H5_CHICK
ID H5_CHICK Reviewed; 190 AA.
AC P02259;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Histone H5;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6300759; DOI=10.1093/nar/11.3.619;
RA Krieg P.A., Robins A.J., D'Andrea R., Wells J.R.E.;
RT "The chicken H5 gene is unlinked to core and H1 histone genes.";
RL Nucleic Acids Res. 11:619-627(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6315952; DOI=10.1016/s0022-2836(83)80191-0;
RA Ruiz-Carrillo A., Affolter M., Renaud J.;
RT "Genomic organization of the genes coding for the six main histones of the
RT chicken: complete sequence of the H5 gene.";
RL J. Mol. Biol. 170:843-859(1983).
RN [3]
RP PROTEIN SEQUENCE OF 2-71.
RX PubMed=1112411; DOI=10.1016/0014-5793(75)80487-x;
RA Garel A., Mazen A., Champagne M., Sautiere P., Kmiecik D., Loy O.,
RA Biserte G.;
RT "Chicken erythrocyte histone H5; I. Amino terminal sequence (70
RT residues).";
RL FEBS Lett. 50:195-199(1975).
RN [4]
RP PROTEIN SEQUENCE OF 72-96.
RX PubMed=1112412; DOI=10.1016/0014-5793(75)80488-1;
RA Sautiere P., Kmiecik D., Loy O., Briand G., Biserte G., Garel A.,
RA Champagne M.;
RT "Chicken erythrocyte histone H5 II. Amino acid sequence adjacent to the
RT phenylalanine residue.";
RL FEBS Lett. 50:200-203(1975).
RN [5]
RP PROTEIN SEQUENCE OF 95-190, AND SEQUENCE REVISION TO 91-92.
RX PubMed=7371850; DOI=10.1016/0014-5793(80)80167-0;
RA Briand G., Kmiecik D., Sautiere P., Wouters D., Borie-Loy O., Biserte G.,
RA Mazen A., Champagne M.;
RT "Chicken erythrocyte histone H5. IV. Sequence of the carboxy-termined half
RT of the molecule (96 residues) and complete sequence.";
RL FEBS Lett. 112:147-151(1980).
RN [6]
RP PHOSPHORYLATION AT SER-23; SER-30; SER-146 AND SER-167.
RX PubMed=6252059; DOI=10.1016/0014-5793(80)80249-3;
RA Martinage A., Mangeat P., Laine B., Couppez M., Sautiere P.,
RA Marchis-Mouren G., Biserte G.;
RT "In vitro phosphorylation of histones H5, H2A, H2B and of the dimer H2A-H2B
RT by a cyclic AMP-dependent protein kinase from rat pancreas.";
RL FEBS Lett. 118:323-329(1980).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 23-101.
RX PubMed=8384699; DOI=10.1038/362219a0;
RA Ramakrishnan V., Finch J.T., Graziano V., Lee P.L., Sweet R.M.;
RT "Crystal structure of globular domain of histone H5 and its implications
RT for nucleosome binding.";
RL Nature 362:219-223(1993).
RN [8]
RP STRUCTURE BY NMR OF 23-101.
RX PubMed=3463990; DOI=10.1073/pnas.83.20.7628;
RA Zarbock J., Clore G.M., Gronenborn A.M.;
RT "Nuclear magnetic resonance study of the globular domain of chicken histone
RT H5: resonance assignment and secondary structure.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:7628-7632(1986).
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:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; J00870; AAA48798.1; -; Genomic_DNA.
DR EMBL; X00169; CAA24994.1; -; mRNA.
DR PIR; A93487; HSCH5.
DR RefSeq; NP_001038138.1; NM_001044673.1.
DR PDB; 1HST; X-ray; 2.60 A; A/B=20-109.
DR PDB; 4QLC; X-ray; 3.50 A; U=23-99.
DR PDB; 5WCU; X-ray; 5.53 A; U/V=23-98.
DR PDBsum; 1HST; -.
DR PDBsum; 4QLC; -.
DR PDBsum; 5WCU; -.
DR AlphaFoldDB; P02259; -.
DR BMRB; P02259; -.
DR SMR; P02259; -.
DR STRING; 9031.ENSGALP00000020094; -.
DR iPTMnet; P02259; -.
DR PaxDb; P02259; -.
DR GeneID; 693250; -.
DR KEGG; gga:693250; -.
DR CTD; 14958; -.
DR VEuPathDB; HostDB:geneid_693250; -.
DR eggNOG; KOG4012; Eukaryota.
DR HOGENOM; CLU_052897_1_1_1; -.
DR InParanoid; P02259; -.
DR OrthoDB; 1565299at2759; -.
DR PhylomeDB; P02259; -.
DR TreeFam; TF313664; -.
DR EvolutionaryTrace; P02259; -.
DR PRO; PR:P02259; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0000786; C:nucleosome; IDA:CAFA.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0031492; F:nucleosomal DNA binding; IMP:CAFA.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IMP:CAFA.
DR GO; GO:0030261; P:chromosome condensation; IBA:GO_Central.
DR GO; GO:0045910; P:negative regulation of DNA recombination; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; IMP:CAFA.
DR CDD; cd00073; H15; 1.
DR DisProt; DP00044; -.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005819; H1/H5.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00538; Linker_histone; 1.
DR PRINTS; PR00624; HISTONEH5.
DR SMART; SM00526; H15; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51504; H15; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Direct protein sequencing; DNA condensation;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1112411"
FT CHAIN 2..190
FT /note="Histone H5"
FT /id="PRO_0000196005"
FT DOMAIN 25..98
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..190
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:6252059"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:6252059"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:6252059"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:6252059"
FT VARIANT 16
FT /note="R -> Q"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:1HST"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:1HST"
FT HELIX 65..78
FT /evidence="ECO:0007829|PDB:1HST"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:1HST"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:1HST"
SQ SEQUENCE 190 AA; 20734 MW; E2BA83C7A39F87DF CRC64;
MTESLVLSPA PAKPKRVKAS RRSASHPTYS EMIAAAIRAE KSRGGSSRQS IQKYIKSHYK
VGHNADLQIK LSIRRLLAAG VLKQTKGVGA SGSFRLAKSD KAKRSPGKKK KAVRRSTSPK
KAARPRKARS PAKKPKATAR KARKKSRASP KKAKKPKTVK AKSRKASKAK KVKRSKPRAK
SGARKSPKKK
