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Database: UniProt
Entry: A0A2K6RRC7_RHIRO
LinkDB: A0A2K6RRC7_RHIRO
Original site: A0A2K6RRC7_RHIRO 
ID   A0A2K6RRC7_RHIRO        Unreviewed;       553 AA.
AC   A0A2K6RRC7;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Heterochromatin protein 1-binding protein 3 {ECO:0000256|ARBA:ARBA00019297};
GN   Name=HP1BP3 {ECO:0000313|Ensembl:ENSRROP00000043592.1};
OS   Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000043592.1, ECO:0000313|Proteomes:UP000233200};
RN   [1] {ECO:0000313|Ensembl:ENSRROP00000043592.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; XP_010362634.1; XM_010364332.1.
DR   AlphaFoldDB; A0A2K6RRC7; -.
DR   SMR; A0A2K6RRC7; -.
DR   STRING; 61622.ENSRROP00000043592; -.
DR   Ensembl; ENSRROT00000068103.1; ENSRROP00000043592.1; ENSRROG00000044832.1.
DR   GeneID; 104663208; -.
DR   KEGG; rro:104663208; -.
DR   CTD; 50809; -.
DR   GeneTree; ENSGT00940000155314; -.
DR   OMA; IQNCKER; -.
DR   OrthoDB; 3029985at2759; -.
DR   Proteomes; UP000233200; Unplaced.
DR   GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR   GO; GO:0031491; F:nucleosome binding; IEA:Ensembl.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR   GO; GO:0070828; P:heterochromatin organization; IEA:Ensembl.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:Ensembl.
DR   GO; GO:0097298; P:regulation of nucleus size; IEA:Ensembl.
DR   CDD; cd00073; H15; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 3.
DR   InterPro; IPR005818; Histone_H1/H5_H15.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR15832:SF1; HETEROCHROMATIN PROTEIN 1-BINDING PROTEIN 3; 1.
DR   PANTHER; PTHR15832; SHC (SRC HOMOLOGY DOMAIN C-TERMINAL) ADAPTOR HOMOLOG; 1.
DR   Pfam; PF00538; Linker_histone; 3.
DR   SMART; SM00526; H15; 3.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 3.
DR   PROSITE; PS51504; H15; 3.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233200}.
FT   DOMAIN          157..232
FT                   /note="H15"
FT                   /evidence="ECO:0000259|PROSITE:PS51504"
FT   DOMAIN          255..330
FT                   /note="H15"
FT                   /evidence="ECO:0000259|PROSITE:PS51504"
FT   DOMAIN          337..413
FT                   /note="H15"
FT                   /evidence="ECO:0000259|PROSITE:PS51504"
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   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        464..481
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   553 AA;  61247 MW;  262DF6CB1AF65A90 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 TPAKSPGKAT SVKQRGSKPT
     PKVSAAQRGK ARPLPKKAPP KAKTPAKKAR PSPTVIKKPS GGSSKKPATS ARKEVKLPGK
     GKSTMKKSFR VKK
//
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