P16401 (H15_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H1.5

Alternative name(s):
Histone H1a

Gene names

Name:	HIST1H1B
Synonyms:	H1F5

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	226 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 Phosphoprotein
Technical term	3D-structure 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.5 Ref.6
	Chain	2 – 226	225	Histone H1.5		PRO_0000195909
Regions
	Domain	39 – 112	74	H15
Amino acid modifications
	Modified residue	2	1	N-acetylserine; partial Ref.6
	Modified residue	2	1	Phosphoserine Ref.10
	Modified residue	4	1	Phosphothreonine Ref.7
	Modified residue	11	1	Phosphothreonine Ref.10 Ref.11
	Modified residue	18	1	Phosphoserine Ref.7 Ref.10 Ref.11 Ref.12 Ref.13
	Modified residue	39	1	Phosphothreonine Ref.10 Ref.11
	Modified residue	44	1	Phosphoserine Ref.10
	Modified residue	93	1	N6-acetyllysine Ref.14
	Modified residue	107	1	Phosphoserine Ref.9
	Modified residue	109	1	N6-acetyllysine Ref.14
	Modified residue	138	1	Phosphothreonine Ref.8
	Modified residue	168	1	N6-acetyllysine Ref.14
	Modified residue	187	1	Phosphothreonine Ref.10
	Modified residue	189	1	Phosphoserine Ref.10
	Modified residue	209	1	N6-acetyllysine Ref.14
Natural variations
	Natural variant	86	1	G → D in a colorectal cancer sample; somatic mutation. Ref.16		VAR_036204
	Natural variant	144	1	K → R. Corresponds to variant rs11970638 [ dbSNP | Ensembl ].		VAR_049308
	Natural variant	211	1	A → T. Corresponds to variant rs34144478 [ dbSNP | Ensembl ].		VAR_049309
Experimental info
	Sequence conflict	216 – 218	3	Missing AA sequence Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P16401 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 0BA1402101766FDF	FASTA	226	22,580
	10 20 30 40 50 60 MSETAPAETA TPAPVEKSPA KKKATKKAAG AGAAKRKATG PPVSELITKA VAASKERNGL 70 80 90 100 110 120 SLAALKKALA AGGYDVEKNN SRIKLGLKSL VSKGTLVQTK GTGASGSFKL NKKAASGEAK 130 140 150 160 170 180 PKAKKAGAAK AKKPAGATPK KAKKAAGAKK AVKKTPKKAK KPAAAGVKKV AKSPKKAKAA 190 200 210 220 AKPKKATKSP AKPKAVKPKA AKPKAAKPKA AKPKAAKAKK AAAKKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the H1.5 gene completes the set of human H1 subtype genes." Albig W., Meergans T., Doenecke D. Gene 184:141-148(1997) [PubMed: 9031620] [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 DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: Liver.
[5]	"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 2-226. Tissue: Spleen.
[6]	Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-17; 37-49; 58-78 AND 89-100, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: Ovarian carcinoma.
[7]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4 AND SER-18, MASS SPECTROMETRY. Tissue: Colon adenocarcinoma.
[8]	"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-138, 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 SER-107, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"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; THR-11; SER-18; THR-39; SER-44; THR-187 AND SER-189, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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 THR-11; SER-18 AND THR-39, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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-18, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"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-18, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-93; LYS-109; LYS-168 AND LYS-209, MASS SPECTROMETRY.
[15]	"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].
[16]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-86.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X83509 Genomic DNA. Translation: CAA58498.1.
AF531304 Genomic DNA. Translation: AAN06704.1.
Z98744 Genomic DNA. Translation: CAB11421.1.
BC069101 mRNA. Translation: AAH69101.1.
BC101581 mRNA. Translation: AAI01582.1.
BC101583 mRNA. Translation: AAI01584.1.

IPI

IPI00217468.

PIR

S51660.

RefSeq

NP_005313.1. NM_005322.2.

UniGene

Hs.131956.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FE2	model	-	A	2-226	[»]
2RHI	X-ray	1.66	B	23-27	[»]

ProteinModelPortal

P16401.

SMR

P16401. Positions 40-112.

ModBase

Search...

Protein-protein interaction databases

STRING

P16401.

PTM databases

PhosphoSite

P16401.

Polymorphism databases

DMDM

19856407.

Proteomic databases

PeptideAtlas

P16401.

PRIDE

P16401.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000331442; ENSP00000330074; ENSG00000184357.

GeneID

3009.

KEGG

hsa:3009.

UCSC

uc003njx.1. human.

Organism-specific databases

CTD

3009.

GeneCards

GC06M027835.

HGNC

HGNC:4719. HIST1H1B.

HPA

CAB012241.

MIM

142711. gene.

neXtProt

NX_P16401.

PharmGKB

PA29097.

GenAtlas

Search...

Phylogenomic databases

eggNOG

maNOG21548.

HOGENOM

HBG446956.

HOVERGEN

HBG009035.

InParanoid

P16401.

OMA

TIAHAAE.

OrthoDB

EOG4H19XG.

PhylomeDB

P16401.

Enzyme and pathway databases

Reactome

REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

P16401.

Bgee

P16401.

CleanEx

HS_HIST1H1B.

Genevestigator

P16401.

GermOnline

ENSG00000184357. 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

11932.

SOURCE

Search...

Entry information

Entry name

H15_HUMAN

Accession

Primary (citable) accession number: P16401
Secondary accession number(s): Q14529, Q3MJ42

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 110 of the entry and version 3 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.