GenomeNet

Database: UniProt
Entry: F1M9D6_RAT
LinkDB: F1M9D6_RAT
Original site: F1M9D6_RAT 
ID   F1M9D6_RAT              Unreviewed;       749 AA.
AC   F1M9D6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 2.
DT   22-JUL-2015, entry version 36.
DE   RecName: Full=Signal transducer and activator of transcription {ECO:0000256|RuleBase:RU046415};
GN   Name=Stat1 {ECO:0000313|EMBL:EDL99092.1,
GN   ECO:0000313|Ensembl:ENSRNOP00000019465, ECO:0000313|RGD:3771};
GN   ORFNames=rCG_22495 {ECO:0000313|EMBL:EDL99092.1};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000019465, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000019465, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000019465,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|EMBL:EDL99092.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BN {ECO:0000313|EMBL:EDL99092.1};
RX   PubMed=15632090; DOI=10.1101/gr.2889405;
RA   Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
RA   Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
RA   Istrail S., Li P., Sutton G.;
RT   "Gene and alternative splicing annotation with AIR.";
RL   Genome Res. 15:54-66(2005).
RN   [3] {ECO:0000313|EMBL:EDL99092.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BN {ECO:0000313|EMBL:EDL99092.1};
RA   Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
RA   Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
RA   Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L.,
RA   Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C.,
RA   Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Ensembl:ENSRNOP00000019465}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000019465};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [5] {ECO:0000213|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU046415}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU046415}.
CC   -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC       {ECO:0000256|RuleBase:RU046415}.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
CC       {ECO:0000256|RuleBase:RU046415}.
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DR   EMBL; AABR07067607; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07067608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07067609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07067610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07067611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07067612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07073481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC094675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH473965; EDL99092.1; -; Genomic_DNA.
DR   RefSeq; NP_116001.2; NM_032612.3.
DR   UniGene; Rn.33229; -.
DR   DIP; DIP-60985N; -.
DR   STRING; 10116.ENSRNOP00000019465; -.
DR   Ensembl; ENSRNOT00000019465; ENSRNOP00000019465; ENSRNOG00000014079.
DR   GeneID; 25124; -.
DR   CTD; 6772; -.
DR   RGD; 3771; Stat1.
DR   GeneTree; ENSGT00760000119236; -.
DR   OMA; WYNMLTT; -.
DR   OrthoDB; EOG73JKTT; -.
DR   Reactome; REACT_275527; Regulation of IFNA signaling.
DR   Reactome; REACT_301042; Interferon alpha/beta signaling.
DR   Reactome; REACT_301200; Downstream signal transduction.
DR   Reactome; REACT_302286; Interferon gamma signaling.
DR   Reactome; REACT_309732; Regulation of IFNG signaling.
DR   Reactome; REACT_314415; Growth hormone receptor signaling.
DR   Reactome; REACT_319332; Interleukin-6 signaling.
DR   Reactome; REACT_335137; Signaling by SCF-KIT.
DR   Reactome; REACT_348632; ISG15 antiviral mechanism.
DR   NextBio; 35582886; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   GO; GO:0030424; C:axon; IDA:RGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0031730; F:CCR5 chemokine receptor binding; IPI:RGD.
DR   GO; GO:0003677; F:DNA binding; IDA:RGD.
DR   GO; GO:0051721; F:protein phosphatase 2A binding; IPI:RGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:RGD.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0008015; P:blood circulation; IMP:RGD.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IDA:RGD.
DR   GO; GO:0007259; P:JAK-STAT cascade; IMP:RGD.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IDA:RGD.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
DR   GO; GO:0051591; P:response to cAMP; IDA:RGD.
DR   GO; GO:0034097; P:response to cytokine; IDA:RGD.
DR   GO; GO:0042493; P:response to drug; IDA:RGD.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR   GO; GO:0009612; P:response to mechanical stimulus; IDA:RGD.
DR   GO; GO:0007584; P:response to nutrient; IDA:RGD.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR   GO; GO:0043434; P:response to peptide hormone; IDA:RGD.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.238.10; -; 1.
DR   Gene3D; 1.10.532.10; -; 1.
DR   Gene3D; 1.20.1050.20; -; 1.
DR   Gene3D; 2.60.40.630; -; 1.
DR   Gene3D; 3.30.505.10; -; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR001217; STAT.
DR   InterPro; IPR022752; STAT1_TAZ2-bd_C.
DR   InterPro; IPR013800; STAT_TF_alpha.
DR   InterPro; IPR015988; STAT_TF_coiled-coil.
DR   InterPro; IPR013801; STAT_TF_DNA-bd.
DR   InterPro; IPR012345; STAT_TF_DNA-bd_sub.
DR   InterPro; IPR013799; STAT_TF_prot_interaction.
DR   PANTHER; PTHR11801; PTHR11801; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF12162; STAT1_TAZ2bind; 1.
DR   Pfam; PF01017; STAT_alpha; 1.
DR   Pfam; PF02864; STAT_bind; 1.
DR   Pfam; PF02865; STAT_int; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00964; STAT_int; 1.
DR   SUPFAM; SSF47655; SSF47655; 1.
DR   SUPFAM; SSF48092; SSF48092; 1.
DR   SUPFAM; SSF49417; SSF49417; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   1: Evidence at protein level;
KW   Activator {ECO:0000256|RuleBase:RU046415};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002494};
KW   Cytoplasm {ECO:0000256|RuleBase:RU046415};
KW   DNA-binding {ECO:0000256|RuleBase:RU046415};
KW   Nucleus {ECO:0000256|RuleBase:RU046415};
KW   Phosphoprotein {ECO:0000256|RuleBase:RU046415};
KW   Proteomics identification {ECO:0000213|PeptideAtlas:F1M9D6};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   SH2 domain {ECO:0000256|RuleBase:RU046415};
KW   Transcription {ECO:0000256|RuleBase:RU046415};
KW   Transcription regulation {ECO:0000256|RuleBase:RU046415}.
SQ   SEQUENCE   749 AA;  87250 MW;  DFD965F18C2A23D7 CRC64;
     MSQWYELQQL DSKFLEQVHQ LYDDSFPMEI RQYLAQWLEK QDWEHAAYDV SFATIRFHDL
     LSQLDDQYSR FSLENNFLLQ HNIRKSKRNL QDNFQEDPVQ MSMIIHNCLK EERKILENAQ
     RFNQAQEGNI QNTVMLDKQK ELDSKVRNVK DQVMCIEHEI KTLEDLQDEY DFKCKTSQNR
     ESEANGVAKS DQKQEQLLLH KMFLMLDNKR KEIIHKIREL LNSIELTQNT LINDELVEWK
     RRQQSACIGG PPNACLDQLQ SWFTIVAESL QQVRQQLKKL EELEQKFTYE QDPITKNKQV
     LSDRTFVLFQ QLIQSSFVVE RQPCMPTHPQ RPLVLKTGVQ FTVKLRLLVK LQELNYNLKV
     KVSFDKDVNE KNTVKGFRKF NILGTHTKVM NMEESTNGSL AAEFRHLQLK EQKNAGNRTN
     EGPLIVTEEL HSLSFETQLC QPGLVIDLET TSLPVVVISN VSQLPSGWAS ILWYNMLVTE
     PRNLSFFLNP PCAWWSQLSE VLSWQFSSVT KRGLNADQLS MLGEKLLGPN AGPDGLIPWT
     RFCKENINDK NFSFWPWIDT ILELIKKHLL CLWNDGCIMG FISKERERAL LKDQQPGTFL
     LRFSESSREG AITFTWVERS QNGGEPDFHA VEPYTKKELS AVTFPDIIRN YKVMAAENIP
     ENPLKYLYPN IDKDHAFGKY YSRPKEAPEP MELDDPKRTG YIKTELISVS EVHPSRLQST
     ENLLPMSPEE FDEMSKIVGS EFDSMMSAV
//
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