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Signal transducer and activator of transcription 1-alpha/beta (Transcription factor ISGF-3 components p91/p84)

 STAT1_HUMAN             Reviewed;         750 AA.
P42224; A8K989; B2RCA0; D2KFR8; D3DPI7; Q53S88; Q53XW4; Q68D00;
Q9UDL5;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
27-SEP-2017, entry version 212.
RecName: Full=Signal transducer and activator of transcription 1-alpha/beta;
AltName: Full=Transcription factor ISGF-3 components p91/p84;
Name=STAT1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), AND PROTEIN SEQUENCE OF
514-524; 654-660 AND 667-672.
PubMed=1502203; DOI=10.1073/pnas.89.16.7836;
Schindler C., Fu X.-Y., Improta T., Aebersold R., Darnell J.E. Jr.;
"Proteins of transcription factor ISGF-3: one gene encodes the 91- and
84-kDa ISGF-3 proteins that are activated by interferon alpha.";
Proc. Natl. Acad. Sci. U.S.A. 89:7836-7839(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
Kristensen I., Veirum J.E., Moeller B.K., Christiansen M.;
"Novel STAT1 alleles in a patient with impaired resistance to
mycobacteria.";
Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
TISSUE=Placenta, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7885841; DOI=10.1093/nar/23.3.459;
Yan R., Qureshi S., Zhong Z., Wen Z., Darnell J.E. Jr.;
"The genomic structure of the STAT genes: multiple exons in coincident
sites in Stat1 and Stat2.";
Nucleic Acids Res. 23:459-463(1995).
[11]
PHOSPHORYLATION IN RESPONSE TO IFN-ALPHA.
PubMed=1638633; DOI=10.1016/0092-8674(92)90106-M;
Fu X.Y.;
"A transcription factor with SH2 and SH3 domains is directly activated
by an interferon alpha-induced cytoplasmic protein tyrosine
kinase(s).";
Cell 70:323-335(1992).
[12]
PHOSPHORYLATION AT SER-727, AND MUTAGENESIS.
PubMed=7543024; DOI=10.1016/0092-8674(95)90311-9;
Wen Z., Zhong Z., Darnell J.E. Jr.;
"Maximal activation of transcription by Stat1 and Stat3 requires both
tyrosine and serine phosphorylation.";
Cell 82:241-250(1995).
[13]
PHOSPHORYLATION AT TYR-701.
PubMed=7657660; DOI=10.1074/jbc.270.35.20775;
Quelle F.W., Thierfelder W., Witthuhn B.A., Tang B., Cohen S.,
Ihle J.N.;
"Phosphorylation and activation of the DNA binding activity of
purified Stat1 by the Janus protein-tyrosine kinases and the epidermal
growth factor receptor.";
J. Biol. Chem. 270:20775-20780(1995).
[14]
TYROSINE PHOSPHORYLATION, HETERODIMERIZATION, DNA-BINDING, AND
MUTAGENESIS.
PubMed=8605877;
Gupta S., Yan H., Wong L.H., Ralph S., Krolewski J., Schindler C.;
"The SH2 domains of Stat1 and Stat2 mediate multiple interactions in
the transduction of IFN-alpha signals.";
EMBO J. 15:1075-1084(1996).
[15]
INTERACTION WITH IFNAR1 AND IFNAR2, AND PHOSPHORYLATION.
PubMed=9121453; DOI=10.1128/MCB.17.4.2048;
Li X., Leung S., Kerr I.M., Stark G.R.;
"Functional subdomains of STAT2 required for preassociation with the
alpha interferon receptor and for signaling.";
Mol. Cell. Biol. 17:2048-2056(1997).
[16]
INTERACTION WITH PIAS1, AND FUNCTION.
TISSUE=B-cell;
PubMed=9724754; DOI=10.1073/pnas.95.18.10626;
Liu B., Liao J., Rao X., Kushner S.A., Chung C.D., Chang D.D.,
Shuai K.;
"Inhibition of Stat1-mediated gene activation by PIAS1.";
Proc. Natl. Acad. Sci. U.S.A. 95:10626-10631(1998).
[17]
REVIEW.
PubMed=10702714; DOI=10.1159/000053968;
Cebulla C.M., Miller D.M., Sedmak D.D.;
"Viral inhibition of interferon signal transduction.";
Intervirology 42:325-330(1999).
[18]
INTERACTION WITH SENDAI VIRUS C PROTEIN.
PubMed=11442634; DOI=10.1046/j.1365-2443.2001.00442.x;
Takeuchi K., Komatsu T., Yokoo J., Kato A., Shioda T., Nagai Y.,
Gotoh B.;
"Sendai virus C protein physically associates with Stat1.";
Genes Cells 6:545-557(2001).
[19]
INTERACTION WITH PTK2/FAK1, AND PHOSPHORYLATION.
PubMed=11278462; DOI=10.1074/jbc.M009063200;
Xie B., Zhao J., Kitagawa M., Durbin J., Madri J.A., Guan J.L.,
Fu X.Y.;
"Focal adhesion kinase activates Stat1 in integrin-mediated cell
migration and adhesion.";
J. Biol. Chem. 276:19512-19523(2001).
[20]
PHOSPHORYLATION, AND DEPHOSPHORYLATION BY PTPN2.
PubMed=12138178; DOI=10.1128/MCB.22.16.5662-5668.2002;
ten Hoeve J., de Jesus Ibarra-Sanchez M., Fu Y., Zhu W., Tremblay M.,
David M., Shuai K.;
"Identification of a nuclear Stat1 protein tyrosine phosphatase.";
Mol. Cell. Biol. 22:5662-5668(2002).
[21]
SUMOYLATION AT LYS-703, FUNCTION, AND MUTAGENESIS OF LYS-703.
PubMed=12855578; DOI=10.1182/blood-2002-12-3816;
Ungureanu D., Vanhatupa S., Kotaja N., Yang J., Aittomaeki S.,
Jaenne O.A., Palvimo J.J., Silvennoinen O.;
"PIAS proteins promote SUMO-1 conjugation to STAT1.";
Blood 102:3311-3313(2003).
[22]
SUMOYLATION AT LYS-703, FUNCTION, AND MUTAGENESIS OF LYS-110 AND
LYS-703.
PubMed=12764129; DOI=10.1074/jbc.M301344200;
Rogers R.S., Horvath C.M., Matunis M.J.;
"SUMO modification of STAT1 and its role in PIAS-mediated inhibition
of gene activation.";
J. Biol. Chem. 278:30091-30097(2003).
[23]
REVIEW ON ROLE IN KIT SIGNALING.
PubMed=15526160; DOI=10.1007/s00018-004-4189-6;
Ronnstrand L.;
"Signal transduction via the stem cell factor receptor/c-Kit.";
Cell. Mol. Life Sci. 61:2535-2548(2004).
[24]
PHOSPHORYLATION AT SER-727, FUNCTION, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF SER-727.
PubMed=15322115; DOI=10.1074/jbc.M407448200;
DeVries T.A., Kalkofen R.L., Matassa A.A., Reyland M.E.;
"Protein kinase Cdelta regulates apoptosis via activation of STAT1.";
J. Biol. Chem. 279:45603-45612(2004).
[25]
ISGYLATION.
PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
"Proteomic identification of proteins conjugated to ISG15 in mouse and
human cells.";
Biochem. Biophys. Res. Commun. 336:496-506(2005).
[26]
INTERACTION WITH HEPATITIS C VIRUS CORE PROTEIN.
PubMed=15825084; DOI=10.1053/j.gastro.2005.02.006;
Lin W., Choe W.H., Hiasa Y., Kamegaya Y., Blackard J.T., Schmidt E.V.,
Chung R.T.;
"Hepatitis C virus expression suppresses interferon signaling by
degrading STAT1.";
Gastroenterology 128:1034-1041(2005).
[27]
PHOSPHORYLATION IN RESPONSE TO ACTIVATED FGFR3, AND PHOSPHORYLATION AT
TYR-701.
PubMed=17561467; DOI=10.1016/j.bone.2006.11.030;
Harada D., Yamanaka Y., Ueda K., Nishimura R., Morishima T., Seino Y.,
Tanaka H.;
"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.";
Bone 41:273-281(2007).
[28]
PHOSPHORYLATION IN RESPONSE TO ACTIVATED FGFR1; FGFR2; FGFR3 AND
FGFR4.
PubMed=17311277; DOI=10.1002/jcp.21014;
Citores L., Bai L., Sorensen V., Olsnes S.;
"Fibroblast growth factor receptor-induced phosphorylation of STAT1 at
the Golgi apparatus without translocation to the nucleus.";
J. Cell. Physiol. 212:148-156(2007).
[29]
PHOSPHORYLATION AT SER-727, INTERACTION WITH PIAS1, SUMOYLATION, AND
MUTAGENESIS OF TYR-701 AND SER-727.
PubMed=17897103; DOI=10.1042/BJ20070620;
Vanhatupa S., Ungureanu D., Paakkunainen M., Silvennoinen O.;
"MAPK-induced Ser727 phosphorylation promotes SUMOylation of STAT1.";
Biochem. J. 409:179-185(2008).
[30]
INTERACTION WITH ERBB4.
PubMed=18721752; DOI=10.1016/j.chembiol.2008.07.006;
Kaushansky A., Gordus A., Budnik B.A., Lane W.S., Rush J.,
MacBeath G.;
"System-wide investigation of ErbB4 reveals 19 sites of Tyr
phosphorylation that are unusually selective in their recruitment
properties.";
Chem. Biol. 15:808-817(2008).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[32]
FUNCTION, AND PHOSPHORYLATION AT TYR-701 IN RESPONSE TO CONSTITUTIVELY
ACTIVATED FGFR3.
PubMed=19088846; DOI=10.1371/journal.pone.0003961;
Krejci P., Salazar L., Kashiwada T.A., Chlebova K., Salasova A.,
Thompson L.M., Bryja V., Kozubik A., Wilcox W.R.;
"Analysis of STAT1 activation by six FGFR3 mutants associated with
skeletal dysplasia undermines dominant role of STAT1 in FGFR3
signaling in cartilage.";
PLoS ONE 3:E3961-E3961(2008).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[34]
INTERACTION WITH PIAS1.
PubMed=19136629; DOI=10.1101/gad.489409;
Weber S., Maass F., Schuemann M., Krause E., Suske G., Bauer U.M.;
"PRMT1-mediated arginine methylation of PIAS1 regulates STAT1
signaling.";
Genes Dev. 23:118-132(2009).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[38]
PHOSPHORYLATION AT TYR-701 IN RESPONSE TO KIT SIGNALING, AND
PHOSPHORYLATION AT SER-727.
PubMed=21135090; DOI=10.1074/jbc.M110.182642;
Chaix A., Lopez S., Voisset E., Gros L., Dubreuil P., De Sepulveda P.;
"Mechanisms of STAT protein activation by oncogenic KIT mutants in
neoplastic mast cells.";
J. Biol. Chem. 286:5956-5966(2011).
[39]
PHOSPHORYLATION AT TYR-701; SER-708 AND SER-727, AND MUTAGENESIS OF
TYR-701; SER-708 AND SER-727.
PubMed=22065572; DOI=10.1074/jbc.M111.285205;
Perwitasari O., Cho H., Diamond M.S., Gale M. Jr.;
"Inhibitor of kappaB kinase epsilon (IKK(epsilon)), STAT1, and IFIT2
proteins define novel innate immune effector pathway against West Nile
virus infection.";
J. Biol. Chem. 286:44412-44423(2011).
[40]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[41]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[42]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[43]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-703, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[44]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-703, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[45]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 136-710, AND COILED-COIL.
PubMed=9630226; DOI=10.1016/S0092-8674(00)81443-9;
Chen X., Vinkemeier U., Zhao Y., Jeruzalmi D., Darnell J.E. Jr.,
Kuriyan J.;
"Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to
DNA.";
Cell 93:827-839(1998).
[46]
VARIANT IMD31A SER-706.
PubMed=11452125; DOI=10.1126/science.1061154;
Dupuis S., Dargemont C., Fieschi C., Thomassin N., Rosenzweig S.,
Harris J., Holland S.M., Schreiber R.D., Casanova J.-L.;
"Impairment of mycobacterial but not viral immunity by a germline
human STAT1 mutation.";
Science 293:300-303(2001).
[47]
VARIANT IMD31B PRO-600.
PubMed=12590259; DOI=10.1038/ng1097;
Dupuis S., Jouanguy E., Al-Hajjar S., Fieschi C., Al-Mohsen I.Z.,
Al-Jumaah S., Yang K., Chapgier A., Eidenschenk C., Eid P.,
Al-Ghonaium A., Tufenkeji H., Frayha H., Al-Gazlan S., Al-Rayes H.,
Schreiber R.D., Gresser I., Casanova J.L.;
"Impaired response to interferon-alpha/beta and lethal viral disease
in human STAT1 deficiency.";
Nat. Genet. 33:388-391(2003).
[48]
INTERACTION WITH NIPAH V AND W PROTEINS.
PubMed=15140960; DOI=10.1128/JVI.78.11.5633-5641.2004;
Shaw M.L., Garcia-Sastre A., Palese P., Basler C.F.;
"Nipah virus V and W proteins have a common STAT1-binding domain yet
inhibit STAT1 activation from the cytoplasmic and nuclear
compartments, respectively.";
J. Virol. 78:5633-5641(2004).
[49]
VARIANTS IMD31A GLN-320 AND HIS-463, AND CHARACTERIZATION OF VARIANTS
GLN-320; HIS-463 AND SER-706.
PubMed=16934001; DOI=10.1371/journal.pgen.0020131;
Chapgier A., Boisson-Dupuis S., Jouanguy E., Vogt G., Feinberg J.,
Prochnicka-Chalufour A., Casrouge A., Yang K., Soudais C., Fieschi C.,
Santos O.F., Bustamante J., Picard C., de Beaucoudrey L., Emile J.F.,
Arkwright P.D., Schreiber R.D., Rolinck-Werninghaus C.,
Rosen-Wolff A., Magdorf K., Roesler J., Casanova J.L.;
"Novel STAT1 alleles in otherwise healthy patients with mycobacterial
disease.";
PLoS Genet. 2:E131-E131(2006).
[50]
VARIANT [LARGE SCALE ANALYSIS] ALA-491.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[51]
VARIANT IMD31B ASN-201, AND CHARACTERIZATION OF VARIANT IMD31B
ASN-201.
PubMed=20841510; DOI=10.1182/blood-2010-04-280586;
Kong X.F., Ciancanelli M., Al-Hajjar S., Alsina L., Zumwalt T.,
Bustamante J., Feinberg J., Audry M., Prando C., Bryant V., Kreins A.,
Bogunovic D., Halwani R., Zhang X.X., Abel L., Chaussabel D.,
Al-Muhsen S., Casanova J.L., Boisson-Dupuis S.;
"A novel form of human STAT1 deficiency impairing early but not late
responses to interferons.";
Blood 116:5895-5906(2010).
[52]
VARIANTS IMD31C 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, AND
CHARACTERIZATION OF VARIANTS IMD31C GLY-165 AND GLN-274.
PubMed=21727188; DOI=10.1084/jem.20110958;
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.;
"Gain-of-function human STAT1 mutations impair IL-17 immunity and
underlie chronic mucocutaneous candidiasis.";
J. Exp. Med. 208:1635-1648(2011).
[53]
VARIANTS IMD31C VAL-267 AND TRP-274.
PubMed=21714643; DOI=10.1056/NEJMoa1100102;
van de Veerdonk F.L., Plantinga T.S., Hoischen A., Smeekens S.P.,
Joosten L.A., Gilissen C., Arts P., Rosentul D.C., Carmichael A.J.,
Smits-van der Graaf C.A., Kullberg B.J., van der Meer J.W., Lilic D.,
Veltman J.A., Netea M.G.;
"STAT1 mutations in autosomal dominant chronic mucocutaneous
candidiasis.";
N. Engl. J. Med. 365:54-61(2011).
[54]
VARIANTS IMD31A GLU-637 AND ARG-673, AND CHARACTERIZATION OF VARIANTS
IMD31A GLU-637 AND ARG-673.
PubMed=22573496; DOI=10.1002/humu.22113;
Tsumura M., Okada S., Sakai H., Yasunaga S., Ohtsubo M., Murata T.,
Obata H., Yasumi T., Kong X.F., Abhyankar A., Heike T., Nakahata T.,
Nishikomori R., Al-Muhsen S., Boisson-Dupuis S., Casanova J.L.,
Alzahrani M., Shehri M.A., Elghazali G., Takihara Y., Kobayashi M.;
"Dominant-negative STAT1 SH2 domain mutations in unrelated patients
with Mendelian susceptibility to mycobacterial disease.";
Hum. Mutat. 33:1377-1387(2012).
[55]
VARIANTS IMD31C GLY-165; LYS-179; GLN-274; TRP-274; ARG-285 AND
MET-385, CHARACTERIZATION OF VARIANTS IMD31C LYS-179; GLN-274;
TRP-274; ARG-285 AND MET-385, AND CHARACTERIZATION OF VARIANT IMD31B
CYS-701.
PubMed=23709754; DOI=10.1136/jmedgenet-2013-101570;
Soltesz B., Toth B., Shabashova N., Bondarenko A., Okada S.,
Cypowyj S., Abhyankar A., Csorba G., Tasko S., Sarkadi A.K., Mehes L.,
Rozsival P., Neumann D., Chernyshova L., Tulassay Z., Puel A.,
Casanova J.L., Sediva A., Litzman J., Marodi L.;
"New and recurrent gain-of-function STAT1 mutations in patients with
chronic mucocutaneous candidiasis from Eastern and Central Europe.";
J. Med. Genet. 50:567-578(2013).
[56]
VARIANTS IMD31C GLU-278 AND ASP-384, AND CHARACTERIZATION OF VARIANTS
IMD31C GLU-278; ASP-384 AND MET-385.
PubMed=25288569; DOI=10.4049/jimmunol.1401467;
Yamazaki Y., Yamada M., Kawai T., Morio T., Onodera M., Ueki M.,
Watanabe N., Takada H., Takezaki S., Chida N., Kobayashi I., Ariga T.;
"Two novel gain-of-function mutations of STAT1 responsible for chronic
mucocutaneous candidiasis disease: impaired production of IL-17A and
IL-22, and the presence of anti-IL-17F autoantibody.";
J. Immunol. 193:4880-4887(2014).
[57]
VARIANT IMD31C ASN-298, AND CHARACTERIZATION OF VARIANT IMD31C
ASN-298.
PubMed=26514428; DOI=10.1016/j.molimm.2015.09.014;
Martinez-Martinez L., Martinez-Saavedra M.T., Fuentes-Prior P.,
Barnadas M., Rubiales M.V., Noda J., Badell I., Rodriguez-Gallego C.,
Calle-Martin O.L.;
"A novel gain-of-function STAT1 mutation resulting in basal
phosphorylation of STAT1 and increased distal IFN-gamma-mediated
responses in chronic mucocutaneous candidiasis.";
Mol. Immunol. 68:597-605(2015).
-!- FUNCTION: 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. {ECO:0000269|PubMed:12764129,
ECO:0000269|PubMed:12855578, ECO:0000269|PubMed:15322115,
ECO:0000269|PubMed:19088846, ECO:0000269|PubMed:9724754}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:11278462, ECO:0000269|PubMed:11442634,
ECO:0000269|PubMed:15140960, ECO:0000269|PubMed:15825084,
ECO:0000269|PubMed:17897103, ECO:0000269|PubMed:18721752,
ECO:0000269|PubMed:19136629, ECO:0000269|PubMed:9121453,
ECO:0000269|PubMed:9724754}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-1057697, EBI-1057697;
P03255-1:- (xeno); NbExp=2; IntAct=EBI-1057697, EBI-6692439;
P03255-2:- (xeno); NbExp=2; IntAct=EBI-1057697, EBI-6859460;
P26664:- (xeno); NbExp=5; IntAct=EBI-1057697, EBI-6941357;
P27958:- (xeno); NbExp=4; IntAct=EBI-1057697, EBI-8753518;
Q16531:DDB1; NbExp=2; IntAct=EBI-1057697, EBI-350322;
O95786:DDX58; NbExp=4; IntAct=EBI-1057697, EBI-995350;
Q01094:E2F1; NbExp=2; IntAct=EBI-1057697, EBI-448924;
P00533:EGFR; NbExp=6; IntAct=EBI-1057697, EBI-297353;
Q8N9N8:EIF1AD; NbExp=4; IntAct=EBI-1057697, EBI-750700;
P04626:ERBB2; NbExp=3; IntAct=EBI-1057697, EBI-641062;
P01100:FOS; NbExp=6; IntAct=EBI-1057697, EBI-852851;
P07239:H1L (xeno); NbExp=3; IntAct=EBI-1057697, EBI-7789600;
P17181:IFNAR1; NbExp=2; IntAct=EBI-1057697, EBI-1547250;
P48551:IFNAR2; NbExp=2; IntAct=EBI-1057697, EBI-958408;
P15260:IFNGR1; NbExp=4; IntAct=EBI-1057697, EBI-1030755;
Q7Z434:MAVS; NbExp=3; IntAct=EBI-1057697, EBI-995373;
Q01804:OTUD4; NbExp=3; IntAct=EBI-1057697, EBI-1054396;
P19793:RXRA; NbExp=2; IntAct=EBI-1057697, EBI-78598;
P52630:STAT2; NbExp=14; IntAct=EBI-1057697, EBI-1546963;
P40763:STAT3; NbExp=3; IntAct=EBI-1057697, EBI-518675;
Q4VW77:UL47 (xeno); NbExp=2; IntAct=EBI-1057697, EBI-11499224;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15322115}.
Nucleus {ECO:0000269|PubMed:15322115}. Note=Translocated into the
nucleus upon tyrosine phosphorylation and dimerization, in
response to IFN-gamma and signaling by activated FGFR1, FGFR2,
FGFR3 or FGFR4.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Alpha; Synonyms=p91;
IsoId=P42224-1; Sequence=Displayed;
Name=Beta; Synonyms=p84;
IsoId=P42224-2; Sequence=VSP_006282;
-!- PTM: 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. {ECO:0000269|PubMed:15322115,
ECO:0000269|PubMed:17561467, ECO:0000269|PubMed:17897103,
ECO:0000269|PubMed:19088846, ECO:0000269|PubMed:21135090,
ECO:0000269|PubMed:22065572, ECO:0000269|PubMed:7543024,
ECO:0000269|PubMed:7657660}.
-!- PTM: 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. {ECO:0000269|PubMed:15322115,
ECO:0000269|PubMed:17897103, ECO:0000269|PubMed:21135090,
ECO:0000269|PubMed:22065572, ECO:0000269|PubMed:7543024}.
-!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
-!- DISEASE: Immunodeficiency 31B (IMD31B) [MIM:613796]: A disorder
characterized by susceptibility to severe mycobacterial and viral
infections. Affected individuals can develop disseminated
infections and die of viral illness. {ECO:0000269|PubMed:12590259,
ECO:0000269|PubMed:20841510, ECO:0000269|PubMed:23709754}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Immunodeficiency 31A (IMD31A) [MIM:614892]: A form of
Mendelian susceptibility to mycobacterial disease, a rare
condition caused by impairment of interferon-gamma mediated
immunity. It is characterized by predisposition to illness caused
by moderately virulent mycobacterial species, such as Bacillus
Calmette-Guerin (BCG) vaccine, 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. Clinical outcome severity depends on the degree of
impairment of interferon-gamma mediated immunity. 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.
IMD31A has low penetrance, and affected individuals have
relatively mild disease and good prognosis. IMD31A confers a
predisposition to mycobacterial infections only, with no increased
susceptibility to viral infections. {ECO:0000269|PubMed:11452125,
ECO:0000269|PubMed:16934001, ECO:0000269|PubMed:22573496}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Immunodeficiency 31C (IMD31C) [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.
{ECO:0000269|PubMed:21714643, ECO:0000269|PubMed:21727188,
ECO:0000269|PubMed:23709754, ECO:0000269|PubMed:25288569,
ECO:0000269|PubMed:26514428}. 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).
{ECO:0000269|PubMed:21714643}.
-!- SIMILARITY: Belongs to the transcription factor STAT family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/stat1/";
-!- WEB RESOURCE: Name=STAT1base; Note=STAT1 mutation db;
URL="http://structure.bmc.lu.se/idbase/STAT1base/";
-!- WEB RESOURCE: Name=Wikipedia; Note=STAT1 entry;
URL="https://en.wikipedia.org/wiki/STAT1";
-----------------------------------------------------------------------
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EMBL; M97935; AAB64012.1; -; mRNA.
EMBL; M97936; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; GU211347; ADA59516.1; -; mRNA.
EMBL; AY865620; AAW56072.1; -; Genomic_DNA.
EMBL; AK292604; BAF85293.1; -; mRNA.
EMBL; AK315002; BAG37497.1; -; mRNA.
EMBL; CR749636; CAH18430.1; -; mRNA.
EMBL; BT007241; AAP35905.1; -; mRNA.
EMBL; AC067945; AAY24183.1; -; Genomic_DNA.
EMBL; CH471058; EAX10850.1; -; Genomic_DNA.
EMBL; CH471058; EAX10851.1; -; Genomic_DNA.
EMBL; CH471058; EAX10852.1; -; Genomic_DNA.
EMBL; CH471058; EAX10855.1; -; Genomic_DNA.
EMBL; BC002704; AAH02704.1; -; mRNA.
EMBL; U18662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U18663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U18664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U18665; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U18666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U18667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U18668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U18669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U18670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS2309.1; -. [P42224-1]
CCDS; CCDS42793.1; -. [P42224-2]
PIR; A46159; A46159.
RefSeq; NP_009330.1; NM_007315.3. [P42224-1]
RefSeq; NP_644671.1; NM_139266.2. [P42224-2]
RefSeq; XP_006712781.1; XM_006712718.1. [P42224-1]
UniGene; Hs.642990; -.
UniGene; Hs.743244; -.
PDB; 1BF5; X-ray; 2.90 A; A=136-710.
PDB; 1YVL; X-ray; 3.00 A; A/B=1-683.
PDB; 2KA6; NMR; -; B=710-750.
PDB; 3WWT; X-ray; 2.00 A; A=1-126.
PDBsum; 1BF5; -.
PDBsum; 1YVL; -.
PDBsum; 2KA6; -.
PDBsum; 3WWT; -.
DisProt; DP00962; -.
ProteinModelPortal; P42224; -.
SMR; P42224; -.
BioGrid; 112649; 156.
CORUM; P42224; -.
DIP; DIP-46140N; -.
IntAct; P42224; 74.
MINT; MINT-120840; -.
STRING; 9606.ENSP00000354394; -.
BindingDB; P42224; -.
ChEMBL; CHEMBL6101; -.
iPTMnet; P42224; -.
PhosphoSitePlus; P42224; -.
SwissPalm; P42224; -.
BioMuta; STAT1; -.
DMDM; 2507413; -.
EPD; P42224; -.
MaxQB; P42224; -.
PaxDb; P42224; -.
PeptideAtlas; P42224; -.
PRIDE; P42224; -.
DNASU; 6772; -.
Ensembl; ENST00000361099; ENSP00000354394; ENSG00000115415. [P42224-1]
Ensembl; ENST00000392322; ENSP00000376136; ENSG00000115415. [P42224-2]
Ensembl; ENST00000409465; ENSP00000386244; ENSG00000115415. [P42224-1]
GeneID; 6772; -.
KEGG; hsa:6772; -.
UCSC; uc002usj.3; human. [P42224-1]
CTD; 6772; -.
DisGeNET; 6772; -.
EuPathDB; HostDB:ENSG00000115415.18; -.
GeneCards; STAT1; -.
HGNC; HGNC:11362; STAT1.
HPA; CAB004049; -.
HPA; HPA000931; -.
HPA; HPA000982; -.
MalaCards; STAT1; -.
MIM; 600555; gene.
MIM; 613796; phenotype.
MIM; 614162; phenotype.
MIM; 614892; phenotype.
neXtProt; NX_P42224; -.
OpenTargets; ENSG00000115415; -.
Orphanet; 391487; Autoimmune enteropathy and endocrinopathy-susceptibility to chronic infections syndrome.
Orphanet; 1334; Chronic mucocutaneous candidosis.
Orphanet; 319595; Mendelian susceptibility to mycobacterial diseases due to partial STAT1 deficiency.
Orphanet; 391311; Susceptibility to viral and mycobacterial infections.
PharmGKB; PA36183; -.
eggNOG; KOG3667; Eukaryota.
eggNOG; ENOG410XPN8; LUCA.
GeneTree; ENSGT00760000119236; -.
HOVERGEN; HBG055669; -.
InParanoid; P42224; -.
KO; K11220; -.
OMA; WYNMLTT; -.
OrthoDB; EOG091G03O3; -.
PhylomeDB; P42224; -.
TreeFam; TF318648; -.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-1839117; Signaling by cytosolic FGFR1 fusion mutants.
Reactome; R-HSA-186763; Downstream signal transduction.
Reactome; R-HSA-447115; Interleukin-12 family signaling.
Reactome; R-HSA-6783589; Interleukin-6 family signaling.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-877300; Interferon gamma signaling.
Reactome; R-HSA-877312; Regulation of IFNG signaling.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
Reactome; R-HSA-912694; Regulation of IFNA signaling.
Reactome; R-HSA-982772; Growth hormone receptor signaling.
SignaLink; P42224; -.
SIGNOR; P42224; -.
ChiTaRS; STAT1; human.
EvolutionaryTrace; P42224; -.
GeneWiki; STAT1; -.
GenomeRNAi; 6772; -.
PMAP-CutDB; P42224; -.
PRO; PR:P42224; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115415; -.
CleanEx; HS_STAT1; -.
ExpressionAtlas; P42224; baseline and differential.
Genevisible; P42224; HS.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0035257; F:nuclear hormone receptor binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0070491; F:repressing transcription factor binding; IPI:UniProtKB.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
GO; GO:0000983; F:transcription factor activity, RNA polymerase II core promoter sequence-specific; IDA:BHF-UCL.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0005164; F:tumor necrosis factor receptor binding; IPI:UniProtKB.
GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
GO; GO:0008015; P:blood circulation; ISS:UniProtKB.
GO; GO:0035458; P:cellular response to interferon-beta; IMP:BHF-UCL.
GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:0007259; P:JAK-STAT cascade; IDA:UniProtKB.
GO; GO:0010742; P:macrophage derived foam cell differentiation; IDA:UniProtKB.
GO; GO:0072162; P:metanephric mesenchymal cell differentiation; ISS:UniProtKB.
GO; GO:0072136; P:metanephric mesenchymal cell proliferation involved in metanephros development; ISS:UniProtKB.
GO; GO:0046725; P:negative regulation by virus of viral protein levels in host cell; IMP:AgBase.
GO; GO:0016525; P:negative regulation of angiogenesis; IMP:UniProtKB.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IMP:UniProtKB.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0003340; P:negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis; ISS:UniProtKB.
GO; GO:0072308; P:negative regulation of metanephric nephron tubule epithelial cell differentiation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:UniProtKB.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISS:UniProtKB.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; TAS:Reactome.
GO; GO:0060338; P:regulation of type I interferon-mediated signaling pathway; TAS:Reactome.
GO; GO:0061326; P:renal tubule development; IMP:UniProtKB.
GO; GO:0051591; P:response to cAMP; ISS:UniProtKB.
GO; GO:0034097; P:response to cytokine; ISS:UniProtKB.
GO; GO:0035456; P:response to interferon-beta; IMP:UniProtKB.
GO; GO:0043434; P:response to peptide hormone; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0060337; P:type I interferon signaling pathway; IDA:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd10372; SH2_STAT1; 1.
Gene3D; 1.10.532.10; -; 1.
Gene3D; 2.60.40.630; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR000980; SH2.
InterPro; IPR001217; STAT.
InterPro; IPR035859; STAT1_SH2.
InterPro; IPR022752; STAT1_TAZ2-bd_C.
InterPro; IPR013800; STAT_TF_alpha.
InterPro; IPR015988; STAT_TF_coiled-coil.
InterPro; IPR013801; STAT_TF_DNA-bd.
InterPro; IPR012345; STAT_TF_DNA-bd_sub.
InterPro; IPR013799; STAT_TF_prot_interaction.
PANTHER; PTHR11801; PTHR11801; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF12162; STAT1_TAZ2bind; 1.
Pfam; PF01017; STAT_alpha; 1.
Pfam; PF02864; STAT_bind; 1.
Pfam; PF02865; STAT_int; 1.
SMART; SM00964; STAT_int; 1.
SUPFAM; SSF47655; SSF47655; 1.
SUPFAM; SSF48092; SSF48092; 1.
SUPFAM; SSF49417; SSF49417; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Antiviral defense; Coiled coil; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; DNA-binding;
Host-virus interaction; Isopeptide bond; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; SH2 domain; Transcription;
Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 750 Signal transducer and activator of
transcription 1-alpha/beta.
/FTId=PRO_0000182410.
DOMAIN 573 670 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
COILED 136 317 {ECO:0000269|PubMed:9630226}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 701 701 Phosphotyrosine; by JAK1, JAK2 or TYK2.
{ECO:0000269|PubMed:17561467,
ECO:0000269|PubMed:19088846,
ECO:0000269|PubMed:21135090,
ECO:0000269|PubMed:22065572,
ECO:0000269|PubMed:7657660}.
MOD_RES 708 708 Phosphoserine; by IKKE.
{ECO:0000269|PubMed:22065572}.
MOD_RES 727 727 Phosphoserine; by MAPK14.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15322115,
ECO:0000269|PubMed:17897103,
ECO:0000269|PubMed:21135090,
ECO:0000269|PubMed:22065572,
ECO:0000269|PubMed:7543024}.
MOD_RES 745 745 Phosphoserine; by IKKE. {ECO:0000250}.
CROSSLNK 703 703 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
CROSSLNK 703 703 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 703 703 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
VAR_SEQ 713 750 Missing (in isoform Beta).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.6}.
/FTId=VSP_006282.
VARIANT 30 30 I -> T (in dbSNP:rs34255470).
/FTId=VAR_034521.
VARIANT 165 165 D -> G (in IMD31C; gain of function
mutation associated with increased STAT1
phosphorylation due to impaired nuclear
dephosphorylation; dbSNP:rs387906764).
{ECO:0000269|PubMed:21727188,
ECO:0000269|PubMed:23709754}.
/FTId=VAR_065934.
VARIANT 165 165 D -> H (in IMD31C; dbSNP:rs387906767).
{ECO:0000269|PubMed:21727188}.
/FTId=VAR_065935.
VARIANT 170 170 Y -> N (in IMD31C; dbSNP:rs387906766).
{ECO:0000269|PubMed:21727188}.
/FTId=VAR_065936.
VARIANT 174 174 C -> R (in IMD31C; dbSNP:rs387906763).
{ECO:0000269|PubMed:21727188}.
/FTId=VAR_065937.
VARIANT 179 179 N -> K (in IMD31C; gain of function;
increases transactivation activity in
response to IFNG; dbSNP:rs587777628).
{ECO:0000269|PubMed:23709754}.
/FTId=VAR_075494.
VARIANT 201 201 K -> N (in IMD31B; 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%; dbSNP:rs587776870).
{ECO:0000269|PubMed:20841510}.
/FTId=VAR_065815.
VARIANT 202 202 M -> I (in IMD31C).
{ECO:0000269|PubMed:21727188}.
/FTId=VAR_065938.
VARIANT 202 202 M -> V (in IMD31C; dbSNP:rs387906762).
{ECO:0000269|PubMed:21727188}.
/FTId=VAR_065939.
VARIANT 267 267 A -> V (in IMD31C; dbSNP:rs387906759).
{ECO:0000269|PubMed:21714643,
ECO:0000269|PubMed:21727188}.
/FTId=VAR_065940.
VARIANT 271 271 Q -> P (in IMD31C; dbSNP:rs387906768).
{ECO:0000269|PubMed:21727188}.
/FTId=VAR_065941.
VARIANT 274 274 R -> Q (in IMD31C; gain of function;
increases STAT1 phosphorylation due to
impaired nuclear dephosphorylation;
increases transactivation activity in
response to IFNG; dbSNP:rs387906760).
{ECO:0000269|PubMed:21727188,
ECO:0000269|PubMed:23709754}.
/FTId=VAR_065942.
VARIANT 274 274 R -> W (in IMD31C; gain of function;
increases phosphorylation in response to
IFNG, IFNA and IL27 due to a loss of
dephosphorylation; dbSNP:rs387906758).
{ECO:0000269|PubMed:21714643,
ECO:0000269|PubMed:21727188,
ECO:0000269|PubMed:23709754}.
/FTId=VAR_065943.
VARIANT 278 278 K -> E (in IMD31C; gain of function;
increases phosphorylation in response to
IFNG and IFNA due to a loss of
dephosphorylation; dbSNP:rs863223398).
{ECO:0000269|PubMed:25288569}.
/FTId=VAR_075495.
VARIANT 285 285 Q -> R (in IMD31C; gain of function;
increases transactivation activity in
response to IFNG; dbSNP:rs587777629).
{ECO:0000269|PubMed:23709754}.
/FTId=VAR_075496.
VARIANT 286 286 K -> I (in IMD31C; dbSNP:rs387906761).
{ECO:0000269|PubMed:21727188}.
/FTId=VAR_065944.
VARIANT 288 288 T -> A (in IMD31C; dbSNP:rs387906765).
{ECO:0000269|PubMed:21727188}.
/FTId=VAR_065945.
VARIANT 298 298 K -> N (in IMD31C; gain of function;
increases basal STAT1 phosphorylation
levels which are 10-20 fold higher than
controls after IFNG stimulation).
{ECO:0000269|PubMed:26514428}.
/FTId=VAR_075497.
VARIANT 320 320 E -> Q (in IMD31A; affects the DNA-
binding activity of the protein;
dbSNP:rs137852680).
{ECO:0000269|PubMed:16934001}.
/FTId=VAR_065816.
VARIANT 384 384 G -> D (in IMD31C; gain of function;
increases phosphorylation in response to
IFNG and IFNA due to a loss of
dephosphorylation; dbSNP:rs796065052).
{ECO:0000269|PubMed:25288569}.
/FTId=VAR_075498.
VARIANT 385 385 T -> M (in IMD31C; gain of function;
increases phosphorylation in response to
IFNG, IFNA and IL27 due to a loss of
dephosphorylation; dbSNP:rs587777630).
{ECO:0000269|PubMed:23709754,
ECO:0000269|PubMed:25288569}.
/FTId=VAR_075499.
VARIANT 463 463 Q -> H (in IMD31A; affects the DNA-
binding activity of the protein;
dbSNP:rs137852679).
{ECO:0000269|PubMed:16934001}.
/FTId=VAR_065817.
VARIANT 491 491 P -> A (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036001.
VARIANT 600 600 L -> P (in IMD31B; found in an infant who
died of a viral-like illness associated
with complete STAT1 deficiency;
dbSNP:rs137852678).
{ECO:0000269|PubMed:12590259}.
/FTId=VAR_018265.
VARIANT 637 637 K -> E (in IMD31A; affects both
phosphorylation and DNA-binding activity;
results in impaired STAT1-mediated
cellular response to IFN-gamma and
interleukin-27; dbSNP:rs587777705).
{ECO:0000269|PubMed:22573496}.
/FTId=VAR_068713.
VARIANT 673 673 K -> R (in IMD31A; impairs tyrosine
phosphorylation; results in impaired
STAT1-mediated cellular response to IFN-
gamma and interleukin-27;
dbSNP:rs587777704).
{ECO:0000269|PubMed:22573496}.
/FTId=VAR_068714.
VARIANT 701 701 Y -> C (in IMD31B; disrupts
transactivation activity in response to
IFNG). {ECO:0000269|PubMed:23709754}.
/FTId=VAR_075500.
VARIANT 706 706 L -> S (in IMD31A; 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;
dbSNP:rs137852677).
{ECO:0000269|PubMed:11452125,
ECO:0000269|PubMed:16934001}.
/FTId=VAR_018266.
MUTAGEN 110 110 K->R: Sumoylated.
{ECO:0000269|PubMed:12764129}.
MUTAGEN 701 701 Y->E: Not phosphorylated at S-708 upon
IFNB induction.
{ECO:0000269|PubMed:17897103,
ECO:0000269|PubMed:22065572}.
MUTAGEN 701 701 Y->F: No effect on basal sumoylation.
Enhances sumoylation in the presence of
MAPK stimulation. Phosphorylated at S-708
upon IFNB induction.
{ECO:0000269|PubMed:17897103,
ECO:0000269|PubMed:22065572}.
MUTAGEN 703 703 K->R: Abolishes sumoylation by SUMO1.
Increased IFN-gamma-mediated
transactivation.
{ECO:0000269|PubMed:12764129,
ECO:0000269|PubMed:12855578}.
MUTAGEN 708 708 S->A: Phosphorylated at Y-701 upon IFNB
induction. {ECO:0000269|PubMed:22065572}.
MUTAGEN 708 708 S->D: Not phosphorylated at Y-701 upon
IFNB induction.
{ECO:0000269|PubMed:22065572}.
MUTAGEN 727 727 S->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.
{ECO:0000269|PubMed:15322115,
ECO:0000269|PubMed:17897103,
ECO:0000269|PubMed:22065572}.
MUTAGEN 727 727 S->D: No change in enhancement of MAPK-
induced sumoylation. Basal interaction
with PIAS1. Interaction with PIAS1
increased on MAPK stimulation.
{ECO:0000269|PubMed:15322115,
ECO:0000269|PubMed:17897103,
ECO:0000269|PubMed:22065572}.
MUTAGEN 727 727 S->E: No change in enhancement of MAPK-
induced sumoylation.
{ECO:0000269|PubMed:15322115,
ECO:0000269|PubMed:17897103,
ECO:0000269|PubMed:22065572}.
CONFLICT 46 46 A -> T (in Ref. 2; ADA59516).
{ECO:0000305}.
CONFLICT 307 307 S -> G (in Ref. 4; BAF85293).
{ECO:0000305}.
CONFLICT 718 718 Q -> R (in Ref. 5; CAH18430).
{ECO:0000305}.
HELIX 3 7 {ECO:0000244|PDB:3WWT}.
HELIX 12 21 {ECO:0000244|PDB:3WWT}.
STRAND 23 26 {ECO:0000244|PDB:3WWT}.
HELIX 28 33 {ECO:0000244|PDB:3WWT}.
HELIX 35 40 {ECO:0000244|PDB:3WWT}.
HELIX 43 46 {ECO:0000244|PDB:3WWT}.
HELIX 50 73 {ECO:0000244|PDB:3WWT}.
HELIX 77 94 {ECO:0000244|PDB:3WWT}.
HELIX 99 120 {ECO:0000244|PDB:3WWT}.
HELIX 121 125 {ECO:0000244|PDB:1YVL}.
HELIX 137 179 {ECO:0000244|PDB:1BF5}.
HELIX 189 192 {ECO:0000244|PDB:1YVL}.
HELIX 193 195 {ECO:0000244|PDB:1YVL}.
HELIX 198 247 {ECO:0000244|PDB:1BF5}.
HELIX 257 286 {ECO:0000244|PDB:1BF5}.
HELIX 293 316 {ECO:0000244|PDB:1BF5}.
STRAND 317 321 {ECO:0000244|PDB:1BF5}.
STRAND 334 336 {ECO:0000244|PDB:1BF5}.
STRAND 339 347 {ECO:0000244|PDB:1BF5}.
HELIX 352 354 {ECO:0000244|PDB:1BF5}.
TURN 355 357 {ECO:0000244|PDB:1BF5}.
STRAND 359 365 {ECO:0000244|PDB:1BF5}.
HELIX 370 373 {ECO:0000244|PDB:1BF5}.
STRAND 374 376 {ECO:0000244|PDB:1BF5}.
STRAND 380 382 {ECO:0000244|PDB:1YVL}.
STRAND 386 389 {ECO:0000244|PDB:1BF5}.
STRAND 391 395 {ECO:0000244|PDB:1BF5}.
TURN 396 398 {ECO:0000244|PDB:1BF5}.
STRAND 399 408 {ECO:0000244|PDB:1BF5}.
STRAND 421 425 {ECO:0000244|PDB:1BF5}.
STRAND 433 441 {ECO:0000244|PDB:1BF5}.
STRAND 444 451 {ECO:0000244|PDB:1BF5}.
STRAND 455 460 {ECO:0000244|PDB:1BF5}.
HELIX 461 463 {ECO:0000244|PDB:1BF5}.
HELIX 464 477 {ECO:0000244|PDB:1BF5}.
HELIX 486 488 {ECO:0000244|PDB:1BF5}.
HELIX 495 509 {ECO:0000244|PDB:1BF5}.
HELIX 516 526 {ECO:0000244|PDB:1BF5}.
HELIX 539 543 {ECO:0000244|PDB:1BF5}.
STRAND 550 552 {ECO:0000244|PDB:1BF5}.
HELIX 554 568 {ECO:0000244|PDB:1BF5}.
HELIX 570 574 {ECO:0000244|PDB:1BF5}.
HELIX 584 590 {ECO:0000244|PDB:1BF5}.
TURN 591 593 {ECO:0000244|PDB:1BF5}.
STRAND 601 603 {ECO:0000244|PDB:1BF5}.
STRAND 612 616 {ECO:0000244|PDB:1BF5}.
STRAND 621 624 {ECO:0000244|PDB:1BF5}.
STRAND 627 631 {ECO:0000244|PDB:1YVL}.
HELIX 636 640 {ECO:0000244|PDB:1BF5}.
HELIX 644 649 {ECO:0000244|PDB:1BF5}.
STRAND 657 659 {ECO:0000244|PDB:1BF5}.
HELIX 673 677 {ECO:0000244|PDB:1BF5}.
TURN 678 680 {ECO:0000244|PDB:1BF5}.
HELIX 728 738 {ECO:0000244|PDB:2KA6}.
TURN 739 742 {ECO:0000244|PDB:2KA6}.
HELIX 743 745 {ECO:0000244|PDB:2KA6}.
TURN 746 748 {ECO:0000244|PDB:2KA6}.
SEQUENCE 750 AA; 87335 MW; 054A813522364BA6 CRC64;
MSQWYELQQL DSKFLEQVHQ LYDDSFPMEI RQYLAQWLEK QDWEHAANDV SFATIRFHDL
LSQLDDQYSR FSLENNFLLQ HNIRKSKRNL QDNFQEDPIQ MSMIIYSCLK EERKILENAQ
RFNQAQSGNI QSTVMLDKQK ELDSKVRNVK DKVMCIEHEI KSLEDLQDEY DFKCKTLQNR
EHETNGVAKS DQKQEQLLLK KMYLMLDNKR KEVVHKIIEL LNVTELTQNA LINDELVEWK
RRQQSACIGG PPNACLDQLQ NWFTIVAESL QQVRQQLKKL EELEQKYTYE HDPITKNKQV
LWDRTFSLFQ QLIQSSFVVE RQPCMPTHPQ RPLVLKTGVQ FTVKLRLLVK LQELNYNLKV
KVLFDKDVNE RNTVKGFRKF NILGTHTKVM NMEESTNGSL AAEFRHLQLK EQKNAGTRTN
EGPLIVTEEL HSLSFETQLC QPGLVIDLET TSLPVVVISN VSQLPSGWAS ILWYNMLVAE
PRNLSFFLTP PCARWAQLSE VLSWQFSSVT KRGLNVDQLN MLGEKLLGPN ASPDGLIPWT
RFCKENINDK NFPFWLWIES ILELIKKHLL PLWNDGCIMG FISKERERAL LKDQQPGTFL
LRFSESSREG AITFTWVERS QNGGEPDFHA VEPYTKKELS AVTFPDIIRN YKVMAAENIP
ENPLKYLYPN IDKDHAFGKY YSRPKEAPEP MELDGPKGTG YIKTELISVS EVHPSRLQTT
DNLLPMSPEE FDEVSRIVGS VEFDSMMNTV


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