Q13586 (STIM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Stromal interaction molecule 1

Gene names

Name:	STIM1
Synonyms:	GOK

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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

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.4 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24 Ref.30
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.6 Ref.7 Ref.15 Ref.25 Ref.26 Ref.29 Ref.30 Ref.31
Subcellular location	Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Cytoplasm › cytoskeleton. Note: Translocates from the endoplasmic reticulum to the cell membrane in response to a depletion of intracellular calcium. Associated with the microtubule network at the growing distal tip of microtubules. Ref.5 Ref.17 Ref.19 Ref.26
Tissue specificity	Ubiquitously expressed in various human primary cells and tumor cell lines. Ref.5 Ref.6
Domain	The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends. Ref.26 The STIM1 Orai1-activating region/CRAC-activating domain (SOAR/CAD) mediates interaction with ORAI1 to activate the channel. Ref.26
Post-translational modification	Glycosylation is required for cell surface expression. Phosphorylated predominantly on Ser residues. Ref.5
Involvement in disease	Immune dysfunction with T-cell inactivation due to calcium entry defect 2 (IDTICED2) [MIM:612783]: An immune disorder characterized by recurrent infections, impaired T-cell activation and proliferative response, decreased T-cell production of cytokines, lymphadenopathy, and normal lymphocytes counts and serum immunoglobulin levels. Additional features include thrombocytopenia, autoimmune hemolytic anemia, non-progressive myopathy, partial iris hypoplasia, hepatosplenomegaly and defective enamel dentition. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.28
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 process	Calcium transport Ion transport Transport
Cellular component	Cell membrane Cytoplasm Cytoskeleton Endoplasmic reticulum Membrane Microtubule
Coding sequence diversity	Polymorphism
Domain	Coiled coil Signal Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of store-operated calcium channel activity Inferred from direct assay Ref.17. Source: UniProtKB blood coagulation Traceable author statement. Source: Reactome calcium ion transport Inferred from electronic annotation. Source: UniProtKB-KW detection of calcium ion Inferred from direct assay Ref.17. Source: UniProtKB
Cellular_component	cortical endoplasmic reticulum Inferred from direct assay Ref.15. Source: UniProtKB integral to endoplasmic reticulum membrane Inferred from direct assay Ref.19Ref.15. Source: UniProtKB integral to plasma membrane Inferred from direct assay Ref.19. Source: UniProtKB microtubule Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	calcium ion binding Inferred from direct assay Ref.17. Source: UniProtKB microtubule plus-end binding Inferred from direct assay Ref.26. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-448878,EBI-448878
CALM	P62157	2	EBI-448878,EBI-397403	From a different organism.
EFCAB4B	Q9BSW2	3	EBI-448878,EBI-739773
ORAI1	Q96D31	11	EBI-448878,EBI-2291476
STIM2	Q9P246	4	EBI-448878,EBI-448891

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Potential

Chain

23 – 685

663

Stromal interaction molecule 1

PRO_0000033326

Regions

Topological domain

23 – 213

191

Extracellular Potential

Transmembrane

214 – 234

21

Helical; Potential

Topological domain

235 – 685

451

Cytoplasmic Potential

Domain

63 – 98

36

EF-hand

Domain

132 – 200

69

SAM

Calcium binding

76 – 87

12

Potential

Region

334 – 444

111

SOAR/CAD

Coiled coil

248 – 442

195

Ref.31

Motif

642 – 645

4

Microtubule tip localization signal

Compositional bias

270 – 336

67

Glu-rich

Compositional bias

600 – 629

30

Pro/Ser-rich

Compositional bias

672 – 685

14

Lys-rich

Amino acid modifications

Modified residue

257

1

Phosphoserine Ref.9

Modified residue

519

1

Phosphoserine Ref.13

Modified residue

524

1

Phosphoserine By similarity

Modified residue

575

1

Phosphoserine Ref.10 Ref.12

Modified residue

608

1

Phosphoserine Ref.8 Ref.11

Modified residue

660

1

Phosphoserine Ref.11 Ref.12

Modified residue

665

1

Phosphothreonine Ref.12

Modified residue

668

1

Phosphoserine Ref.11 Ref.12

Glycosylation

131

1

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

Glycosylation

171

1

N-linked (GlcNAc...) Ref.7 Ref.16 Ref.22 Ref.27

Natural variations

Natural variant

538

1

P → S.
Corresponds to variant rs35960304 [ dbSNP | Ensembl ].

VAR_061878

Experimental info

Mutagenesis

76

1

D → A or N: Increases Ca(2+) influx even when Ca(2+) stores are not depleted. Ref.17 Ref.20 Ref.26

Mutagenesis

78

1

D → N: Increases Ca(2+) influx even when Ca(2+) stores are not depleted. Ref.20 Ref.26

Mutagenesis

87

1

E → A or Q: Increases Ca(2+) influx through activation of CRAC channels, even when Ca(2+) stores are not depleted. Ref.20 Ref.24 Ref.26

Mutagenesis

644 – 645

2

IP → NN: Loss of interaction with MAPRE1 and association with the growing microtubule plus ends. Ref.26

Sequence conflict

556

1

S → R in AAC51627. Ref.1

Secondary structure

1

.

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.

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.

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685

Helix Strand Turn

Details...

Helix

64 – 73

10

Beta strand

80 – 83

4

Turn

85 – 90

6

Helix

91 – 95

5

Helix

102 – 108

7

Beta strand

110 – 112

3

Helix

117 – 126

10

Helix

128 – 131

4

Helix

134 – 145

12

Helix

150 – 157

8

Helix

163 – 167

5

Helix

171 – 174

4

Helix

183 – 199

17

Helix

345 – 391

47

Helix

393 – 397

5

Helix

400 – 404

5

Helix

408 – 437

30

Sequences

	Sequence		Length	Mass (Da)
	Q13586 [UniParc]. Last modified October 14, 2008. Version 3. Checksum: FFB5E7CB3D68A7A6	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

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] [Europe PMC] [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. , 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].
[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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: POSSIBLE ROLE IN CANCER DEVELOPMENT.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: SUBUNIT, GLYCOSYLATION AT ASN-131 AND ASN-171.
[8]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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, MASS SPECTROMETRY. Tissue: T-cell.
[10]	"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, MASS SPECTROMETRY. Tissue: Platelet.
[11]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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].
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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, MASS SPECTROMETRY. Tissue: Platelet.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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, MASS SPECTROMETRY. Tissue: Liver.
[28]	"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 IDTICED2.
[29]	"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.
[30]	"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.
[31]	"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 REGION, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

IPI

IPI00299063.

RefSeq

NP_003147.2. NM_003156.3.

UniGene

Hs.501735.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2K60	NMR	-	A	58-201	[»]
3TEQ	X-ray	1.90	A/B/C/D	344-444	[»]

ProteinModelPortal

Q13586.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31121N.

IntAct

Q13586. 8 interactions.

STRING

9606.ENSP00000300737.

Protein family/group databases

TCDB

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

PTM databases

PhosphoSite

Q13586.

Polymorphism databases

DMDM

209572721.

Proteomic databases

PaxDb

Q13586.

PRIDE

Q13586.

Protocols and materials databases

DNASU

6786.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000300737; ENSP00000300737; ENSG00000167323.

GeneID

6786.

KEGG

hsa:6786.

UCSC

uc001lyv.2. human.

Organism-specific databases

CTD

6786.

GeneCards

GC11P003882.

H-InvDB

HIX0009379.

HGNC

HGNC:11386. STIM1.

HPA

HPA011088.
HPA012123.

MIM

605921. gene.
612783. phenotype.

neXtProt

NX_Q13586.

Orphanet

169090. Severe combined immunodeficiency due to CRAC channel dysfunction.

PharmGKB

PA36195.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG307699.

HOGENOM

HOG000261647.

HOVERGEN

HBG054652.

InParanoid

Q13586.

KO

K16059.

OMA

NIHKQMD.

OrthoDB

EOG4F4S9M.

PhylomeDB

Q13586.

Enzyme and pathway databases

Pathway_Interaction_DB

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

Reactome

REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q13586.

Bgee

Q13586.

CleanEx

HS_STIM1.

Genevestigator

Q13586.

Family and domain databases

Gene3D

1.10.150.50. 1 hit.

InterPro

IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
[Graphical view]

Pfam

PF07647. SAM_2. 1 hit.
[Graphical view]

SMART

SM00454. SAM. 1 hit.
[Graphical view]

SUPFAM

SSF47769. SAM_homology. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

ChiTaRS

STIM1. human.

EvolutionaryTrace

Q13586.

GenomeRNAi

6786.

NextBio

26496.

SOURCE

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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:	May 1, 2013
This is version 130 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.