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 16-JUN-2009, entry version 67. DE RecName: Full=Histone H1.11L; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; OC Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=87250632; PubMed=3597432; RA Coles L.S., Robins A.J., Madley L.K., Wells J.R.E.; RT "Characterization of the chicken histone H1 gene complement. RT Generation of 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 MEDLINE=94032251; 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 RT domain of histone H1: sequential assignment and secondary structure."; RL Biochemistry 32:11345-11351(1993). CC -!- FUNCTION: Histones H1 are necessary for the condensation of CC nucleosome chains into higher order structures. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SIMILARITY: Belongs to the histone H1/H5 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M17019; AAA48789.1; -; Genomic_DNA. DR IPI; IPI00581595; -. DR PIR; B28456; B28456. DR RefSeq; NP_001035733.1; -. DR UniGene; Gga.41653; -. DR PDB; 1GHC; NMR; -; A=41-113. DR PDBsum; 1GHC; -. DR SMR; P08287; 41-114. DR Ensembl; ENSGALG00000011759; Gallus gallus. DR GeneID; 427892; -. DR KEGG; gga:427892; -. DR HOGENOM; P08287; -. DR HOVERGEN; P08287; -. DR OMA; P08287; IRRVIKN. DR GO; GO:0000786; C:nucleosome; IEA:InterPro. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro. DR InterPro; IPR005818; Histone_H1/H5. DR InterPro; IPR005819; Histone_H5. DR InterPro; IPR011991; Wing_hlx_DNA_bd. DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1. DR Pfam; PF00538; Linker_histone; 1. DR PRINTS; PR00624; HISTONEH5. DR SMART; SM00526; H15; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Chromosomal protein; DNA-binding; Nucleus. FT INIT_MET 1 1 Removed. FT CHAIN 2 225 Histone H1.11L. FT /FTId=PRO_0000195931. FT REGION 41 114 Globular. FT MOD_RES 2 2 N-acetylserine (By similarity). FT STRAND 41 43 FT HELIX 44 54 FT STRAND 56 59 FT HELIX 66 68 FT STRAND 69 74 FT STRAND 77 80 FT HELIX 81 87 FT TURN 88 90 FT HELIX 91 94 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 //