CBX5_HUMAN
ID CBX5_HUMAN Reviewed; 191 AA.
AC P45973; B2R8T9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Chromobox protein homolog 5;
DE AltName: Full=Antigen p25;
DE AltName: Full=Heterochromatin protein 1 homolog alpha;
DE Short=HP1 alpha;
GN Name=CBX5; Synonyms=HP1A;
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].
RX PubMed=8505380; DOI=10.1242/jcs.104.2.573;
RA Saunders W.S., Chue C., Goebl M., Craig C., Clark R.F., Powers J.A.,
RA Eissenberg J.C., Elgin S.C.R., Rothfield N.F., Earnshaw W.C.;
RT "Molecular cloning of a human homologue of Drosophila heterochromatin
RT protein HP1 using anti-centromere autoantibodies with anti-chromo
RT specificity.";
RL J. Cell Sci. 104:573-582(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-191.
RX PubMed=8663349; DOI=10.1074/jbc.271.25.14653;
RA Ye Q., Worman H.J.;
RT "Interaction between an integral protein of the nuclear envelope inner
RT membrane and human chromodomain proteins homologous to Drosophila HP1.";
RL J. Biol. Chem. 271:14653-14656(1996).
RN [6]
RP PROTEIN SEQUENCE OF 33-40; 56-68; 126-154 AND 160-184, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP INTERACTION WITH LBR AND CBX3.
RX PubMed=9169472; DOI=10.1074/jbc.272.23.14983;
RA Ye Q., Callebaut I., Pezhman A., Courvalin J.-C., Worman H.J.;
RT "Domain-specific interactions of human HP1-type chromodomain proteins and
RT inner nuclear membrane protein LBR.";
RL J. Biol. Chem. 272:14983-14989(1997).
RN [8]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=10460410; DOI=10.1007/s004120050372;
RA Minc E., Allory Y., Worman H.J., Courvalin J.-C., Buendia B.;
RT "Localization and phosphorylation of HP1 proteins during the cell cycle in
RT mammalian cells.";
RL Chromosoma 108:220-234(1999).
RN [9]
RP INTERACTION WITH TRIM24.
RX PubMed=11313457; DOI=10.1128/mcb.21.10.3314-3324.2001;
RA Seeler J.-S., Marchio A., Losson R., Desterro J.M.P., Hay R.T., Chambon P.,
RA Dejean A.;
RT "Common properties of nuclear protein SP100 and TIF1alpha chromatin factor:
RT role of SUMO modification.";
RL Mol. Cell. Biol. 21:3314-3324(2001).
RN [10]
RP INTERACTION WITH HISTONE H3 LYS-9.
RX PubMed=11242053; DOI=10.1038/35065132;
RA Lachner M., O'Carroll D., Rea S., Mechtler K., Jenuwein T.;
RT "Methylation of histone H3 lysine 9 creates a binding site for HP1
RT proteins.";
RL Nature 410:116-120(2001).
RN [11]
RP INTERACTION WITH MIS12 AND DSN1.
RX PubMed=15502821; DOI=10.1038/ncb1187;
RA Obuse C., Iwasaki O., Kiyomitsu T., Goshima G., Toyoda Y., Yanagida M.;
RT "A conserved Mis12 centromere complex is linked to heterochromatic HP1 and
RT outer kinetochore protein Zwint-1.";
RL Nat. Cell Biol. 6:1135-1141(2004).
RN [12]
RP INTERACTION WITH ATRX; CHAF1A; LBR; NIPBL; SP100; STAM2 AND TRIM28.
RX PubMed=15882967; DOI=10.1016/j.bbrc.2005.04.016;
RA Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III;
RT "The mammalian heterochromatin protein 1 binds diverse nuclear proteins
RT through a common motif that targets the chromoshadow domain.";
RL Biochem. Biophys. Res. Commun. 331:929-937(2005).
RN [13]
RP INTERACTION WITH JC VIRUS AGNOPROTEIN (MICROBIAL INFECTION).
RX PubMed=15864296; DOI=10.1038/sj.embor.7400406;
RA Okada Y., Suzuki T., Sunden Y., Orba Y., Kose S., Imamoto N., Takahashi H.,
RA Tanaka S., Hall W.W., Nagashima K., Sawa H.;
RT "Dissociation of heterochromatin protein 1 from lamin B receptor induced by
RT human polyomavirus agnoprotein: role in nuclear egress of viral
RT particles.";
RL EMBO Rep. 6:452-457(2005).
RN [14]
RP INTERACTION WITH SETDB1.
RX PubMed=15899859; DOI=10.1128/mcb.25.11.4552-4564.2005;
RA Verschure P.J., van der Kraan I., de Leeuw W., van der Vlag J.,
RA Carpenter A.E., Belmont A.S., van Driel R.;
RT "In vivo HP1 targeting causes large-scale chromatin condensation and
RT enhanced histone lysine methylation.";
RL Mol. Cell. Biol. 25:4552-4564(2005).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-12; SER-13; SER-14
RP AND SER-92, AND 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 [18]
RP INTERACTION WITH HNRNPU, AND SUBCELLULAR LOCATION.
RX PubMed=19617346; DOI=10.1074/jbc.m109.037929;
RA Ameyar-Zazoua M., Souidi M., Fritsch L., Robin P., Thomas A., Hamiche A.,
RA Percipalle P., Ait-Si-Ali S., Harel-Bellan A.;
RT "Physical and functional interaction between heterochromatin protein 1alpha
RT and the RNA-binding protein heterogeneous nuclear ribonucleoprotein U.";
RL J. Biol. Chem. 284:27974-27979(2009).
RN [19]
RP INTERACTION WITH RRP1B.
RX PubMed=19710015; DOI=10.1074/jbc.m109.023457;
RA Crawford N.P., Yang H., Mattaini K.R., Hunter K.W.;
RT "The metastasis efficiency modifier ribosomal RNA processing 1 homolog B
RT (RRP1B) is a chromatin-associated factor.";
RL J. Biol. Chem. 284:28660-28673(2009).
RN [20]
RP FUNCTION, AND HISTONE-BINDING.
RX PubMed=19783980; DOI=10.1038/nature08448;
RA Dawson M.A., Bannister A.J., Gottgens B., Foster S.D., Bartke T.,
RA Green A.R., Kouzarides T.;
RT "JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from chromatin.";
RL Nature 461:819-822(2009).
RN [21]
RP INTERACTION WITH BAHD1.
RX PubMed=19666599; DOI=10.1073/pnas.0901259106;
RA Bierne H., Tham T.N., Batsche E., Dumay A., Leguillou M.,
RA Kerneis-Golsteyn S., Regnault B., Seeler J.S., Muchardt C., Feunteun J.,
RA Cossart P.;
RT "Human BAHD1 promotes heterochromatic gene silencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:13826-13831(2009).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-14; SER-92 AND
RP SER-97, AND 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 [23]
RP INTERACTION WITH CHAMP1 AND POGZ.
RX PubMed=20850016; DOI=10.1016/j.cell.2010.08.020;
RA Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F.,
RA Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M.;
RT "Quantitative interaction proteomics and genome-wide profiling of
RT epigenetic histone marks and their readers.";
RL Cell 142:967-980(2010).
RN [24]
RP RETRACTED PAPER.
RX PubMed=19880879; DOI=10.1074/jbc.m109.065862;
RA Lee S.W., Cho Y.S., Na J.M., Park U.H., Kang M., Kim E.J., Um S.J.;
RT "ASXL1 represses retinoic acid receptor-mediated transcription through
RT associating with HP1 and LSD1.";
RL J. Biol. Chem. 285:18-29(2010).
RN [25]
RP RETRACTION NOTICE OF PUBMED:19880879 NOTICE FOR PUBMED:19880879.
RX PubMed=25750265; DOI=10.1074/jbc.a109.065862;
RA Lee S.W., Cho Y.S., Na J.M., Park U.H., Kang M., Kim E.J., Um S.J.;
RT "Retraction: 'ASXL1 represses retinoic acid receptor-mediated transcription
RT through associating with HP1 and LSD1'.";
RL J. Biol. Chem. 290:6008-6008(2015).
RN [26]
RP INTERACTION WITH POGZ; TRIM28; CHAF1A; NIPBL AND INCENP, AND MUTAGENESIS OF
RP ILE-165 AND TRP-174.
RX PubMed=20562864; DOI=10.1038/ncb2075;
RA Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N.,
RA Kimura H., Obuse C.;
RT "Human POGZ modulates dissociation of HP1alpha from mitotic chromosome arms
RT through Aurora B activation.";
RL Nat. Cell Biol. 12:719-727(2010).
RN [27]
RP UBIQUITINATION.
RX PubMed=20498703; DOI=10.1371/journal.pone.0010620;
RA Chaturvedi P., Parnaik V.K.;
RT "Lamin A rod domain mutants target heterochromatin protein 1alpha and beta
RT for proteasomal degradation by activation of F-box protein, FBXW10.";
RL PLoS ONE 5:E10620-E10620(2010).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-12; SER-13; SER-14;
RP SER-92 AND SER-97, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [30]
RP INTERACTION WITH INCENP, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-174.
RX PubMed=21346195; DOI=10.1091/mbc.e11-01-0009;
RA Kang J., Chaudhary J., Dong H., Kim S., Brautigam C.A., Yu H.;
RT "Mitotic centromeric targeting of HP1 and its binding to Sgo1 are
RT dispensable for sister-chromatid cohesion in human cells.";
RL Mol. Biol. Cell 22:1181-1190(2011).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-14; SER-95 AND
RP SER-97, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [32]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-92 AND SER-95, 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 [34]
RP INTERACTION WITH LRIF1.
RX PubMed=23542155; DOI=10.1038/nsmb.2532;
RA Nozawa R.S., Nagao K., Igami K.T., Shibata S., Shirai N., Nozaki N.,
RA Sado T., Kimura H., Obuse C.;
RT "Human inactive X chromosome is compacted through a PRC2-independent
RT SMCHD1-HBiX1 pathway.";
RL Nat. Struct. Mol. Biol. 20:566-573(2013).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-12; SER-13 AND
RP SER-14, AND 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 [36]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32 AND LYS-102, 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 [37]
RP INTERACTION WITH PRR14.
RX PubMed=25906157; DOI=10.1038/cddis.2015.103;
RA Yang M., Yuan Z.M.;
RT "A novel role of PRR14 in the regulation of skeletal myogenesis.";
RL Cell Death Dis. 6:E1734-E1734(2015).
RN [38]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32 AND LYS-102, 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 [39]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32 AND LYS-102, 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 [40]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-91; LYS-102; LYS-106;
RP LYS-154 AND LYS-184, 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 [41]
RP INTERACTION WITH ZNF263.
RX PubMed=32051553; DOI=10.1038/s41388-020-1206-7;
RA Yu Z., Feng J., Wang W., Deng Z., Zhang Y., Xiao L., Wang Z., Liu C.,
RA Liu Q., Chen S., Wu M.;
RT "The EGFR-ZNF263 signaling axis silences SIX3 in glioblastoma
RT epigenetically.";
RL Oncogene 39:3163-3178(2020).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 18-75 IN COMPLEX WITH
RP TRIMETHYLATED HISTONE H3 PEPTIDE, SUBUNIT, AND X-RAY CRYSTALLOGRAPHY (2.48
RP ANGSTROMS) OF 110-173.
RX PubMed=21047797; DOI=10.1074/jbc.m110.191411;
RA Kaustov L., Ouyang H., Amaya M., Lemak A., Nady N., Duan S., Wasney G.A.,
RA Li Z., Vedadi M., Schapira M., Min J., Arrowsmith C.H.;
RT "Recognition and specificity determinants of the human cbx chromodomains.";
RL J. Biol. Chem. 286:521-529(2011).
RN [43]
RP INTERACTION WITH HP1BP3, AND MUTAGENESIS OF TRP-174.
RX PubMed=20042602; DOI=10.1074/jbc.m109.092833;
RA Hayashihara K., Uchiyama S., Shimamoto S., Kobayashi S., Tomschik M.,
RA Wakamatsu H., No D., Sugahara H., Hori N., Noda M., Ohkubo T.,
RA Zlatanova J., Matsunaga S., Fukui K.;
RT "The middle region of an HP1-binding protein, HP1-BP74, associates with
RT linker DNA at the entry/exit site of nucleosomal DNA.";
RL J. Biol. Chem. 285:6498-6507(2010).
CC -!- FUNCTION: Component of heterochromatin that recognizes and binds
CC histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic
CC repression. In contrast, it is excluded from chromatin when 'Tyr-41' of
CC histone H3 is phosphorylated (H3Y41ph). Can interact with lamin-B
CC receptor (LBR). This interaction can contribute to the association of
CC the heterochromatin with the inner nuclear membrane. Involved in the
CC formation of functional kinetochore through interaction with MIS12
CC complex proteins. {ECO:0000269|PubMed:19783980}.
CC -!- SUBUNIT: Interacts directly with ATRX, CHAF1A, LBR, NIPBL, SP100, STAM2
CC and TRIM28 via the chromoshadow domain (PubMed:15882967,
CC PubMed:9169472). Can interact directly with CBX3 via the chromoshadow
CC domain (PubMed:9169472). Interacts with KMT5B and KMT5C (By
CC similarity). Interacts with HP1BP3 (PubMed:20042602). Interacts with
CC histone H3 methylated at 'Lys-9' (PubMed:11242053, PubMed:21047797).
CC Interacts with BAHD1, MIS12 and DSN1 (PubMed:15502821,
CC PubMed:19666599). Interacts with POGZ; POGZ and PXVXL motif-containing
CC proteins such as INCENP and TRIM28 compete for interaction with CBX5
CC (PubMed:20562864, PubMed:20850016, PubMed:21346195). Interacts with
CC INCENP and TRIM24 (PubMed:11313457). Interacts with CHAMP1
CC (PubMed:20850016). Interacts with PRR14 (via N-terminus)
CC (PubMed:25906157). Interacts with RRP1B (PubMed:19710015). Interacts
CC with HNRNPU (via C-terminus); this interaction is, at least in part,
CC RNA-dependent (PubMed:19617346). Interacts with LRIF1 (via PxVxL motif)
CC (PubMed:23542155). Interacts with ZNF263; recruited to the SIX3
CC promoter along with other proteins involved in chromatin modification
CC and transcriptional corepression where it contributes to
CC transcriptional repression (PubMed:32051553). May form homodimers (By
CC similarity). Interacts with SMYD5 (By similarity).
CC {ECO:0000250|UniProtKB:Q61686, ECO:0000269|PubMed:11242053,
CC ECO:0000269|PubMed:11313457, ECO:0000269|PubMed:15502821,
CC ECO:0000269|PubMed:15882967, ECO:0000269|PubMed:15899859,
CC ECO:0000269|PubMed:19617346, ECO:0000269|PubMed:19666599,
CC ECO:0000269|PubMed:19710015, ECO:0000269|PubMed:20042602,
CC ECO:0000269|PubMed:20562864, ECO:0000269|PubMed:20850016,
CC ECO:0000269|PubMed:21047797, ECO:0000269|PubMed:21346195,
CC ECO:0000269|PubMed:23542155, ECO:0000269|PubMed:25906157,
CC ECO:0000269|PubMed:32051553, ECO:0000269|PubMed:9169472}.
CC -!- SUBUNIT: (Microbial infection) Interacts with JC virus agnoprotein;
CC this interaction induces the dissociation of CBX5 from LBR, resulting
CC in destabilization of the nuclear envelope.
CC {ECO:0000269|PubMed:15864296}.
CC -!- INTERACTION:
CC P45973; Q9H2P0: ADNP; NbExp=3; IntAct=EBI-78219, EBI-1764854;
CC P45973; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-78219, EBI-2875816;
CC P45973; O75143-2: ATG13; NbExp=3; IntAct=EBI-78219, EBI-20151086;
CC P45973; P46100: ATRX; NbExp=2; IntAct=EBI-78219, EBI-396461;
CC P45973; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-78219, EBI-742750;
CC P45973; P45973: CBX5; NbExp=2; IntAct=EBI-78219, EBI-78219;
CC P45973; Q13111: CHAF1A; NbExp=8; IntAct=EBI-78219, EBI-1020839;
CC P45973; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-78219, EBI-9087876;
CC P45973; Q9UMR2: DDX19B; NbExp=3; IntAct=EBI-78219, EBI-719232;
CC P45973; P09471: GNAO1; NbExp=3; IntAct=EBI-78219, EBI-715087;
CC P45973; P84243: H3-3B; NbExp=2; IntAct=EBI-78219, EBI-120658;
CC P45973; Q16695: H3-4; NbExp=2; IntAct=EBI-78219, EBI-358900;
CC P45973; P68431: H3C12; NbExp=11; IntAct=EBI-78219, EBI-79722;
CC P45973; P62805: H4C9; NbExp=3; IntAct=EBI-78219, EBI-302023;
CC P45973; Q9NQS7: INCENP; NbExp=11; IntAct=EBI-78219, EBI-307907;
CC P45973; P28838: LAP3; NbExp=3; IntAct=EBI-78219, EBI-2339312;
CC P45973; Q14739: LBR; NbExp=4; IntAct=EBI-78219, EBI-1055147;
CC P45973; Q8N448: LNX2; NbExp=3; IntAct=EBI-78219, EBI-2340947;
CC P45973; Q5T3J3: LRIF1; NbExp=11; IntAct=EBI-78219, EBI-473196;
CC P45973; Q9UIS9: MBD1; NbExp=6; IntAct=EBI-78219, EBI-867196;
CC P45973; Q14728: MFSD10; NbExp=3; IntAct=EBI-78219, EBI-11337904;
CC P45973; P01106: MYC; NbExp=3; IntAct=EBI-78219, EBI-447544;
CC P45973; Q9BZ95: NSD3; NbExp=2; IntAct=EBI-78219, EBI-3390132;
CC P45973; Q9BZ95-3: NSD3; NbExp=3; IntAct=EBI-78219, EBI-22002759;
CC P45973; Q96IY1: NSL1; NbExp=6; IntAct=EBI-78219, EBI-2554690;
CC P45973; Q9NUD9: PIGV; NbExp=3; IntAct=EBI-78219, EBI-25836582;
CC P45973; Q7Z3K3: POGZ; NbExp=8; IntAct=EBI-78219, EBI-1389308;
CC P45973; Q07869: PPARA; NbExp=3; IntAct=EBI-78219, EBI-78615;
CC P45973; Q9BWN1: PRR14; NbExp=10; IntAct=EBI-78219, EBI-748167;
CC P45973; Q9BQF6: SENP7; NbExp=4; IntAct=EBI-78219, EBI-766251;
CC P45973; Q5FBB7: SGO1; NbExp=4; IntAct=EBI-78219, EBI-989069;
CC P45973; Q8NCS7: SLC44A5; NbExp=3; IntAct=EBI-78219, EBI-21504521;
CC P45973; Q16560-2: SNRNP35; NbExp=3; IntAct=EBI-78219, EBI-12938570;
CC P45973; P23497-2: SP100; NbExp=7; IntAct=EBI-78219, EBI-6589365;
CC P45973; O43463: SUV39H1; NbExp=16; IntAct=EBI-78219, EBI-349968;
CC P45973; O15273: TCAP; NbExp=4; IntAct=EBI-78219, EBI-954089;
CC P45973; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-78219, EBI-765817;
CC P45973; Q13263: TRIM28; NbExp=11; IntAct=EBI-78219, EBI-78139;
CC P45973; Q14191: WRN; NbExp=3; IntAct=EBI-78219, EBI-368417;
CC P45973; P25490: YY1; NbExp=3; IntAct=EBI-78219, EBI-765538;
CC P45973; Q8ND82: ZNF280C; NbExp=3; IntAct=EBI-78219, EBI-8831272;
CC P45973; Q6N043-2: ZNF280D; NbExp=3; IntAct=EBI-78219, EBI-12027202;
CC P45973; Q5ZUS4: legAS4; Xeno; NbExp=6; IntAct=EBI-78219, EBI-8871796;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10460410,
CC ECO:0000269|PubMed:19617346}. Chromosome {ECO:0000269|PubMed:10460410}.
CC Chromosome, centromere {ECO:0000269|PubMed:10460410,
CC ECO:0000269|PubMed:21346195}. Note=Colocalizes with HNRNPU in the
CC nucleus (PubMed:19617346). Component of centromeric and pericentromeric
CC heterochromatin. Associates with chromosomes during mitosis. Associates
CC specifically with chromatin during metaphase and anaphase.
CC {ECO:0000269|PubMed:19617346}.
CC -!- PTM: Phosphorylation of HP1 and LBR may be responsible for some of the
CC alterations in chromatin organization and nuclear structure which occur
CC at various times during the cell cycle (By similarity). Phosphorylated
CC during interphase and possibly hyper-phosphorylated during mitosis.
CC {ECO:0000250, ECO:0000269|PubMed:10460410}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:20498703}.
CC -!- CAUTION: Was previously reported to interact with ASXL1. However, this
CC publication has been retracted. {ECO:0000305|PubMed:19880879,
CC ECO:0000305|PubMed:25750265}.
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DR EMBL; S62077; AAB26994.1; -; mRNA.
DR EMBL; L07515; AAA72327.1; -; mRNA.
DR EMBL; AK313506; BAG36286.1; -; mRNA.
DR EMBL; CH471054; EAW96759.1; -; Genomic_DNA.
DR EMBL; BC006821; AAH06821.1; -; mRNA.
DR EMBL; U26311; AAC50553.1; -; mRNA.
DR CCDS; CCDS8875.1; -.
DR PIR; G01808; G01808.
DR RefSeq; NP_001120793.1; NM_001127321.1.
DR RefSeq; NP_001120794.1; NM_001127322.1.
DR RefSeq; NP_036249.1; NM_012117.2.
DR PDB; 3FDT; X-ray; 2.00 A; A=18-75.
DR PDB; 3I3C; X-ray; 2.48 A; A/B/C/D=110-173.
DR PDBsum; 3FDT; -.
DR PDBsum; 3I3C; -.
DR AlphaFoldDB; P45973; -.
DR BMRB; P45973; -.
DR SMR; P45973; -.
DR BioGRID; 117030; 306.
DR CORUM; P45973; -.
DR DIP; DIP-5986N; -.
DR IntAct; P45973; 200.
DR MINT; P45973; -.
DR STRING; 9606.ENSP00000209875; -.
DR BindingDB; P45973; -.
DR ChEMBL; CHEMBL3826867; -.
DR DrugBank; DB09130; Copper.
DR MoonDB; P45973; Predicted.
DR GlyGen; P45973; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P45973; -.
DR PhosphoSitePlus; P45973; -.
DR SwissPalm; P45973; -.
DR BioMuta; CBX5; -.
DR DMDM; 1170338; -.
DR EPD; P45973; -.
DR jPOST; P45973; -.
DR MassIVE; P45973; -.
DR PaxDb; P45973; -.
DR PeptideAtlas; P45973; -.
DR PRIDE; P45973; -.
DR ProteomicsDB; 55691; -.
DR TopDownProteomics; P45973; -.
DR ABCD; P45973; 2 sequenced antibodies.
DR Antibodypedia; 4311; 941 antibodies from 45 providers.
DR DNASU; 23468; -.
DR Ensembl; ENST00000209875.9; ENSP00000209875.4; ENSG00000094916.16.
DR Ensembl; ENST00000439541.6; ENSP00000401009.2; ENSG00000094916.16.
DR Ensembl; ENST00000550411.5; ENSP00000449207.1; ENSG00000094916.16.
DR GeneID; 23468; -.
DR KEGG; hsa:23468; -.
DR MANE-Select; ENST00000209875.9; ENSP00000209875.4; NM_012117.3; NP_036249.1.
DR CTD; 23468; -.
DR DisGeNET; 23468; -.
DR GeneCards; CBX5; -.
DR HGNC; HGNC:1555; CBX5.
DR HPA; ENSG00000094916; Tissue enhanced (choroid).
DR MIM; 604478; gene.
DR neXtProt; NX_P45973; -.
DR OpenTargets; ENSG00000094916; -.
DR PharmGKB; PA26130; -.
DR VEuPathDB; HostDB:ENSG00000094916; -.
DR eggNOG; KOG1911; Eukaryota.
DR GeneTree; ENSGT00940000158801; -.
DR HOGENOM; CLU_045874_1_0_1; -.
DR InParanoid; P45973; -.
DR OMA; KCPLKML; -.
DR OrthoDB; 1628171at2759; -.
DR PhylomeDB; P45973; -.
DR TreeFam; TF350503; -.
DR PathwayCommons; P45973; -.
DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; P45973; -.
DR SIGNOR; P45973; -.
DR BioGRID-ORCS; 23468; 10 hits in 1079 CRISPR screens.
DR ChiTaRS; CBX5; human.
DR EvolutionaryTrace; P45973; -.
DR GeneWiki; CBX5_(gene); -.
DR GenomeRNAi; 23468; -.
DR Pharos; P45973; Tbio.
DR PRO; PR:P45973; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P45973; protein.
DR Bgee; ENSG00000094916; Expressed in tendon of biceps brachii and 201 other tissues.
DR ExpressionAtlas; P45973; baseline and differential.
DR Genevisible; P45973; HS.
DR GO; GO:0010369; C:chromocenter; IEA:Ensembl.
DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL.
DR GO; GO:0000792; C:heterochromatin; TAS:ProtInc.
DR GO; GO:0000118; C:histone deacetylase complex; ISS:BHF-UCL.
DR GO; GO:0035097; C:histone methyltransferase complex; ISS:BHF-UCL.
DR GO; GO:0000776; C:kinetochore; IEA:Ensembl.
DR GO; GO:0005635; C:nuclear envelope; TAS:ProtInc.
DR GO; GO:0005730; C:nucleolus; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005721; C:pericentric heterochromatin; ISS:BHF-UCL.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0090734; C:site of DNA damage; IMP:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; ISS:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:BHF-UCL.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISS:BHF-UCL.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR IDEAL; IID00659; -.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR017984; Chromo_dom_subgr.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR008251; Chromo_shadow_dom.
DR InterPro; IPR023779; Chromodomain_CS.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF01393; Chromo_shadow; 1.
DR PRINTS; PR00504; CHROMODOMAIN.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00300; ChSh; 1.
DR SUPFAM; SSF54160; SSF54160; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Centromere; Chromosome;
KW Direct protein sequencing; Host-virus interaction; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..191
FT /note="Chromobox protein homolog 5"
FT /id="PRO_0000080208"
FT DOMAIN 20..78
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 121..179
FT /note="Chromo 2; shadow subtype"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REGION 70..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13185"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT CROSSLNK 32
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 91
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 102
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 106
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 184
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MUTAGEN 165
FT /note="I->E: No effect on interaction with POGZ. Abolishes
FT interaction with TRIM28, CHAF1A and NIPBL."
FT /evidence="ECO:0000269|PubMed:20562864"
FT MUTAGEN 174
FT /note="W->A: Abolishes interaction with TRIM28, CHAF1A,
FT NIPBL and HP1BP3, fails to localize to centromeres in
FT mitosis."
FT /evidence="ECO:0000269|PubMed:20042602,
FT ECO:0000269|PubMed:20562864, ECO:0000269|PubMed:21346195"
FT STRAND 19..31
FT /evidence="ECO:0007829|PDB:3FDT"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:3FDT"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:3FDT"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:3FDT"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:3FDT"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:3FDT"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:3I3C"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:3I3C"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:3I3C"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:3I3C"
FT HELIX 153..159
FT /evidence="ECO:0007829|PDB:3I3C"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:3I3C"
SQ SEQUENCE 191 AA; 22225 MW; 16FFC476367093B1 CRC64;
MGKKTKRTAD SSSSEDEEEY VVEKVLDRRV VKGQVEYLLK WKGFSEEHNT WEPEKNLDCP
ELISEFMKKY KKMKEGENNK PREKSESNKR KSNFSNSADD IKSKKKREQS NDIARGFERG
LEPEKIIGAT DSCGDLMFLM KWKDTDEADL VLAKEANVKC PQIVIAFYEE RLTWHAYPED
AENKEKETAK S
