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Q13586

- STIM1_HUMAN

UniProt

Q13586 - STIM1_HUMAN

Protein

Stromal interaction molecule 1

Gene

STIM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 3 (14 Oct 2008)
      Previous versions | rss
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    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/ORAI1.12 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. protein binding Source: UniProtKB
    6. 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

    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

    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 (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.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 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. 1 Publication
    VAR_069892
    Natural varianti84 – 841D → 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. 1 Publication
    VAR_069893
    Natural varianti109 – 1091H → 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. 1 Publication
    VAR_069894
    Natural varianti109 – 1091H → 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. 1 Publication
    VAR_069895

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi76 – 761D → A or N: Increases Ca(2+) influx even when Ca(2+) stores are not depleted. 3 Publications
    Mutagenesisi78 – 781D → N: Increases Ca(2+) influx even when Ca(2+) stores are not depleted. 2 Publications
    Mutagenesisi87 – 871E → A or Q: Increases Ca(2+) influx through activation of CRAC channels, even when Ca(2+) stores are not depleted. 4 Publications
    Mutagenesisi108 – 1081F → D: Constitutive localization in punctae at the cell membrane and constitutive activation of CRAC channels; when associated with D-110. 2 Publications
    Mutagenesisi110 – 1101G → D: Constitutive localization in punctae at the cell membrane and constitutive activation of CRAC channels; when associated with D-108. 2 Publications
    Mutagenesisi195 – 1951L → R: Constitutive localization in punctae at the cell membrane and constitutive activation of CRAC channels. 2 Publications
    Mutagenesisi318 – 3225EEELE → QQQLQ: Constitutive activation of CRAC channels. 1 Publication
    Mutagenesisi324 – 3241V → P: Reduces activation of CRAC channels. 2 Publications
    Mutagenesisi347 – 3471L → R: Abolishes colocalization with ORAI1 and activation of CRAC channels. 2 Publications
    Mutagenesisi351 – 3511L → R: Abolishes colocalization with ORAI1 and activation of CRAC channels. 2 Publications
    Mutagenesisi361 – 3622YY → KK: Abolishes activation of CRAC channels. 1 Publication
    Mutagenesisi380 – 3801A → R: Constitutive activation of CRAC channels. 2 Publications
    Mutagenesisi382 – 3865KIKKK → EIEEE: Abolishes activation of CRAC channels. 1 Publication
    Mutagenesisi383 – 3831I → R: Abolishes activation of CRAC channels. 1 Publication
    Mutagenesisi644 – 6452IP → NN: Loss of interaction with MAPRE1 and association with the growing microtubule plus ends. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi160565. phenotype.
    612783. phenotype.
    Orphaneti317430. Combined immunodeficiency due to STIM1 deficiency.
    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...)2 Publications
    Glycosylationi171 – 1711N-linked (GlcNAc...)5 Publications
    Modified residuei257 – 2571Phosphoserine2 Publications
    Modified residuei504 – 5041PhosphothreonineBy similarity
    Modified residuei512 – 5121PhosphoserineBy similarity
    Modified residuei519 – 5191Phosphoserine2 Publications
    Modified residuei575 – 5751Phosphoserine3 Publications
    Modified residuei608 – 6081Phosphoserine3 Publications
    Modified residuei660 – 6601Phosphoserine3 Publications
    Modified residuei665 – 6651Phosphothreonine2 Publications
    Modified residuei668 – 6681Phosphoserine3 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

    ArrayExpressiQ13586.
    BgeeiQ13586.
    CleanExiHS_STIM1.
    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
    ORAI1Q96D3115EBI-448878,EBI-2291476
    PDIA3P301013EBI-448878,EBI-979862
    STIM2Q9P2464EBI-448878,EBI-448891

    Protein-protein interaction databases

    BioGridi112662. 10 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.
    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

    MDVCVRLALW LLWGLLLHQG QSLSHSHSEK ATGTSSGANS EESTAAEFCR    50
    IDKPLCHSED EKLSFEAVRN IHKLMDDDAN GDVDVEESDE FLREDLNYHD 100
    PTVKHSTFHG EDKLISVEDL WKAWKSSEVY NWTVDEVVQW LITYVELPQY 150
    EETFRKLQLS GHAMPRLAVT NTTMTGTVLK MTDRSHRQKL QLKALDTVLF 200
    GPPLLTRHNH LKDFMLVVSI VIGVGGCWFA YIQNRYSKEH MKKMMKDLEG 250
    LHRAEQSLHD LQERLHKAQE EHRTVEVEKV HLEKKLRDEI NLAKQEAQRL 300
    KELREGTENE RSRQKYAEEE LEQVREALRK AEKELESHSS WYAPEALQKW 350
    LQLTHEVEVQ YYNIKKQNAE KQLLVAKEGA EKIKKKRNTL FGTFHVAHSS 400
    SLDDVDHKIL TAKQALSEVT AALRERLHRW QQIEILCGFQ IVNNPGIHSL 450
    VAALNIDPSW MGSTRPNPAH FIMTDDVDDM DEEIVSPLSM QSPSLQSSVR 500
    QRLTEPQHGL GSQRDLTHSD SESSLHMSDR QRVAPKPPQM SRAADEALNA 550
    MTSNGSHRLI EGVHPGSLVE KLPDSPALAK KALLALNHGL DKAHSLMELS 600
    PSAPPGGSPH LDSSRSHSPS SPDPDTPSPV GDSRALQASR NTRIPHLAGK 650
    KAVAEEDNGS IGEETDSSPG RKKFPLKIFK KPLKK 685
    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 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. 1 Publication
    VAR_069892
    Natural varianti84 – 841D → 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. 1 Publication
    VAR_069893
    Natural varianti109 – 1091H → 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. 1 Publication
    VAR_069894
    Natural varianti109 – 1091H → 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. 1 Publication
    VAR_069895
    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.
    NP_003147.2. NM_003156.3.
    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.
    NP_003147.2. NM_003156.3.
    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. 10 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.
    605921. gene.
    612783. phenotype.
    neXtProti NX_Q13586.
    Orphaneti 317430. Combined immunodeficiency due to STIM1 deficiency.
    2593. Tubular aggregate myopathy.
    PharmGKBi PA36195.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG307699.
    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

    ArrayExpressi Q13586.
    Bgeei Q13586.
    CleanExi HS_STIM1.
    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

    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. "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.
    36. "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.
    37. "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.
    38. "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.
    39. Cited for: VARIANT IMD10 CYS-429.
    40. 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.

    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 1, 2014
    This is version 145 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