HINT1
entrez
3094
canonical
uniprot
P49773
canonical
ensembl
ENSG00000169567
resolver
ensp
ENSP00000304229
resolver
ensp
ENSP00000426860
resolver
ensp
ENSP00000427008
resolver
ensp
ENSP00000427499
resolver
ensp
ENSP00000502370
resolver
enst
ENST00000304043
resolver
enst
ENST00000506908
resolver
enst
ENST00000508488
resolver
enst
ENST00000511475
resolver
enst
ENST00000675491
resolver
genesymbol
HINT1
resolver
genesymbol_syn
HINT
resolver
genesymbol_syn
PKCI1
resolver
genesymbol_syn
PRKCNH1
resolver
hgnc
HGNC:4912
resolver
uniprot
A0A384NPU2
resolver
uniprot
D6RD60
resolver
uniprot
D6RE99
resolver
uniprot
Q9H5W8
resolver
uniprot_entry
A0A384NPU2_HUMAN
resolver
uniprot_entry
D6RD60_HUMAN
resolver
uniprot_entry
D6RE99_HUMAN
resolver
uniprot_entry
HINT1_HUMAN
resolver
uniprot_sec
Q9H5W8
resolver
amino_acid_sequence
MADEIAKAQVARPGGDTIFGKIIRKEIPAKIIFEDDRCLAFHDISPQAPTHFLVIPKKHISQISVAEDDDESLLGHLMIVGKKCAADLGLNKGYRMVVNEGSDGGQSVYHVHLHVLGGRQMHWPPG
uniprot
proteins
disease_involvement
DISEASE: Neuromyotonia and axonal neuropathy, autosomal recessive (NMAN) [MIM:137200]: An autosomal recessive neurologic disorder characterized by onset in the first or second decade of a peripheral axonal neuropathy predominantly affecting motor more than sensory nerves. The axonal neuropathy is reminiscent of Charcot-Marie-Tooth disease type 2 and distal hereditary motor neuropathy. Individuals with NMAN also have delayed muscle relaxation and action myotonia associated with neuromyotonic discharges on needle EMG resulting from hyperexcitability of the peripheral nerves. {ECO:0000269|PubMed:16835243, ECO:0000269|PubMed:22961002, ECO:0000269|PubMed:28691797, ECO:0000269|PubMed:29787766, ECO:0000269|PubMed:31088288}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.22.-
uniprot
proteins
ec_number
3.9.1.-
uniprot
proteins
function
FUNCTION: Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2 (PubMed:15703176, PubMed:16835243, PubMed:17217311, PubMed:17337452, PubMed:22329685, PubMed:23614568, PubMed:28691797, PubMed:29787766, PubMed:31990367). Hydrolyzes adenosine 5'monophosphomorpholidate (AMP-morpholidate) and guanosine 5'monophosphomorpholidate (GMP-morpholidate) (PubMed:15703176, PubMed:16835243). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) generated by lysine tRNA ligase, as well as Met-AMP, His-AMP and Asp-AMP, lysyl-GMP (GMP-N-epsilon-(N-alpha-acetyl lysine methyl ester)) and AMP-N-alanine methyl ester (PubMed:15703176, PubMed:17337452, PubMed:22329685). Hydrolyzes 3-indolepropionic acyl-adenylate, tryptamine adenosine phosphoramidate monoester and other fluorogenic purine nucleoside tryptamine phosphoramidates in vitro (PubMed:17217311, PubMed:17337452, PubMed:23614568, PubMed:28691797, PubMed:29787766, PubMed:31990367). Can also convert adenosine 5'-O-phosphorothioate and guanosine 5'-O-phosphorothioate to the corresponding nucleoside 5'-O-phosphates with concomitant release of hydrogen sulfide (PubMed:30772266). In addition, functions as scaffolding protein that modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex and by the complex formed with MITF and CTNNB1 (PubMed:16014379, PubMed:22647378). Modulates p53/TP53 levels and p53/TP53-mediated apoptosis (PubMed:16835243). Modulates proteasomal degradation of target proteins by the SCF (SKP2-CUL1-F-box protein) E3 ubiquitin-protein ligase complex (PubMed:19112177). Also exhibits SUMO-specific isopeptidase activity, deconjugating SUMO1 from RGS17 (PubMed:31088288). Deconjugates SUMO1 from RANGAP1 (By similarity). {ECO:0000250|UniProtKB:P80912, ECO:0000269|PubMed:15703176, ECO:0000269|PubMed:16014379, ECO:0000269|PubMed:16835243, ECO:0000269|PubMed:17217311, ECO:0000269|PubMed:17337452, ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:22329685, ECO:0000269|PubMed:22647378, ECO:0000269|PubMed:23614568, ECO:0000269|PubMed:28691797, ECO:0000269|PubMed:29787766, ECO:0000269|PubMed:30772266, ECO:0000269|PubMed:31088288, ECO:0000269|PubMed:31990367}.
uniprot
proteins
mass_dalton
13802
uniprot
proteins
mutagenesis
MUTAGEN 33; /note="F->S: Loss of SUMO-specific isopeptidase activity."; /evidence="ECO:0000269|PubMed:31088288"; MUTAGEN 34; /note="E->K: Reduced SUMO-specific isopeptidase activity."; /evidence="ECO:0000269|PubMed:31088288"; MUTAGEN 38; /note="C->R: No effect on SUMO-specific isopeptidase activity."; /evidence="ECO:0000269|PubMed:31088288"; MUTAGEN 43; /note="D->N: Approximately 50-fold increased affinity for tryptamine adenosine phosphoramidate."; /evidence="ECO:0000269|PubMed:29787766"; MUTAGEN 44; /note="I->F: Approximately 10-fold increased affinity for tryptamine adenosine phosphoramidate."; /evidence="ECO:0000269|PubMed:29787766"; MUTAGEN 44; /note="I->W: Approximately 30-fold increased affinity for tryptamine adenosine phosphoramidate."; /evidence="ECO:0000269|PubMed:29787766"; MUTAGEN 51; /note="H->A: No effect on affinity for 3-indolepropionic acyl-adenylate but a 13.8-fold increased affinity for tryptamine adenosine phosphoramidate monoester."; /evidence="ECO:0000269|PubMed:23614568"; MUTAGEN 57; /note="K->N: Loss of SUMO-specific isopeptidase activity."; /evidence="ECO:0000269|PubMed:31088288"; MUTAGEN 97; /note="V->D: Loss of dimerization. Strongly reduced adenosine 5'-monophosphoramidase activity. A 110-fold increased affinity for 3-indolepropionic acyl-adenylate and a 100-fold increased affinity for tryptamine adenosine phosphoramidate monoester."; /evidence="ECO:0000269|PubMed:17337452"; MUTAGEN 97; /note="V->E: Loss of dimerization. Strongly reduced adenosine 5'-monophosphoramidase activity. A 128-fold increased affinity for 3-indolepropionic acyl-adenylate and a 1000-fold increased affinity for tryptamine adenosine phosphoramidate monoester."; /evidence="ECO:0000269|PubMed:17337452"; MUTAGEN 97; /note="V->M: Loss of SUMO-specific isopeptidase activity."; /evidence="ECO:0000269|PubMed:31088288"; MUTAGEN 105; /note="G->A: Reduces adenosine 5'-monophosphoramidase activity."; /evidence="ECO:0000269|PubMed:16835243"; MUTAGEN 107; /note="S->A: Reduces adenosine 5'-monophosphoramidase activity."; /evidence="ECO:0000269|PubMed:16835243"; MUTAGEN 110; /note="H->A: No significant effect on affinity for 3-indolepropionic acyl-adenylate and tryptamine adenosine phosphoramidate monoester."; /evidence="ECO:0000269|PubMed:23614568"; MUTAGEN 114; /note="H->A: Nearly abolishes adenosine 5'-monophosphoramidase activity. A 3-fold increased affinity for 3-indolepropionic acyl-adenylate and a 2-fold increased affinity for tryptamine adenosine phosphoramidate monoester."; /evidence="ECO:0000269|PubMed:22329685, ECO:0000269|PubMed:23614568"; MUTAGEN 114; /note="H->R: Loss of SUMO-specific isopeptidase activity."; /evidence="ECO:0000269|PubMed:31088288"; MUTAGEN 123; /note="W->A: Nearly abolishes adenosine 5'-monophosphoramidase activity."; /evidence="ECO:0000269|PubMed:22329685
uniprot
proteins
post_translational_modification
PTM: Deubiquitinated by USP40, leading to stabilization. {ECO:0000250|UniProtKB:P70349}.
uniprot
proteins
protein_family
HINT family
uniprot
proteins
pubmed
10958787
uniprot
proteins
pubmed
12665801
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15703176
uniprot
proteins
pubmed
16014379
uniprot
proteins
pubmed
16835243
uniprot
proteins
pubmed
17217311
uniprot
proteins
pubmed
17337452
uniprot
proteins
pubmed
19112177
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22329685
uniprot
proteins
pubmed
22647378
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
22869114
uniprot
proteins
pubmed
22961002
uniprot
proteins
pubmed
23614568
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
28691797
uniprot
proteins
pubmed
29787766
uniprot
proteins
pubmed
30772266
uniprot
proteins
pubmed
31088288
uniprot
proteins
pubmed
31990367
uniprot
proteins
pubmed
39190717
uniprot
proteins
pubmed
7644499
uniprot
proteins
pubmed
8643579
uniprot
proteins
pubmed
8812426
uniprot
proteins
pubmed
9323207
uniprot
proteins
pubmed
9770345
uniprot
proteins
sequence_length
126
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10958787, ECO:0000269|PubMed:16014379, ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:8812426}. Nucleus {ECO:0000269|PubMed:10958787, ECO:0000269|PubMed:16014379, ECO:0000269|PubMed:19112177, ECO:0000269|PubMed:9770345}. Note=Interaction with CDK7 leads to a more nuclear localization. {ECO:0000269|PubMed:10958787}.
uniprot
proteins