Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P42229

- STA5A_HUMAN

UniProt

P42229 - STA5A_HUMAN

Protein

Signal transducer and activator of transcription 5A

Gene

STAT5A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Carries out a dual function: signal transduction and activation of transcription. Mediates cellular responses to the cytokine KITLG/SCF and other growth factors. Mediates cellular responses to ERBB4. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the GAS element and activates PRL-induced transcription. Regulates the expression of milk proteins during lactation.2 Publications

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. protein binding Source: UniProtKB
    3. RNA polymerase II core promoter sequence-specific DNA binding Source: Ensembl
    4. sequence-specific DNA binding transcription factor activity Source: ProtInc
    5. signal transducer activity Source: Ensembl

    GO - Biological processi

    1. 2-oxoglutarate metabolic process Source: BHF-UCL
    2. allantoin metabolic process Source: BHF-UCL
    3. citrate metabolic process Source: BHF-UCL
    4. creatine metabolic process Source: BHF-UCL
    5. creatinine metabolic process Source: BHF-UCL
    6. development of secondary female sexual characteristics Source: Ensembl
    7. development of secondary male sexual characteristics Source: Ensembl
    8. epithelial cell differentiation involved in prostate gland development Source: Ensembl
    9. fatty acid metabolic process Source: BHF-UCL
    10. female pregnancy Source: Ensembl
    11. isoleucine metabolic process Source: BHF-UCL
    12. JAK-STAT cascade Source: ProtInc
    13. JAK-STAT cascade involved in growth hormone signaling pathway Source: Reactome
    14. lactation Source: UniProtKB-KW
    15. lipid storage Source: Ensembl
    16. luteinization Source: Ensembl
    17. mammary gland epithelium development Source: Ensembl
    18. natural killer cell differentiation Source: Ensembl
    19. negative regulation of erythrocyte differentiation Source: Ensembl
    20. negative regulation of mast cell apoptotic process Source: Ensembl
    21. oxaloacetate metabolic process Source: BHF-UCL
    22. peptidyl-tyrosine phosphorylation Source: Ensembl
    23. Peyer's patch development Source: Ensembl
    24. positive regulation of activated T cell proliferation Source: Ensembl
    25. positive regulation of B cell differentiation Source: Ensembl
    26. positive regulation of gamma-delta T cell differentiation Source: Ensembl
    27. positive regulation of inflammatory response Source: Ensembl
    28. positive regulation of interleukin-2 biosynthetic process Source: Ensembl
    29. positive regulation of mast cell differentiation Source: Ensembl
    30. positive regulation of mast cell proliferation Source: Ensembl
    31. positive regulation of mitotic cell cycle Source: Ensembl
    32. positive regulation of multicellular organism growth Source: Ensembl
    33. positive regulation of natural killer cell differentiation Source: Ensembl
    34. positive regulation of natural killer cell mediated cytotoxicity Source: Ensembl
    35. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    36. prolactin signaling pathway Source: UniProtKB
    37. prostate gland epithelium morphogenesis Source: Ensembl
    38. regulation of cell adhesion Source: Ensembl
    39. regulation of epithelial cell differentiation Source: Ensembl
    40. regulation of multicellular organism growth Source: BHF-UCL
    41. regulation of steroid metabolic process Source: Ensembl
    42. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    43. succinate metabolic process Source: BHF-UCL
    44. taurine metabolic process Source: BHF-UCL
    45. T cell differentiation in thymus Source: Ensembl
    46. T cell homeostasis Source: Ensembl
    47. transcription, DNA-templated Source: UniProtKB-KW
    48. valine metabolic process Source: BHF-UCL

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Lactation, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_111040. Signaling by SCF-KIT.
    REACT_111133. Growth hormone receptor signaling.
    REACT_115529. Interleukin-7 signaling.
    REACT_115697. Prolactin receptor signaling.
    REACT_116022. Nuclear signaling by ERBB4.
    REACT_121141. Signaling by FGFR1 fusion mutants.
    REACT_169118. Signaling by Leptin.
    REACT_17025. Downstream signal transduction.
    REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_27283. Interleukin-2 signaling.
    SignaLinkiP42229.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Signal transducer and activator of transcription 5A
    Gene namesi
    Name:STAT5A
    Synonyms:STAT5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:11366. STAT5A.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Translocated into the nucleus in response to phosphorylation.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA338.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 794794Signal transducer and activator of transcription 5APRO_0000182423Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei128 – 1281PhosphoserineBy similarity
    Modified residuei193 – 1931Phosphoserine1 Publication
    Modified residuei694 – 6941Phosphotyrosine; by JAK22 Publications

    Post-translational modificationi

    Tyrosine phosphorylated in response to KITLG/SCF, IL2, IL3, IL7, IL15, CSF2/GMCSF, GH1, PRL, EPO and THPO. Activated KIT promotes phosphorylation on tyrosine residues and subsequent translocation to the nucleus. Tyrosine phosphorylated in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4. Tyrosine phosphorylation is required for DNA-binding activity and dimerization. Serine phosphorylation is also required for maximal transcriptional activity By similarity. Tyrosine phosphorylated in response to signaling via activated FLT3; wild-type FLT3 results in much weaker phosphorylation than constitutively activated mutant FLT3. Alternatively, can be phosphorylated by JAK2 at Tyr-694. Dephosphorylation on tyrosine residues by PTPN2 negatively regulates prolactin signaling pathway.By similarity5 Publications
    ISGylated.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP42229.
    PaxDbiP42229.
    PeptideAtlasiP42229.
    PRIDEiP42229.

    PTM databases

    PhosphoSiteiP42229.

    Expressioni

    Gene expression databases

    ArrayExpressiP42229.
    BgeeiP42229.
    CleanExiHS_STAT5A.
    GenevestigatoriP42229.

    Organism-specific databases

    HPAiCAB003860.
    HPA027873.

    Interactioni

    Subunit structurei

    Forms a homodimer or a heterodimer with a related family member. Binds NR3C1 By similarity. Interacts with NCOA1 and SOCS7. Interacts with ERBB4.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AGAP2Q99490-23EBI-749537,EBI-7737644
    PTPN1P180312EBI-749537,EBI-968788

    Protein-protein interaction databases

    BioGridi112653. 55 interactions.
    DIPiDIP-396N.
    IntActiP42229. 33 interactions.
    MINTiMINT-223002.
    STRINGi9606.ENSP00000341208.

    Structurei

    3D structure databases

    ProteinModelPortaliP42229.
    SMRiP42229. Positions 138-690.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini589 – 68698SH2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    SH2 domain

    Phylogenomic databases

    eggNOGiNOG245085.
    HOGENOMiHOG000230988.
    HOVERGENiHBG107486.
    InParanoidiP42229.
    KOiK11223.
    OMAiPQNPDHV.
    OrthoDBiEOG73JKTT.
    PhylomeDBiP42229.
    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.
    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.
    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.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P42229-1) [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

    MAGWIQAQQL QGDALRQMQV LYGQHFPIEV RHYLAQWIES QPWDAIDLDN    50
    PQDRAQATQL LEGLVQELQK KAEHQVGEDG FLLKIKLGHY ATQLQKTYDR 100
    CPLELVRCIR HILYNEQRLV REANNCSSPA GILVDAMSQK HLQINQTFEE 150
    LRLVTQDTEN ELKKLQQTQE YFIIQYQESL RIQAQFAQLA QLSPQERLSR 200
    ETALQQKQVS LEAWLQREAQ TLQQYRVELA EKHQKTLQLL RKQQTIILDD 250
    ELIQWKRRQQ LAGNGGPPEG SLDVLQSWCE KLAEIIWQNR QQIRRAEHLC 300
    QQLPIPGPVE EMLAEVNATI TDIISALVTS TFIIEKQPPQ VLKTQTKFAA 350
    TVRLLVGGKL NVHMNPPQVK ATIISEQQAK SLLKNENTRN ECSGEILNNC 400
    CVMEYHQATG TLSAHFRNMS LKRIKRADRR GAESVTEEKF TVLFESQFSV 450
    GSNELVFQVK TLSLPVVVIV HGSQDHNATA TVLWDNAFAE PGRVPFAVPD 500
    KVLWPQLCEA LNMKFKAEVQ SNRGLTKENL VFLAQKLFNN SSSHLEDYSG 550
    LSVSWSQFNR ENLPGWNYTF WQWFDGVMEV LKKHHKPHWN DGAILGFVNK 600
    QQAHDLLINK PDGTFLLRFS DSEIGGITIA WKFDSPERNL WNLKPFTTRD 650
    FSIRSLADRL GDLSYLIYVF PDRPKDEVFS KYYTPVLAKA VDGYVKPQIK 700
    QVVPEFVNAS ADAGGSSATY MDQAPSPAVC PQAPYNMYPQ NPDHVLDQDG 750
    EFDLDETMDV ARHVEELLRR PMDSLDSRLS PPAGLFTSAR GSLS 794
    Length:794
    Mass (Da):90,647
    Last modified:November 1, 1995 - v1
    Checksum:iC64237295F88CFBE
    GO
    Isoform 2 (identifier: P42229-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         96-125: Missing.

    Show »
    Length:764
    Mass (Da):86,949
    Checksum:i20FC15C3CDFA26FE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti88 – 881G → R in AAB06589. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti389 – 3891R → H.
    Corresponds to variant rs2230134 [ dbSNP | Ensembl ].
    VAR_052073

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei96 – 12530Missing in isoform 2. 2 PublicationsVSP_053332Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L41142 mRNA. Translation: AAA73962.1.
    U43185 mRNA. Translation: AAB06589.1.
    DQ471288 mRNA. Translation: ABF17939.1.
    AK301457 mRNA. Translation: BAH13486.1.
    AC087691 Genomic DNA. No translation available.
    AC099811 Genomic DNA. No translation available.
    BC027036 mRNA. Translation: AAH27036.1.
    CCDSiCCDS11424.1. [P42229-1]
    PIRiG02317.
    RefSeqiNP_001275647.1. NM_001288718.1. [P42229-1]
    NP_001275648.1. NM_001288719.1. [P42229-2]
    NP_001275649.1. NM_001288720.1.
    NP_003143.2. NM_003152.3. [P42229-1]
    UniGeneiHs.437058.

    Genome annotation databases

    EnsembliENST00000345506; ENSP00000341208; ENSG00000126561. [P42229-1]
    ENST00000546010; ENSP00000443107; ENSG00000126561. [P42229-2]
    ENST00000590949; ENSP00000468749; ENSG00000126561. [P42229-1]
    GeneIDi6776.
    KEGGihsa:6776.
    UCSCiuc002hzj.2. human. [P42229-1]

    Polymorphism databases

    DMDMi1174462.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    STAT5 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L41142 mRNA. Translation: AAA73962.1 .
    U43185 mRNA. Translation: AAB06589.1 .
    DQ471288 mRNA. Translation: ABF17939.1 .
    AK301457 mRNA. Translation: BAH13486.1 .
    AC087691 Genomic DNA. No translation available.
    AC099811 Genomic DNA. No translation available.
    BC027036 mRNA. Translation: AAH27036.1 .
    CCDSi CCDS11424.1. [P42229-1 ]
    PIRi G02317.
    RefSeqi NP_001275647.1. NM_001288718.1. [P42229-1 ]
    NP_001275648.1. NM_001288719.1. [P42229-2 ]
    NP_001275649.1. NM_001288720.1.
    NP_003143.2. NM_003152.3. [P42229-1 ]
    UniGenei Hs.437058.

    3D structure databases

    ProteinModelPortali P42229.
    SMRi P42229. Positions 138-690.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112653. 55 interactions.
    DIPi DIP-396N.
    IntActi P42229. 33 interactions.
    MINTi MINT-223002.
    STRINGi 9606.ENSP00000341208.

    Chemistry

    BindingDBi P42229.
    ChEMBLi CHEMBL5403.

    PTM databases

    PhosphoSitei P42229.

    Polymorphism databases

    DMDMi 1174462.

    Proteomic databases

    MaxQBi P42229.
    PaxDbi P42229.
    PeptideAtlasi P42229.
    PRIDEi P42229.

    Protocols and materials databases

    DNASUi 6776.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000345506 ; ENSP00000341208 ; ENSG00000126561 . [P42229-1 ]
    ENST00000546010 ; ENSP00000443107 ; ENSG00000126561 . [P42229-2 ]
    ENST00000590949 ; ENSP00000468749 ; ENSG00000126561 . [P42229-1 ]
    GeneIDi 6776.
    KEGGi hsa:6776.
    UCSCi uc002hzj.2. human. [P42229-1 ]

    Organism-specific databases

    CTDi 6776.
    GeneCardsi GC17P040439.
    HGNCi HGNC:11366. STAT5A.
    HPAi CAB003860.
    HPA027873.
    MIMi 601511. gene.
    neXtProti NX_P42229.
    PharmGKBi PA338.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG245085.
    HOGENOMi HOG000230988.
    HOVERGENi HBG107486.
    InParanoidi P42229.
    KOi K11223.
    OMAi PQNPDHV.
    OrthoDBi EOG73JKTT.
    PhylomeDBi P42229.
    TreeFami TF318648.

    Enzyme and pathway databases

    Reactomei REACT_111040. Signaling by SCF-KIT.
    REACT_111133. Growth hormone receptor signaling.
    REACT_115529. Interleukin-7 signaling.
    REACT_115697. Prolactin receptor signaling.
    REACT_116022. Nuclear signaling by ERBB4.
    REACT_121141. Signaling by FGFR1 fusion mutants.
    REACT_169118. Signaling by Leptin.
    REACT_17025. Downstream signal transduction.
    REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_27283. Interleukin-2 signaling.
    SignaLinki P42229.

    Miscellaneous databases

    ChiTaRSi STAT5A. human.
    GeneWikii STAT5A.
    GenomeRNAii 6776.
    NextBioi 26450.
    PROi P42229.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P42229.
    Bgeei P42229.
    CleanExi HS_STAT5A.
    Genevestigatori P42229.

    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.
    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.
    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. "Identification and purification of human Stat proteins activated in response to interleukin-2."
      Hou J., Schindler U., Henzel W.J., Wong S.C., McKnight S.L.
      Immunity 2:321-329(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Lin J.X., Mietz J., Modi W.S., John S., Leonard W.J.
      Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Cloning and characterization of a variant of human stat5a, missing a portion of the n-terminal region, with dominant negative effects on the growth of breast cancer cells and [beta]-casein gene expression."
      Tan D., Deng C., Luben R.A., Walker A.M.
      Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
    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 2).
      Tissue: Synovium.
    5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Cervix.
    7. "A nuclear protein tyrosine phosphatase TC-PTP is a potential negative regulator of the PRL-mediated signaling pathway: dephosphorylation and deactivation of signal transducer and activator of transcription 5a and 5b by TC-PTP in nucleus."
      Aoki N., Matsuda T.
      Mol. Endocrinol. 16:58-69(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PROLACTIN SIGNALING PATHWAY, PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPN2.
    8. "NCoA-1/SRC-1 is an essential coactivator of STAT5 that binds to the FDL motif in the alpha-helical region of the STAT5 transactivation domain."
      Litterst C.M., Kliem S., Marilley D., Pfitzner E.
      J. Biol. Chem. 278:45340-45351(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCOA1.
    9. "STAT5a activation mediates the epithelial to mesenchymal transition induced by oncogenic RhoA."
      Benitah S.A., Valeron P.F., Rui H., Lacal J.C.
      Mol. Biol. Cell 14:40-53(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-694 BY JAK2.
    10. "FLT3 mutations in the activation loop of tyrosine kinase domain are frequently found in infant ALL with MLL rearrangements and pediatric ALL with hyperdiploidy."
      Taketani T., Taki T., Sugita K., Furuichi Y., Ishii E., Hanada R., Tsuchida M., Sugita K., Ida K., Hayashi Y.
      Blood 103:1085-1088(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
    11. "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.
    12. "The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by functioning as a STAT5A nuclear chaperone."
      Williams C.C., Allison J.G., Vidal G.A., Burow M.E., Beckman B.S., Marrero L., Jones F.E.
      J. Cell Biol. 167:469-478(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ERBB4, SUBCELLULAR LOCATION, FUNCTION.
    13. "Suppressor of cytokine signaling 7 inhibits prolactin, growth hormone, and leptin signaling by interacting with STAT5 or STAT3 and attenuating their nuclear translocation."
      Martens N., Uzan G., Wery M., Hooghe R., Hooghe-Peters E.L., Gertler A.
      J. Biol. Chem. 280:13817-13823(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SOCS7.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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-694 IN RESPONSE TO KIT SIGNALING.

    Entry informationi

    Entry nameiSTA5A_HUMAN
    AccessioniPrimary (citable) accession number: P42229
    Secondary accession number(s): Q1KLZ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 150 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3