H5_COLLI
ID H5_COLLI Reviewed; 38 AA.
AC P02260;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Histone H5;
DE Flags: Fragment;
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=559492; DOI=10.1016/0006-291x(77)91673-4;
RA Yaguchi M., Roy C., Dove M., Seligy V.;
RT "Amino acid sequence homologies between H1 and H5 histones.";
RL Biochem. Biophys. Res. Commun. 76:100-106(1977).
CC -!- FUNCTION: Histone H5 performs the same function as H1, being necessary
CC for the condensation of nucleosome chains into higher order structures,
CC and replaces histone H1 in certain cells.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- TISSUE SPECIFICITY: Erythroid cells.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000305}.
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DR PIR; A02590; HSPY5.
DR AlphaFoldDB; P02260; -.
DR SMR; P02260; -.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Chromosome; Direct protein sequencing; DNA condensation; DNA-binding;
KW Nucleus.
FT CHAIN 1..>38
FT /note="Histone H5"
FT /id="PRO_0000196006"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 38
SQ SEQUENCE 38 AA; 3933 MW; 79122C0EF9552572 CRC64;
TESPIPVPAP APAAKPKPKR VSKRPASHPP YSDMIAAA