HP1B3_RAT
ID HP1B3_RAT Reviewed; 553 AA.
AC Q6P747;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Heterochromatin protein 1-binding protein 3;
GN Name=Hp1bp3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51; THR-85; SER-441; SER-442
RP AND SER-445, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- SUBUNIT: Interacts (via PxVxL motif) with CBX5.
CC {ECO:0000250|UniProtKB:Q5SSJ5}.
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 -!- 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}.
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DR EMBL; BC061837; AAH61837.1; -; mRNA.
DR RefSeq; NP_954539.1; NM_199108.1.
DR AlphaFoldDB; Q6P747; -.
DR SMR; Q6P747; -.
DR BioGRID; 260500; 4.
DR IntAct; Q6P747; 3.
DR STRING; 10116.ENSRNOP00000019696; -.
DR iPTMnet; Q6P747; -.
DR PhosphoSitePlus; Q6P747; -.
DR PaxDb; Q6P747; -.
DR PRIDE; Q6P747; -.
DR Ensembl; ENSRNOT00000075852; ENSRNOP00000067949; ENSRNOG00000014445.
DR GeneID; 313647; -.
DR KEGG; rno:313647; -.
DR CTD; 50809; -.
DR RGD; 735099; Hp1bp3.
DR eggNOG; KOG4012; Eukaryota.
DR GeneTree; ENSGT00940000155314; -.
DR InParanoid; Q6P747; -.
DR OrthoDB; 903215at2759; -.
DR PhylomeDB; Q6P747; -.
DR PRO; PR:Q6P747; -.
DR Proteomes; UP000002494; Chromosome 5.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
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; Chromosome; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT CHAIN 2..553
FT /note="Heterochromatin protein 1-binding protein 3"
FT /id="PRO_0000339644"
FT DOMAIN 157..232
FT /note="H15 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT DOMAIN 253..328
FT /note="H15 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT DOMAIN 335..411
FT /note="H15 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 30..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..251
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 253..257
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 94..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..446
FT /note="Acidic 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:0007744|PubMed:22673903"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT MOD_RES 190
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3TEA8"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 256
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
SQ SEQUENCE 553 AA; 60807 MW; 1647A55B69ABEFEB CRC64;
MATDMSQGEL IHPKALPLIV GAQLIHADKL GEKADDSTMP IRRAVNSTRE TPPKSKLAEG
EEEKPEPDGS SEESISTVEE PENETPPAPS REAEQPKGEP ESGEKEESKS AEETKKEEKD
QSKEKEKKVK KTIPAWATLS ASQLARAQKQ TPMASSPRPK MDAILTEAIK ACFQKSGASV
VAIRKYIIHK YPSLDLERRG YLLKQALKRE LNRGVIKQVK GKGASGSFVV VQKSKTPQKS
KNRKKGSAVD PEPQVKLEDV LPLAFTRLCE PKEASYSLIR KYVSQYYPKL RVDIRPQLLK
NALQRAVERG QLEQITGKGA SGTFQLKKSG EKPLLGGSLM EYAILSAIAA MNEPKTCSTT
ALKKYVLENH PGTNSNYQMH LLKKTLQKCE KNGWLEQISG KGFSGTFQLC FPYYPSPGVL
FPKKVSDGSE DEDEEEDEEE SSEDSEDEEP PPKRSLQKKT PAKPQGKTAS MKQRGAKPAR
KVPAAQRGKV RPLPKKAPPK AKTPARKGRP APSAVKKPSG STSKKPVANA RKEAKLPGKG
KSAMKKKSFK TKK
