A-1112 and A-1119. Restores the endocytic defect after short stimuli without perturbing the rate ofexocytosis; when associated with 106-AA-1107; A-1112 and A-1119. Does not restore the endocytic defect during persistent activity; when associated with 106-AA-1107; A-1112 and A-1119. Partially restores vesicle re-availability; when associated with 106-AA-1107; A-1112 and A-1119."; /evidence="ECO:0000269|PubMed:18093523
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
10048485
uniprot
proteins
pubmed
10224048
uniprot
proteins
pubmed
10542231
uniprot
proteins
pubmed
10830953
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17257598
uniprot
proteins
pubmed
18093523
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23804563
uniprot
proteins
pubmed
23804577
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
27435091
uniprot
proteins
pubmed
27496670
uniprot
proteins
pubmed
28502045
uniprot
proteins
pubmed
31751865
uniprot
proteins
pubmed
33349335
uniprot
proteins
pubmed
40969890
uniprot
proteins
pubmed
9428629
uniprot
proteins
sequence_length
1573
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O18964}. Presynapse {ECO:0000269|PubMed:18093523}. Membrane {ECO:0000250|UniProtKB:Q62910}. Note=Concentrates at clathrin-coated endocytic intermediates in nerve terminals. Also recruited to clathrin- and dynamin-coated intermediates. {ECO:0000250|UniProtKB:Q62910}.
uniprot
proteins