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P43276 (H15_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H1.5
Alternative name(s):
H1 VAR.5
H1b
Gene names
Name:Hist1h1b
Synonyms:H1f5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length223 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Citrullination at Arg-54 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance.

Sequence similarities

Belongs to the histone H1/H5 family.

Contains 1 H15 (linker histone H1/H5 globular) domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Msx1P132973EBI-903960,EBI-903969

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 223222Histone H1.5
PRO_0000195918

Regions

Domain36 – 10974H15

Amino acid modifications

Modified residue21N-acetylserine Ref.5 Ref.7
Modified residue21Phosphoserine By similarity
Modified residue171N6-acetyllysine Ref.7
Modified residue181Phosphoserine Ref.5
Modified residue271N6-methyllysine By similarity
Modified residue341N6-succinyllysine Ref.7
Modified residue361Phosphothreonine By similarity
Modified residue461N6-acetyllysine Ref.7
Modified residue541Citrulline
Modified residue751N6-acetyllysine Ref.7
Modified residue1351Phosphothreonine By similarity
Modified residue1651N6-acetyllysine By similarity
Modified residue1701Phosphoserine By similarity

Experimental info

Sequence conflict611A → T in BAB32001. Ref.3
Sequence conflict1201A → V in BAB32001. Ref.3
Sequence conflict1371K → N in BAB32001. Ref.3
Sequence conflict1951S → F in BAB32001. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P43276 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: B9C26AC31C2716B6

FASTA22322,576
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"Citrullination regulates pluripotency and histone H1 binding to chromatin."
Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S., Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C., Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.
Nature 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: CITRULLINATION AT ARG-54.
[7]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-17; LYS-46 AND LYS-75, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.
PIRA35245.
S49492.
RefSeqNP_064418.1. NM_020034.1.
UniGeneMm.221314.

3D structure databases

ProteinModelPortalP43276.
SMRP43276. Positions 37-109.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid208131. 1 interaction.
IntActP43276. 3 interactions.
MINTMINT-1868570.

PTM databases

PhosphoSiteP43276.

Proteomic databases

PRIDEP43276.

Protocols and materials databases

DNASU56702.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000080511; ENSMUSP00000079356; ENSMUSG00000058773.
GeneID56702.
KEGGmmu:56702.
UCSCuc007pri.1. mouse.

Organism-specific databases

CTD3009.
MGIMGI:1861461. Hist1h1b.

Phylogenomic databases

GeneTreeENSGT00670000097781.
HOGENOMHOG000251627.
HOVERGENHBG009035.
InParanoidP43276.
KOK11275.
OrthoDBEOG74TX2T.
TreeFamTF313664.

Gene expression databases

ArrayExpressP43276.
BgeeP43276.
CleanExMM_HIST1H1B.
GenevestigatorP43276.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR005818. Histone_H1/H5_H15.
IPR005819. Histone_H5.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00538. Linker_histone. 1 hit.
[Graphical view]
PRINTSPR00624. HISTONEH5.
SMARTSM00526. H15. 1 hit.
[Graphical view]
PROSITEPS51504. H15. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio313147.
PROP43276.
SOURCESearch...

Entry information

Entry nameH15_MOUSE
AccessionPrimary (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: March 19, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot