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H11L_CHICK
ID   H11L_CHICK              Reviewed;         225 AA.
AC   P08287;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Histone H1.11L;
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=3597432; DOI=10.1016/s0021-9258(18)47984-7;
RA   Coles L.S., Robins A.J., Madley L.K., Wells J.R.E.;
RT   "Characterization of the chicken histone H1 gene complement. Generation of
RT   a complete set of vertebrate H1 protein sequences.";
RL   J. Biol. Chem. 262:9656-9663(1987).
RN   [2]
RP   STRUCTURE BY NMR OF 41-114.
RX   PubMed=8218199; DOI=10.1021/bi00093a011;
RA   Cerf C., Lippens G., Muyldermans S., Segers A., Ramakrishnan V.,
RA   Wodak S.J., Hallenga K., Wyns L.;
RT   "Homo- and heteronuclear two-dimensional NMR studies of the globular domain
RT   of histone H1: sequential assignment and secondary structure.";
RL   Biochemistry 32:11345-11351(1993).
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; M17019; AAA48789.1; -; Genomic_DNA.
DR   PIR; B28456; B28456.
DR   RefSeq; NP_001035733.1; NM_001040643.1.
DR   PDB; 1GHC; NMR; -; A=41-114.
DR   PDBsum; 1GHC; -.
DR   AlphaFoldDB; P08287; -.
DR   SMR; P08287; -.
DR   STRING; 9031.ENSGALP00000037266; -.
DR   PaxDb; P08287; -.
DR   GeneID; 427892; -.
DR   KEGG; gga:427892; -.
DR   CTD; 427892; -.
DR   VEuPathDB; HostDB:geneid_427892; -.
DR   eggNOG; KOG4012; Eukaryota.
DR   HOGENOM; CLU_052897_7_0_1; -.
DR   InParanoid; P08287; -.
DR   OrthoDB; 1565299at2759; -.
DR   TreeFam; TF313664; -.
DR   EvolutionaryTrace; P08287; -.
DR   PRO; PR:P08287; -.
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   3D-structure; Acetylation; Chromosome; DNA-binding; Nucleus;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..225
FT                   /note="Histone H1.11L"
FT                   /id="PRO_0000195931"
FT   DOMAIN          41..114
FT                   /note="H15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          94..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..167
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..225
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:1GHC"
FT   HELIX           45..55
FT                   /evidence="ECO:0007829|PDB:1GHC"
FT   STRAND          57..60
FT                   /evidence="ECO:0007829|PDB:1GHC"
FT   HELIX           67..69
FT                   /evidence="ECO:0007829|PDB:1GHC"
FT   STRAND          70..75
FT                   /evidence="ECO:0007829|PDB:1GHC"
FT   STRAND          78..81
FT                   /evidence="ECO:0007829|PDB:1GHC"
FT   HELIX           82..88
FT                   /evidence="ECO:0007829|PDB:1GHC"
FT   TURN            89..91
FT                   /evidence="ECO:0007829|PDB:1GHC"
FT   HELIX           92..95
FT                   /evidence="ECO:0007829|PDB:1GHC"
SQ   SEQUENCE   225 AA;  22528 MW;  BFDA6897A7D5599F CRC64;
     MSETAPAPAA EAAPAAAPAP AKAAAKKPKK AAGGAKARKP AGPSVTELIT KAVSASKERK
     GLSLAALKKA LAAGGYDVEK NNSRIKLGLK SLVSKGTLVQ TKGTGASGSF RLSKKPGEVK
     EKAPKKKASA AKPKKPAAKK PAAAAKKPKK AVAVKKSPKK AKKPAASATK KSAKSPKKVT
     KAVKPKKAVA AKSPAKAKAV KPKAAKPKAA KPKAAKAKKA AAKKK
 
 
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