STIM1
entrez
6786
canonical
uniprot
Q13586
canonical
ensembl
ENSG00000167323
resolver
ensp
ENSP00000300737
resolver
ensp
ENSP00000432210
resolver
ensp
ENSP00000433266
resolver
ensp
ENSP00000436208
resolver
ensp
ENSP00000478059
resolver
ensp
ENSP00000514024
resolver
ensp
ENSP00000514025
resolver
ensp
ENSP00000514026
resolver
ensp
ENSP00000514027
resolver
ensp
ENSP00000514028
resolver
ensp
ENSP00000532681
resolver
ensp
ENSP00000532682
resolver
enst
ENST00000525403
resolver
enst
ENST00000526596
resolver
enst
ENST00000616714
resolver
enst
ENST00000698910
resolver
enst
ENST00000698911
resolver
enst
ENST00000698912
resolver
enst
ENST00000698913
resolver
enst
ENST00000698914
resolver
genesymbol
STIM1
resolver
genesymbol_syn
GOK
resolver
hgnc
HGNC:11386
resolver
uniprot
A0A087WTQ4
resolver
uniprot
A0A8V8TMF0
resolver
uniprot
A0A8V8TMG1
resolver
uniprot
A0A8V8TNW0
resolver
uniprot
A0A8V8TP73
resolver
uniprot
E9PQJ4
resolver
uniprot
E9PRZ7
resolver
uniprot
G0XQ39
resolver
uniprot
H0YDB2
resolver
uniprot
Q8N382
resolver
uniprot_entry
A0A087WTQ4_HUMAN
resolver
uniprot_entry
A0A8V8TMF0_HUMAN
resolver
uniprot_entry
A0A8V8TMG1_HUMAN
resolver
uniprot_entry
A0A8V8TNW0_HUMAN
resolver
uniprot_entry
A0A8V8TP73_HUMAN
resolver
uniprot_entry
E9PRZ7_HUMAN
resolver
uniprot_entry
G0XQ39_HUMAN
resolver
uniprot_entry
H0YDB2_HUMAN
resolver
uniprot_entry
STIM1_HUMAN
resolver
uniprot_sec
E9PQJ4
resolver
uniprot_sec
Q8N382
resolver
amino_acid_sequence
MDVCVRLALWLLWGLLLHQGQSLSHSHSEKATGTSSGANSEESTAAEFCRIDKPLCHSEDEKLSFEAVRNIHKLMDDDANGDVDVEESDEFLREDLNYHDPTVKHSTFHGEDKLISVEDLWKAWKSSEVYNWTVDEVVQWLITYVELPQYEETFRKLQLSGHAMPRLAVTNTTMTGTVLKMTDRSHRQKLQLKALDTVLFGPPLLTRHNHLKDFMLVVSIVIGVGGCWFAYIQNRYSKEHMKKMMKDLEGLHRAEQSLHDLQERLHKAQEEHRTVEVEKVHLEKKLRDEINLAKQEAQRLKELREGTENERSRQKYAEEELEQVREALRKAEKELESHSSWYAPEALQKWLQLTHEVEVQYYNIKKQNAEKQLLVAKEGAEKIKKKRNTLFGTFHVAHSSSLDDVDHKILTAKQALSEVTAALRERLHRWQQIEILCGFQIVNNPGIHSLVAALNIDPSWMGSTRPNPAHFIMTDDVDDMDEEIVSPLSMQSPSLQSSVRQRLTEPQHGLGSQRDLTHSDSESSLHMSDRQRVAPKPPQMSRAADEALNAMTSNGSHRLIEGVHPGSLVEKLPDSPALAKKALLALNHGLDKAHSLMELSPSAPPGGSPHLDSSRSHSPSSPDPDTPSPVGDSRALQASRNTRIPHLAGKKAVAEEDNGSIGEETDSSPGRKKFPLKIFKKPLKK
uniprot
proteins
disease_involvement
DISEASE: Immunodeficiency 10 (IMD10) [MIM:612783]: An immune disorder characterized by recurrent infections, impaired activation and proliferative response of T-cells, decreased T-cell production of cytokines, lymphadenopathy, and normal lymphocytes counts and serum immunoglobulin levels. Additional features include thrombocytopenia, autoimmune hemolytic anemia, myopathy, partial iris hypoplasia, hepatosplenomegaly and defective enamel dentition. {ECO:0000269|PubMed:19420366, ECO:0000269|PubMed:22190180}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Myopathy, tubular aggregate, 1 (TAM1) [MIM:160565]: A rare congenital myopathy characterized by regular arrays of membrane tubules on muscle biopsies without additional histopathological hallmarks. Tubular aggregates in muscle are structures of variable appearance consisting of an outer tubule containing either one or more microtubule-like structures or amorphous material. They may occur in a variety of circumstances, including inherited myopathies, alcohol- and drug-induced myopathies, exercise-induced cramps or muscle weakness. {ECO:0000269|PubMed:23332920, ECO:0000269|PubMed:24570283, ECO:0000269|PubMed:25326555, ECO:0000269|PubMed:25953320}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Stormorken syndrome (STRMK) [MIM:185070]: A rare autosomal dominant disease characterized by mild bleeding tendency, thrombocytopathy, thrombocytopenia, mild anemia, asplenia, tubular aggregate myopathy, miosis, headache, and ichthyosis. {ECO:0000269|PubMed:24591628, ECO:0000269|PubMed:24619930, ECO:0000269|PubMed:25577287}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Acts as a Ca(2+) sensor that gates two major inward rectifying Ca(2+) channels at the plasma membrane: Ca(2+) release-activated Ca(2+) (CRAC) channels and arachidonate-regulated Ca(2+)-selective (ARC) channels (PubMed:15866891, PubMed:16005298, PubMed:16208375, PubMed:16537481, PubMed:16733527, PubMed:16766533, PubMed:16807233, PubMed:18854159, PubMed:19182790, PubMed:19249086, PubMed:19622606, PubMed:19706554, PubMed:22464749, PubMed:24069340, PubMed:24351972, PubMed:24591628, PubMed:25326555, PubMed:26322679, PubMed:28219928, PubMed:32415068). Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Upon Ca(2+) depletion, translocates from the endoplasmic reticulum to the plasma membrane where it activates CRAC channel pore-forming subunits ORA1, ORA2 and ORAI3 to generate sustained and oscillatory Ca(2+) entry (PubMed:16208375, PubMed:16537481, PubMed:32415068). Involved in enamel formation (PubMed:24621671). Plays a role in regulating the type I interferon response by retaining the signaling adapter STING at the endoplasmic reticulum (PubMed:30643259). {ECO:0000269|PubMed:15866891, ECO:0000269|PubMed:16005298, ECO:0000269|PubMed:16208375, ECO:0000269|PubMed:16537481, ECO:0000269|PubMed:16733527, ECO:0000269|PubMed:16766533, ECO:0000269|PubMed:16807233, ECO:0000269|PubMed:18854159, ECO:0000269|PubMed:19182790, ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:19622606, ECO:0000269|PubMed:19706554, ECO:0000269|PubMed:22464749, ECO:0000269|PubMed:24069340, ECO:0000269|PubMed:24351972, ECO:0000269|PubMed:24591628, ECO:0000269|PubMed:24621671, ECO:0000269|PubMed:25326555, ECO:0000269|PubMed:26322679, ECO:0000269|PubMed:28219928, ECO:0000269|PubMed:30643259, ECO:0000269|PubMed:32415068}.
uniprot
proteins
mass_dalton
77423
uniprot
proteins
mutagenesis
MUTAGEN 76; /note="D->A,N: Increases Ca(2+) influx even when Ca(2+) stores are not depleted. Promotes constitutive activation of the Ca2+ release-activated Ca2+ (CRAC) channel."; /evidence="ECO:0000269|PubMed:16005298, ECO:0000269|PubMed:16807233, ECO:0000269|PubMed:24591628, ECO:0000269|PubMed:26322679"; MUTAGEN 78; /note="D->N: Increases Ca(2+) influx even when Ca(2+) stores are not depleted."; /evidence="ECO:0000269|PubMed:16807233"; MUTAGEN 87; /note="E->A,Q: Increases Ca(2+) influx through activation of CRAC channels, even when Ca(2+) stores are not depleted."; /evidence="ECO:0000269|PubMed:16537481, ECO:0000269|PubMed:16807233, ECO:0000269|PubMed:18854159"; MUTAGEN 108; /note="F->D: Constitutive localization in punctae at the cell membrane and constitutive activation of CRAC channels; when associated with D-110."; /evidence="ECO:0000269|PubMed:18854159"; MUTAGEN 110; /note="G->D: Constitutive localization in punctae at the cell membrane and constitutive activation of CRAC channels; when associated with D-108."; /evidence="ECO:0000269|PubMed:18854159"; MUTAGEN 131; /note="N->Q: Impairs ORAI1 ARC channel currents; when associated with Q-171."; /evidence="ECO:0000269|PubMed:19622606"; MUTAGEN 171; /note="N->Q: Impairs ORAI1 ARC channel currents; when associated with Q-131."; /evidence="ECO:0000269|PubMed:19622606"; MUTAGEN 195; /note="L->R: Constitutive localization in punctae at the cell membrane and constitutive activation of CRAC channels."; /evidence="ECO:0000269|PubMed:18854159"; MUTAGEN 258; /note="L->G: Promotes constitutive activation of the Ca2+ release-activated Ca2+ (CRAC) channel."; /evidence="ECO:0000269|PubMed:26322679"; MUTAGEN 318..322; /note="EEELE->QQQLQ: Constitutive activation of CRAC channels."; /evidence="ECO:0000269|PubMed:24351972"; MUTAGEN 324; /note="V->P: Reduces activation of CRAC channels."; /evidence="ECO:0000269|PubMed:24351972"; MUTAGEN 347; /note="L->A: Impairs ORAI1 CRAC channel gating; when associated with A-348. Impairs the interaction and clustering with ORAI1 in punctae at the cell membrane; when associated with A-348."; /evidence="ECO:0000269|PubMed:19182790"; MUTAGEN 347; /note="L->R: Abolishes colocalization with ORAI1 and activation of CRAC channels."; /evidence="ECO:0000269|PubMed:24351972"; MUTAGEN 348; /note="Q->A: Impairs ORAI1 CRAC channel gating; when associated with A-347. Impairs the interaction and clustering with ORAI1 in punctae at the cell membrane; when associated with A-347."; /evidence="ECO:0000269|PubMed:19182790"; MUTAGEN 351; /note="L->R: Abolishes colocalization with ORAI1 and activation of CRAC channels."; /evidence="ECO:0000269|PubMed:24351972"; MUTAGEN 361..362; /note="YY->KK: Abolishes activation of CRAC channels."; /evidence="ECO:0000269|PubMed:24351972"; MUTAGEN 380; /note="A->R: Constitutive activation of CRAC channels."; /evidence="ECO:0000269|PubMed:24351972"; MUTAGEN 382..386; /note="KIKKK->EIEEE: Abolishes activation of CRAC channels."; /evidence="ECO:0000269|PubMed:24351972"; MUTAGEN 383; /note="I->R: Abolishes activation of CRAC channels."; /evidence="ECO:0000269|PubMed:24351972"; MUTAGEN 475; /note="D->A: Decreases fast Ca(2+)-dependent inactivation of ORAI3 channels; when associated with A-476, A-478, A-479."; /evidence="ECO:0000269|PubMed:19706554"; MUTAGEN 476; /note="D->A: Decreases fast Ca(2+)-dependent inactivation of ORAI3 channels; when associated with A-475, A-478, A-479."; /evidence="ECO:0000269|PubMed:19706554"; MUTAGEN 478; /note="Missing: Decreases fast Ca(2+)-dependent inactivation of ORAI3 channels; when associated with A-475, A-476, A-479."; /evidence="ECO:0000269|PubMed:19706554"; MUTAGEN 479; /note="D->A: Decreases fast Ca(2+)-dependent inactivation of ORAI3 channels; when associated with A-475, A-476, A-478."; /evidence="ECO:0000269|PubMed:19706554"; MUTAGEN 481; /note="D->A: Decreases fast Ca(2+)-dependent inactivation of ORAI3 channels; when associated with A-482 and A-483."; /evidence="ECO:0000269|PubMed:19706554"; MUTAGEN 482; /note="E->A: Decreases fast Ca(2+)-dependent inactivation of ORAI3 channels; when associated with A-481 and A-483."; /evidence="ECO:0000269|PubMed:19706554"; MUTAGEN 483; /note="E->A: Decreases fast Ca(2+)-dependent inactivation of ORAI3 channels; when associated with A-481 and A-482."; /evidence="ECO:0000269|PubMed:19706554"; MUTAGEN 644..645; /note="IP->NN: Loss of interaction with MAPRE1 and association with the growing microtubule plus ends."; /evidence="ECO:0000269|PubMed:19632184
uniprot
proteins
post_translational_modification
PTM: Glycosylation is required for cell surface expression. {ECO:0000269|PubMed:11004585, ECO:0000269|PubMed:11983428, ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:19159218}.; PTM: Phosphorylated predominantly on Ser residues. {ECO:0000269|PubMed:11004585}.; PTM: Cleaved by coronavirus 3C-like proteinase nsp5 at Gln-496. {ECO:0000269|PubMed:41289387}.
uniprot
proteins
pubmed
11004585
uniprot
proteins
pubmed
11463338
uniprot
proteins
pubmed
11983428
uniprot
proteins
pubmed
12754519
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15866891
uniprot
proteins
pubmed
16005298
uniprot
proteins
pubmed
16208375
uniprot
proteins
pubmed
16263699
uniprot
proteins
pubmed
16537481
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
16733527
uniprot
proteins
pubmed
16766533
uniprot
proteins
pubmed
16807233
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17905723
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18854159
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19182790
uniprot
proteins
pubmed
19249086
uniprot
proteins
pubmed
19367720
uniprot
proteins
pubmed
19420366
uniprot
proteins
pubmed
19622606
uniprot
proteins
pubmed
19632184
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19706554
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20418871
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22084111
uniprot
proteins
pubmed
22190180
uniprot
proteins
pubmed
22451904
uniprot
proteins
pubmed
22464749
uniprot
proteins
pubmed
22494970
uniprot
proteins
pubmed
22586105
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23332920
uniprot
proteins
pubmed
24069340
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24351972
uniprot
proteins
pubmed
24570283
uniprot
proteins
pubmed
24591628
uniprot
proteins
pubmed
24619930
uniprot
proteins
pubmed
24621671
uniprot
proteins
pubmed
25326555
uniprot
proteins
pubmed
25384971
uniprot
proteins
pubmed
25577287
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
25953320
uniprot
proteins
pubmed
25996873
uniprot
proteins
pubmed
26322679
uniprot
proteins
pubmed
27185316
uniprot
proteins
pubmed
28219928
uniprot
proteins
pubmed
30481768
uniprot
proteins
pubmed
30643259
uniprot
proteins
pubmed
32415068
uniprot
proteins
pubmed
40498864
uniprot
proteins
pubmed
41289387
uniprot
proteins
pubmed
8921403
uniprot
proteins
pubmed
9377559
uniprot
proteins
sequence_length
685
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein {ECO:0000269|PubMed:11004585, ECO:0000269|PubMed:16005298, ECO:0000269|PubMed:16208375, ECO:0000269|PubMed:18854159, ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:19706554, ECO:0000269|PubMed:27185316, ECO:0000269|PubMed:28219928}. Endoplasmic reticulum membrane; Single-pass type I membrane protein {ECO:0000269|PubMed:16005298, ECO:0000269|PubMed:16208375, ECO:0000269|PubMed:18854159, ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:26322679, ECO:0000269|PubMed:27185316, ECO:0000269|PubMed:30643259}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19632184}. Sarcoplasmic reticulum {ECO:0000269|PubMed:25326555}. Note=Translocates from the endoplasmic reticulum to the cell membrane in response to a depletion of intracellular calcium and is detected at punctae corresponding to junctions between the endoplasmic reticulum and the cell membrane (PubMed:16005298, PubMed:16208375, PubMed:18854159, PubMed:19182790, PubMed:19249086). Associated with the microtubule network at the growing distal tip of microtubules (PubMed:19632184). Colocalizes with ORAI1 at the cell membrane (PubMed:27185316). Colocalizes preferentially with CASQ1 at endoplasmic reticulum in response to a depletion of intracellular calcium (PubMed:27185316). {ECO:0000269|PubMed:16005298, ECO:0000269|PubMed:16208375, ECO:0000269|PubMed:18854159, ECO:0000269|PubMed:19182790, ECO:0000269|PubMed:19249086, ECO:0000269|PubMed:19632184, ECO:0000269|PubMed:27185316}.
uniprot
proteins
transmembrane_region
TRANSMEM 214..234; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins