Stromal interaction molecule 1 precursor

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Reviewed, UniProtKB/Swiss-Prot Q13586 (STIM1_HUMAN)

Last modified June 16, 2009. Version 87. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
Stromal interaction molecule 1

Gene names

Name:	STIM1
Synonyms:	GOK

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	685 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Plays a role in mediating 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.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.16 Ref.17
Subunit structure	Forms homooligomers and heterooligomers with STIM2. Ref.6 Ref.7
Subcellular location	Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Note: Translocates from the endoplasmic reticulum to the cell membrane in response to a depletion of intracellular calcium. Ref.9 Ref.11 Ref.5
Tissue specificity	Ubiquitously expressed in various human primary cells and tumor cell lines. Ref.6 Ref.5
Post-translational modification	Glycosylation is required for cell surface expression. Phosphorylated predominantly on Ser residues. Ref.5 Ref.12 Ref.18 Ref.19 Ref.20 Ref.21
Involvement in disease	Defects in STIM1 may cause rhabdomyosarcoma and rhabdoid tumors. Ref.4
Sequence similarities	Contains 1 EF-hand domain. Contains 1 SAM (sterile alpha motif) domain.

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Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Cell membrane Endoplasmic reticulum Membrane
Domain	Coiled coil Signal Transmembrane
Ligand	Calcium
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	activation of store-operated calcium channel activity Ref.9 Inferred from direct assay. Source: UniProtKB calcium ion transport Inferred from electronic annotation. Source: UniProtKB-KW detection of calcium ion Ref.9 Inferred from direct assay. Source: UniProtKB
Cellular component	integral to endoplasmic reticulum membrane Ref.11 Inferred from direct assay. Source: UniProtKB integral to plasma membrane Ref.11 Inferred from direct assay. Source: UniProtKB
Molecular function	calcium ion binding Ref.9 Inferred from direct assay. Source: UniProtKB protein binding Ref.6 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
STIM2	Q9P246	2	EBI-448878,EBI-448891

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

Potential

Chain

23 – 685

663

Stromal interaction molecule 1

PRO_0000033326

Regions

Topological domain

23 – 213

191

Extracellular Potential

Transmembrane

214 – 234

Potential

Topological domain

235 – 685

451

Cytoplasmic Potential

Domain

63 – 98

EF-hand

Domain

132 – 200

SAM

Calcium binding

76 – 87

Potential

Coiled coil

248 – 388

141

Potential

Compositional bias

270 – 336

Glu-rich

Compositional bias

600 – 629

Pro/Ser-rich

Compositional bias

672 – 685

Lys-rich

Amino acid modifications

Modified residue

257

Phosphoserine By similarity

Modified residue

420

Phosphothreonine Ref.19

Modified residue

519

Phosphoserine By similarity

Modified residue

524

Phosphoserine By similarity

Modified residue

575

Phosphoserine Ref.12 Ref.18 Ref.20 Ref.21

Modified residue

608

Phosphoserine Ref.12 Ref.21

Modified residue

660

Phosphoserine Ref.21

Modified residue

665

Phosphothreonine By similarity

Modified residue

668

Phosphoserine Ref.21

Glycosylation

131

N-linked (GlcNAc...) Ref.7

Glycosylation

171

N-linked (GlcNAc...) Ref.7 Ref.8 Ref.15

Experimental info

Mutagenesis

D → A or N: Increases Ca(2+) influx even when Ca(2+) stores are not depleted. Ref.9 Ref.13

Mutagenesis

D → N: Increases Ca(2+) influx even when Ca(2+) stores are not depleted. Ref.13

Mutagenesis

E → A or Q: Increases Ca(2+) influx through activation of CRAC channels, even when Ca(2+) stores are not depleted. Ref.13 Ref.17

Sequence conflict

556

S → R in AAC51627. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q13586-1 [UniParc].

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

685

77,423

        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

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References

	« Hide 'large scale' referencesShow '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: 8921403] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal liver and Placenta.
[2]	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. Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas.
[4]	"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: 9377559] [Abstract] Cited for: DISEASE.
[5]	"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: 11004585] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, PHOSPHORYLATION.
[6]	"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: 11463338] [Abstract] Cited for: SUBUNIT, TISSUE SPECIFICITY.
[7]	"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: 11983428] [Abstract] Cited for: SUBUNIT, GLYCOSYLATION AT ASN-131 AND ASN-171.
[8]	"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: 12754519] [Abstract] Cited for: GLYCOSYLATION AT ASN-171.
[9]	"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: 16005298] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-76.
[10]	"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: 15866891] [Abstract] Cited for: FUNCTION.
[11]	"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: 16208375] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[12]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575 AND SER-608, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"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: 16807233] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-76; ASP-78 AND GLU-87.
[14]	"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: 16766533] [Abstract] Cited for: FUNCTION.
[15]	"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: 16263699] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-171, MASS SPECTROMETRY. Tissue: Platelet.
[16]	"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: 16733527] [Abstract] Cited for: FUNCTION.
[17]	"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: 16537481] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLU-87.
[18]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, MASS SPECTROMETRY. Tissue: Epithelium.
[19]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-420, MASS SPECTROMETRY.
[20]	"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: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, MASS SPECTROMETRY. Tissue: Platelet.
[21]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575; SER-608; SER-660 AND SER-668, MASS SPECTROMETRY.
[22]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[23]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-171, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

U52426 mRNA. Translation: AAC51627.1.
CH471158 Genomic DNA. Translation: EAX02581.1.
BC021300 mRNA. Translation: AAH21300.1.

IPI

IPI00299063.

RefSeq

NP_003147.2.

UniGene

Hs.501735

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2K60	NMR	-	A	58-201	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q13586. 1 interaction.

Protein family/group databases

TCDB

1.A.52.1.1. Ca2+ release-activated Ca2+ (CRAC) channel (CRAC-C) family.

PTM databases

PhosphoSite

Q13586.

Proteomic databases

PRIDE

Q13586.

Genome annotation databases

Ensembl

ENSG00000167323. Homo sapiens. [Contig view]

GeneID

6786.

KEGG

hsa:6786.

Organism-specific databases

GeneCards

GC11P003833.

H-InvDB

HIX0009379.

HGNC

HGNC:11386. STIM1.

HPA

HPA011088.
HPA012123.

MIM

605921. gene.

PharmGKB

PA36195.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q13586.

HOVERGEN

Q13586.

OMA

Q13586. MAPKPPQ.

Enzyme and pathway databases

Pathway_Interaction_DB

tcrpathway. TCR signaling in naive CD4+ T cells.
cd8tcrpathway. TCR signaling in naive CD8+ T cells.

Gene expression databases

ArrayExpress

Q13586.

Bgee

Q13586.

CleanEx

HS_STIM1.

Family and domain databases

InterPro

IPR018247. EF_HAND_1.
IPR001660. SAM.
IPR011510. SAM_2.
[Graphical view]

Pfam

PF07647. SAM_2. 1 hit.
[Graphical view]

SMART

SM00454. SAM. 1 hit.
[Graphical view]

PROSITE

PS00018. EF_HAND_1. False negative.
PS50222. EF_HAND_2. False negative.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

26496.

SOURCE

Search...

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Entry information

Entry name

STIM1_HUMAN

Accession

Primary (citable) accession number: Q13586
Secondary accession number(s): Q8N382

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 2, 2001
Last sequence update:	October 14, 2008
Last modified:	June 16, 2009
This is version 87 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 11

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents