ID H11_BOVIN Reviewed; 104 AA. AC P02253; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 22-JUL-2008, entry version 56. DE RecName: Full=Histone H1.1; DE AltName: Full=CTL-1; DE Flags: Fragment; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=81142290; PubMed=7204387; RA Liao L.W., Cole R.D.; RT "The amino acid sequence of residues 1-104 of CTL-1, a bovine H1 RT histone."; RL J. Biol. Chem. 256:3024-3029(1981). RN [2] RP AMINO-ACID COMPOSITION OF TRYPTIC PEPTIDES. RX MEDLINE=72068710; PubMed=5167020; RA Rall S.C., Cole R.D.; RT "Amino acid sequence and sequence variability of the amino-terminal RT regions of lysine-rich histones."; RL J. Biol. Chem. 246:7175-7190(1971). RN [3] RP PHOSPHORYLATION AT SER-103. RX MEDLINE=88271620; PubMed=3134256; DOI=10.1016/0014-5793(88)81296-1; RA Jakes S., Hastings T.G., Reimann E.M., Schlender K.K.; RT "Identification of the phosphoserine residue in histone H1 RT phosphorylated by protein kinase C."; RL FEBS Lett. 234:31-34(1988). 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 PIR; A92316; HSBO11. DR UniGene; Bt.85301; -. DR HSSP; P08287; 1GHC. DR Ensembl; ENSBTAG00000011677; Bos taurus. DR HOVERGEN; P02253; -. 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 Acetylation; Chromosomal protein; Direct protein sequencing; KW DNA-binding; Nucleus; Phosphoprotein. FT CHAIN 1 >104 Histone H1.1. FT /FTId=PRO_0000195903. FT REGION 35 >104 Globular. FT MOD_RES 1 1 N-acetylserine. FT MOD_RES 35 35 Phosphoserine (Potential). FT MOD_RES 103 103 Phosphoserine; by PKC. FT NON_TER 104 104 SQ SEQUENCE 104 AA; 10365 MW; 801BF289751E41B2 CRC64; SETAPAAPAA APPAEKTPVK KKAAKKPAGA RRKASGPPVS ELITKAVAAS KERSGVSLAA LKKALAAAGY DVEKNNSRIK LGLKSLVSKG TLVQTKGTGA SGSF //