HP1B3_HUMAN
ID HP1B3_HUMAN Reviewed; 553 AA.
AC Q5SSJ5; A6NI71; A8K5D7; B3KMZ8; B4E210; Q05BI0; Q5SSJ6; Q5SWC6; Q6PIM9;
AC Q8NDF0; Q9UHY0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Heterochromatin protein 1-binding protein 3;
DE AltName: Full=Protein HP1-BP74 {ECO:0000303|PubMed:20042602};
GN Name=HP1BP3;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Teratocarcinoma, 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Brain, and Testis;
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 PROTEIN SEQUENCE OF 132-146; 176-184; 275-282; 284-291; 294-302 AND
RP 312-329, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Calvo F., Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248 AND SER-249, 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 [12]
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 [13]
RP INTERACTION WITH CBX5, DOMAIN, SUBCELLULAR LOCATION, AND STRUCTURE BY NMR
RP OF 153-237.
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).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-6; SER-142; SER-155; SER-156; SER-248 AND SER-249,
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441; SER-442 AND SER-446, AND
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; THR-51; SER-155 AND
RP SER-249, AND 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 [18]
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 [19]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=24830416; DOI=10.1074/mcp.m113.034975;
RA Dutta B., Ren Y., Hao P., Sim K.H., Cheow E., Adav S., Tam J.P., Sze S.K.;
RT "Profiling of the chromatin-associated proteome identifies HP1BP3 as a
RT novel regulator of cell cycle progression.";
RL Mol. Cell. Proteomics 13:2183-2197(2014).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
RX PubMed=25100860; DOI=10.1074/mcp.m114.038232;
RA Dutta B., Ren Y., Lim S.K., Tam J.P., Sze S.K.;
RT "Quantitative profiling of chromatome dynamics reveals a novel role for
RT HP1BP3 in hypoxia-induced oncogenesis.";
RL Mol. Cell. Proteomics 13:3236-3249(2014).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-64; LYS-97 AND LYS-258, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
CC -!- FUNCTION: Component of heterochromatin that maintains heterochromatin
CC integrity during G1/S progression and regulates the duration of G1
CC phase to critically influence cell proliferative capacity
CC (PubMed:24830416). Mediates chromatin condensation during hypoxia,
CC leading to increased tumor cell viability, radio-resistance, chemo-
CC resistance and self-renewal(PubMed:25100860).
CC {ECO:0000269|PubMed:24830416, ECO:0000269|PubMed:25100860}.
CC -!- SUBUNIT: Interacts (via PxVxL motif) with CBX5 (via Trp-174).
CC {ECO:0000269|PubMed:20042602}.
CC -!- INTERACTION:
CC Q5SSJ5; P50222: MEOX2; NbExp=3; IntAct=EBI-2880687, EBI-748397;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24830416}. Chromosome
CC {ECO:0000269|PubMed:20042602, ECO:0000269|PubMed:24830416}.
CC Note=localized in nuclei but not in nucleoli in interphase. Colocalized
CC with chromosomes in mitosis, with a gradually increased during G1
CC progression and a maximum level during late G1 phase (G1/S).
CC {ECO:0000269|PubMed:24830416}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5SSJ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SSJ5-2; Sequence=VSP_034169;
CC Name=3;
CC IsoId=Q5SSJ5-3; Sequence=VSP_034168;
CC Name=4;
CC IsoId=Q5SSJ5-5; Sequence=VSP_034170, VSP_034171;
CC -!- DOMAIN: A central region that included the first H15 (linker histone
CC H1/H5 globular) domain binds at the entry/exit site of the nucleosomal
CC DNA. {ECO:0000269|PubMed:20042602}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF14871.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF113534; AAF14871.1; ALT_FRAME; mRNA.
DR EMBL; AK023129; BAG51160.1; -; mRNA.
DR EMBL; AK291252; BAF83941.1; -; mRNA.
DR EMBL; AK304065; BAG64972.1; -; mRNA.
DR EMBL; AL833978; CAD38822.1; -; mRNA.
DR EMBL; AL606477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL663074; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471134; EAW94953.1; -; Genomic_DNA.
DR EMBL; BC032139; AAH32139.1; -; mRNA.
DR EMBL; BC045660; AAH45660.1; -; mRNA.
DR CCDS; CCDS30621.1; -. [Q5SSJ5-1]
DR RefSeq; NP_057371.2; NM_016287.3. [Q5SSJ5-1]
DR RefSeq; XP_005245932.1; XM_005245875.4.
DR RefSeq; XP_005245933.1; XM_005245876.3.
DR RefSeq; XP_005245934.1; XM_005245877.4.
DR RefSeq; XP_005245935.1; XM_005245878.4.
DR RefSeq; XP_005245936.1; XM_005245879.4.
DR RefSeq; XP_011539834.1; XM_011541532.1. [Q5SSJ5-2]
DR RefSeq; XP_011539835.1; XM_011541533.1. [Q5SSJ5-2]
DR RefSeq; XP_011539836.1; XM_011541534.2.
DR RefSeq; XP_016856882.1; XM_017001393.1.
DR RefSeq; XP_016856883.1; XM_017001394.1.
DR PDB; 2RQP; NMR; -; A=153-237.
DR PDBsum; 2RQP; -.
DR AlphaFoldDB; Q5SSJ5; -.
DR SMR; Q5SSJ5; -.
DR BioGRID; 119128; 236.
DR IntAct; Q5SSJ5; 79.
DR MINT; Q5SSJ5; -.
DR STRING; 9606.ENSP00000312625; -.
DR DrugBank; DB11638; Artenimol.
DR GlyGen; Q5SSJ5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5SSJ5; -.
DR MetOSite; Q5SSJ5; -.
DR PhosphoSitePlus; Q5SSJ5; -.
DR SwissPalm; Q5SSJ5; -.
DR BioMuta; HP1BP3; -.
DR DMDM; 74743691; -.
DR CPTAC; CPTAC-82; -.
DR CPTAC; CPTAC-83; -.
DR CPTAC; CPTAC-925; -.
DR EPD; Q5SSJ5; -.
DR jPOST; Q5SSJ5; -.
DR MassIVE; Q5SSJ5; -.
DR MaxQB; Q5SSJ5; -.
DR PaxDb; Q5SSJ5; -.
DR PeptideAtlas; Q5SSJ5; -.
DR PRIDE; Q5SSJ5; -.
DR ProteomicsDB; 63880; -. [Q5SSJ5-1]
DR ProteomicsDB; 63881; -. [Q5SSJ5-2]
DR ProteomicsDB; 63882; -. [Q5SSJ5-3]
DR ProteomicsDB; 63883; -. [Q5SSJ5-5]
DR Antibodypedia; 29832; 86 antibodies from 21 providers.
DR DNASU; 50809; -.
DR Ensembl; ENST00000312239.10; ENSP00000312625.5; ENSG00000127483.19. [Q5SSJ5-1]
DR Ensembl; ENST00000375000.5; ENSP00000364139.1; ENSG00000127483.19. [Q5SSJ5-5]
DR Ensembl; ENST00000375003.6; ENSP00000364142.2; ENSG00000127483.19. [Q5SSJ5-3]
DR Ensembl; ENST00000438032.6; ENSP00000403039.2; ENSG00000127483.19. [Q5SSJ5-1]
DR GeneID; 50809; -.
DR KEGG; hsa:50809; -.
DR MANE-Select; ENST00000438032.6; ENSP00000403039.2; NM_001372052.1; NP_001358981.1.
DR UCSC; uc001bdw.2; human. [Q5SSJ5-1]
DR CTD; 50809; -.
DR DisGeNET; 50809; -.
DR GeneCards; HP1BP3; -.
DR HGNC; HGNC:24973; HP1BP3.
DR HPA; ENSG00000127483; Low tissue specificity.
DR MIM; 616072; gene.
DR neXtProt; NX_Q5SSJ5; -.
DR OpenTargets; ENSG00000127483; -.
DR PharmGKB; PA142671673; -.
DR VEuPathDB; HostDB:ENSG00000127483; -.
DR eggNOG; KOG4012; Eukaryota.
DR GeneTree; ENSGT00940000155314; -.
DR HOGENOM; CLU_035727_0_0_1; -.
DR InParanoid; Q5SSJ5; -.
DR OMA; DDTMPIR; -.
DR OrthoDB; 903215at2759; -.
DR PhylomeDB; Q5SSJ5; -.
DR TreeFam; TF106395; -.
DR PathwayCommons; Q5SSJ5; -.
DR SignaLink; Q5SSJ5; -.
DR BioGRID-ORCS; 50809; 14 hits in 1093 CRISPR screens.
DR ChiTaRS; HP1BP3; human.
DR EvolutionaryTrace; Q5SSJ5; -.
DR GeneWiki; HP1BP3; -.
DR GenomeRNAi; 50809; -.
DR Pharos; Q5SSJ5; Tbio.
DR PRO; PR:Q5SSJ5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5SSJ5; protein.
DR Bgee; ENSG00000127483; Expressed in Brodmann (1909) area 23 and 200 other tissues.
DR ExpressionAtlas; Q5SSJ5; baseline and differential.
DR Genevisible; Q5SSJ5; HS.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0031491; F:nucleosome binding; IDA:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
DR GO; GO:0070828; P:heterochromatin organization; IMP:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0097298; P:regulation of nucleus size; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR CDD; cd00073; H15; 1.
DR Gene3D; 1.10.10.10; -; 3.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR033061; HP1BP3.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR15832:SF1; PTHR15832:SF1; 1.
DR Pfam; PF00538; Linker_histone; 3.
DR SMART; SM00526; H15; 3.
DR SUPFAM; SSF46785; SSF46785; 3.
DR PROSITE; PS51504; H15; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromosome;
KW Direct protein sequencing; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CHAIN 2..553
FT /note="Heterochromatin protein 1-binding protein 3"
FT /id="PRO_0000339642"
FT DOMAIN 157..232
FT /note="H15 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT DOMAIN 255..330
FT /note="H15 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT DOMAIN 337..413
FT /note="H15 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 29..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 255..259
FT /note="PxVxL motif"
FT /evidence="ECO:0000303|PubMed:20042602"
FT COMPBIAS 65..79
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..447
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6P747"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 190
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3TEA8"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 64
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 97
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 258
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..152
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_034168"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_034169"
FT VAR_SEQ 117..133
FT /note="DEKDQSKEKEKKVKKTI -> ERADSIHSTLFIIGQNS (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034170"
FT VAR_SEQ 134..553
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034171"
FT CONFLICT 262
FT /note="V -> G (in Ref. 1; AAF14871)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="F -> S (in Ref. 2; BAF83941)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="P -> S (in Ref. 2; BAG64972)"
FT /evidence="ECO:0000305"
FT HELIX 161..175
FT /evidence="ECO:0007829|PDB:2RQP"
FT HELIX 180..190
FT /evidence="ECO:0007829|PDB:2RQP"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:2RQP"
FT TURN 198..202
FT /evidence="ECO:0007829|PDB:2RQP"
FT HELIX 203..214
FT /evidence="ECO:0007829|PDB:2RQP"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:2RQP"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:2RQP"
SQ SEQUENCE 553 AA; 61207 MW; D18B28EE0156F09B CRC64;
MATDTSQGEL VHPKALPLIV GAQLIHADKL GEKVEDSTMP IRRTVNSTRE TPPKSKLAEG
EEEKPEPDIS SEESVSTVEE QENETPPATS SEAEQPKGEP ENEEKEENKS SEETKKDEKD
QSKEKEKKVK KTIPSWATLS ASQLARAQKQ TPMASSPRPK MDAILTEAIK ACFQKSGASV
VAIRKYIIHK YPSLELERRG YLLKQALKRE LNRGVIKQVK GKGASGSFVV VQKSRKTPQK
SRNRKNRSSA VDPEPQVKLE DVLPLAFTRL CEPKEASYSL IRKYVSQYYP KLRVDIRPQL
LKNALQRAVE RGQLEQITGK GASGTFQLKK SGEKPLLGGS LMEYAILSAI AAMNEPKTCS
TTALKKYVLE NHPGTNSNYQ MHLLKKTLQK CEKNGWMEQI SGKGFSGTFQ LCFPYYPSPG
VLFPKKEPDD SRDEDEDEDE SSEEDSEDEE PPPKRRLQKK TPAKSPGKAA SVKQRGSKPA
PKVSAAQRGK ARPLPKKAPP KAKTPAKKTR PSSTVIKKPS GGSSKKPATS ARKEVKLPGK
GKSTMKKSFR VKK
