H101_CHICK
ID H101_CHICK Reviewed; 219 AA.
AC P08284;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Histone H1.01;
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=4000927; DOI=10.1093/nar/13.2.585;
RA Coles L.S., Wells J.R.E.;
RT "An H1 histone gene-specific 5' element and evolution of H1 and H5 genes.";
RL Nucleic Acids Res. 13:585-594(1985).
RN [2]
RP PROTEIN SEQUENCE OF 2-18; 35-47 AND 66-76, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V., Black E.J., Gillespie D.A.;
RL Submitted (JAN-2007) to UniProtKB.
CC -!- FUNCTION: Histones H1 are necessary for the condensation of nucleosome
CC chains into higher-order structures.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; X01752; CAA25889.1; -; Genomic_DNA.
DR PIR; A23055; A23055.
DR RefSeq; NP_001035732.1; NM_001040642.1.
DR AlphaFoldDB; P08284; -.
DR SMR; P08284; -.
DR PaxDb; P08284; -.
DR GeneID; 417954; -.
DR KEGG; gga:417954; -.
DR CTD; 417954; -.
DR VEuPathDB; HostDB:geneid_417954; -.
DR InParanoid; P08284; -.
DR OMA; FIPFIRC; -.
DR OrthoDB; 1565299at2759; -.
DR TreeFam; TF313664; -.
DR PRO; PR:P08284; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
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; IEA:InterPro.
DR CDD; cd00073; H15; 1.
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 Acetylation; Chromosome; Direct protein sequencing; DNA-binding; Nucleus;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..219
FT /note="Histone H1.01"
FT /id="PRO_0000195928"
FT DOMAIN 37..110
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..163
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..219
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.2"
SQ SEQUENCE 219 AA; 22044 MW; BEDB8FE238DC39F4 CRC64;
MSETAPAAAP DAPAPGAKAA AKKPKKAAGG AKARKPAGPS VTELITKAVS ASKERKGLSL
AALKKALAAG GYDVEKNNSR IKLGLKSLVS KGTLVQTKGT GASGSFRLNK KPGEVKEKAP
RKRATAAKPK KPAAKKPAAA AKKPKKAAAV KKSPKKAKKP AAAATKKAAK SPKKAAKAGR
PKKAAKSPAK AKAVKPKAAK PKATKPKAAK AKKTAAKKK
