Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q13586 (STIM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Stromal interaction molecule 1
Gene names
Name:STIM1
Synonyms:GOK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length685 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in mediating store-operated Ca2+ entry (SOCE), a Ca2+ influx following depletion of intracellular Ca2+ stores. Acts as Ca2+ sensor in the endoplasmic reticulum via its EF-hand domain. Upon Ca2+ depletion, translocates from the endoplasmic reticulum to the plasma membrane where it activates the Ca2+ release-activated Ca2+ (CRAC) channel subunit, TMEM142A/ORAI1. Ref.6 Ref.14 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.26 Ref.27 Ref.33 Ref.34 Ref.36 Ref.37

Subunit structure

Forms homooligomers and heterooligomers with STIM2. Interacts with ORAI1. Interacts with MAPRE1; probably required for targeting to the growing microtubule plus ends. Interacts with EFCAB4B/CRACR2A; the interaction is direct and takes place in absence of Ca2+. Forms a complex with EFCAB4B/CRACR2A and ORAI1 at low concentration of Ca2+, the complex dissociates at elevated Ca2+ concentrations. Interacts with TMEM66/SARAF, promoting a slow inactivation of STIM1-dependent SOCE activity, possibly by facilitating the deoligomerization of STIM1. Interacts with ASPH (isoform 8) Ref.8 Ref.9 Ref.14 Ref.18 Ref.28 Ref.29 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37

Subcellular location

Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Cytoplasmcytoskeleton. 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. Associated with the microtubule network at the growing distal tip of microtubules. Ref.7 Ref.14 Ref.20 Ref.22 Ref.29 Ref.34

Tissue specificity

Ubiquitously expressed in various human primary cells and tumor cell lines. Ref.7 Ref.8

Domain

The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends. Ref.29 Ref.35

The STIM1 Orai1-activating region/CRAC-activating domain (SOAR/CAD) mediates interaction with ORAI1 to activate the channel. Ref.29 Ref.35

Post-translational modification

Glycosylation is required for cell surface expression.

Phosphorylated predominantly on Ser residues. Ref.7

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.31 Ref.38

Myopathy, tubular aggregate (TAM) [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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.39

Miscellaneous

Transfection of STIM1 into cells derived from a rhabdoid tumor and from a rhabdomyosarcoma that do not express detectable levels of STIM1 can induce cell death, suggesting a possible role in the control of rhabdomyosarcomas and rhabdoid tumors.

Sequence similarities

Contains 1 EF-hand domain.

Contains 1 SAM (sterile alpha motif) domain.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Endoplasmic reticulum
Membrane
Microtubule
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainCoiled coil
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of store-operated calcium channel activity

Inferred from direct assay Ref.20. Source: UniProtKB

blood coagulation

Traceable author statement. Source: Reactome

detection of calcium ion

Inferred from direct assay Ref.20. Source: UniProtKB

regulation of calcium ion transport

Inferred from direct assay Ref.20. Source: UniProtKB

regulation of store-operated calcium entry

Inferred from electronic annotation. Source: Ensembl

store-operated calcium entry

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcortical endoplasmic reticulum

Inferred from direct assay Ref.18. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay. Source: HPA

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

growth cone

Inferred from electronic annotation. Source: Ensembl

integral component of endoplasmic reticulum membrane

Inferred from direct assay Ref.22Ref.18. Source: UniProtKB

integral component of plasma membrane

Inferred from direct assay Ref.22. Source: UniProtKB

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncalcium channel regulator activity

Inferred from electronic annotation. Source: Ensembl

calcium ion binding

Inferred from direct assay Ref.20. Source: UniProtKB

identical protein binding

Inferred from physical interaction Ref.14Ref.32PubMed 21427704. Source: IntAct

microtubule plus-end binding

Inferred from direct assay Ref.29. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8Ref.28Ref.29Ref.32Ref.33Ref.18. Source: UniProtKB

store-operated calcium channel activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13586-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q13586-2)

The sequence of this isoform differs from the canonical sequence as follows:
     515-540: DLTHSDSESSLHMSDRQRVAPKPPQM → GSSLKANRLSSKGFDPFRFGVLPPHE
     541-685: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 685663Stromal interaction molecule 1
PRO_0000033326

Regions

Topological domain23 – 213191Extracellular Potential
Transmembrane214 – 23421Helical; Potential
Topological domain235 – 685451Cytoplasmic Potential
Domain63 – 9836EF-hand
Domain132 – 20069SAM
Calcium binding76 – 8712 Ref.34
Region334 – 444111SOAR/CAD
Coiled coil248 – 442195 Ref.35 Ref.36 Ref.37
Motif642 – 6454Microtubule tip localization signal
Compositional bias270 – 33667Glu-rich
Compositional bias600 – 62930Pro/Ser-rich
Compositional bias672 – 68514Lys-rich

Amino acid modifications

Modified residue2571Phosphoserine Ref.11
Modified residue5041Phosphothreonine By similarity
Modified residue5121Phosphoserine By similarity
Modified residue5191Phosphoserine Ref.16
Modified residue5751Phosphoserine Ref.12 Ref.15
Modified residue6081Phosphoserine Ref.10 Ref.13
Modified residue6601Phosphoserine Ref.13 Ref.15
Modified residue6651Phosphothreonine Ref.15
Modified residue6681Phosphoserine Ref.13 Ref.15
Glycosylation1311N-linked (GlcNAc...) Ref.9
Glycosylation1711N-linked (GlcNAc...) Ref.9 Ref.19 Ref.25 Ref.30

Natural variations

Alternative sequence515 – 54026DLTHS…KPPQM → GSSLKANRLSSKGFDPFRFG VLPPHE in isoform 2.
VSP_055150
Alternative sequence541 – 685145Missing in isoform 2.
VSP_055151
Natural variant721H → Q in TAM; myoblasts with the mutation have significantly increased clustering of STIM1, regardless of calcium levels, indicating that calcium sensing in the sarcoplasmic reticulum is impaired. Ref.39
VAR_069892
Natural variant841D → G in TAM; myoblasts with the mutation have significantly increased clustering of STIM1, regardless of calcium levels, indicating that calcium sensing in the sarcoplasmic reticulum is impaired. Ref.39
VAR_069893
Natural variant1091H → N in TAM; myoblasts with the mutation have significantly increased clustering of STIM1, regardless of calcium levels, indicating that calcium sensing in the sarcoplasmic reticulum is impaired. Ref.39
VAR_069894
Natural variant1091H → R in TAM; myoblasts with the mutation have significantly increased clustering of STIM1, regardless of calcium levels, indicating that calcium sensing in the sarcoplasmic reticulum is impaired. Ref.39
VAR_069895
Natural variant4291R → C in IMD10. Ref.38
VAR_069896
Natural variant5381P → S.
Corresponds to variant rs35960304 [ dbSNP | Ensembl ].
VAR_061878

Experimental info

Mutagenesis761D → A or N: Increases Ca(2+) influx even when Ca(2+) stores are not depleted. Ref.20 Ref.23 Ref.29
Mutagenesis781D → N: Increases Ca(2+) influx even when Ca(2+) stores are not depleted. Ref.23 Ref.29
Mutagenesis871E → A or Q: Increases Ca(2+) influx through activation of CRAC channels, even when Ca(2+) stores are not depleted. Ref.23 Ref.27 Ref.29 Ref.34
Mutagenesis1081F → D: Constitutive localization in punctae at the cell membrane and constitutive activation of CRAC channels; when associated with D-110. Ref.29 Ref.34
Mutagenesis1101G → D: Constitutive localization in punctae at the cell membrane and constitutive activation of CRAC channels; when associated with D-108. Ref.29 Ref.34
Mutagenesis1951L → R: Constitutive localization in punctae at the cell membrane and constitutive activation of CRAC channels. Ref.29 Ref.34
Mutagenesis318 – 3225EEELE → QQQLQ: Constitutive activation of CRAC channels. Ref.29 Ref.36
Mutagenesis3241V → P: Reduces activation of CRAC channels. Ref.29 Ref.36
Mutagenesis3471L → R: Abolishes colocalization with ORAI1 and activation of CRAC channels. Ref.29 Ref.36
Mutagenesis3511L → R: Abolishes colocalization with ORAI1 and activation of CRAC channels. Ref.29 Ref.36
Mutagenesis361 – 3622YY → KK: Abolishes activation of CRAC channels. Ref.29
Mutagenesis3801A → R: Constitutive activation of CRAC channels. Ref.29 Ref.36
Mutagenesis382 – 3865KIKKK → EIEEE: Abolishes activation of CRAC channels. Ref.29 Ref.36
Mutagenesis3831I → R: Abolishes activation of CRAC channels. Ref.29
Mutagenesis644 – 6452IP → NN: Loss of interaction with MAPRE1 and association with the growing microtubule plus ends. Ref.29
Sequence conflict5051E → G in AK314928. Ref.2
Sequence conflict5561S → R in AAC51627. Ref.1

Secondary structure

........................................ 685
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 14, 2008. Version 3.
Checksum: FFB5E7CB3D68A7A6

FASTA68577,423
        10         20         30         40         50         60 
MDVCVRLALW LLWGLLLHQG QSLSHSHSEK ATGTSSGANS EESTAAEFCR IDKPLCHSED 

        70         80         90        100        110        120 
EKLSFEAVRN IHKLMDDDAN GDVDVEESDE FLREDLNYHD PTVKHSTFHG EDKLISVEDL 

       130        140        150        160        170        180 
WKAWKSSEVY NWTVDEVVQW LITYVELPQY EETFRKLQLS GHAMPRLAVT NTTMTGTVLK 

       190        200        210        220        230        240 
MTDRSHRQKL QLKALDTVLF GPPLLTRHNH LKDFMLVVSI VIGVGGCWFA YIQNRYSKEH 

       250        260        270        280        290        300 
MKKMMKDLEG LHRAEQSLHD LQERLHKAQE EHRTVEVEKV HLEKKLRDEI NLAKQEAQRL 

       310        320        330        340        350        360 
KELREGTENE RSRQKYAEEE LEQVREALRK AEKELESHSS WYAPEALQKW LQLTHEVEVQ 

       370        380        390        400        410        420 
YYNIKKQNAE KQLLVAKEGA EKIKKKRNTL FGTFHVAHSS SLDDVDHKIL TAKQALSEVT 

       430        440        450        460        470        480 
AALRERLHRW QQIEILCGFQ IVNNPGIHSL VAALNIDPSW MGSTRPNPAH FIMTDDVDDM 

       490        500        510        520        530        540 
DEEIVSPLSM QSPSLQSSVR QRLTEPQHGL GSQRDLTHSD SESSLHMSDR QRVAPKPPQM 

       550        560        570        580        590        600 
SRAADEALNA MTSNGSHRLI EGVHPGSLVE KLPDSPALAK KALLALNHGL DKAHSLMELS 

       610        620        630        640        650        660 
PSAPPGGSPH LDSSRSHSPS SPDPDTPSPV GDSRALQASR NTRIPHLAGK KAVAEEDNGS 

       670        680 
IGEETDSSPG RKKFPLKIFK KPLKK 

« Hide

Isoform 2 [UniParc].

Checksum: 2470E8D059BFF6FB
Show »

FASTA54062,133

References

« Hide 'large scale' references
[1]"Molecular cloning of a novel human gene (D11S4896E) at chromosomal region 11p15.5."
Parker N.J., Begley C.G., Smith P.J., Fox R.M.
Genomics 37:253-256(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Fetal liver and Placenta.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[3]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Pancreas.
[6]"GOK: a gene at 11p15 involved in rhabdomyosarcoma and rhabdoid tumor development."
Sabbioni S., Barbanti-Brodano G., Croce C.M., Negrini M.
Cancer Res. 57:4493-4497(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE ROLE IN CANCER DEVELOPMENT.
[7]"STIM1: a novel phosphoprotein located at the cell surface."
Manji S.S., Parker N.J., Williams R.T., van Stekelenburg L., Pearson R.B., Dziadek M., Smith P.J.
Biochim. Biophys. Acta 1481:147-155(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, PHOSPHORYLATION.
[8]"Identification and characterization of the STIM (stromal interaction molecule) gene family: coding for a novel class of transmembrane proteins."
Williams R.T., Manji S.S.M., Parker N.J., Hancock M.S., van Stekelenburg L., Eid J.-P., Senior P.V., Kazenwadel J.S., Shandala T., Saint R., Smith P.J., Dziadek M.A.
Biochem. J. 357:673-685(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, TISSUE SPECIFICITY.
[9]"Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation."
Williams R.T., Senior P.V., van Stekelenburg L., Layton J.E., Smith P.J., Dziadek M.A.
Biochim. Biophys. Acta 1596:131-137(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, GLYCOSYLATION AT ASN-131 AND ASN-171.
[10]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[12]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-660 AND SER-668, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1."
Park C.Y., Hoover P.J., Mullins F.M., Bachhawat P., Covington E.D., Raunser S., Walz T., Garcia K.C., Dolmetsch R.E., Lewis R.S.
Cell 136:876-890(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ORAI1, SUBCELLULAR LOCATION, SUBUNIT.
[15]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575; SER-660; THR-665 AND SER-668, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Junctate is a Ca2+-sensing structural component of Orai1 and stromal interaction molecule 1 (STIM1)."
Srikanth S., Jew M., Kim K.D., Yee M.K., Abramson J., Gwack Y.
Proc. Natl. Acad. Sci. U.S.A. 109:8682-8687(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ASPH.
[19]"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Zhang H., Li X.-J., Martin D.B., Aebersold R.
Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-171.
[20]"STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered Ca2+ influx."
Liou J., Kim M.L., Heo W.D., Jones J.T., Myers J.W., Ferrell J.E. Jr., Meyer T.
Curr. Biol. 15:1235-1241(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-76.
[21]"STIM1, an essential and conserved component of store-operated Ca2+ channel function."
Roos J., DiGregorio P.J., Yeromin A.V., Ohlsen K., Lioudyno M., Zhang S., Safrina O., Kozak J.A., Wagner S.L., Cahalan M.D., Velicelebi G., Stauderman K.A.
J. Cell Biol. 169:435-445(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]"STIM1 is a Ca2+ sensor that activates CRAC channels and migrates from the Ca2+ store to the plasma membrane."
Zhang S.L., Yu Y., Roos J., Kozak J.A., Deerinck T.J., Ellisman M.H., Stauderman K.A., Cahalan M.D.
Nature 437:902-905(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[23]"Large store-operated calcium selective currents due to co-expression of Orai1 or Orai2 with the intracellular calcium sensor, Stim1."
Mercer J.C., Dehaven W.I., Smyth J.T., Wedel B., Boyles R.R., Bird G.S., Putney J.W. Jr.
J. Biol. Chem. 281:24979-24990(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-76; ASP-78 AND GLU-87.
[24]"Orai1 and STIM reconstitute store-operated calcium channel function."
Soboloff J., Spassova M.A., Tang X.D., Hewavitharana T., Xu W., Gill D.L.
J. Biol. Chem. 281:20661-20665(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[25]"Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
Lewandrowski U., Moebius J., Walter U., Sickmann A.
Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-171.
Tissue: Platelet.
[26]"Amplification of CRAC current by STIM1 and CRACM1 (Orai1)."
Peinelt C., Vig M., Koomoa D.L., Beck A., Nadler M.J.S., Koblan-Huberson M., Lis A., Fleig A., Penner R., Kinet J.-P.
Nat. Cell Biol. 8:771-773(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[27]"STIM1 has a plasma membrane role in the activation of store-operated Ca(2+) channels."
Spassova M.A., Soboloff J., He L.-P., Xu W., Dziadek M.A., Gill D.L.
Proc. Natl. Acad. Sci. U.S.A. 103:4040-4045(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLU-87.
[28]"STIM2 protein mediates distinct store-dependent and store-independent modes of CRAC channel activation."
Parvez S., Beck A., Peinelt C., Soboloff J., Lis A., Monteilh-Zoller M., Gill D.L., Fleig A., Penner R.
FASEB J. 22:752-761(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ORAI1.
[29]"An EB1-binding motif acts as a microtubule tip localization signal."
Honnappa S., Gouveia S.M., Weisbrich A., Damberger F.F., Bhavesh N.S., Jawhari H., Grigoriev I., van Rijssel F.J., Buey R.M., Lawera A., Jelesarov I., Winkler F.K., Wuthrich K., Akhmanova A., Steinmetz M.O.
Cell 138:366-376(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAPRE1, SUBCELLULAR LOCATION, DOMAIN MICROTUBULE TIP LOCALIZATION SIGNAL, MUTAGENESIS OF 644-ILE-PRO-645.
[30]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-171.
Tissue: Liver.
[31]"STIM1 mutation associated with a syndrome of immunodeficiency and autoimmunity."
Picard C., McCarl C.A., Papolos A., Khalil S., Luthy K., Hivroz C., LeDeist F., Rieux-Laucat F., Rechavi G., Rao A., Fischer A., Feske S.
N. Engl. J. Med. 360:1971-1980(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN IMD10.
[32]"A novel EF-hand protein, CRACR2A, is a cytosolic Ca2+ sensor that stabilizes CRAC channels in T cells."
Srikanth S., Jung H.J., Kim K.D., Souda P., Whitelegge J., Gwack Y.
Nat. Cell Biol. 12:436-446(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EFCAB4B.
[33]"SARAF inactivates the store operated calcium entry machinery to prevent excess calcium refilling."
Palty R., Raveh A., Kaminsky I., Meller R., Reuveny E.
Cell 149:425-438(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TMEM66.
[34]"Structural and mechanistic insights into STIM1-mediated initiation of store-operated calcium entry."
Stathopulos P.B., Zheng L., Li G.Y., Plevin M.J., Ikura M.
Cell 135:110-122(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 58-201 IN COMPLEX WITH CALCIUM, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, CALCIUM-BINDING, MUTAGENESIS OF GLU-87; PHE-108; GLY-110 AND LEU-195.
[35]"Structural and mechanistic insights into the activation of Stromal interaction molecule 1 (STIM1)."
Yang X., Jin H., Cai X., Li S., Shen Y.
Proc. Natl. Acad. Sci. U.S.A. 109:5657-5662(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 344-444, COILED-COIL DOMAIN, SUBUNIT.
[36]"STIM1/Orai1 coiled-coil interplay in the regulation of store-operated calcium entry."
Stathopulos P.B., Schindl R., Fahrner M., Zheng L., Gasmi-Seabrook G.M., Muik M., Romanin C., Ikura M.
Nat. Commun. 4:2963-2963(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 312-387 IN COMPLEX WITH ORAI1, INTERACTION WITH ORAI1, SUBUNIT, FUNCTION, COILED COIL, MUTAGENESIS OF 318-GLU--GLU-322; VAL-324; LEU-347; LEU-351; 361-TYR-TYR-362; ALA-380 AND 382-LYS--LYS-386, IDENTIFICATION BY MASS SPECTROMETRY.
[37]"The inhibitory helix controls the intramolecular conformational switching of the C-terminus of STIM1."
Cui B., Yang X., Li S., Lin Z., Wang Z., Dong C., Shen Y.
PLoS ONE 8:E74735-E74735(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 237-340, FUNCTION, COILED COIL, SUBUNIT.
[38]"Antiviral and regulatory T cell immunity in a patient with stromal interaction molecule 1 deficiency."
Fuchs S., Rensing-Ehl A., Speckmann C., Bengsch B., Schmitt-Graeff A., Bondzio I., Maul-Pavicic A., Bass T., Vraetz T., Strahm B., Ankermann T., Benson M., Caliebe A., Foelster-Holst R., Kaiser P., Thimme R., Schamel W.W., Schwarz K., Feske S., Ehl S.
J. Immunol. 188:1523-1533(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT IMD10 CYS-429.
[39]"Constitutive activation of the calcium sensor STIM1 causes tubular-aggregate myopathy."
Boehm J., Chevessier F., Maues De Paula A., Koch C., Attarian S., Feger C., Hantai D., Laforet P., Ghorab K., Vallat J.M., Fardeau M., Figarella-Branger D., Pouget J., Romero N.B., Koch M., Ebel C., Levy N., Krahn M. expand/collapse author list , Eymard B., Bartoli M., Laporte J.
Am. J. Hum. Genet. 92:271-278(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TAM GLN-72; GLY-84; ARG-109 AND ASN-109, CHARACTERIZATION OF VARIANTS TAM GLN-72; GLY-84; ARG-109 AND ASN-109.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U52426 mRNA. Translation: AAC51627.1.
AK314928 mRNA. No translation available.
AC015689 Genomic DNA. No translation available.
AC087441 Genomic DNA. No translation available.
AC090587 Genomic DNA. No translation available.
AC090804 Genomic DNA. No translation available.
AC107970 Genomic DNA. No translation available.
CH471158 Genomic DNA. Translation: EAX02581.1.
BC021300 mRNA. Translation: AAH21300.1.
CCDSCCDS7749.1.
RefSeqNP_001264891.1. NM_001277962.1.
NP_003147.2. NM_003156.3.
UniGeneHs.501735.
Hs.657794.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2K60NMR-A58-201[»]
2MAJNMR-A/C312-387[»]
2MAKNMR-A/C312-387[»]
3TEQX-ray1.90A/B/C/D344-444[»]
4O9BX-ray2.60A/B/C/D237-340[»]
ProteinModelPortalQ13586.
SMRQ13586. Positions 55-201, 247-444.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112662. 8 interactions.
DIPDIP-31121N.
IntActQ13586. 10 interactions.
STRING9606.ENSP00000300737.

Protein family/group databases

TCDB1.A.52.1.1. the ca(2+) release-activated ca(2+) (crac) channel (crac-c) family.

PTM databases

PhosphoSiteQ13586.

Polymorphism databases

DMDM209572721.

Proteomic databases

MaxQBQ13586.
PaxDbQ13586.
PRIDEQ13586.

Protocols and materials databases

DNASU6786.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000300737; ENSP00000300737; ENSG00000167323.
ENST00000527651; ENSP00000436208; ENSG00000167323.
GeneID6786.
KEGGhsa:6786.
UCSCuc001lyv.2. human.

Organism-specific databases

CTD6786.
GeneCardsGC11P003882.
H-InvDBHIX0009379.
HGNCHGNC:11386. STIM1.
HPAHPA011088.
HPA012123.
MIM160565. phenotype.
605921. gene.
612783. phenotype.
neXtProtNX_Q13586.
Orphanet317430. Combined immunodeficiency due to STIM1 deficiency.
2593. Tubular aggregate myopathy.
PharmGKBPA36195.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG307699.
HOGENOMHOG000261647.
HOVERGENHBG054652.
InParanoidQ13586.
KOK16059.
OMAIDKPLCD.
OrthoDBEOG7XSTDR.
PhylomeDBQ13586.
TreeFamTF313487.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ13586.
BgeeQ13586.
CleanExHS_STIM1.
GenevestigatorQ13586.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
InterProIPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
[Graphical view]
PfamPF07647. SAM_2. 1 hit.
[Graphical view]
SMARTSM00454. SAM. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
PROSITEPS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSTIM1. human.
EvolutionaryTraceQ13586.
GeneWikiSTIM1.
GenomeRNAi6786.
NextBio26496.
PROQ13586.
SOURCESearch...

Entry information

Entry nameSTIM1_HUMAN
AccessionPrimary (citable) accession number: Q13586
Secondary accession number(s): E9PQJ4, Q8N382
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: October 14, 2008
Last modified: July 9, 2014
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM