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UniProtKB/Swiss-Prot entry P02253


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name H11_BOVIN
Primary accession number P02253
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 56)
Name and origin of the protein
Protein name Histone H1.1 [Fragment]
Synonym CTL-1
Gene name None
From
Bos taurus (Bovine) [TaxID: 9913] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Protein existence 1: Evidence at protein level;
References
[1]
PROTEIN SEQUENCE.
PubMed=7204387 [NCBI, ExPASy, EBI, Israel, Japan]
Liao L.W., Cole R.D.;
"The amino acid sequence of residues 1-104 of CTL-1, a bovine H1 histone.";
J. Biol. Chem. 256:3024-3029(1981).
[2]
AMINO-ACID COMPOSITION OF TRYPTIC PEPTIDES.
PubMed=5167020 [NCBI, ExPASy, EBI, Israel, Japan]
Rall S.C., Cole R.D.;
"Amino acid sequence and sequence variability of the amino-terminal regions of lysine-rich histones.";
J. Biol. Chem. 246:7175-7190(1971).
[3]
PHOSPHORYLATION AT SER-103.
DOI=10.1016/0014-5793(88)81296-1; PubMed=3134256 [NCBI, ExPASy, EBI, Israel, Japan]
Jakes S., Hastings T.G., Reimann E.M., Schlender K.K.;
"Identification of the phosphoserine residue in histone H1 phosphorylated by protein kinase C.";
FEBS Lett. 234:31-34(1988).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
PIR A92316; HSBO11.
UniGene Bt.85301
3D structure databases
HSSP P08287; 1GHC. [HSSP ENTRY / PDB]
ModBase P02253.
Family and domain databases
InterPro IPR005818; Histone_H1/H5.
IPR005819; Histone_H5.
IPR011991; Wing_hlx_DNA_bd.
Graphical view of domain structure.
Gene3D G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
Pfam PF00538; Linker_histone; 1.
Pfam graphical view of domain structure.
PRINTS PR00624; HISTONEH5.
SMART SM00526; H15; 1.
SMART graphical view of domain structure.
BLOCKS P02253.
Genome annotation databases
Ensembl ENSBTAG00000011677; Bos taurus. [Contig view]
Phylogenomic databases
HOVERGEN P02253; -.
Other
ProtoNet P02253.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Chromosomal protein; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   >104  >104     Histone H1.1. PRO_0000195903
REGION   35   >104  >70     Globular. 
MOD_RES   1      1        N-acetylserine. 
MOD_RES   35     35        Phosphoserine (Potential). 
MOD_RES   103    103        Phosphoserine; by PKC. 
NON_TER   104    104         
Sequence information
Length: 104 AA [This is the length of the partial sequence of the unprocessed precursor] Molecular weight: 10365 Da [This is the MW of the partial sequence of the unprocessed precursor] CRC64: 801BF289751E41B2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
SETAPAAPAA APPAEKTPVK KKAAKKPAGA RRKASGPPVS ELITKAVAAS KERSGVSLAA 

        70         80         90        100 
LKKALAAAGY DVEKNNSRIK LGLKSLVSKG TLVQTKGTGA SGSF 

P02253 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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