HP1B3_MOUSE
ID HP1B3_MOUSE Reviewed; 554 AA.
AC Q3TEA8; A2AM64; A2AM68; Q3TM38; Q3TU07; Q61688; Q8BT17; Q8C6H2; Q8C911;
AC Q8VE06; Q99KR0; Q9DBI1;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Heterochromatin protein 1-binding protein 3;
GN Name=Hp1bp3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, Liver, Lung, Skin, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 43-324, FUNCTION, AND INTERACTION WITH CBX5.
RX PubMed=8978696;
RA le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H., Jeanmougin F.,
RA Losson R., Chambon P.;
RT "A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic
RT control of transcription by nuclear receptors.";
RL EMBO J. 15:6701-6715(1996).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-192, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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. May play a
CC role in hypoxia-induced oncogenesis. {ECO:0000250|UniProtKB:Q5SSJ5,
CC ECO:0000269|PubMed:8978696}.
CC -!- SUBUNIT: Interacts (via PxVxL motif) with CBX5 (via Trp-174).
CC {ECO:0000250|UniProtKB:Q5SSJ5, ECO:0000269|PubMed:8978696}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5SSJ5}.
CC Chromosome {ECO:0000250|UniProtKB:Q5SSJ5}. Note=localized in nuclei but
CC not in nucleoli in interphase. Colocalized with chromosomes in mitosis,
CC with a gradually increased during G1 progression and a maximum level
CC during late G1 phase (G1/S). {ECO:0000250|UniProtKB:Q5SSJ5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3TEA8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TEA8-2; Sequence=VSP_034175;
CC Name=3;
CC IsoId=Q3TEA8-3; Sequence=VSP_034174;
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:0000250|UniProtKB:Q5SSJ5}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC35912.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK004938; BAB23683.1; -; mRNA.
DR EMBL; AK028181; BAC25794.1; -; mRNA.
DR EMBL; AK043260; BAC31507.1; -; mRNA.
DR EMBL; AK075725; BAC35912.1; ALT_FRAME; mRNA.
DR EMBL; AK161041; BAE36164.1; -; mRNA.
DR EMBL; AK166161; BAE38604.1; -; mRNA.
DR EMBL; AK169740; BAE41340.1; -; mRNA.
DR EMBL; AL807249; CAM18860.1; -; Genomic_DNA.
DR EMBL; AL807249; CAM18863.1; -; Genomic_DNA.
DR EMBL; BC004053; AAH04053.1; -; mRNA.
DR EMBL; BC020024; AAH20024.1; -; mRNA.
DR EMBL; X99642; CAA67961.1; -; mRNA.
DR CCDS; CCDS38927.1; -. [Q3TEA8-1]
DR CCDS; CCDS51334.1; -. [Q3TEA8-3]
DR RefSeq; NP_001116368.1; NM_001122896.2. [Q3TEA8-3]
DR RefSeq; NP_001116369.1; NM_001122897.2. [Q3TEA8-1]
DR RefSeq; NP_001272407.1; NM_001285478.1. [Q3TEA8-1]
DR RefSeq; NP_001272408.1; NM_001285479.1.
DR RefSeq; NP_001272409.1; NM_001285480.1.
DR RefSeq; NP_001272410.1; NM_001285481.1. [Q3TEA8-2]
DR RefSeq; NP_034600.2; NM_010470.3. [Q3TEA8-1]
DR RefSeq; XP_006538631.1; XM_006538568.3. [Q3TEA8-1]
DR RefSeq; XP_006538633.1; XM_006538570.2. [Q3TEA8-3]
DR AlphaFoldDB; Q3TEA8; -.
DR SMR; Q3TEA8; -.
DR BioGRID; 200401; 12.
DR IntAct; Q3TEA8; 6.
DR MINT; Q3TEA8; -.
DR STRING; 10090.ENSMUSP00000101453; -.
DR iPTMnet; Q3TEA8; -.
DR PhosphoSitePlus; Q3TEA8; -.
DR EPD; Q3TEA8; -.
DR jPOST; Q3TEA8; -.
DR MaxQB; Q3TEA8; -.
DR PaxDb; Q3TEA8; -.
DR PeptideAtlas; Q3TEA8; -.
DR PRIDE; Q3TEA8; -.
DR ProteomicsDB; 273133; -. [Q3TEA8-1]
DR ProteomicsDB; 273134; -. [Q3TEA8-2]
DR ProteomicsDB; 273135; -. [Q3TEA8-3]
DR Antibodypedia; 29832; 86 antibodies from 21 providers.
DR DNASU; 15441; -.
DR Ensembl; ENSMUST00000030541; ENSMUSP00000030541; ENSMUSG00000028759. [Q3TEA8-1]
DR Ensembl; ENSMUST00000097836; ENSMUSP00000095447; ENSMUSG00000028759. [Q3TEA8-3]
DR Ensembl; ENSMUST00000165861; ENSMUSP00000132614; ENSMUSG00000028759. [Q3TEA8-1]
DR GeneID; 15441; -.
DR KEGG; mmu:15441; -.
DR UCSC; uc008vkg.3; mouse. [Q3TEA8-1]
DR UCSC; uc008vki.3; mouse. [Q3TEA8-2]
DR CTD; 50809; -.
DR MGI; MGI:109369; Hp1bp3.
DR VEuPathDB; HostDB:ENSMUSG00000028759; -.
DR eggNOG; KOG4012; Eukaryota.
DR GeneTree; ENSGT00940000155314; -.
DR HOGENOM; CLU_035727_1_0_1; -.
DR InParanoid; Q3TEA8; -.
DR OMA; DDTMPIR; -.
DR OrthoDB; 903215at2759; -.
DR PhylomeDB; Q3TEA8; -.
DR TreeFam; TF106395; -.
DR BioGRID-ORCS; 15441; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Hp1bp3; mouse.
DR PRO; PR:Q3TEA8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q3TEA8; protein.
DR Bgee; ENSMUSG00000028759; Expressed in embryonic brain and 262 other tissues.
DR ExpressionAtlas; Q3TEA8; baseline and differential.
DR Genevisible; Q3TEA8; MM.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0031491; F:nucleosome binding; ISS:UniProtKB.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
DR GO; GO:0070828; P:heterochromatin organization; ISS:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0097298; P:regulation of nucleus size; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR CDD; cd00073; H15; 1.
DR Gene3D; 1.10.10.10; -; 3.
DR InterPro; IPR005819; H1/H5.
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 PRINTS; PR00624; HISTONEH5.
DR SMART; SM00526; H15; 3.
DR SUPFAM; SSF46785; SSF46785; 3.
DR PROSITE; PS51504; H15; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromosome; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT CHAIN 2..554
FT /note="Heterochromatin protein 1-binding protein 3"
FT /id="PRO_0000339643"
FT DOMAIN 159..234
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 30..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 255..259
FT /note="PxVxL motif"
FT /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT COMPBIAS 65..79
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..448
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT MOD_RES 51
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6P747"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT MOD_RES 192
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT CROSSLNK 64
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT CROSSLNK 97
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT CROSSLNK 258
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034174"
FT VAR_SEQ 67..79
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034175"
FT CONFLICT 68
FT /note="D -> N (in Ref. 1; BAE36164)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="N -> S (in Ref. 4; CAA67961 and 3; AAH20024)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="K -> E (in Ref. 1; BAB23683)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="C -> S (in Ref. 2; CAM18860/CAM18863)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="G -> D (in Ref. 4; CAA67961 and 3; AAH04053/
FT AAH20024)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="R -> K (in Ref. 4; CAA67961 and 3; AAH04053/
FT AAH20024)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="Missing (in Ref. 1; BAC25794)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="K -> R (in Ref. 1; BAE38604)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="E -> D (in Ref. 3; AAH04053/AAH20024)"
FT /evidence="ECO:0000305"
FT CONFLICT 440..441
FT /note="Missing (in Ref. 3; AAH04053)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="K -> E (in Ref. 1; BAE36164)"
FT /evidence="ECO:0000305"
FT MOD_RES Q3TEA8-2:72
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 554 AA; 60867 MW; A49C4F7C42D1BE64 CRC64;
MATDMSQGEL IHPKALPLIV GAQLIHADKL GEKAEDTTMP IRRAVNSTRE TPPKSKLAEG
EEEKPEPDGS SEESISTVEE QENETPPATS SEAEQPKGEP ESGEKEENNN KSAEEPKKDE
KDQSKEKEKK VKKTIPAWAT LSASQLARAQ RQTPMASSPR PKMDAILTEA IKACFQKTGA
SVVAIRKYII HKYPSLGLER RGYLLKQALK RELNRGVIRQ VKGKGASGSF VVVQKSKPPQ
KSKNRKKGSA LDPEPQVKLE DVLPLAFTRL CEPKEASYSL IRKYVSQYYP KLRVDIRPQL
LKNALQRAVE RGQLEQITGK GASGTFQLKK SGEKPLLGGS LMEYAILSAI AAMNEPKTCS
TTALKKYVLE NHPGANSNYQ MHLLKKTLQK CEKNGWLEQI SGKGFSGTFQ LSFPYYPSPG
VLFPKKESGG SDDEDEDDDD DESSEDSEDE EPPPKRSLQK KTPAKSQGKT ASMKQRGSKP
ARKVPAAQRG KVRPLPKKAP PKAKTPARKA RPSPSVIKKP SGSSSRKPIA SARKEAKLPG
KGKSAMKKSF KTKK
