P43276 (H15_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H1.5

Alternative name(s):
H1 VAR.5
H1b

Gene names

Name:	Hist1h1b
Synonyms:	H1f5

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	223 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 heterochromatin By similarity.
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.
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 Methylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	muscle organ development Inferred from physical interaction PubMed 15192231. Source: MGI 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 direct assay PubMed 15562002PubMed 9182532. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Msx1	P13297	3	EBI-903960,EBI-903969

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 223	222	Histone H1.5		PRO_0000195918
Regions
	Domain	36 – 109	74	H15
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.5
	Modified residue	2	1	Phosphoserine By similarity
	Modified residue	4	1	Phosphothreonine Ref.6
	Modified residue	18	1	Phosphoserine Ref.5 Ref.7
	Modified residue	27	1	N6-methyllysine By similarity
	Modified residue	36	1	Phosphothreonine By similarity
	Modified residue	135	1	Phosphothreonine By similarity
	Modified residue	165	1	N6-acetyllysine By similarity
	Modified residue	170	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	61	1	A → T in BAB32001. Ref.3
	Sequence conflict	120	1	A → V in BAB32001. Ref.3
	Sequence conflict	137	1	K → N in BAB32001. Ref.3
	Sequence conflict	195	1	S → F in BAB32001. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P43276 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: B9C26AC31C2716B6	FASTA	223	22,576
	10 20 30 40 50 60 MSETAPAETA APAPVEKSPA KKKTTKKAGA AKRKATGPPV SELITKAVSA SKERGGVSLP 70 80 90 100 110 120 ALKKALAAGG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG ASGSFKLNKK AASGEAKPKA 130 140 150 160 170 180 KKTGAAKAKK PAGATPKKPK KTAGAKKTVK KTPKKAKKPA AAGVKKVAKS PKKAKAAAKP 190 200 210 220 KKAAKSPAKP KAVKSKASKP KVTKPKTAKP KAAKAKKAVS KKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of two murine H1 histone genes and chromosomal mapping of the H1 gene complement." Drabent B., Franke K., Bode C., Kosciessa U., Bouterfa H., Hameister H., Doenecke D. Mamm. Genome 6:505-511(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BALB/c. Tissue: Blood.
[2]	"Characterization of the mouse histone gene cluster on chromosome 13: 45 histone genes in three patches spread over 1Mb." Wang Z.-F., Krasikov T., Frey M.R., Wang J., Matera A.G., Marzluff W.F. Genome Res. 6:688-701(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: C57BL/6.
[3]	"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].
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-220. Strain: C57BL/6J. Tissue: Embryonic kidney.
[5]	"Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION AT SER-18, MASS SPECTROMETRY. Tissue: Brain.
[6]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z46227 Genomic DNA. Translation: CAA86299.1. U62922 Genomic DNA. Translation: AAB05798.1. AY158904 Genomic DNA. Translation: AAO06215.1. AK020117 mRNA. Translation: BAB32001.1.
IPI	IPI00230133.
PIR	A35245. S49492.
RefSeq	NP_064418.1. NM_020034.1.
UniGene	Mm.221314.
3D structure databases
ProteinModelPortal	P43276.
SMR	P43276. Positions 37-109.
ModBase	Search...
Protein-protein interaction databases
IntAct	P43276. 2 interactions.
PTM databases
PhosphoSite	P43276.
Proteomic databases
PRIDE	P43276.
Protocols and materials databases
DNASU	56702.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000080511; ENSMUSP00000079356; ENSMUSG00000058773.
GeneID	56702.
KEGG	mmu:56702.
Organism-specific databases
CTD	3009.
MGI	MGI:1861461. Hist1h1b.
Phylogenomic databases
GeneTree	ENSGT00670000097781.
HOGENOM	HOG000251627.
HOVERGEN	HBG009035.
InParanoid	P43276.
KO	K11275.
OMA	KWPPRRN.
OrthoDB	EOG4H19XG.
Gene expression databases
ArrayExpress	P43276.
Bgee	P43276.
CleanEx	MM_HIST1H1B.
Genevestigator	P43276.
GermOnline	ENSMUSG00000058773. Mus musculus.
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	313147.
SOURCE	Search...

Entry information

Entry name

H15_MOUSE

Accession

Primary (citable) accession number: P43276
Secondary accession number(s): Q9CRM8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program