PIAS1_HUMAN
ID PIAS1_HUMAN Reviewed; 651 AA.
AC O75925; B2RB67; B3KSY9; C5J4B4; Q147X4; Q99751; Q9UN02;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=E3 SUMO-protein ligase PIAS1;
DE EC=2.3.2.-;
DE AltName: Full=DEAD/H box-binding protein 1;
DE AltName: Full=E3 SUMO-protein transferase PIAS1 {ECO:0000305};
DE AltName: Full=Gu-binding protein;
DE Short=GBP;
DE AltName: Full=Protein inhibitor of activated STAT protein 1;
DE AltName: Full=RNA helicase II-binding protein;
GN Name=PIAS1; Synonyms=DDXBP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH STAT1.
RC TISSUE=B-cell;
RX PubMed=9724754; DOI=10.1073/pnas.95.18.10626;
RA Liu B., Liao J., Rao X., Kushner S.A., Chung C.D., Chang D.D., Shuai K.;
RT "Inhibition of Stat1-mediated gene activation by PIAS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:10626-10631(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10628744; DOI=10.1210/mend.14.1.0408;
RA Tan J., Hall S.H., Hamil K.G., Grossman G., Petrusz P., Liao J., Shuai K.,
RA French F.S.;
RT "Protein inhibitor of activated STAT-1 (signal transducer and activator of
RT transcription-1) is a nuclear receptor coregulator expressed in human
RT testis.";
RL Mol. Endocrinol. 14:14-26(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=19906316; DOI=10.1186/1471-2164-10-518;
RA Wang P., Yu P., Gao P., Shi T., Ma D.;
RT "Discovery of novel human transcript variants by analysis of intronic
RT single-block EST with polyadenylation site.";
RL BMC Genomics 10:518-518(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Amygdala, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-651 (ISOFORM 1), INTERACTION WITH DDX21,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=B-cell;
RX PubMed=9177271; DOI=10.1006/bbrc.1997.6642;
RA Valdez B.C., Henning D., Perlaky L., Busch R.K., Busch H.;
RT "Cloning and characterization of Gu/RH-II binding protein.";
RL Biochem. Biophys. Res. Commun. 234:335-340(1997).
RN [8]
RP INTERACTION WITH CSRP2.
RX PubMed=11672422; DOI=10.1042/0264-6021:3590485;
RA Weiskirchen R., Moser M., Weiskirchen S., Erdel M., Dahmen S., Buettner R.,
RA Gressner A.M.;
RT "LIM-domain protein cysteine- and glycine-rich protein 2 (CRP2) is a novel
RT marker of hepatic stellate cells and binding partner of the protein
RT inhibitor of activated STAT1.";
RL Biochem. J. 359:485-496(2001).
RN [9]
RP INTERACTION WITH UBE2I; SUMO1 AND TP53, AND MUTAGENESIS OF CYS-351.
RX PubMed=11583632; DOI=10.1016/s1097-2765(01)00349-5;
RA Kahyo T., Nishida T., Yasuda H.;
RT "Involvement of PIAS1 in the sumoylation of tumor suppressor p53.";
RL Mol. Cell 8:713-718(2001).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=11439351; DOI=10.1038/sj.onc.1204489;
RA Gross M., Liu B., Tan J.-A., French F.S., Carey M., Shuai K.;
RT "Distinct effects of PIAS proteins on androgen-mediated gene activation in
RT prostate cancer cells.";
RL Oncogene 20:3880-3887(2001).
RN [11]
RP INTERACTION WITH AXIN1.
RX PubMed=12223491; DOI=10.1074/jbc.m208099200;
RA Rui H.L., Fan E., Zhou H.M., Xu Z., Zhang Y., Lin S.C.;
RT "SUMO-1 modification of the C-terminal KVEKVD of Axin is required for JNK
RT activation but has no effect on Wnt signaling.";
RL J. Biol. Chem. 277:42981-42986(2002).
RN [12]
RP SUMOYLATION OF MDM2, AND SUBCELLULAR LOCATION.
RX PubMed=12393906; DOI=10.1074/jbc.m208319200;
RA Miyauchi Y., Yogosawa S., Honda R., Nishida T., Yasuda H.;
RT "Sumoylation of Mdm2 by protein inhibitor of activated STAT (PIAS) and
RT RanBP2 enzymes.";
RL J. Biol. Chem. 277:50131-50136(2002).
RN [13]
RP INTERACTION WITH SP3 AND UBE2I.
RX PubMed=12356736; DOI=10.1093/emboj/cdf510;
RA Sapetschnig A., Rischitor G., Braun H., Doll A., Schergaut M., Melchior F.,
RA Suske G.;
RT "Transcription factor Sp3 is silenced through SUMO modification by PIAS1.";
RL EMBO J. 21:5206-5215(2002).
RN [14]
RP INTERACTION WITH JUN AND TP53, AND SUMOYLATION.
RX PubMed=11867732; DOI=10.1073/pnas.052559499;
RA Schmidt D., Mueller S.;
RT "Members of the PIAS family act as SUMO ligases for c-Jun and p53 and
RT repress p53 activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2872-2877(2002).
RN [15]
RP INTERACTION WITH SATB2.
RX PubMed=14701874; DOI=10.1101/gad.1153003;
RA Dobreva G., Dambacher J., Grosschedl R.;
RT "SUMO modification of a novel MAR-binding protein, SATB2, modulates
RT immunoglobulin mu gene expression.";
RL Genes Dev. 17:3048-3061(2003).
RN [16]
RP FUNCTION, AND INTERACTION WITH PTK2/FAK1.
RX PubMed=14500712; DOI=10.1074/jbc.m308562200;
RA Kadare G., Toutant M., Formstecher E., Corvol J.C., Carnaud M.,
RA Boutterin M.C., Girault J.A.;
RT "PIAS1-mediated sumoylation of focal adhesion kinase activates its
RT autophosphorylation.";
RL J. Biol. Chem. 278:47434-47440(2003).
RN [17]
RP INTERACTION WITH PLAG1.
RX PubMed=15208321; DOI=10.1074/jbc.m401753200;
RA Van Dyck F., Delvaux E.L.D., Van de Ven W.J.M., Chavez M.V.;
RT "Repression of the transactivating capacity of the oncoprotein PLAG1 by
RT SUMOylation.";
RL J. Biol. Chem. 279:36121-36131(2004).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [19]
RP INTERACTION WITH KLF8.
RX PubMed=16617055; DOI=10.1074/jbc.m513135200;
RA Wei H., Wang X., Gan B., Urvalek A.M., Melkoumian Z.K., Guan J.-L.,
RA Zhao J.;
RT "Sumoylation delimits KLF8 transcriptional activity associated with the
RT cell cycle regulation.";
RL J. Biol. Chem. 281:16664-16671(2006).
RN [20]
RP INTERACTION WITH CHUK.
RX PubMed=17540171; DOI=10.1016/j.cell.2007.03.056;
RA Liu B., Yang Y., Chernishof V., Loo R.R., Jang H., Tahk S., Yang R.,
RA Mink S., Shultz D., Bellone C.J., Loo J.A., Shuai K.;
RT "Proinflammatory stimuli induce IKKalpha-mediated phosphorylation of PIAS1
RT to restrict inflammation and immunity.";
RL Cell 129:903-914(2007).
RN [21]
RP INTERACTION WITH DDX5.
RX PubMed=17369852; DOI=10.1038/sj.onc.1210387;
RA Jacobs A.M., Nicol S.M., Hislop R.G., Jaffray E.G., Hay R.T.,
RA Fuller-Pace F.V.;
RT "SUMO modification of the DEAD box protein p68 modulates its
RT transcriptional activity and promotes its interaction with HDAC1.";
RL Oncogene 26:5866-5876(2007).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503 AND SER-522, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [23]
RP RETRACTED PAPER.
RX PubMed=19136629; DOI=10.1101/gad.489409;
RA Weber S., Maass F., Schuemann M., Krause E., Suske G., Bauer U.M.;
RT "PRMT1-mediated arginine methylation of PIAS1 regulates STAT1 signaling.";
RL Genes Dev. 23:118-132(2009).
RN [24]
RP RETRACTION NOTICE OF PUBMED:19136629.
RX PubMed=21724836;
RA Weber S., Maass F., Schuemann M., Krause E., Suske G., Bauer U.M.;
RT "Retraction. PRMT1-mediated arginine methylation of PIAS1 regulates STAT1
RT signaling.";
RL Genes Dev. 25:1451-1451(2011).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503 AND SER-510, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [26]
RP INTERACTION WITH EBOLAVIRUS VP35 (MICROBIAL INFECTION).
RX PubMed=19557165; DOI=10.1371/journal.ppat.1000493;
RA Chang T.H., Kubota T., Matsuoka M., Jones S., Bradfute S.B., Bray M.,
RA Ozato K.;
RT "Ebola Zaire virus blocks type I interferon production by exploiting the
RT host SUMO modification machinery.";
RL PLoS Pathog. 5:e1000493-e1000493(2009).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [28]
RP FUNCTION, AND INTERACTION WITH MTA1.
RX PubMed=21965678; DOI=10.1074/jbc.m111.267237;
RA Cong L., Pakala S.B., Ohshiro K., Li D.Q., Kumar R.;
RT "SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1
RT (MTA1) synergistically regulate its transcriptional repressor function.";
RL J. Biol. Chem. 286:43793-43808(2011).
RN [29]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485; SER-488 AND SER-503, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467; SER-468 AND SER-503, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [32]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-46 AND LYS-238, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [33]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-46; LYS-137 AND LYS-238, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [34]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-46 AND LYS-137, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [35]
RP INTERACTION WITH SUMO1P1/SUMO5.
RX PubMed=27211601; DOI=10.1038/srep26509;
RA Liang Y.C., Lee C.C., Yao Y.L., Lai C.C., Schmitz M.L., Yang W.M.;
RT "SUMO5, a novel poly-sumo isoform, regulates pml nuclear bodies.";
RL Sci. Rep. 6:26509-26509(2016).
RN [36]
RP INTERACTION WITH PRDM1.
RX PubMed=28842558; DOI=10.1038/s41467-017-00476-w;
RA Wang W.F., Yan L., Liu Z., Liu L.X., Lin J., Liu Z.Y., Chen X.P., Zhang W.,
RA Xu Z.Z., Shi T., Li J.M., Zhao Y.L., Meng G., Xia Y., Li J.Y., Zhu J.;
RT "HSP70-Hrd1 axis precludes the oncorepressor potential of N-terminal
RT misfolded Blimp-1s in lymphoma cells.";
RL Nat. Commun. 8:363-363(2017).
RN [37]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-40; LYS-46; LYS-137; LYS-238;
RP LYS-453 AND LYS-493, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [38]
RP STRUCTURE BY NMR OF 1-65, AND INTERACTION WITH TP53 AND DNA-BINDING.
RX PubMed=15133049; DOI=10.1074/jbc.m403561200;
RA Okubo S., Hara F., Tsuchida Y., Shimotakahara S., Suzuki S., Hatanaka H.,
RA Yokoyama S., Tanaka H., Yasuda H., Shindo H.;
RT "NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its
RT interaction with tumor suppressor p53 and A/T-rich DNA oligomers.";
RL J. Biol. Chem. 279:31455-31461(2004).
CC -!- FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO)
CC ligase, stabilizing the interaction between UBE2I and the substrate,
CC and as a SUMO-tethering factor. Plays a crucial role as a
CC transcriptional coregulation in various cellular pathways, including
CC the STAT pathway, the p53 pathway and the steroid hormone signaling
CC pathway. In vitro, binds A/T-rich DNA. The effects of this
CC transcriptional coregulation, transactivation or silencing, may vary
CC depending upon the biological context. Sumoylates PML (at'Lys-65' and
CC 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated
CC degradation. PIAS1-mediated sumoylation of PML promotes its interaction
CC with CSNK2A1/CK2 which in turn promotes PML phosphorylation and
CC degradation (By similarity). Enhances the sumoylation of MTA1 and may
CC participate in its paralog-selective sumoylation. Plays a dynamic role
CC in adipogenesis by promoting the SUMOylation and degradation of CEBPB
CC (By similarity). {ECO:0000250|UniProtKB:O88907,
CC ECO:0000269|PubMed:14500712, ECO:0000269|PubMed:21965678}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Interacts with NCOA2 and AR. Interacts with NR2C1; the
CC interaction promotes its sumoylation (By similarity). Interacts with
CC DDX21, CSRP2, AXIN1, JUN, UBE2I, SUMO1, SATB2, PLAG1, TP53 and STAT1
CC (dimer), following IFNA1-stimulation. Interacts with SP3
CC (preferentially when SUMO-modified). Interacts with KLF8; the
CC interaction results in SUMO ligation and repression of KLF8
CC transcriptional activity and of its cell cycle progression into G(1)
CC phase. Interacts with CHUK/IKKA; this interaction induces PIAS1
CC phosphorylation. Interacts with PTK2/FAK1; the interaction promotes its
CC sumoylation. Interacts with DDX5. Interacts with PML (By similarity).
CC Interacts with MTA1. Interacts with SUMO1P1/SUMO5 (PubMed:27211601).
CC Interacts with PRDM1/Blimp-1 (PubMed:28842558). {ECO:0000250,
CC ECO:0000269|PubMed:11583632, ECO:0000269|PubMed:11672422,
CC ECO:0000269|PubMed:11867732, ECO:0000269|PubMed:12223491,
CC ECO:0000269|PubMed:12356736, ECO:0000269|PubMed:14500712,
CC ECO:0000269|PubMed:14701874, ECO:0000269|PubMed:15133049,
CC ECO:0000269|PubMed:15208321, ECO:0000269|PubMed:16617055,
CC ECO:0000269|PubMed:17369852, ECO:0000269|PubMed:17540171,
CC ECO:0000269|PubMed:21965678, ECO:0000269|PubMed:27211601,
CC ECO:0000269|PubMed:28842558, ECO:0000269|PubMed:9177271,
CC ECO:0000269|PubMed:9724754}.
CC -!- SUBUNIT: (Microbial infection) Interacts with ebolavirus VP35; this
CC interaction mediates the sumoylation of IRF7 and contributes to the
CC viral inhibition of IFN-type I production.
CC {ECO:0000269|PubMed:19557165}.
CC -!- INTERACTION:
CC O75925; P01023: A2M; NbExp=3; IntAct=EBI-629434, EBI-640741;
CC O75925; A0A0S2Z5Q7: ALS2; NbExp=3; IntAct=EBI-629434, EBI-25928834;
CC O75925; Q92870-2: APBB2; NbExp=3; IntAct=EBI-629434, EBI-21535880;
CC O75925; P45381: ASPA; NbExp=3; IntAct=EBI-629434, EBI-750475;
CC O75925; P54253: ATXN1; NbExp=7; IntAct=EBI-629434, EBI-930964;
CC O75925; Q9UBB4: ATXN10; NbExp=3; IntAct=EBI-629434, EBI-702390;
CC O75925; P54252: ATXN3; NbExp=9; IntAct=EBI-629434, EBI-946046;
CC O75925; Q9UKL3: CASP8AP2; NbExp=4; IntAct=EBI-629434, EBI-2339650;
CC O75925; P48643: CCT5; NbExp=3; IntAct=EBI-629434, EBI-355710;
CC O75925; G5E9A7: DMWD; NbExp=3; IntAct=EBI-629434, EBI-10976677;
CC O75925; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-629434, EBI-21603100;
CC O75925; Q13216-2: ERCC8; NbExp=3; IntAct=EBI-629434, EBI-16466949;
CC O75925; Q16595: FXN; NbExp=3; IntAct=EBI-629434, EBI-949340;
CC O75925; Q53GS7: GLE1; NbExp=3; IntAct=EBI-629434, EBI-1955541;
CC O75925; P28799: GRN; NbExp=3; IntAct=EBI-629434, EBI-747754;
CC O75925; P07686: HEXB; NbExp=3; IntAct=EBI-629434, EBI-7133736;
CC O75925; P28358: HOXD10; NbExp=3; IntAct=EBI-629434, EBI-12690664;
CC O75925; P04792: HSPB1; NbExp=3; IntAct=EBI-629434, EBI-352682;
CC O75925; O43464: HTRA2; NbExp=3; IntAct=EBI-629434, EBI-517086;
CC O75925; P42858: HTT; NbExp=19; IntAct=EBI-629434, EBI-466029;
CC O75925; O60333-2: KIF1B; NbExp=3; IntAct=EBI-629434, EBI-10975473;
CC O75925; P02545: LMNA; NbExp=3; IntAct=EBI-629434, EBI-351935;
CC O75925; P02545-2: LMNA; NbExp=3; IntAct=EBI-629434, EBI-351953;
CC O75925; Q9UIS9: MBD1; NbExp=3; IntAct=EBI-629434, EBI-867196;
CC O75925; P51608: MECP2; NbExp=3; IntAct=EBI-629434, EBI-1189067;
CC O75925; P19404: NDUFV2; NbExp=3; IntAct=EBI-629434, EBI-713665;
CC O75925; P35240: NF2; NbExp=3; IntAct=EBI-629434, EBI-1014472;
CC O75925; P35240-4: NF2; NbExp=3; IntAct=EBI-629434, EBI-1014514;
CC O75925; P29474: NOS3; NbExp=3; IntAct=EBI-629434, EBI-1391623;
CC O75925; O43933: PEX1; NbExp=3; IntAct=EBI-629434, EBI-988601;
CC O75925; O00628: PEX7; NbExp=3; IntAct=EBI-629434, EBI-5238811;
CC O75925; O14832: PHYH; NbExp=3; IntAct=EBI-629434, EBI-721853;
CC O75925; P50897: PPT1; NbExp=3; IntAct=EBI-629434, EBI-1237011;
CC O75925; O75626: PRDM1; NbExp=2; IntAct=EBI-629434, EBI-948789;
CC O75925; P05129: PRKCG; NbExp=3; IntAct=EBI-629434, EBI-949799;
CC O75925; P41219: PRPH; NbExp=3; IntAct=EBI-629434, EBI-752074;
CC O75925; Q16637: SMN2; NbExp=3; IntAct=EBI-629434, EBI-395421;
CC O75925; P37840: SNCA; NbExp=3; IntAct=EBI-629434, EBI-985879;
CC O75925; Q16143: SNCB; NbExp=3; IntAct=EBI-629434, EBI-727106;
CC O75925; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-629434, EBI-5235340;
CC O75925; Q6NUL7: SPTLC1; NbExp=3; IntAct=EBI-629434, EBI-25912847;
CC O75925; Q9NUW8: TDP1; NbExp=3; IntAct=EBI-629434, EBI-2902553;
CC O75925; P04637: TP53; NbExp=4; IntAct=EBI-629434, EBI-366083;
CC O75925; O76024: WFS1; NbExp=3; IntAct=EBI-629434, EBI-720609;
CC O75925; P54577: YARS1; NbExp=3; IntAct=EBI-629434, EBI-1048893;
CC O75925; Q9P1N4; NbExp=3; IntAct=EBI-629434, EBI-25878161;
CC O75925; PRO_0000037946 [P29991]; Xeno; NbExp=3; IntAct=EBI-629434, EBI-8826488;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:12393906,
CC ECO:0000269|PubMed:9177271}. Nucleus, PML body {ECO:0000250}.
CC Note=Interaction with CSRP2 may induce a partial redistribution along
CC the cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O75925-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75925-2; Sequence=VSP_056219;
CC Name=3;
CC IsoId=O75925-3; Sequence=VSP_057195, VSP_057196;
CC -!- TISSUE SPECIFICITY: Expressed in numerous tissues with highest level in
CC testis. {ECO:0000269|PubMed:11439351, ECO:0000269|PubMed:9177271}.
CC -!- DOMAIN: The LXXLL motif is a transcriptional coregulator signature.
CC -!- DOMAIN: The SP-RING-type domain is required for promoting EKLF
CC sumoylation. {ECO:0000250}.
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:11867732,
CC ECO:0000269|PubMed:12393906}.
CC -!- SIMILARITY: Belongs to the PIAS family. {ECO:0000305}.
CC -!- CAUTION: A paper showing that PRMT1-mediated arginine methylation of
CC PIAS1 regulates STAT1 signaling has been retracted, because some of the
CC data was found to be deliberately falsified.
CC {ECO:0000305|PubMed:19136629, ECO:0000305|PubMed:21724836}.
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DR EMBL; AF077951; AAC36702.1; -; mRNA.
DR EMBL; AF167160; AAD49722.1; -; mRNA.
DR EMBL; FJ997900; ACR77525.1; -; mRNA.
DR EMBL; AK094641; BAG52901.1; -; mRNA.
DR EMBL; AK314515; BAG37114.1; -; mRNA.
DR EMBL; AC107871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC135628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC118587; AAI18588.1; -; mRNA.
DR EMBL; BC121797; AAI21798.1; -; mRNA.
DR EMBL; U78524; AAB58488.1; -; mRNA.
DR CCDS; CCDS45290.1; -. [O75925-1]
DR CCDS; CCDS81902.1; -. [O75925-2]
DR RefSeq; NP_001307616.1; NM_001320687.1. [O75925-2]
DR RefSeq; NP_057250.1; NM_016166.2. [O75925-1]
DR RefSeq; XP_016878177.1; XM_017022688.1. [O75925-2]
DR PDB; 1V66; NMR; -; A=1-65.
DR PDBsum; 1V66; -.
DR AlphaFoldDB; O75925; -.
DR BMRB; O75925; -.
DR SMR; O75925; -.
DR BioGRID; 114124; 156.
DR CORUM; O75925; -.
DR DIP; DIP-5970N; -.
DR ELM; O75925; -.
DR IntAct; O75925; 111.
DR MINT; O75925; -.
DR STRING; 9606.ENSP00000249636; -.
DR iPTMnet; O75925; -.
DR PhosphoSitePlus; O75925; -.
DR BioMuta; PIAS1; -.
DR EPD; O75925; -.
DR jPOST; O75925; -.
DR MassIVE; O75925; -.
DR MaxQB; O75925; -.
DR PaxDb; O75925; -.
DR PeptideAtlas; O75925; -.
DR PRIDE; O75925; -.
DR ProteomicsDB; 3657; -.
DR ProteomicsDB; 50293; -. [O75925-1]
DR Antibodypedia; 26284; 370 antibodies from 35 providers.
DR DNASU; 8554; -.
DR Ensembl; ENST00000249636.11; ENSP00000249636.6; ENSG00000033800.14. [O75925-1]
DR Ensembl; ENST00000545237.1; ENSP00000438574.1; ENSG00000033800.14. [O75925-2]
DR GeneID; 8554; -.
DR KEGG; hsa:8554; -.
DR MANE-Select; ENST00000249636.11; ENSP00000249636.6; NM_016166.3; NP_057250.1.
DR UCSC; uc002aqz.4; human. [O75925-1]
DR CTD; 8554; -.
DR DisGeNET; 8554; -.
DR GeneCards; PIAS1; -.
DR HGNC; HGNC:2752; PIAS1.
DR HPA; ENSG00000033800; Low tissue specificity.
DR MIM; 603566; gene.
DR neXtProt; NX_O75925; -.
DR OpenTargets; ENSG00000033800; -.
DR PharmGKB; PA33285; -.
DR VEuPathDB; HostDB:ENSG00000033800; -.
DR eggNOG; KOG2169; Eukaryota.
DR GeneTree; ENSGT01030000234539; -.
DR HOGENOM; CLU_020768_3_0_1; -.
DR InParanoid; O75925; -.
DR OMA; CFVSKQM; -.
DR OrthoDB; 1205949at2759; -.
DR PhylomeDB; O75925; -.
DR TreeFam; TF323787; -.
DR PathwayCommons; O75925; -.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-HSA-3232118; SUMOylation of transcription factors.
DR Reactome; R-HSA-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-HSA-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-HSA-877312; Regulation of IFNG signaling.
DR SignaLink; O75925; -.
DR SIGNOR; O75925; -.
DR UniPathway; UPA00886; -.
DR BioGRID-ORCS; 8554; 78 hits in 1057 CRISPR screens.
DR ChiTaRS; PIAS1; human.
DR EvolutionaryTrace; O75925; -.
DR GeneWiki; PIAS1; -.
DR GenomeRNAi; 8554; -.
DR Pharos; O75925; Tbio.
DR PRO; PR:O75925; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O75925; protein.
DR Bgee; ENSG00000033800; Expressed in secondary oocyte and 213 other tissues.
DR ExpressionAtlas; O75925; baseline and differential.
DR Genevisible; O75925; HS.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0061665; F:SUMO ligase activity; IDA:UniProtKB.
DR GO; GO:0019789; F:SUMO transferase activity; EXP:Reactome.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0033235; P:positive regulation of protein sumoylation; IDA:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; IDA:BHF-UCL.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; TAS:ProtInc.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 2.60.120.780; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR027227; PIAS1.
DR InterPro; IPR023321; PINIT.
DR InterPro; IPR038654; PINIT_sf.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10782:SF11; PTHR10782:SF11; 1.
DR Pfam; PF14324; PINIT; 1.
DR Pfam; PF02891; zf-MIZ; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS51466; PINIT; 1.
DR PROSITE; PS50800; SAP; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; DNA-binding;
KW Host-virus interaction; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..651
FT /note="E3 SUMO-protein ligase PIAS1"
FT /id="PRO_0000218974"
FT DOMAIN 11..45
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 124..288
FT /note="PINIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00799"
FT REPEAT 520..523
FT /note="1"
FT REPEAT 557..560
FT /note="2"
FT REPEAT 598..601
FT /note="3; approximate"
FT REPEAT 612..615
FT /note="4; approximate"
FT ZN_FING 320..405
FT /note="SP-RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT REGION 462..473
FT /note="SUMO1-binding"
FT /evidence="ECO:0000250"
FT REGION 465..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..615
FT /note="4 X 4 AA repeats of N-T-S-L"
FT REGION 599..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 19..23
FT /note="LXXLL motif"
FT MOTIF 56..64
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 368..380
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 480..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88907"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 487
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O88907"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 40
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 46
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 137
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 238
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 453
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 493
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..7
FT /note="MADSAEL -> MFTLQDSYV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056219"
FT VAR_SEQ 312..325
FT /note="IKEKLTADPDSEIA -> STYDKLISLIQLFC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19906316"
FT /id="VSP_057195"
FT VAR_SEQ 326..651
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19906316"
FT /id="VSP_057196"
FT MUTAGEN 351
FT /note="C->A,S: Loss of UBE2I-binding; almost complete loss
FT of promotion of TP53 sumoylation; no loss of SUMO1- and
FT TP53-binding."
FT /evidence="ECO:0000269|PubMed:11583632"
FT CONFLICT 119
FT /note="E -> K (in Ref. 1; AAC36702)"
FT /evidence="ECO:0000305"
FT CONFLICT 266..268
FT /note="IVV -> MC (in Ref. 1; AAC36702)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="S -> T (in Ref. 6; AAB58488)"
FT /evidence="ECO:0000305"
FT HELIX 6..11
FT /evidence="ECO:0007829|PDB:1V66"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:1V66"
FT HELIX 34..46
FT /evidence="ECO:0007829|PDB:1V66"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:1V66"
SQ SEQUENCE 651 AA; 71836 MW; AA69338221124119 CRC64;
MADSAELKQM VMSLRVSELQ VLLGYAGRNK HGRKHELLTK ALHLLKAGCS PAVQMKIKEL
YRRRFPQKIM TPADLSIPNV HSSPMPATLS PSTIPQLTYD GHPASSPLLP VSLLGPKHEL
ELPHLTSALH PVHPDIKLQK LPFYDLLDEL IKPTSLASDN SQRFRETCFA FALTPQQVQQ
ISSSMDISGT KCDFTVQVQL RFCLSETSCP QEDHFPPNLC VKVNTKPCSL PGYLPPTKNG
VEPKRPSRPI NITSLVRLST TVPNTIVVSW TAEIGRNYSM AVYLVKQLSS TVLLQRLRAK
GIRNPDHSRA LIKEKLTADP DSEIATTSLR VSLLCPLGKM RLTIPCRALT CSHLQCFDAT
LYIQMNEKKP TWVCPVCDKK APYEHLIIDG LFMEILKYCT DCDEIQFKED GTWAPMRSKK
EVQEVSASYN GVDGCLSSTL EHQVASHHQS SNKNKKVEVI DLTIDSSSDE EEEEPSAKRT
CPSLSPTSPL NNKGILSLPH QASPVSRTPS LPAVDTSYIN TSLIQDYRHP FHMTPMPYDL
QGLDFFPFLS GDNQHYNTSL LAAAAAAVSD DQDLLHSSRF FPYTSSQMFL DQLSAGGSTS
LPTTNGSSSG SNSSLVSSNS LRESHSHTVT NRSSTDTASI FGIIPDIISL D
