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Q13586

- STIM1_HUMAN

UniProt

Q13586 - STIM1_HUMAN

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Protein

Stromal interaction molecule 1

Gene

STIM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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/ORAI1.13 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi76 – 8712Add
BLAST

GO - Molecular functioni

  1. calcium channel regulator activity Source: Ensembl
  2. calcium ion binding Source: UniProtKB
  3. identical protein binding Source: IntAct
  4. microtubule plus-end binding Source: UniProtKB
  5. store-operated calcium channel activity Source: Ensembl

GO - Biological processi

  1. activation of store-operated calcium channel activity Source: UniProtKB
  2. blood coagulation Source: Reactome
  3. detection of calcium ion Source: UniProtKB
  4. regulation of calcium ion transport Source: UniProtKB
  5. regulation of store-operated calcium entry Source: Ensembl
  6. store-operated calcium entry Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_162. Elevation of cytosolic Ca2+ levels.

Protein family/group databases

TCDBi1.A.52.1.1. the ca(2+) release-activated ca(2+) (crac) channel (crac-c) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Stromal interaction molecule 1
Gene namesi
Name:STIM1
Synonyms:GOK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:11386. STIM1.

Subcellular locationi

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.

GO - Cellular componenti

  1. cortical endoplasmic reticulum Source: UniProtKB
  2. endoplasmic reticulum Source: HPA
  3. endoplasmic reticulum membrane Source: Reactome
  4. growth cone Source: Ensembl
  5. integral component of endoplasmic reticulum membrane Source: UniProtKB
  6. integral component of plasma membrane Source: UniProtKB
  7. microtubule Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Endoplasmic reticulum, Membrane, Microtubule

Pathology & Biotechi

Involvement in diseasei

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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti429 – 4291R → C in IMD10. 1 Publication
VAR_069896
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti72 – 721H → Q in TAM1; myoblasts with the mutation have significantly increased clustering of STIM1, regardless of calcium levels, indicating that calcium sensing in the sarcoplasmic reticulum is impaired. 1 Publication
VAR_069892
Natural varianti84 – 841D → G in TAM1; myoblasts with the mutation have significantly increased clustering of STIM1, regardless of calcium levels, indicating that calcium sensing in the sarcoplasmic reticulum is impaired. 1 Publication
VAR_069893
Natural varianti109 – 1091H → N in TAM1; myoblasts with the mutation have significantly increased clustering of STIM1, regardless of calcium levels, indicating that calcium sensing in the sarcoplasmic reticulum is impaired. 1 Publication
VAR_069894
Natural varianti109 – 1091H → R in TAM1; myoblasts with the mutation have significantly increased clustering of STIM1, regardless of calcium levels, indicating that calcium sensing in the sarcoplasmic reticulum is impaired. 1 Publication
VAR_069895
Amelogenesis imperfecta, hypomaturation type, 2A5 (AI2A5) [MIM:615887]: A defect of enamel formation. The disorder involves both primary and secondary dentitions. The teeth have a shiny agar jelly appearance and the enamel is softer than normal. Brown pigment is present in middle layers of enamel.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti426 – 4261R → C in AI2A5; autosomal recessive. 1 Publication
VAR_071477
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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti304 – 3041R → W in STRMK; autosomal dominant; promotes constitutive activation of the Ca2+ release-activated Ca2+ (CRAC) channel. 2 Publications
VAR_071476

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi76 – 761D → A or N: Increases Ca(2+) influx even when Ca(2+) stores are not depleted. Promotes constitutive activation of the Ca2+ release-activated Ca2+ (CRAC) channel. 3 Publications
Mutagenesisi78 – 781D → N: Increases Ca(2+) influx even when Ca(2+) stores are not depleted. 1 Publication
Mutagenesisi87 – 871E → A or Q: Increases Ca(2+) influx through activation of CRAC channels, even when Ca(2+) stores are not depleted. 3 Publications
Mutagenesisi108 – 1081F → D: Constitutive localization in punctae at the cell membrane and constitutive activation of CRAC channels; when associated with D-110. 1 Publication
Mutagenesisi110 – 1101G → D: Constitutive localization in punctae at the cell membrane and constitutive activation of CRAC channels; when associated with D-108. 1 Publication
Mutagenesisi195 – 1951L → R: Constitutive localization in punctae at the cell membrane and constitutive activation of CRAC channels. 1 Publication
Mutagenesisi318 – 3225EEELE → QQQLQ: Constitutive activation of CRAC channels. 1 Publication
Mutagenesisi324 – 3241V → P: Reduces activation of CRAC channels. 1 Publication
Mutagenesisi347 – 3471L → R: Abolishes colocalization with ORAI1 and activation of CRAC channels. 1 Publication
Mutagenesisi351 – 3511L → R: Abolishes colocalization with ORAI1 and activation of CRAC channels. 1 Publication
Mutagenesisi361 – 3622YY → KK: Abolishes activation of CRAC channels. 1 Publication
Mutagenesisi380 – 3801A → R: Constitutive activation of CRAC channels. 1 Publication
Mutagenesisi382 – 3865KIKKK → EIEEE: Abolishes activation of CRAC channels. 1 Publication
Mutagenesisi383 – 3831I → R: Abolishes activation of CRAC channels.
Mutagenesisi644 – 6452IP → NN: Loss of interaction with MAPRE1 and association with the growing microtubule plus ends. 1 Publication

Keywords - Diseasei

Amelogenesis imperfecta, Disease mutation

Organism-specific databases

MIMi160565. phenotype.
185070. phenotype.
612783. phenotype.
615887. phenotype.
Orphaneti317430. Combined immunodeficiency due to STIM1 deficiency.
3204. Stormorken-Sjaastad-Langslet syndrome.
2593. Tubular aggregate myopathy.
PharmGKBiPA36195.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 685663Stromal interaction molecule 1PRO_0000033326Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi131 – 1311N-linked (GlcNAc...)1 Publication
Glycosylationi171 – 1711N-linked (GlcNAc...)4 Publications
Modified residuei257 – 2571Phosphoserine1 Publication
Modified residuei504 – 5041PhosphothreonineBy similarity
Modified residuei512 – 5121PhosphoserineBy similarity
Modified residuei519 – 5191Phosphoserine1 Publication
Modified residuei575 – 5751Phosphoserine2 Publications
Modified residuei608 – 6081Phosphoserine2 Publications
Modified residuei660 – 6601Phosphoserine2 Publications
Modified residuei665 – 6651Phosphothreonine1 Publication
Modified residuei668 – 6681Phosphoserine2 Publications

Post-translational modificationi

Glycosylation is required for cell surface expression.5 Publications
Phosphorylated predominantly on Ser residues.7 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ13586.
PaxDbiQ13586.
PRIDEiQ13586.

PTM databases

PhosphoSiteiQ13586.

Expressioni

Tissue specificityi

Ubiquitously expressed in various human primary cells and tumor cell lines.2 Publications

Gene expression databases

BgeeiQ13586.
CleanExiHS_STIM1.
ExpressionAtlasiQ13586. baseline and differential.
GenevestigatoriQ13586.

Organism-specific databases

HPAiHPA011088.
HPA012123.

Interactioni

Subunit structurei

Forms homooligomers and heterooligomers with STIM2. Interacts with ORAI1. Interacts with MAPRE1; probably required for targeting to the growing microtubule plus ends. Interacts with CRACR2A/EFCAB4B; the interaction is direct and takes place in absence of Ca2+. Forms a complex with CRACR2A/EFCAB4B and ORAI1 at low concentration of Ca2+, the complex dissociates at elevated Ca2+ concentrations. Interacts with SARAF, promoting a slow inactivation of STIM1-dependent SOCE activity, possibly by facilitating the deoligomerization of STIM1. Interacts with ASPH (isoform 8). Interacts with SLC35G1; intracellular Ca2+-dependent. May interact with ATP1A1, ATP2A2, ATP2B1, ATP2B4, KPNB1 and XPO1; through SLC35G1.13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself6EBI-448878,EBI-448878
CALMP621572EBI-448878,EBI-397403From a different organism.
EFCAB4BQ9BSW23EBI-448878,EBI-739773
ORAI1Q96D3116EBI-448878,EBI-2291476
PDIA3P301013EBI-448878,EBI-979862
STIM2Q9P2464EBI-448878,EBI-448891

Protein-protein interaction databases

BioGridi112662. 15 interactions.
DIPiDIP-31121N.
IntActiQ13586. 10 interactions.
STRINGi9606.ENSP00000300737.

Structurei

Secondary structure

1
685
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi64 – 7310
Beta strandi80 – 834
Turni85 – 906
Helixi91 – 955
Helixi102 – 1087
Beta strandi110 – 1123
Helixi117 – 12610
Helixi128 – 1314
Helixi134 – 14512
Helixi150 – 1578
Helixi163 – 1675
Helixi171 – 1744
Helixi183 – 19917
Helixi249 – 27123
Turni272 – 2754
Helixi276 – 33459
Helixi339 – 3413
Helixi345 – 39147
Helixi393 – 3975
Helixi400 – 4045
Helixi408 – 43730

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ13586.
SMRiQ13586. Positions 55-201, 247-444.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13586.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 213191ExtracellularSequence AnalysisAdd
BLAST
Topological domaini235 – 685451CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei214 – 23421HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 9836EF-handAdd
BLAST
Domaini132 – 20069SAMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni334 – 444111SOAR/CADAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili248 – 4421953 PublicationsAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi642 – 6454Microtubule tip localization signal

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi270 – 33667Glu-richAdd
BLAST
Compositional biasi600 – 62930Pro/Ser-richAdd
BLAST
Compositional biasi672 – 68514Lys-richAdd
BLAST

Domaini

The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends.1 Publication
The STIM1 Orai1-activating region/CRAC-activating domain (SOAR/CAD) mediates interaction with ORAI1 to activate the channel.1 Publication

Sequence similaritiesi

Contains 1 EF-hand domain.Curated
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG307699.
GeneTreeiENSGT00390000000214.
HOGENOMiHOG000261647.
HOVERGENiHBG054652.
InParanoidiQ13586.
KOiK16059.
OMAiIDKPLCD.
OrthoDBiEOG7XSTDR.
PhylomeDBiQ13586.
TreeFamiTF313487.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
InterProiIPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
[Graphical view]
PfamiPF07647. SAM_2. 1 hit.
[Graphical view]
SMARTiSM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
PROSITEiPS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13586-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MDVCVRLALW LLWGLLLHQG QSLSHSHSEK ATGTSSGANS EESTAAEFCR
60 70 80 90 100
IDKPLCHSED EKLSFEAVRN IHKLMDDDAN GDVDVEESDE FLREDLNYHD
110 120 130 140 150
PTVKHSTFHG EDKLISVEDL WKAWKSSEVY NWTVDEVVQW LITYVELPQY
160 170 180 190 200
EETFRKLQLS GHAMPRLAVT NTTMTGTVLK MTDRSHRQKL QLKALDTVLF
210 220 230 240 250
GPPLLTRHNH LKDFMLVVSI VIGVGGCWFA YIQNRYSKEH MKKMMKDLEG
260 270 280 290 300
LHRAEQSLHD LQERLHKAQE EHRTVEVEKV HLEKKLRDEI NLAKQEAQRL
310 320 330 340 350
KELREGTENE RSRQKYAEEE LEQVREALRK AEKELESHSS WYAPEALQKW
360 370 380 390 400
LQLTHEVEVQ YYNIKKQNAE KQLLVAKEGA EKIKKKRNTL FGTFHVAHSS
410 420 430 440 450
SLDDVDHKIL TAKQALSEVT AALRERLHRW QQIEILCGFQ IVNNPGIHSL
460 470 480 490 500
VAALNIDPSW MGSTRPNPAH FIMTDDVDDM DEEIVSPLSM QSPSLQSSVR
510 520 530 540 550
QRLTEPQHGL GSQRDLTHSD SESSLHMSDR QRVAPKPPQM SRAADEALNA
560 570 580 590 600
MTSNGSHRLI EGVHPGSLVE KLPDSPALAK KALLALNHGL DKAHSLMELS
610 620 630 640 650
PSAPPGGSPH LDSSRSHSPS SPDPDTPSPV GDSRALQASR NTRIPHLAGK
660 670 680
KAVAEEDNGS IGEETDSSPG RKKFPLKIFK KPLKK
Length:685
Mass (Da):77,423
Last modified:October 14, 2008 - v3
Checksum:iFFB5E7CB3D68A7A6
GO
Isoform 2 (identifier: Q13586-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     515-540: DLTHSDSESSLHMSDRQRVAPKPPQM → GSSLKANRLSSKGFDPFRFGVLPPHE
     541-685: Missing.

Note: No experimental confirmation available.

Show »
Length:540
Mass (Da):62,133
Checksum:i2470E8D059BFF6FB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti505 – 5051E → G in AK314928. (PubMed:14702039)Curated
Sequence conflicti556 – 5561S → R in AAC51627. (PubMed:8921403)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti72 – 721H → Q in TAM1; myoblasts with the mutation have significantly increased clustering of STIM1, regardless of calcium levels, indicating that calcium sensing in the sarcoplasmic reticulum is impaired. 1 Publication
VAR_069892
Natural varianti84 – 841D → G in TAM1; myoblasts with the mutation have significantly increased clustering of STIM1, regardless of calcium levels, indicating that calcium sensing in the sarcoplasmic reticulum is impaired. 1 Publication
VAR_069893
Natural varianti109 – 1091H → N in TAM1; myoblasts with the mutation have significantly increased clustering of STIM1, regardless of calcium levels, indicating that calcium sensing in the sarcoplasmic reticulum is impaired. 1 Publication
VAR_069894
Natural varianti109 – 1091H → R in TAM1; myoblasts with the mutation have significantly increased clustering of STIM1, regardless of calcium levels, indicating that calcium sensing in the sarcoplasmic reticulum is impaired. 1 Publication
VAR_069895
Natural varianti304 – 3041R → W in STRMK; autosomal dominant; promotes constitutive activation of the Ca2+ release-activated Ca2+ (CRAC) channel. 2 Publications
VAR_071476
Natural varianti426 – 4261R → C in AI2A5; autosomal recessive. 1 Publication
VAR_071477
Natural varianti429 – 4291R → C in IMD10. 1 Publication
VAR_069896
Natural varianti538 – 5381P → S.
Corresponds to variant rs35960304 [ dbSNP | Ensembl ].
VAR_061878

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei515 – 54026DLTHS…KPPQM → GSSLKANRLSSKGFDPFRFG VLPPHE in isoform 2. 1 PublicationVSP_055150Add
BLAST
Alternative sequencei541 – 685145Missing in isoform 2. 1 PublicationVSP_055151Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS60706.1. [Q13586-2]
CCDS7749.1. [Q13586-1]
RefSeqiNP_001264891.1. NM_001277962.1. [Q13586-2]
NP_003147.2. NM_003156.3. [Q13586-1]
UniGeneiHs.501735.
Hs.657794.

Genome annotation databases

EnsembliENST00000300737; ENSP00000300737; ENSG00000167323. [Q13586-1]
ENST00000527651; ENSP00000436208; ENSG00000167323. [Q13586-2]
GeneIDi6786.
KEGGihsa:6786.
UCSCiuc001lyv.2. human. [Q13586-1]

Polymorphism databases

DMDMi209572721.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS60706.1. [Q13586-2 ]
CCDS7749.1. [Q13586-1 ]
RefSeqi NP_001264891.1. NM_001277962.1. [Q13586-2 ]
NP_003147.2. NM_003156.3. [Q13586-1 ]
UniGenei Hs.501735.
Hs.657794.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2K60 NMR - A 58-201 [» ]
2MAJ NMR - A/C 312-387 [» ]
2MAK NMR - A/C 312-387 [» ]
3TEQ X-ray 1.90 A/B/C/D 344-444 [» ]
4O9B X-ray 2.60 A/B/C/D 237-340 [» ]
ProteinModelPortali Q13586.
SMRi Q13586. Positions 55-201, 247-444.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112662. 15 interactions.
DIPi DIP-31121N.
IntActi Q13586. 10 interactions.
STRINGi 9606.ENSP00000300737.

Protein family/group databases

TCDBi 1.A.52.1.1. the ca(2+) release-activated ca(2+) (crac) channel (crac-c) family.

PTM databases

PhosphoSitei Q13586.

Polymorphism databases

DMDMi 209572721.

Proteomic databases

MaxQBi Q13586.
PaxDbi Q13586.
PRIDEi Q13586.

Protocols and materials databases

DNASUi 6786.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000300737 ; ENSP00000300737 ; ENSG00000167323 . [Q13586-1 ]
ENST00000527651 ; ENSP00000436208 ; ENSG00000167323 . [Q13586-2 ]
GeneIDi 6786.
KEGGi hsa:6786.
UCSCi uc001lyv.2. human. [Q13586-1 ]

Organism-specific databases

CTDi 6786.
GeneCardsi GC11P003882.
H-InvDB HIX0009379.
HGNCi HGNC:11386. STIM1.
HPAi HPA011088.
HPA012123.
MIMi 160565. phenotype.
185070. phenotype.
605921. gene.
612783. phenotype.
615887. phenotype.
neXtProti NX_Q13586.
Orphaneti 317430. Combined immunodeficiency due to STIM1 deficiency.
3204. Stormorken-Sjaastad-Langslet syndrome.
2593. Tubular aggregate myopathy.
PharmGKBi PA36195.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG307699.
GeneTreei ENSGT00390000000214.
HOGENOMi HOG000261647.
HOVERGENi HBG054652.
InParanoidi Q13586.
KOi K16059.
OMAi IDKPLCD.
OrthoDBi EOG7XSTDR.
PhylomeDBi Q13586.
TreeFami TF313487.

Enzyme and pathway databases

Reactomei REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_162. Elevation of cytosolic Ca2+ levels.

Miscellaneous databases

ChiTaRSi STIM1. human.
EvolutionaryTracei Q13586.
GeneWikii STIM1.
GenomeRNAii 6786.
NextBioi 26496.
PROi Q13586.
SOURCEi Search...

Gene expression databases

Bgeei Q13586.
CleanExi HS_STIM1.
ExpressionAtlasi Q13586. baseline and differential.
Genevestigatori Q13586.

Family and domain databases

Gene3Di 1.10.150.50. 1 hit.
InterProi IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
[Graphical view ]
Pfami PF07647. SAM_2. 1 hit.
[Graphical view ]
SMARTi SM00454. SAM. 1 hit.
[Graphical view ]
SUPFAMi SSF47769. SSF47769. 1 hit.
PROSITEi PS50105. SAM_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  13. 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. 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. 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. 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. 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. 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 CRACR2A.
  33. "POST, partner of stromal interaction molecule 1 (STIM1), targets STIM1 to multiple transporters."
    Krapivinsky G., Krapivinsky L., Stotz S.C., Manasian Y., Clapham D.E.
    Proc. Natl. Acad. Sci. U.S.A. 108:19234-19239(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATP1A1; ATP2A2; ATP2B1; ATP2B4; KPNB1; SLC35G1 AND XPO1.
  34. "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 SARAF.
  35. Cited for: INVOLVEMENT IN STRMK, VARIANT STRMK TRP-304.
  36. Cited for: INVOLVEMENT IN AI2A5, VARIANT AI2A5 CYS-426.
  37. "Activating mutations in STIM1 and ORAI1 cause overlapping syndromes of tubular myopathy and congenital miosis."
    Nesin V., Wiley G., Kousi M., Ong E.C., Lehmann T., Nicholl D.J., Suri M., Shahrizaila N., Katsanis N., Gaffney P.M., Wierenga K.J., Tsiokas L.
    Proc. Natl. Acad. Sci. U.S.A. 111:4197-4202(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INVOLVEMENT IN STRMK, VARIANT STRMK TRP-304, CHARACTERIZATION OF VARIANT STRMK TRP-304, MUTAGENESIS OF ASP-76.
  38. "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.
  39. "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.
  40. "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.
  41. "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.
  42. Cited for: VARIANT IMD10 CYS-429.
  43. Cited for: VARIANTS TAM1 GLN-72; GLY-84; ARG-109 AND ASN-109, CHARACTERIZATION OF VARIANTS TAM1 GLN-72; GLY-84; ARG-109 AND ASN-109.

Entry informationi

Entry nameiSTIM1_HUMAN
AccessioniPrimary (citable) accession number: Q13586
Secondary accession number(s): E9PQJ4, Q8N382
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: October 14, 2008
Last modified: October 29, 2014
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3