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P42224

- STAT1_HUMAN

UniProt

P42224 - STAT1_HUMAN

Protein

Signal transducer and activator of transcription 1-alpha/beta

Gene

STAT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 179 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Signal transducer and transcription activator that mediates cellular responses to interferons (IFNs), cytokine KITLG/SCF and other cytokines and other growth factors. Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, signaling via protein kinases leads to activation of Jak kinases (TYK2 and JAK1) and to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize and associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of IFN-stimulated genes (ISG), which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated. It then forms a homodimer termed IFN-gamma-activated factor (GAF), migrates into the nucleus and binds to the IFN gamma activated sequence (GAS) to drive the expression of the target genes, inducing a cellular antiviral state. Becomes activated in response to KITLG/SCF and KIT signaling. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4.5 Publications

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. double-stranded DNA binding Source: UniProtKB
    3. enzyme binding Source: UniProtKB
    4. identical protein binding Source: IntAct
    5. protein binding Source: UniProtKB
    6. protein homodimerization activity Source: UniProtKB
    7. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
    8. RNA polymerase II core promoter sequence-specific DNA binding Source: BHF-UCL
    9. RNA polymerase II core promoter sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    10. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    11. signal transducer activity Source: InterPro
    12. tumor necrosis factor receptor binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB
    2. blood circulation Source: UniProtKB
    3. cellular response to insulin stimulus Source: Ensembl
    4. cellular response to interferon-beta Source: BHF-UCL
    5. cytokine-mediated signaling pathway Source: Reactome
    6. defense response to virus Source: UniProtKB-KW
    7. interferon-gamma-mediated signaling pathway Source: UniProtKB
    8. JAK-STAT cascade Source: UniProtKB
    9. JAK-STAT cascade involved in growth hormone signaling pathway Source: Reactome
    10. lipopolysaccharide-mediated signaling pathway Source: Ensembl
    11. metanephric mesenchymal cell differentiation Source: UniProtKB
    12. metanephric mesenchymal cell proliferation involved in metanephros development Source: UniProtKB
    13. negative regulation of angiogenesis Source: UniProtKB
    14. negative regulation of endothelial cell proliferation Source: UniProtKB
    15. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    16. negative regulation of macrophage fusion Source: Ensembl
    17. negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis Source: UniProtKB
    18. negative regulation of metanephric nephron tubule epithelial cell differentiation Source: UniProtKB
    19. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    20. positive regulation of mesenchymal cell proliferation Source: UniProtKB
    21. positive regulation of smooth muscle cell proliferation Source: UniProtKB
    22. positive regulation of transcription, DNA-templated Source: UniProtKB
    23. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    24. regulation of apoptotic process Source: UniProtKB
    25. regulation of interferon-gamma-mediated signaling pathway Source: Reactome
    26. regulation of type I interferon-mediated signaling pathway Source: Reactome
    27. renal tubule development Source: UniProtKB
    28. response to cAMP Source: UniProtKB
    29. response to cytokine Source: UniProtKB
    30. response to drug Source: Ensembl
    31. response to exogenous dsRNA Source: Ensembl
    32. response to hydrogen peroxide Source: Ensembl
    33. response to mechanical stimulus Source: Ensembl
    34. response to nutrient Source: Ensembl
    35. response to peptide hormone Source: UniProtKB
    36. transcription from RNA polymerase II promoter Source: GOC
    37. tumor necrosis factor-mediated signaling pathway Source: UniProtKB
    38. type I interferon signaling pathway Source: UniProtKB
    39. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Antiviral defense, Host-virus interaction, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_111040. Signaling by SCF-KIT.
    REACT_111133. Growth hormone receptor signaling.
    REACT_115831. ISG15 antiviral mechanism.
    REACT_121141. Signaling by FGFR1 fusion mutants.
    REACT_17025. Downstream signal transduction.
    REACT_24980. Regulation of IFNG signaling.
    REACT_25078. Interferon gamma signaling.
    REACT_25162. Interferon alpha/beta signaling.
    REACT_25216. Regulation of IFNA signaling.
    REACT_27307. Interleukin-6 signaling.
    SignaLinkiP42224.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Signal transducer and activator of transcription 1-alpha/beta
    Alternative name(s):
    Transcription factor ISGF-3 components p91/p84
    Gene namesi
    Name:STAT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:11362. STAT1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Translocated into the nucleus upon tyrosine phosphorylation and dimerization, in response to IFN-gamma and signaling by activated FGFR1, FGFR2, FGFR3 or FGFR4.

    GO - Cellular componenti

    1. axon Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: Reactome
    4. dendrite Source: UniProtKB
    5. nuclear chromatin Source: BHF-UCL
    6. nucleolus Source: HPA
    7. nucleoplasm Source: Reactome
    8. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    STAT1 deficiency complete (STAT1D) [MIM:613796]: A disorder characterized by susceptibility to severe mycobacterial and viral infections. Affected individuals can develop disseminated infections and die of viral illness.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti201 – 2011K → N in STAT1D; not deleterious in terms of most STAT1 functions; causes abnormal splicing out of exon 8 from most mRNAs thereby decreasing protein levels by approximately 70%. 1 Publication
    VAR_065815
    Natural varianti600 – 6001L → P in STAT1D; found in an infant who died of a viral-like illness associated with complete STAT1 deficiency. 1 Publication
    VAR_018265
    Mendelian susceptibility to mycobacterial disease (MSMD) [MIM:209950]: This rare condition confers predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine and environmental non-tuberculous mycobacteria, and by the more virulent Mycobacterium tuberculosis. Other microorganisms rarely cause severe clinical disease in individuals with susceptibility to mycobacterial infections, with the exception of Salmonella which infects less than 50% of these individuals. The pathogenic mechanism underlying MSMD is the impairment of interferon-gamma mediated immunity, whose severity determines the clinical outcome. Some patients die of overwhelming mycobacterial disease with lepromatous-like lesions in early childhood, whereas others develop, later in life, disseminated but curable infections with tuberculoid granulomas. MSMD is a genetically heterogeneous disease with autosomal recessive, autosomal dominant or X-linked inheritance.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti320 – 3201E → Q in MSMD; affects the DNA-binding activity of the protein. 1 Publication
    VAR_065816
    Natural varianti463 – 4631Q → H in MSMD; affects the DNA-binding activity of the protein. 1 Publication
    VAR_065817
    Natural varianti637 – 6371K → E in MSMD; affects both phosphorylation and DNA-binding activity; results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27. 1 Publication
    VAR_068713
    Natural varianti673 – 6731K → R in MSMD; impairs tyrosine phosphorylation; results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27. 1 Publication
    VAR_068714
    Natural varianti706 – 7061L → S in MSMD; loss of GAF and ISGF3 activation; impairs the nuclear accumulation of GAF but not of ISGF3 in heterozygous cells stimulated by IFNs; affects phosphorylation of the protein. 1 Publication
    VAR_018266
    Candidiasis, familial, 7 (CANDF7) [MIM:614162]: A primary immunodeficiency disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry. STAT1 mutations in patients with autosomal dominant candidiasis lead to defective responses of type 1 and type 17 helper T-cells, characterized by reduced production of interferon-alpha, interleukin-17, and interleukin-22. These cytokines are crucial for the antifungal defense of skin and mucosa (PubMed:21714643).1 Publication
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti165 – 1651D → G in CANDF7; gain of function mutation associated with increased STAT1 phosphorylation due to impaired nuclear dephosphorylation. 1 Publication
    VAR_065934
    Natural varianti165 – 1651D → H in CANDF7. 1 Publication
    VAR_065935
    Natural varianti170 – 1701Y → N in CANDF7. 1 Publication
    VAR_065936
    Natural varianti174 – 1741C → R in CANDF7. 1 Publication
    VAR_065937
    Natural varianti202 – 2021M → I in CANDF7. 1 Publication
    VAR_065938
    Natural varianti202 – 2021M → V in CANDF7. 1 Publication
    VAR_065939
    Natural varianti267 – 2671A → V in CANDF7. 2 Publications
    VAR_065940
    Natural varianti271 – 2711Q → P in CANDF7. 1 Publication
    VAR_065941
    Natural varianti274 – 2741R → Q in CANDF7; gain of function mutation associated with increased STAT1 phosphorylation due to impaired nuclear dephosphorylation. 1 Publication
    VAR_065942
    Natural varianti274 – 2741R → W in CANDF7. 2 Publications
    VAR_065943
    Natural varianti286 – 2861K → I in CANDF7. 1 Publication
    VAR_065944
    Natural varianti288 – 2881T → A in CANDF7. 1 Publication
    VAR_065945

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi110 – 1101K → R: Sumoylated. 1 Publication
    Mutagenesisi701 – 7011Y → E: Not phosphorylated at S-708 upon IFNB induction. 2 Publications
    Mutagenesisi701 – 7011Y → F: No effect on basal sumoylation. Enhances sumoylation in the presence of MAPK stimulation. Phosphorylated at S-708 upon IFNB induction. 2 Publications
    Mutagenesisi703 – 7031K → R: Abolishes sumoylation by SUMO1. Increased IFN-gamma-mediated transactivation. 2 Publications
    Mutagenesisi708 – 7081S → A: Phosphorylated at Y-701 upon IFNB induction. 1 Publication
    Mutagenesisi708 – 7081S → D: Not phosphorylated at Y-701 upon IFNB induction. 1 Publication
    Mutagenesisi727 – 7271S → A: Decreased transcriptional activation. No effect on basal sumoylation. No enhancement of sumoylation on MAPK stimulation. No PRKCD-induced apoptosis. Upon IFNB induction, phosphorylated at Y-701 but not at S-708. 3 Publications
    Mutagenesisi727 – 7271S → D: No change in enhancement of MAPK-induced sumoylation. Basal interaction with PIAS1. Interaction with PIAS1 increased on MAPK stimulation. 3 Publications
    Mutagenesisi727 – 7271S → E: No change in enhancement of MAPK-induced sumoylation. 3 Publications

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi209950. phenotype.
    613796. phenotype.
    614162. phenotype.
    Orphaneti391487. Autoimmune enteropathy and endocrinopathy-susceptibility to chronic infections syndrome.
    1334. Chronic mucocutaneous candidiasis.
    319595. Mendelian susceptibility to mycobacterial diseases due to partial STAT1 deficiency.
    391311. Susceptibility to viral and mycobacterial infections.
    PharmGKBiPA36183.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 750749Signal transducer and activator of transcription 1-alpha/betaPRO_0000182410Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei701 – 7011Phosphotyrosine; by JAK1, JAK2 or TYK25 Publications
    Cross-linki703 – 703Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei708 – 7081Phosphoserine; by IKKE1 Publication
    Modified residuei727 – 7271Phosphoserine; by MAPK149 Publications
    Modified residuei745 – 7451Phosphoserine; by IKKEBy similarity

    Post-translational modificationi

    Phosphorylated on tyrosine and serine residues in response to a variety of cytokines/growth hormones including IFN-alpha, IFN-gamma, PDGF and EGF. Activated KIT promotes phosphorylation on tyrosine residues and subsequent translocation to the nucleus. Upon EGF stimulation, phosphorylation on Tyr-701 (lacking in beta form) by JAK1, JAK2 or TYK2 promotes dimerization and subsequent translocation to the nucleus. Growth hormone (GH) activates STAT1 signaling only via JAK2. Tyrosine phosphorylated in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4. Phosphorylation on Ser-727 by several kinases including MAPK14, ERK1/2 and CAMKII on IFN-gamma stimulation, regulates STAT1 transcriptional activity. Phosphorylation on Ser-727 promotes sumoylation though increasing interaction with PIAS. Phosphorylation on Ser-727 by PRKCD induces apoptosis in response to DNA-damaging agents. Phosphorylated on tyrosine residues when PTK2/FAK1 is activated; most likely this is catalyzed by a SRC family kinase. Dephosphorylation on tyrosine residues by PTPN2 negatively regulates interferon-mediated signaling. Upon viral infection or IFN induction, phosphorylation on Ser-708 occurs much later than phosphorylation on Tyr-701 and is required for the binding of ISGF3 on the ISREs of a subset of IFN-stimulated genes IKBKE-dependent. Phosphorylation at Tyr-701 and Ser-708 are mutually exclusive, phosphorylation at Ser-708 requires previous dephosphorylation of Tyr-701.12 Publications
    Sumoylated with SUMO1, SUMO2 and SUMO3. Sumoylation is enhanced by IFN-gamma-induced phosphorylation on Ser-727, and by interaction with PIAS proteins. Enhances the transactivation activity.9 Publications
    ISGylated.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP42224.
    PaxDbiP42224.
    PeptideAtlasiP42224.
    PRIDEiP42224.

    PTM databases

    PhosphoSiteiP42224.

    Miscellaneous databases

    PMAP-CutDBP42224.

    Expressioni

    Gene expression databases

    ArrayExpressiP42224.
    BgeeiP42224.
    CleanExiHS_STAT1.
    GenevestigatoriP42224.

    Organism-specific databases

    HPAiCAB004049.
    HPA000931.
    HPA000982.

    Interactioni

    Subunit structurei

    Isoform alpha homodimerizes upon IFN-gamma induced phosphorylation. Heterodimer with STAT2 upon IFN-alpha/beta induced phosphorylation. The heterodimer STAT1:STAT2 forms the interferon-stimulated gene factor 3 complex (ISGF3) with IRF9. Interacts (phosphorylated at Ser 727) with PIAS1 (dimethylated on arginine); the interaction results in release of STAT1 from its target gene. Interacts with IFNAR1; the interaction requires the phosphorylation of IFNAR1 at 'Tyr-466'. Interacts with IFNAR2, NMI, PTK2/FAK1 and SRC. Interacts with ERBB4 (phosphorylated). Interacts with Sendai virus C', C, Y1 and Y2 proteins, Nipah virus P, V and W proteins, and rabies virus phosphoprotein preventing activation of ISRE and GAS promoter. Interacts with HCV core protein; the interaction results in STAT1 degradation.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-1057697,EBI-1057697
    P03255-12EBI-1057697,EBI-6692439From a different organism.
    P03255-22EBI-1057697,EBI-6859460From a different organism.
    P266645EBI-1057697,EBI-6941357From a different organism.
    P279582EBI-1057697,EBI-6377335From a different organism.
    DDB1Q165312EBI-1057697,EBI-350322
    DDX58O957864EBI-1057697,EBI-995350
    E2F1Q010942EBI-1057697,EBI-448924
    ERBB2P046263EBI-1057697,EBI-641062
    H1LP072393EBI-1057697,EBI-7789600From a different organism.
    IFNGR1P152605EBI-1057697,EBI-1030755
    MAVSQ7Z4343EBI-1057697,EBI-995373
    RXRAP197932EBI-1057697,EBI-78598
    STAT2P5263014EBI-1057697,EBI-1546963
    STAT3P407633EBI-1057697,EBI-518675

    Protein-protein interaction databases

    BioGridi112649. 130 interactions.
    DIPiDIP-218N.
    IntActiP42224. 58 interactions.
    MINTiMINT-120840.
    STRINGi9606.ENSP00000354394.

    Structurei

    Secondary structure

    1
    750
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 75
    Turni12 – 143
    Helixi15 – 195
    Helixi28 – 336
    Helixi35 – 406
    Helixi43 – 464
    Helixi50 – 7425
    Helixi77 – 9418
    Helixi98 – 11720
    Helixi121 – 1255
    Helixi137 – 17943
    Helixi189 – 1924
    Helixi193 – 1953
    Helixi198 – 24750
    Helixi257 – 28630
    Helixi293 – 31624
    Beta strandi317 – 3215
    Beta strandi334 – 3363
    Beta strandi339 – 3479
    Helixi352 – 3543
    Turni355 – 3573
    Beta strandi359 – 3657
    Helixi370 – 3734
    Beta strandi374 – 3763
    Beta strandi380 – 3823
    Beta strandi386 – 3894
    Beta strandi391 – 3955
    Turni396 – 3983
    Beta strandi399 – 40810
    Beta strandi421 – 4255
    Beta strandi433 – 4419
    Beta strandi444 – 4518
    Beta strandi455 – 4606
    Helixi461 – 4633
    Helixi464 – 47714
    Helixi486 – 4883
    Helixi495 – 50915
    Helixi516 – 52611
    Helixi539 – 5435
    Beta strandi550 – 5523
    Helixi554 – 56815
    Helixi570 – 5745
    Helixi584 – 5907
    Turni591 – 5933
    Beta strandi601 – 6033
    Beta strandi612 – 6165
    Beta strandi621 – 6244
    Beta strandi627 – 6315
    Helixi636 – 6405
    Helixi644 – 6496
    Beta strandi657 – 6593
    Helixi673 – 6775
    Turni678 – 6803
    Helixi728 – 73811
    Turni739 – 7424
    Helixi743 – 7453
    Turni746 – 7483

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BF5X-ray2.90A136-710[»]
    1YVLX-ray3.00A/B1-683[»]
    2KA6NMR-B710-750[»]
    ProteinModelPortaliP42224.
    SMRiP42224. Positions 2-750.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP42224.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini573 – 67098SH2PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili136 – 3171821 PublicationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the transcription factor STAT family.Curated
    Contains 1 SH2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, SH2 domain

    Phylogenomic databases

    eggNOGiNOG310130.
    HOVERGENiHBG055669.
    InParanoidiP42224.
    KOiK11220.
    OMAiKNKQVLW.
    OrthoDBiEOG73JKTT.
    PhylomeDBiP42224.
    TreeFamiTF318648.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    1.10.532.10. 1 hit.
    1.20.1050.20. 1 hit.
    2.60.40.630. 1 hit.
    3.30.505.10. 1 hit.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR008967. p53-like_TF_DNA-bd.
    IPR000980. SH2.
    IPR001217. STAT.
    IPR022752. STAT1_TAZ2-bd_C.
    IPR013800. STAT_TF_alpha.
    IPR015988. STAT_TF_coiled-coil.
    IPR013801. STAT_TF_DNA-bd.
    IPR012345. STAT_TF_DNA-bd_sub.
    IPR013799. STAT_TF_prot_interaction.
    [Graphical view]
    PANTHERiPTHR11801. PTHR11801. 1 hit.
    PfamiPF00017. SH2. 1 hit.
    PF12162. STAT1_TAZ2bind. 1 hit.
    PF01017. STAT_alpha. 1 hit.
    PF02864. STAT_bind. 1 hit.
    PF02865. STAT_int. 1 hit.
    [Graphical view]
    SMARTiSM00252. SH2. 1 hit.
    SM00964. STAT_int. 1 hit.
    [Graphical view]
    SUPFAMiSSF47655. SSF47655. 1 hit.
    SSF48092. SSF48092. 1 hit.
    SSF49417. SSF49417. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEiPS50001. SH2. 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 Alpha (identifier: P42224-1) [UniParc]FASTAAdd to Basket

    Also known as: p91

    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

    MSQWYELQQL DSKFLEQVHQ LYDDSFPMEI RQYLAQWLEK QDWEHAANDV    50
    SFATIRFHDL LSQLDDQYSR FSLENNFLLQ HNIRKSKRNL QDNFQEDPIQ 100
    MSMIIYSCLK EERKILENAQ RFNQAQSGNI QSTVMLDKQK ELDSKVRNVK 150
    DKVMCIEHEI KSLEDLQDEY DFKCKTLQNR EHETNGVAKS DQKQEQLLLK 200
    KMYLMLDNKR KEVVHKIIEL LNVTELTQNA LINDELVEWK RRQQSACIGG 250
    PPNACLDQLQ NWFTIVAESL QQVRQQLKKL EELEQKYTYE HDPITKNKQV 300
    LWDRTFSLFQ QLIQSSFVVE RQPCMPTHPQ RPLVLKTGVQ FTVKLRLLVK 350
    LQELNYNLKV KVLFDKDVNE RNTVKGFRKF NILGTHTKVM NMEESTNGSL 400
    AAEFRHLQLK EQKNAGTRTN EGPLIVTEEL HSLSFETQLC QPGLVIDLET 450
    TSLPVVVISN VSQLPSGWAS ILWYNMLVAE PRNLSFFLTP PCARWAQLSE 500
    VLSWQFSSVT KRGLNVDQLN MLGEKLLGPN ASPDGLIPWT RFCKENINDK 550
    NFPFWLWIES ILELIKKHLL PLWNDGCIMG FISKERERAL LKDQQPGTFL 600
    LRFSESSREG AITFTWVERS QNGGEPDFHA VEPYTKKELS AVTFPDIIRN 650
    YKVMAAENIP ENPLKYLYPN IDKDHAFGKY YSRPKEAPEP MELDGPKGTG 700
    YIKTELISVS EVHPSRLQTT DNLLPMSPEE FDEVSRIVGS VEFDSMMNTV 750
    Length:750
    Mass (Da):87,335
    Last modified:November 1, 1997 - v2
    Checksum:i054A813522364BA6
    GO
    Isoform Beta (identifier: P42224-2) [UniParc]FASTAAdd to Basket

    Also known as: p84

    The sequence of this isoform differs from the canonical sequence as follows:
         713-750: Missing.

    Show »
    Length:712
    Mass (Da):83,043
    Checksum:i31408601223700BB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti46 – 461A → T in ADA59516. 1 PublicationCurated
    Sequence conflicti307 – 3071S → G in BAF85293. (PubMed:14702039)Curated
    Sequence conflicti718 – 7181Q → R in CAH18430. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti30 – 301I → T.
    Corresponds to variant rs34255470 [ dbSNP | Ensembl ].
    VAR_034521
    Natural varianti165 – 1651D → G in CANDF7; gain of function mutation associated with increased STAT1 phosphorylation due to impaired nuclear dephosphorylation. 1 Publication
    VAR_065934
    Natural varianti165 – 1651D → H in CANDF7. 1 Publication
    VAR_065935
    Natural varianti170 – 1701Y → N in CANDF7. 1 Publication
    VAR_065936
    Natural varianti174 – 1741C → R in CANDF7. 1 Publication
    VAR_065937
    Natural varianti201 – 2011K → N in STAT1D; not deleterious in terms of most STAT1 functions; causes abnormal splicing out of exon 8 from most mRNAs thereby decreasing protein levels by approximately 70%. 1 Publication
    VAR_065815
    Natural varianti202 – 2021M → I in CANDF7. 1 Publication
    VAR_065938
    Natural varianti202 – 2021M → V in CANDF7. 1 Publication
    VAR_065939
    Natural varianti267 – 2671A → V in CANDF7. 2 Publications
    VAR_065940
    Natural varianti271 – 2711Q → P in CANDF7. 1 Publication
    VAR_065941
    Natural varianti274 – 2741R → Q in CANDF7; gain of function mutation associated with increased STAT1 phosphorylation due to impaired nuclear dephosphorylation. 1 Publication
    VAR_065942
    Natural varianti274 – 2741R → W in CANDF7. 2 Publications
    VAR_065943
    Natural varianti286 – 2861K → I in CANDF7. 1 Publication
    VAR_065944
    Natural varianti288 – 2881T → A in CANDF7. 1 Publication
    VAR_065945
    Natural varianti320 – 3201E → Q in MSMD; affects the DNA-binding activity of the protein. 1 Publication
    VAR_065816
    Natural varianti463 – 4631Q → H in MSMD; affects the DNA-binding activity of the protein. 1 Publication
    VAR_065817
    Natural varianti491 – 4911P → A in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036001
    Natural varianti600 – 6001L → P in STAT1D; found in an infant who died of a viral-like illness associated with complete STAT1 deficiency. 1 Publication
    VAR_018265
    Natural varianti637 – 6371K → E in MSMD; affects both phosphorylation and DNA-binding activity; results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27. 1 Publication
    VAR_068713
    Natural varianti673 – 6731K → R in MSMD; impairs tyrosine phosphorylation; results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27. 1 Publication
    VAR_068714
    Natural varianti706 – 7061L → S in MSMD; loss of GAF and ISGF3 activation; impairs the nuclear accumulation of GAF but not of ISGF3 in heterozygous cells stimulated by IFNs; affects phosphorylation of the protein. 1 Publication
    VAR_018266

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei713 – 75038Missing in isoform Beta. 2 PublicationsVSP_006282Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M97935 mRNA. Translation: AAB64012.1.
    M97936 mRNA. No translation available.
    GU211347 mRNA. Translation: ADA59516.1.
    AY865620 Genomic DNA. Translation: AAW56072.1.
    AK292604 mRNA. Translation: BAF85293.1.
    AK315002 mRNA. Translation: BAG37497.1.
    CR749636 mRNA. Translation: CAH18430.1.
    BT007241 mRNA. Translation: AAP35905.1.
    AC067945 Genomic DNA. Translation: AAY24183.1.
    CH471058 Genomic DNA. Translation: EAX10850.1.
    CH471058 Genomic DNA. Translation: EAX10851.1.
    CH471058 Genomic DNA. Translation: EAX10852.1.
    CH471058 Genomic DNA. Translation: EAX10855.1.
    BC002704 mRNA. Translation: AAH02704.1.
    U18662 Genomic DNA. No translation available.
    U18663 Genomic DNA. No translation available.
    U18664 Genomic DNA. No translation available.
    U18665 Genomic DNA. No translation available.
    U18666 Genomic DNA. No translation available.
    U18667 Genomic DNA. No translation available.
    U18668 Genomic DNA. No translation available.
    U18669 Genomic DNA. No translation available.
    U18670 Genomic DNA. No translation available.
    CCDSiCCDS2309.1. [P42224-1]
    CCDS42793.1. [P42224-2]
    PIRiA46159.
    RefSeqiNP_009330.1. NM_007315.3. [P42224-1]
    NP_644671.1. NM_139266.2. [P42224-2]
    XP_006712781.1. XM_006712718.1. [P42224-1]
    UniGeneiHs.642990.
    Hs.743244.

    Genome annotation databases

    EnsembliENST00000361099; ENSP00000354394; ENSG00000115415. [P42224-1]
    ENST00000392322; ENSP00000376136; ENSG00000115415. [P42224-2]
    ENST00000409465; ENSP00000386244; ENSG00000115415. [P42224-1]
    GeneIDi6772.
    KEGGihsa:6772.
    UCSCiuc002usj.2. human. [P42224-1]

    Polymorphism databases

    DMDMi2507413.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    STAT1base

    STAT1 mutation db

    Wikipedia

    STAT1 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M97935 mRNA. Translation: AAB64012.1 .
    M97936 mRNA. No translation available.
    GU211347 mRNA. Translation: ADA59516.1 .
    AY865620 Genomic DNA. Translation: AAW56072.1 .
    AK292604 mRNA. Translation: BAF85293.1 .
    AK315002 mRNA. Translation: BAG37497.1 .
    CR749636 mRNA. Translation: CAH18430.1 .
    BT007241 mRNA. Translation: AAP35905.1 .
    AC067945 Genomic DNA. Translation: AAY24183.1 .
    CH471058 Genomic DNA. Translation: EAX10850.1 .
    CH471058 Genomic DNA. Translation: EAX10851.1 .
    CH471058 Genomic DNA. Translation: EAX10852.1 .
    CH471058 Genomic DNA. Translation: EAX10855.1 .
    BC002704 mRNA. Translation: AAH02704.1 .
    U18662 Genomic DNA. No translation available.
    U18663 Genomic DNA. No translation available.
    U18664 Genomic DNA. No translation available.
    U18665 Genomic DNA. No translation available.
    U18666 Genomic DNA. No translation available.
    U18667 Genomic DNA. No translation available.
    U18668 Genomic DNA. No translation available.
    U18669 Genomic DNA. No translation available.
    U18670 Genomic DNA. No translation available.
    CCDSi CCDS2309.1. [P42224-1 ]
    CCDS42793.1. [P42224-2 ]
    PIRi A46159.
    RefSeqi NP_009330.1. NM_007315.3. [P42224-1 ]
    NP_644671.1. NM_139266.2. [P42224-2 ]
    XP_006712781.1. XM_006712718.1. [P42224-1 ]
    UniGenei Hs.642990.
    Hs.743244.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BF5 X-ray 2.90 A 136-710 [» ]
    1YVL X-ray 3.00 A/B 1-683 [» ]
    2KA6 NMR - B 710-750 [» ]
    ProteinModelPortali P42224.
    SMRi P42224. Positions 2-750.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112649. 130 interactions.
    DIPi DIP-218N.
    IntActi P42224. 58 interactions.
    MINTi MINT-120840.
    STRINGi 9606.ENSP00000354394.

    Chemistry

    BindingDBi P42224.
    ChEMBLi CHEMBL6101.
    DrugBanki DB01073. Fludarabine.

    PTM databases

    PhosphoSitei P42224.

    Polymorphism databases

    DMDMi 2507413.

    Proteomic databases

    MaxQBi P42224.
    PaxDbi P42224.
    PeptideAtlasi P42224.
    PRIDEi P42224.

    Protocols and materials databases

    DNASUi 6772.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361099 ; ENSP00000354394 ; ENSG00000115415 . [P42224-1 ]
    ENST00000392322 ; ENSP00000376136 ; ENSG00000115415 . [P42224-2 ]
    ENST00000409465 ; ENSP00000386244 ; ENSG00000115415 . [P42224-1 ]
    GeneIDi 6772.
    KEGGi hsa:6772.
    UCSCi uc002usj.2. human. [P42224-1 ]

    Organism-specific databases

    CTDi 6772.
    GeneCardsi GC02M191829.
    HGNCi HGNC:11362. STAT1.
    HPAi CAB004049.
    HPA000931.
    HPA000982.
    MIMi 209950. phenotype.
    600555. gene.
    613796. phenotype.
    614162. phenotype.
    neXtProti NX_P42224.
    Orphaneti 391487. Autoimmune enteropathy and endocrinopathy-susceptibility to chronic infections syndrome.
    1334. Chronic mucocutaneous candidiasis.
    319595. Mendelian susceptibility to mycobacterial diseases due to partial STAT1 deficiency.
    391311. Susceptibility to viral and mycobacterial infections.
    PharmGKBi PA36183.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG310130.
    HOVERGENi HBG055669.
    InParanoidi P42224.
    KOi K11220.
    OMAi KNKQVLW.
    OrthoDBi EOG73JKTT.
    PhylomeDBi P42224.
    TreeFami TF318648.

    Enzyme and pathway databases

    Reactomei REACT_111040. Signaling by SCF-KIT.
    REACT_111133. Growth hormone receptor signaling.
    REACT_115831. ISG15 antiviral mechanism.
    REACT_121141. Signaling by FGFR1 fusion mutants.
    REACT_17025. Downstream signal transduction.
    REACT_24980. Regulation of IFNG signaling.
    REACT_25078. Interferon gamma signaling.
    REACT_25162. Interferon alpha/beta signaling.
    REACT_25216. Regulation of IFNA signaling.
    REACT_27307. Interleukin-6 signaling.
    SignaLinki P42224.

    Miscellaneous databases

    ChiTaRSi STAT1. human.
    EvolutionaryTracei P42224.
    GeneWikii STAT1.
    GenomeRNAii 6772.
    NextBioi 26428.
    PMAP-CutDB P42224.
    PROi P42224.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P42224.
    Bgeei P42224.
    CleanExi HS_STAT1.
    Genevestigatori P42224.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    1.10.532.10. 1 hit.
    1.20.1050.20. 1 hit.
    2.60.40.630. 1 hit.
    3.30.505.10. 1 hit.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR008967. p53-like_TF_DNA-bd.
    IPR000980. SH2.
    IPR001217. STAT.
    IPR022752. STAT1_TAZ2-bd_C.
    IPR013800. STAT_TF_alpha.
    IPR015988. STAT_TF_coiled-coil.
    IPR013801. STAT_TF_DNA-bd.
    IPR012345. STAT_TF_DNA-bd_sub.
    IPR013799. STAT_TF_prot_interaction.
    [Graphical view ]
    PANTHERi PTHR11801. PTHR11801. 1 hit.
    Pfami PF00017. SH2. 1 hit.
    PF12162. STAT1_TAZ2bind. 1 hit.
    PF01017. STAT_alpha. 1 hit.
    PF02864. STAT_bind. 1 hit.
    PF02865. STAT_int. 1 hit.
    [Graphical view ]
    SMARTi SM00252. SH2. 1 hit.
    SM00964. STAT_int. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47655. SSF47655. 1 hit.
    SSF48092. SSF48092. 1 hit.
    SSF49417. SSF49417. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEi PS50001. SH2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Proteins of transcription factor ISGF-3: one gene encodes the 91- and 84-kDa ISGF-3 proteins that are activated by interferon alpha."
      Schindler C., Fu X.-Y., Improta T., Aebersold R., Darnell J.E. Jr.
      Proc. Natl. Acad. Sci. U.S.A. 89:7836-7839(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), PROTEIN SEQUENCE OF 514-524; 654-660 AND 667-672.
    2. "Novel STAT1 alleles in a patient with impaired resistance to mycobacteria."
      Kristensen I., Veirum J.E., Moeller B.K., Christiansen M.
      Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
    3. NIEHS SNPs program
      Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "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 ALPHA).
      Tissue: Placenta and Testis.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
    6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
    7. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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 BETA).
      Tissue: Brain.
    10. "The genomic structure of the STAT genes: multiple exons in coincident sites in Stat1 and Stat2."
      Yan R., Qureshi S., Zhong Z., Wen Z., Darnell J.E. Jr.
      Nucleic Acids Res. 23:459-463(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    11. "A transcription factor with SH2 and SH3 domains is directly activated by an interferon alpha-induced cytoplasmic protein tyrosine kinase(s)."
      Fu X.Y.
      Cell 70:323-335(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION IN RESPONSE TO IFN-ALPHA.
    12. "Maximal activation of transcription by Stat1 and Stat3 requires both tyrosine and serine phosphorylation."
      Wen Z., Zhong Z., Darnell J.E. Jr.
      Cell 82:241-250(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-727, MUTAGENESIS.
    13. "Phosphorylation and activation of the DNA binding activity of purified Stat1 by the Janus protein-tyrosine kinases and the epidermal growth factor receptor."
      Quelle F.W., Thierfelder W., Witthuhn B.A., Tang B., Cohen S., Ihle J.N.
      J. Biol. Chem. 270:20775-20780(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-701.
    14. "The SH2 domains of Stat1 and Stat2 mediate multiple interactions in the transduction of IFN-alpha signals."
      Gupta S., Yan H., Wong L.H., Ralph S., Krolewski J., Schindler C.
      EMBO J. 15:1075-1084(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: TYROSINE PHOSPHORYLATION, HETERODIMERIZATION, DNA-BINDING, MUTAGENESIS.
    15. "Functional subdomains of STAT2 required for preassociation with the alpha interferon receptor and for signaling."
      Li X., Leung S., Kerr I.M., Stark G.R.
      Mol. Cell. Biol. 17:2048-2056(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IFNAR1 AND IFNAR2, PHOSPHORYLATION.
    16. Cited for: INTERACTION WITH PIAS1, FUNCTION.
      Tissue: B-cell.
    17. "Viral inhibition of interferon signal transduction."
      Cebulla C.M., Miller D.M., Sedmak D.D.
      Intervirology 42:325-330(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    18. "Sendai virus C protein physically associates with Stat1."
      Takeuchi K., Komatsu T., Yokoo J., Kato A., Shioda T., Nagai Y., Gotoh B.
      Genes Cells 6:545-557(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SENDAI VIRUS C PROTEIN.
    19. "Focal adhesion kinase activates Stat1 in integrin-mediated cell migration and adhesion."
      Xie B., Zhao J., Kitagawa M., Durbin J., Madri J.A., Guan J.L., Fu X.Y.
      J. Biol. Chem. 276:19512-19523(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTK2/FAK1, PHOSPHORYLATION.
    20. Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPN2.
    21. Cited for: SUMOYLATION AT LYS-703, FUNCTION, MUTAGENESIS OF LYS-703.
    22. "SUMO modification of STAT1 and its role in PIAS-mediated inhibition of gene activation."
      Rogers R.S., Horvath C.M., Matunis M.J.
      J. Biol. Chem. 278:30091-30097(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-703, FUNCTION, MUTAGENESIS OF LYS-110 AND LYS-703.
    23. "Signal transduction via the stem cell factor receptor/c-Kit."
      Ronnstrand L.
      Cell. Mol. Life Sci. 61:2535-2548(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON ROLE IN KIT SIGNALING.
    24. "Protein kinase Cdelta regulates apoptosis via activation of STAT1."
      DeVries T.A., Kalkofen R.L., Matassa A.A., Reyland M.E.
      J. Biol. Chem. 279:45603-45612(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-727, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-727.
    25. Cited for: ISGYLATION.
    26. "Hepatitis C virus expression suppresses interferon signaling by degrading STAT1."
      Lin W., Choe W.H., Hiasa Y., Kamegaya Y., Blackard J.T., Schmidt E.V., Chung R.T.
      Gastroenterology 128:1034-1041(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HEPATITIS C VIRUS CORE PROTEIN.
    27. "Sustained phosphorylation of mutated FGFR3 is a crucial feature of genetic dwarfism and induces apoptosis in the ATDC5 chondrogenic cell line via PLCgamma-activated STAT1."
      Harada D., Yamanaka Y., Ueda K., Nishimura R., Morishima T., Seino Y., Tanaka H.
      Bone 41:273-281(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION IN RESPONSE TO ACTIVATED FGFR3, PHOSPHORYLATION AT TYR-701.
    28. "Fibroblast growth factor receptor-induced phosphorylation of STAT1 at the Golgi apparatus without translocation to the nucleus."
      Citores L., Bai L., Sorensen V., Olsnes S.
      J. Cell. Physiol. 212:148-156(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION IN RESPONSE TO ACTIVATED FGFR1; FGFR2; FGFR3 AND FGFR4.
    29. "MAPK-induced Ser727 phosphorylation promotes SUMOylation of STAT1."
      Vanhatupa S., Ungureanu D., Paakkunainen M., Silvennoinen O.
      Biochem. J. 409:179-185(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-727, INTERACTION WITH PIAS1, SUMOYLATION, MUTAGENESIS OF TYR-701 AND SER-727.
    30. "System-wide investigation of ErbB4 reveals 19 sites of Tyr phosphorylation that are unusually selective in their recruitment properties."
      Kaushansky A., Gordus A., Budnik B.A., Lane W.S., Rush J., MacBeath G.
      Chem. Biol. 15:808-817(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ERBB4.
    31. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    32. "Analysis of STAT1 activation by six FGFR3 mutants associated with skeletal dysplasia undermines dominant role of STAT1 in FGFR3 signaling in cartilage."
      Krejci P., Salazar L., Kashiwada T.A., Chlebova K., Salasova A., Thompson L.M., Bryja V., Kozubik A., Wilcox W.R.
      PLoS ONE 3:E3961-E3961(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT TYR-701 IN RESPONSE TO CONSTITUTIVELY ACTIVATED FGFR3.
    33. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    34. "PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling."
      Weber S., Maass F., Schuemann M., Krause E., Suske G., Bauer U.M.
      Genes Dev. 23:118-132(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIAS1.
    35. "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-727, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    36. "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-727, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    37. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    38. "Mechanisms of STAT protein activation by oncogenic KIT mutants in neoplastic mast cells."
      Chaix A., Lopez S., Voisset E., Gros L., Dubreuil P., De Sepulveda P.
      J. Biol. Chem. 286:5956-5966(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-701 IN RESPONSE TO KIT SIGNALING, PHOSPHORYLATION AT SER-727.
    39. "Inhibitor of kappaB kinase epsilon (IKK(epsilon)), STAT1, and IFIT2 proteins define novel innate immune effector pathway against West Nile virus infection."
      Perwitasari O., Cho H., Diamond M.S., Gale M. Jr.
      J. Biol. Chem. 286:44412-44423(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-701; SER-708 AND SER-727, MUTAGENESIS OF TYR-701; SER-708 AND SER-727.
    40. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    41. "Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA."
      Chen X., Vinkemeier U., Zhao Y., Jeruzalmi D., Darnell J.E. Jr., Kuriyan J.
      Cell 93:827-839(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 136-710, COILED-COIL.
    42. "Impairment of mycobacterial but not viral immunity by a germline human STAT1 mutation."
      Dupuis S., Dargemont C., Fieschi C., Thomassin N., Rosenzweig S., Harris J., Holland S.M., Schreiber R.D., Casanova J.-L.
      Science 293:300-303(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MSMD SER-706.
    43. Cited for: VARIANT STAT1D PRO-600.
    44. "Nipah virus V and W proteins have a common STAT1-binding domain yet inhibit STAT1 activation from the cytoplasmic and nuclear compartments, respectively."
      Shaw M.L., Garcia-Sastre A., Palese P., Basler C.F.
      J. Virol. 78:5633-5641(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NIPAH V AND W PROTEINS.
    45. Cited for: VARIANTS MSMD GLN-320 AND HIS-463, CHARACTERIZATION OF VARIANTS GLN-320; HIS-463 AND SER-706.
    46. Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-491.
    47. Cited for: VARIANT STAT1D ASN-201, CHARACTERIZATION OF VARIANT STAT1D ASN-201.
    48. "Gain-of-function human STAT1 mutations impair IL-17 immunity and underlie chronic mucocutaneous candidiasis."
      Liu L., Okada S., Kong X.F., Kreins A.Y., Cypowyj S., Abhyankar A., Toubiana J., Itan Y., Audry M., Nitschke P., Masson C., Toth B., Flatot J., Migaud M., Chrabieh M., Kochetkov T., Bolze A., Borghesi A.
      , Toulon A., Hiller J., Eyerich S., Eyerich K., Gulacsy V., Chernyshova L., Chernyshov V., Bondarenko A., Maria Cortes Grimaldo R., Blancas-Galicia L., Madrigal Beas I.M., Roesler J., Magdorf K., Engelhard D., Thumerelle C., Burgel P.R., Hoernes M., Drexel B., Seger R., Kusuma T., Jansson A.F., Sawalle-Belohradsky J., Belohradsky B., Jouanguy E., Bustamante J., Bue M., Karin N., Wildbaum G., Bodemer C., Lortholary O., Fischer A., Blanche S., Al-Muhsen S., Reichenbach J., Kobayashi M., Rosales F.E., Lozano C.T., Kilic S.S., Oleastro M., Etzioni A., Traidl-Hoffmann C., Renner E.D., Abel L., Picard C., Marodi L., Boisson-Dupuis S., Puel A., Casanova J.L.
      J. Exp. Med. 208:1635-1648(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CANDF7 GLY-165; HIS-165; ASN-170; ARG-174; ILE-202; VAL-202; VAL-267; PRO-271; GLN-274; TRP-274; ILE-286 AND ALA-288, CHARACTERIZATION OF VARIANTS CANDF7 GLY-165 AND GLN-274.
    49. Cited for: VARIANTS CANDF7 VAL-267 AND TRP-274.
    50. Cited for: VARIANTS MSMD GLU-637 AND ARG-673, CHARACTERIZATION OF VARIANTS MSMD GLU-637 AND ARG-673.

    Entry informationi

    Entry nameiSTAT1_HUMAN
    AccessioniPrimary (citable) accession number: P42224
    Secondary accession number(s): A8K989
    , B2RCA0, D2KFR8, D3DPI7, Q53S88, Q53XW4, Q68D00, Q9UDL5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 179 of the entry and version 2 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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