P02253 (H12_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H1.2

Alternative name(s):
CTL-1

Gene names

Name:

HIST1H1C

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	213 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation By similarity.
Subcellular location	Nucleus. Chromosome. Note: Mainly localizes in euchromatin By similarity.
Domain	The C-terminal domain is required for high-affinity binding to chromatin By similarity.
Post-translational modification	Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes By similarity.
Sequence similarities	Belongs to the histone H1/H5 family. Contains 1 H15 (linker histone H1/H5 globular) domain.

Ontologies

Keywords
Cellular component	Chromosome Nucleus
Ligand	DNA-binding
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	nucleosome assembly Inferred from electronic annotation. Source: InterPro
Cellular_component	nucleosome Inferred from electronic annotation. Source: InterPro nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.3
	Chain	2 – 213	212	Histone H1.2		PRO_0000195903
Regions
	Domain	36 – 109	74	H15
Amino acid modifications
	Modified residue	2	1	N-acetylserine
	Modified residue	2	1	N-acetylserine; partial By similarity
	Modified residue	2	1	Phosphoserine By similarity
	Modified residue	34	1	N6-crotonyl-L-lysine; alternate By similarity
	Modified residue	34	1	N6-methyllysine; alternate By similarity
	Modified residue	64	1	N6-crotonyl-L-lysine By similarity
	Modified residue	85	1	N6-crotonyl-L-lysine By similarity
	Modified residue	90	1	N6-crotonyl-L-lysine By similarity
	Modified residue	97	1	N6-crotonyl-L-lysine By similarity
	Modified residue	104	1	Phosphoserine; by PKC Ref.5
	Modified residue	146	1	Phosphothreonine By similarity
	Modified residue	159	1	N6-crotonyl-L-lysine By similarity
	Modified residue	168	1	N6-crotonyl-L-lysine By similarity
	Modified residue	187	1	N6-methyllysine; by EHMT1 and EHMT2 By similarity
	Cross-link	17		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
	Cross-link	206		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P02253 [UniParc]. Last modified October 3, 2012. Version 2. Checksum: B5D69F890B6FB5DD	FASTA	213	21,356
	10 20 30 40 50 60 MSETAPAAPA AAPPAEKTPV KKKAAKKPAG ARRKASGPPV SELITKAVAA SKERSGVSLA 70 80 90 100 110 120 ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG ASGSFKLNKK AATGEAKPKA 130 140 150 160 170 180 KKAGAAKPKK AAGAAKKTKK ATGAATPKKT AKKTPKKAKK PAAAAVTKKV AKSPKKAKAA 190 200 210 KPKKAAKSAA KAVKPKAAKP KVAKPKKAAP KKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of taurine cattle: a window to ruminant biology and evolution." The bovine genome sequencing and analysis consortium Science 324:522-528(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Hereford.
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Fetal cerebellum.
[3]	"The amino acid sequence of residues 1-104 of CTL-1, a bovine H1 histone." Liao L.W., Cole R.D. J. Biol. Chem. 256:3024-3029(1981) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-105.
[4]	"Amino acid sequence and sequence variability of the amino-terminal regions of lysine-rich histones." Rall S.C., Cole R.D. J. Biol. Chem. 246:7175-7190(1971) [PubMed] [Europe PMC] [Abstract] Cited for: AMINO-ACID COMPOSITION OF TRYPTIC PEPTIDES.
[5]	"Identification of the phosphoserine residue in histone H1 phosphorylated by protein kinase C." Jakes S., Hastings T.G., Reimann E.M., Schlender K.K. FEBS Lett. 234:31-34(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-104.
[6]	"A proposal for a coherent mammalian histone H1 nomenclature correlated with amino acid sequences." Parseghian M.H., Henschen A.H., Krieglstein K.G., Hamkalo B.A. Protein Sci. 3:575-587(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NOMENCLATURE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DAAA02055500 Genomic DNA. No translation available. BC133454 mRNA. Translation: AAI33455.1.
IPI	IPI00699808.
PIR	HSBO11. A92316.
RefSeq	NP_001076894.1. NM_001083425.1.
UniGene	Bt.2728.
3D structure databases
ProteinModelPortal	P02253.
SMR	P02253. Positions 36-109.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1519695.
STRING	9913.ENSBTAP00000015499.
Proteomic databases
PaxDb	P02253.
PRIDE	P02253.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000015499; ENSBTAP00000015499; ENSBTAG00000011677.
GeneID	513971.
KEGG	bta:513971.
Organism-specific databases
CTD	3006.
Phylogenomic databases
eggNOG	NOG258621.
GeneTree	ENSGT00670000097781.
HOVERGEN	HBG009035.
InParanoid	P02253.
KO	K11275.
OMA	MSETAPX.
Family and domain databases
Gene3D	1.10.10.10. 1 hit.
InterPro	IPR005818. Histone_H1/H5. IPR005819. Histone_H5. IPR011991. WHTH_DNA-bd_dom. [Graphical view]
Pfam	PF00538. Linker_histone. 1 hit. [Graphical view]
PRINTS	PR00624. HISTONEH5.
SMART	SM00526. H15. 1 hit. [Graphical view]
PROSITE	PS51504. H15. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20871120.

Entry information

Entry name

H12_BOVIN

Accession

Primary (citable) accession number: P02253
Secondary accession number(s): A3KN02

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	October 3, 2012
Last modified:	May 1, 2013
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program