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Protein

Signal transducer and activator of transcription 5A

Gene

STAT5A

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

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

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:11366. STAT5A.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA338.

Polymorphism and mutation databases

BioMutaiSTAT5A.
DMDMi1174462.

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 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 similarity4 Publications
ISGylated.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP42229.
PaxDbiP42229.
PeptideAtlasiP42229.
PRIDEiP42229.

PTM databases

PhosphoSiteiP42229.

Expressioni

Gene expression databases

BgeeiP42229.
CleanExiHS_STAT5A.
ExpressionAtlasiP42229. baseline and differential.
GenevisibleiP42229. HS.

Organism-specific databases

HPAiCAB003860.
HPA027873.
HPA042128.
HPA049883.
HPA051156.

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
EGFRP005333EBI-749537,EBI-297353
PTPN1P180312EBI-749537,EBI-968788
TCF12Q990813EBI-749537,EBI-722877

Protein-protein interaction databases

BioGridi112653. 57 interactions.
DIPiDIP-396N.
IntActiP42229. 37 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.
GeneTreeiENSGT00760000119236.
HOGENOMiHOG000230988.
HOVERGENiHBG107486.
InParanoidiP42229.
KOiK11223.
OMAiIDLDETM.
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. AlignAdd to basket

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

        10         20         30         40         50
MAGWIQAQQL QGDALRQMQV LYGQHFPIEV RHYLAQWIES QPWDAIDLDN
60 70 80 90 100
PQDRAQATQL LEGLVQELQK KAEHQVGEDG FLLKIKLGHY ATQLQKTYDR
110 120 130 140 150
CPLELVRCIR HILYNEQRLV REANNCSSPA GILVDAMSQK HLQINQTFEE
160 170 180 190 200
LRLVTQDTEN ELKKLQQTQE YFIIQYQESL RIQAQFAQLA QLSPQERLSR
210 220 230 240 250
ETALQQKQVS LEAWLQREAQ TLQQYRVELA EKHQKTLQLL RKQQTIILDD
260 270 280 290 300
ELIQWKRRQQ LAGNGGPPEG SLDVLQSWCE KLAEIIWQNR QQIRRAEHLC
310 320 330 340 350
QQLPIPGPVE EMLAEVNATI TDIISALVTS TFIIEKQPPQ VLKTQTKFAA
360 370 380 390 400
TVRLLVGGKL NVHMNPPQVK ATIISEQQAK SLLKNENTRN ECSGEILNNC
410 420 430 440 450
CVMEYHQATG TLSAHFRNMS LKRIKRADRR GAESVTEEKF TVLFESQFSV
460 470 480 490 500
GSNELVFQVK TLSLPVVVIV HGSQDHNATA TVLWDNAFAE PGRVPFAVPD
510 520 530 540 550
KVLWPQLCEA LNMKFKAEVQ SNRGLTKENL VFLAQKLFNN SSSHLEDYSG
560 570 580 590 600
LSVSWSQFNR ENLPGWNYTF WQWFDGVMEV LKKHHKPHWN DGAILGFVNK
610 620 630 640 650
QQAHDLLINK PDGTFLLRFS DSEIGGITIA WKFDSPERNL WNLKPFTTRD
660 670 680 690 700
FSIRSLADRL GDLSYLIYVF PDRPKDEVFS KYYTPVLAKA VDGYVKPQIK
710 720 730 740 750
QVVPEFVNAS ADAGGSSATY MDQAPSPAVC PQAPYNMYPQ NPDHVLDQDG
760 770 780 790
EFDLDETMDV ARHVEELLRR PMDSLDSRLS PPAGLFTSAR GSLS
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 (Ref. 2) Curated

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:
EMBLi
GenBanki
DDBJi
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]
CCDS74067.1. [P42229-2]
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.
ENST00000546010; ENSP00000443107; ENSG00000126561. [P42229-2]
ENST00000590949; ENSP00000468749; ENSG00000126561.
GeneIDi6776.
KEGGihsa:6776.
UCSCiuc002hzj.2. human. [P42229-1]
uc010cyc.2. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

STAT5 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS74067.1. [P42229-2]
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi112653. 57 interactions.
DIPiDIP-396N.
IntActiP42229. 37 interactions.
MINTiMINT-223002.
STRINGi9606.ENSP00000341208.

Chemistry

BindingDBiP42229.
ChEMBLiCHEMBL5403.

PTM databases

PhosphoSiteiP42229.

Polymorphism and mutation databases

BioMutaiSTAT5A.
DMDMi1174462.

Proteomic databases

MaxQBiP42229.
PaxDbiP42229.
PeptideAtlasiP42229.
PRIDEiP42229.

Protocols and materials databases

DNASUi6776.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000345506; ENSP00000341208; ENSG00000126561.
ENST00000546010; ENSP00000443107; ENSG00000126561. [P42229-2]
ENST00000590949; ENSP00000468749; ENSG00000126561.
GeneIDi6776.
KEGGihsa:6776.
UCSCiuc002hzj.2. human. [P42229-1]
uc010cyc.2. human.

Organism-specific databases

CTDi6776.
GeneCardsiGC17P040439.
HGNCiHGNC:11366. STAT5A.
HPAiCAB003860.
HPA027873.
HPA042128.
HPA049883.
HPA051156.
MIMi601511. gene.
neXtProtiNX_P42229.
PharmGKBiPA338.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG245085.
GeneTreeiENSGT00760000119236.
HOGENOMiHOG000230988.
HOVERGENiHBG107486.
InParanoidiP42229.
KOiK11223.
OMAiIDLDETM.
OrthoDBiEOG73JKTT.
PhylomeDBiP42229.
TreeFamiTF318648.

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.

Miscellaneous databases

ChiTaRSiSTAT5A. human.
GeneWikiiSTAT5A.
GenomeRNAii6776.
NextBioi26450.
PROiP42229.
SOURCEiSearch...

Gene expression databases

BgeeiP42229.
CleanExiHS_STAT5A.
ExpressionAtlasiP42229. baseline and differential.
GenevisibleiP42229. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 159 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.