P16403 (H12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H1.2

Alternative name(s):
Histone H1d

Gene names

Name:	HIST1H1C
Synonyms:	H1F2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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	Histones H1 are necessary for the condensation of nucleosome chains into higher order structures.
Subcellular location	Nucleus. Chromosome.
Sequence similarities	Belongs to the histone H1/H5 family. Contains 1 H15 (linker histone H1/H5 globular) domain.

Ontologies

Keywords
Cellular component	Chromosome Nucleus
Coding sequence diversity	Polymorphism
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 Non-traceable author statement. Source: UniProtKB
Cellular component	nucleosome Non-traceable author statement. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.4 Ref.5 Ref.6
	Chain	2 – 213	212	Histone H1.2		PRO_0000195906
Regions
	Domain	36 – 109	74	H15
Amino acid modifications
	Modified residue	2	1	N-acetylserine; partial Ref.5 Ref.6 Ref.12
	Modified residue	2	1	Phosphoserine Ref.11 Ref.15
	Modified residue	4	1	Phosphothreonine Ref.15
	Modified residue	31	1	Phosphothreonine Ref.7 Ref.9
	Modified residue	34	1	N6-methyllysine Ref.5
	Modified residue	36	1	Phosphoserine Ref.8 Ref.9 Ref.11 Ref.13 Ref.14 Ref.16
	Modified residue	146	1	Phosphothreonine Ref.11
	Modified residue	173	1	Phosphoserine Ref.7
	Cross-link	17		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.12
	Cross-link	206		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.10
Natural variations
	Natural variant	18	1	A → V. Corresponds to variant rs2230653 [ dbSNP | Ensembl ].		VAR_003618
	Natural variant	113	1	S → A. Corresponds to variant rs34810376 [ dbSNP | Ensembl ].		VAR_049304
	Natural variant	124	1	G → A. Corresponds to variant rs12111009 [ dbSNP | Ensembl ].		VAR_049305

Sequences

	Sequence		Length	Mass (Da)
	P16403 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: AA66EA1901D8D56B	FASTA	213	21,365
	10 20 30 40 50 60 MSETAPAAPA AAPPAEKAPV KKKAAKKAGG TPRKASGPPV SELITKAVAA SKERSGVSLA 70 80 90 100 110 120 ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG ASGSFKLNKK AASGEAKPKV 130 140 150 160 170 180 KKAGGTKPKK PVGAAKKPKK AAGGATPKKS AKKTPKKAKK PAAATVTKKV AKSPKKAKVA 190 200 210 KPKKAAKSAA KAVKPKAAKP KVVKPKKAAP KKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human H1 histones: conserved and varied sequence elements in two H1 subtype genes." Eick S., Nicolai M., Mumberg D., Doenecke D. Eur. J. Cell Biol. 49:110-115(1989) [PubMed: 2759094] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The human and mouse replication-dependent histone genes." Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J. Genomics 80:487-498(2002) [PubMed: 12408966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Uterus.
[4]	"Human spleen histone H1. Isolation and amino acid sequences of three minor variants, H1a, H1c, and H1d." Ohe Y., Hayashi H., Iwai K. J. Biochem. 106:844-857(1989) [PubMed: 2613692] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-213. Tissue: Spleen.
[5]	Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-17; 34-46; 55-75 AND 86-97, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, METHYLATION AT LYS-34, MASS SPECTROMETRY. Tissue: Ovarian carcinoma.
[6]	Bienvenut W.V., Waridel P., Quadroni M. Submitted (MAR-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-17; 34-46; 55-63 AND 65-75, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31 AND SER-173, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31 AND SER-36, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry." Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D. Proteomics 7:868-874(2007) [PubMed: 17370265] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-206, MASS SPECTROMETRY. Tissue: Mammary cancer.
[11]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-36 AND THR-146, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry." Meierhofer D., Wang X., Huang L., Kaiser P. J. Proteome Res. 7:4566-4576(2008) [PubMed: 18781797] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-17, MASS SPECTROMETRY.
[13]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed: 19367720] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, MASS SPECTROMETRY. Tissue: T-cell.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-4, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X57129 Genomic DNA. Translation: CAA40408.1. AF531300 Genomic DNA. Translation: AAN06700.1. BC002649 mRNA. No translation available.
IPI	IPI00217465.
PIR	HSHU11. S26364.
RefSeq	NP_005310.1. NM_005319.3.
UniGene	Hs.7644.
3D structure databases
ProteinModelPortal	P16403.
SMR	P16403. Positions 36-109.
ModBase	Search...
Protein-protein interaction databases
IntAct	P16403. 12 interactions.
MINT	MINT-1149485.
STRING	P16403.
PTM databases
PhosphoSite	P16403.
Polymorphism databases
DMDM	417101.
Proteomic databases
PeptideAtlas	P16403.
PRIDE	P16403.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000343677; ENSP00000339566; ENSG00000187837.
GeneID	3006.
KEGG	hsa:3006.
UCSC	uc003nfw.1. human.
Organism-specific databases
CTD	3006.
GeneCards	GC06M025998.
H-InvDB	HIX0005637.
HGNC	HGNC:4716. HIST1H1C.
HPA	CAB011507.
MIM	142710. gene.
neXtProt	NX_P16403.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG20982.
GeneTree	ENSGT00550000074201.
HOGENOM	HBG446956.
HOVERGEN	HBG009035.
InParanoid	P16403.
OMA	MSETAPX.
OrthoDB	EOG4H19XG.
PhylomeDB	P16403.
Enzyme and pathway databases
Reactome	REACT_578. Apoptosis.
Gene expression databases
ArrayExpress	P16403.
Bgee	P16403.
CleanEx	HS_HIST1H1C.
Genevestigator	P16403.
GermOnline	ENSG00000187837. Homo sapiens.
Family and domain databases
InterPro	IPR005818. Histone_H1/H5. IPR005819. Histone_H5. IPR011991. WHTH_trsnscrt_rep_DNA-bd. [Graphical view]
Gene3D	G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
KO	K11275.
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	11920.
SOURCE	Search...

Entry information

Entry name

H12_HUMAN

Accession

Primary (citable) accession number: P16403

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.