P16401 (H15_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H1.5

Alternative name(s):
Histone H1a
Histone H1b
Histone H1s-3

Gene names

Name:	HIST1H1B
Synonyms:	H1F5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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	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: According to Ref.9 more commonly found in heterochromatin. According to Ref.7 associates with actively transcribed chromatin and not heterochromatin. Ref.7 Ref.8 Ref.9
Tissue specificity	Ubiquitous. Expressed in the majority of the cell lines tested and in testis. Ref.1
Domain	The C-terminal domain is required for high-affinity binding to chromatin By similarity.
Post-translational modification	H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter By similarity. Phosphorylated at Thr-11 by GSK3B during mitosis in prometaphase and dephosphorylated in telophase. Ref.12
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 Methylation 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	nuclear chromatin Inferred from direct assay PubMed 19882353. Source: UniProtKB nucleosome Non-traceable author statement. Source: UniProtKB
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 Ref.16 Ref.18
	Modified residue	2	1	Phosphoserine Ref.18
	Modified residue	4	1	Phosphothreonine By similarity
	Modified residue	11	1	Phosphothreonine; by GSK3 Ref.11 Ref.12
	Modified residue	18	1	Phosphoserine Ref.11 Ref.14 Ref.16 Ref.18
	Modified residue	27	1	N6-methyllysine Ref.13
	Modified residue	39	1	Phosphothreonine Ref.11
	Modified residue	138	1	Phosphothreonine Ref.16 Ref.18
	Modified residue	168	1	N6-acetyllysine Ref.15
	Modified residue	173	1	Phosphoserine
Natural variations
	Natural variant	86	1	G → D in a colorectal cancer sample; somatic mutation. Ref.19		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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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]	"The distribution of somatic H1 subtypes is non-random on active vs. inactive chromatin: distribution in human fetal fibroblasts." Parseghian M.H., Newcomb R.L., Winokur S.T., Hamkalo B.A. Chromosome Res. 8:405-424(2000) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[8]	"Distribution of somatic H1 subtypes is non-random on active vs. inactive chromatin II: distribution in human adult fibroblasts." Parseghian M.H., Newcomb R.L., Hamkalo B.A. J. Cell. Biochem. 83:643-659(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[9]	"H1 family histones in the nucleus. Control of binding and localization by the C-terminal domain." Th'ng J.P., Sung R., Ye M., Hendzel M.J. J. Biol. Chem. 280:27809-27814(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[10]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11; SER-18 AND THR-39, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"M phase-specific phosphorylation of histone H1.5 at threonine 10 by GSK-3." Happel N., Stoldt S., Schmidt B., Doenecke D. J. Mol. Biol. 386:339-350(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-11 BY GSK3B.
[13]	"Mapping of lysine monomethylation of linker histones in human breast and its cancer." Lu A., Zougman A., Pudelko M., Bebenek M., Ziolkowski P., Mann M., Wisniewski J.R. J. Proteome Res. 8:4207-4215(2009) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT LYS-27.
[14]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-168, MASS SPECTROMETRY.
[16]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND THR-138, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-18 AND THR-138, MASS SPECTROMETRY.
[19]	"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] [Europe PMC] [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.

ModBase

Search...

Protein-protein interaction databases

IntAct

P16401. 3 interactions.

STRING

9606.ENSP00000330074.

PTM databases

PhosphoSite

P16401.

Polymorphism databases

DMDM

19856407.

Proteomic databases

PaxDb

P16401.

PeptideAtlas

P16401.

PRIDE

P16401.

Protocols and materials databases

DNASU

3009.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000331442; ENSP00000330074; ENSG00000184357.

GeneID

3009.

KEGG

hsa:3009.

UCSC

uc003njx.3. 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

NOG258621.

HOGENOM

HOG000251627.

HOVERGEN

HBG009035.

InParanoid

P16401.

KO

K11275.

OMA

TRVAKAK.

OrthoDB

EOG4H19XG.

Enzyme and pathway databases

Reactome

REACT_578. Apoptosis.

Gene expression databases

Bgee

P16401.

CleanEx

HS_HIST1H1B.

Genevestigator

P16401.

GermOnline

ENSG00000184357. Homo sapiens.

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

EvolutionaryTrace

P16401.

GenomeRNAi

3009.

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:	May 1, 2013
This is version 124 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.