HP1B3_BOVIN
ID HP1B3_BOVIN Reviewed; 555 AA.
AC Q08DU9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Heterochromatin protein 1-binding protein 3;
GN Name=HP1BP3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; BC123556; AAI23557.1; -; mRNA.
DR RefSeq; NP_001068904.1; NM_001075436.1.
DR RefSeq; XP_005203156.1; XM_005203099.3.
DR RefSeq; XP_005203157.1; XM_005203100.2.
DR AlphaFoldDB; Q08DU9; -.
DR SMR; Q08DU9; -.
DR STRING; 9913.ENSBTAP00000024825; -.
DR PaxDb; Q08DU9; -.
DR PeptideAtlas; Q08DU9; -.
DR PRIDE; Q08DU9; -.
DR Ensembl; ENSBTAT00000024825; ENSBTAP00000024825; ENSBTAG00000018656.
DR Ensembl; ENSBTAT00000076273; ENSBTAP00000068482; ENSBTAG00000018656.
DR GeneID; 510194; -.
DR KEGG; bta:510194; -.
DR CTD; 50809; -.
DR VEuPathDB; HostDB:ENSBTAG00000018656; -.
DR VGNC; VGNC:29935; HP1BP3.
DR eggNOG; KOG4012; Eukaryota.
DR GeneTree; ENSGT00940000155314; -.
DR HOGENOM; CLU_035727_1_0_1; -.
DR InParanoid; Q08DU9; -.
DR OMA; DDTMPIR; -.
DR OrthoDB; 903215at2759; -.
DR TreeFam; TF106395; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000018656; Expressed in thymus and 106 other tissues.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
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: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; 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 2: Evidence at transcript 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..555
FT /note="Heterochromatin protein 1-binding protein 3"
FT /id="PRO_0000339641"
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 227..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..70
FT /note="Basic and 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..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..449
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:0000250|UniProtKB:Q5SSJ5"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6P747"
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 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5SSJ5"
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 448
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"
SQ SEQUENCE 555 AA; 61477 MW; 3943998AB5A0B984 CRC64;
MATDTSQGEL VHPKALPLIV GAQLIHADKL GEKVEDNTMP IRRAVNSTRE TPPKSKLAEG
VEEKPEPDVS SEESISTVEE QENETPPATS SETEQPKGQP ENEEKEENKP SEETKKDEKD
QSKEKEKKVK KTIPSWATLS ASQLARAQKQ TPMASSPRPK MDAILTEAIK ACFQKSGASV
VAIRKYIIHK YPSLELERRG YLLKQALKRE LNRGVIKQVK GKGASGSFVV VQKSRKPPQK
SRNRKNRSSA VDPEPQVKLE DILPLAFTRL CEPKEASYSL IRKYVSQYYP KLRVDIRPQL
LKNALQRAVE RGQLEQITGK GASGTFQLKK SGEKPLLGGS LMEYAILSAI AAMNEPKTCS
TTALKKYVLE NHPGTNSNYQ MHLLKKTLQR CEKNGWMEQI SGKGFSGTFQ LCFPYYPSPG
VLFPKKEPDD SKDEDEDEDE DDSSEEDSED EEPPPKRRLQ KKTPVKSPGK AAAMKQRGSK
LAPKVPAAQR GKTRPLPKKA PPKAKSPAKK ARPSPSVIKK PSGSSSKKPA ASVRKEVKLP
GKGKSTMKKS FKAKK
