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P42226 (STAT6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Signal transducer and activator of transcription 6
Alternative name(s):
IL-4 Stat
Gene names
Name:STAT6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length847 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Carries out a dual function: signal transduction and activation of transcription. Involved in IL4/interleukin-4- and IL3/interleukin-3-mediated signaling. Ref.9

Subunit structure

Forms a homodimer or a heterodimer with a related family member By similarity. Interacts with NCOA1 via its C-terminal LXXLL motif. Ref.8

Subcellular location

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

Post-translational modification

Tyrosine phosphorylated following stimulation by IL4/interleukin-4 and IL3/interleukin-3 By similarity. Dephosphorylation on tyrosine residues by PTPN2 negatively regulates the IL4/interleukin-4 mediated signaling. Ref.9

Sequence similarities

Belongs to the transcription factor STAT family.

Contains 1 SH2 domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSH2 domain
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT-helper 1 cell lineage commitment

Inferred from electronic annotation. Source: Ensembl

cellular response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

cellular response to reactive nitrogen species

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

interleukin-4-mediated signaling pathway

Inferred from mutant phenotype Ref.9. Source: UniProtKB

mammary gland epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

mammary gland morphogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

negative regulation of type 2 immune response

Inferred from electronic annotation. Source: Ensembl

positive regulation of isotype switching to IgE isotypes

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of type I interferon production

Traceable author statement. Source: Reactome

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Traceable author statement PubMed 8810328. Source: ProtInc

signal transduction

Traceable author statement PubMed 10747856. Source: ProtInc

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

membrane raft

Inferred from electronic annotation. Source: Ensembl

nuclear chromatin

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionRNA polymerase II core promoter sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

calcium ion binding

Inferred from electronic annotation. Source: InterPro

identical protein binding

Inferred from physical interaction PubMed 22000020. Source: IntAct

protein phosphatase binding

Inferred from physical interaction Ref.9. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Traceable author statement PubMed 10747856. Source: ProtInc

signal transducer activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P42226-1)

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.
Isoform 2 (identifier: P42226-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-174: Missing.
     175-177: PSE → MEQ
Isoform 3 (identifier: P42226-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-110: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 847846Signal transducer and activator of transcription 6
PRO_0000182433

Regions

Domain517 – 632116SH2
Motif802 – 8065LXXLL motif

Amino acid modifications

Modified residue21N-acetylserine Ref.10
Modified residue6411Phosphotyrosine; by JAK By similarity

Natural variations

Alternative sequence1 – 174174Missing in isoform 2.
VSP_031871
Alternative sequence1 – 110110Missing in isoform 3.
VSP_045282
Alternative sequence175 – 1773PSE → MEQ in isoform 2.
VSP_031872
Natural variant1811M → R. Ref.5
Corresponds to variant rs3024952 [ dbSNP | Ensembl ].
VAR_013094
Natural variant4191D → N.
Corresponds to variant rs11172102 [ dbSNP | Ensembl ].
VAR_059812

Experimental info

Mutagenesis8021L → A: Abolishes the interaction with NCOA1; when associated with A-805. Ref.8
Mutagenesis8051L → A: Abolishes the interaction with NCOA1; when associated with A-802. Ref.8
Sequence conflict1491E → Q in AAC67525. Ref.2
Sequence conflict2461G → D in BAH14513. Ref.4
Sequence conflict7331S → N in AAC67525. Ref.2

Secondary structure

... 847
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: F35075F1C1F2A677

FASTA84794,135
        10         20         30         40         50         60 
MSLWGLVSKM PPEKVQRLYV DFPQHLRHLL GDWLESQPWE FLVGSDAFCC NLASALLSDT 

        70         80         90        100        110        120 
VQHLQASVGE QGEGSTILQH ISTLESIYQR DPLKLVATFR QILQGEKKAV MEQFRHLPMP 

       130        140        150        160        170        180 
FHWKQEELKF KTGLRRLQHR VGEIHLLREA LQKGAEAGQV SLHSLIETPA NGTGPSEALA 

       190        200        210        220        230        240 
MLLQETTGEL EAAKALVLKR IQIWKRQQQL AGNGAPFEES LAPLQERCES LVDIYSQLQQ 

       250        260        270        280        290        300 
EVGAAGGELE PKTRASLTGR LDEVLRTLVT SCFLVEKQPP QVLKTQTKFQ AGVRFLLGLR 

       310        320        330        340        350        360 
FLGAPAKPPL VRADMVTEKQ ARELSVPQGP GAGAESTGEI INNTVPLENS IPGNCCSALF 

       370        380        390        400        410        420 
KNLLLKKIKR CERKGTESVT EEKCAVLFSA SFTLGPGKLP IQLQALSLPL VVIVHGNQDN 

       430        440        450        460        470        480 
NAKATILWDN AFSEMDRVPF VVAERVPWEK MCETLNLKFM AEVGTNRGLL PEHFLFLAQK 

       490        500        510        520        530        540 
IFNDNSLSME AFQHRSVSWS QFNKEILLGR GFTFWQWFDG VLDLTKRCLR SYWSDRLIIG 

       550        560        570        580        590        600 
FISKQYVTSL LLNEPDGTFL LRFSDSEIGG ITIAHVIRGQ DGSPQIENIQ PFSAKDLSIR 

       610        620        630        640        650        660 
SLGDRIRDLA QLKNLYPKKP KDEAFRSHYK PEQMGKDGRG YVPATIKMTV ERDQPLPTPE 

       670        680        690        700        710        720 
LQMPTMVPSY DLGMAPDSSM SMQLGPDMVP QVYPPHSHSI PPYQGLSPEE SVNVLSAFQE 

       730        740        750        760        770        780 
PHLQMPPSLG QMSLPFDQPH PQGLLPCQPQ EHAVSSPDPL LCSDVTMVED SCLSQPVTAF 

       790        800        810        820        830        840 
PQGTWIGEDI FPPLLPPTEQ DLTKLLLEGQ GESGGGSLGA QPLLQPSHYG QSGISMSHMD 


LRANPSW 

« Hide

Isoform 2 [UniParc].

Checksum: 7A050ADF43A669BB
Show »

FASTA67374,456
Isoform 3 [UniParc].

Checksum: 8A076ABC6053A831
Show »

FASTA73781,748

References

« Hide 'large scale' references
[1]"An interleukin-4-induced transcription factor: IL-4 Stat."
Hou J., Schindler U., Henzel W.J., Ho T., Brasseur M., McKnight S.L.
Science 265:1701-1706(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Localization of the human stat6 gene to chromosome 12q13.3-q14.1, a region implicated in multiple solid tumors."
Patel B.K., Keck C.L., O'Leary R.S., Popescu N.C., LaRochelle W.J.
Genomics 52:192-200(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"STAT6 mRNA, nirs splice variant 2."
Tabata Y., Sameshima E., Hayashi A., Iida K., Mitsuyama M., Kanai S., Furuya T., Saito T.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[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. expand/collapse author list , 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] (ISOFORMS 1 AND 3).
Tissue: Tongue.
[5]SeattleSNPs variation discovery resource
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-181.
[6]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: Uterus.
[8]"An LXXLL motif in the transactivation domain of STAT6 mediates recruitment of NCoA-1/SRC-1."
Litterst C.M., Pfitzner E.
J. Biol. Chem. 277:36052-36060(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NCOA1, MUTAGENESIS OF LEU-802 AND LEU-805.
[9]"T-cell protein tyrosine phosphatase, distinctively expressed in activated-B-cell-like diffuse large B-cell lymphomas, is the nuclear phosphatase of STAT6."
Lu X., Chen J., Sasmono R.T., Hsi E.D., Sarosiek K.A., Tiganis T., Lossos I.S.
Mol. Cell. Biol. 27:2166-2179(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN IL4 SIGNALING, PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPN2.
[10]"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].
[11]"Structure of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif of the STAT6 transactivation domain."
Razeto A., Ramakrishnan V., Litterst C.M., Giller K., Griesinger C., Carlomagno T., Lakomek N., Heimburg T., Lodrini M., Pfitzner E., Becker S.
J. Mol. Biol. 336:319-329(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 795-808 IN COMPLEX WITH 257-385 OF NCOA1.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U16031 mRNA. Translation: AAA57193.1.
AF067575, AF067572, AF067573 Genomic DNA. Translation: AAC67525.1.
AB103089 mRNA. Translation: BAD89432.1.
AK290431 mRNA. Translation: BAF83120.1.
AK316142 mRNA. Translation: BAH14513.1.
AF417842 Genomic DNA. Translation: AAL06595.1.
AC023237 Genomic DNA. No translation available.
BC075852 mRNA. Translation: AAH75852.1.
PIRA54740.
RefSeqNP_001171549.1. NM_001178078.1.
NP_001171550.1. NM_001178079.1.
NP_001171551.1. NM_001178080.1.
NP_003144.3. NM_003153.4.
UniGeneHs.524518.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OJ5X-ray2.20B795-808[»]
ProteinModelPortalP42226.
SMRP42226. Positions 13-631.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112655. 59 interactions.
IntActP42226. 31 interactions.
MINTMINT-8020389.
STRING9606.ENSP00000300134.

Chemistry

BindingDBP42226.
ChEMBLCHEMBL5401.

PTM databases

PhosphoSiteP42226.

Polymorphism databases

DMDM1174459.

Proteomic databases

PaxDbP42226.
PRIDEP42226.

Protocols and materials databases

DNASU6778.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000300134; ENSP00000300134; ENSG00000166888. [P42226-1]
ENST00000454075; ENSP00000401486; ENSG00000166888. [P42226-1]
ENST00000537215; ENSP00000444530; ENSG00000166888. [P42226-3]
ENST00000538913; ENSP00000445409; ENSG00000166888. [P42226-3]
ENST00000543873; ENSP00000438451; ENSG00000166888. [P42226-1]
ENST00000556155; ENSP00000451742; ENSG00000166888. [P42226-1]
GeneID6778.
KEGGhsa:6778.
UCSCuc001sna.3. human. [P42226-1]

Organism-specific databases

CTD6778.
GeneCardsGC12M057489.
HGNCHGNC:11368. STAT6.
HPAHPA001861.
MIM601512. gene.
neXtProtNX_P42226.
Orphanet2126. Solitary fibrous tumor.
PharmGKBPA339.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG278979.
HOGENOMHOG000230988.
HOVERGENHBG107486.
InParanoidP42226.
KOK11225.
OMAKFQAGVR.
OrthoDBEOG73JKTT.
PhylomeDBP42226.
TreeFamTF318648.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_6900. Immune System.
SignaLinkP42226.

Gene expression databases

ArrayExpressP42226.
BgeeP42226.
CleanExHS_STAT6.
GenevestigatorP42226.

Family and domain databases

Gene3D1.10.238.10. 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.
InterProIPR011992. EF-hand-dom_pair.
IPR008967. p53-like_TF_DNA-bd.
IPR000980. SH2.
IPR001217. STAT.
IPR028187. STAT6_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]
PANTHERPTHR11801. PTHR11801. 1 hit.
PfamPF00017. SH2. 1 hit.
PF14596. STAT6_C. 1 hit.
PF01017. STAT_alpha. 1 hit.
PF02864. STAT_bind. 1 hit.
PF02865. STAT_int. 1 hit.
[Graphical view]
SMARTSM00252. SH2. 1 hit.
SM00964. STAT_int. 1 hit.
[Graphical view]
SUPFAMSSF47655. SSF47655. 1 hit.
SSF48092. SSF48092. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEPS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSTAT6. human.
EvolutionaryTraceP42226.
GeneWikiSTAT6.
GenomeRNAi6778.
NextBio26458.
PROP42226.
SOURCESearch...

Entry information

Entry nameSTAT6_HUMAN
AccessionPrimary (citable) accession number: P42226
Secondary accession number(s): A8K316 expand/collapse secondary AC list , B7ZA27, F5GXI9, Q5FBW5, Q71UP4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM