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P43276

- H15_MOUSE

UniProt

P43276 - H15_MOUSE

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Protein
Histone H1.5
Gene
Hist1h1b, H1f5
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. DNA binding Source: MGI
  2. protein binding Source: IntAct

GO - Biological processi

  1. muscle organ development Source: MGI
  2. nucleosome assembly Source: InterPro
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H1.5
Alternative name(s):
H1 VAR.5
H1b
Gene namesi
Name:Hist1h1b
Synonyms:H1f5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:1861461. Hist1h1b.

Subcellular locationi

Nucleus. Chromosome
Note: Mainly localizes in heterochromatin By similarity.

GO - Cellular componenti

  1. nucleosome Source: InterPro
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 223222Histone H1.5
PRO_0000195918Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei2 – 21Phosphoserine By similarity
Modified residuei17 – 171N6-acetyllysine1 Publication
Modified residuei18 – 181Phosphoserine1 Publication
Modified residuei27 – 271N6-methyllysine By similarity
Modified residuei34 – 341N6-succinyllysine1 Publication
Modified residuei36 – 361Phosphothreonine By similarity
Modified residuei46 – 461N6-acetyllysine1 Publication
Modified residuei54 – 541Citrulline
Modified residuei75 – 751N6-acetyllysine1 Publication
Modified residuei135 – 1351Phosphothreonine By similarity
Modified residuei152 – 1521Phosphothreonine By similarity
Modified residuei165 – 1651N6-acetyllysine By similarity
Modified residuei170 – 1701Phosphoserine By similarity
Modified residuei186 – 1861Phosphoserine By similarity

Post-translational modificationi

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.

Keywords - PTMi

Acetylation, Citrullination, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP43276.
PRIDEiP43276.

PTM databases

PhosphoSiteiP43276.

Expressioni

Gene expression databases

ArrayExpressiP43276.
BgeeiP43276.
CleanExiMM_HIST1H1B.
GenevestigatoriP43276.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Msx1P132973EBI-903960,EBI-903969

Protein-protein interaction databases

BioGridi208131. 1 interaction.
IntActiP43276. 3 interactions.
MINTiMINT-1868570.

Structurei

3D structure databases

ProteinModelPortaliP43276.
SMRiP43276. Positions 37-109.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 10974H15
Add
BLAST

Domaini

The C-terminal domain is required for high-affinity binding to chromatin By similarity.

Sequence similaritiesi

Belongs to the histone H1/H5 family.

Phylogenomic databases

GeneTreeiENSGT00670000097781.
HOGENOMiHOG000251627.
HOVERGENiHBG009035.
InParanoidiP43276.
KOiK11275.
OMAiFIRKGMD.
OrthoDBiEOG74TX2T.
TreeFamiTF313664.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR005818. Histone_H1/H5_H15.
IPR005819. Histone_H5.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00538. Linker_histone. 1 hit.
[Graphical view]
PRINTSiPR00624. HISTONEH5.
SMARTiSM00526. H15. 1 hit.
[Graphical view]
PROSITEiPS51504. H15. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P43276-1 [UniParc]FASTAAdd to Basket

« Hide

MSETAPAETA APAPVEKSPA KKKTTKKAGA AKRKATGPPV SELITKAVSA    50
SKERGGVSLP ALKKALAAGG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG 100
ASGSFKLNKK AASGEAKPKA KKTGAAKAKK PAGATPKKPK KTAGAKKTVK 150
KTPKKAKKPA AAGVKKVAKS PKKAKAAAKP KKAAKSPAKP KAVKSKASKP 200
KVTKPKTAKP KAAKAKKAVS KKK 223
Length:223
Mass (Da):22,576
Last modified:January 23, 2007 - v2
Checksum:iB9C26AC31C2716B6
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611A → T in BAB32001. 1 Publication
Sequence conflicti120 – 1201A → V in BAB32001. 1 Publication
Sequence conflicti137 – 1371K → N in BAB32001. 1 Publication
Sequence conflicti195 – 1951S → F in BAB32001. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z46227 Genomic DNA. Translation: CAA86299.1.
U62922 Genomic DNA. Translation: AAB05798.1.
AY158904 Genomic DNA. Translation: AAO06215.1.
AK020117 mRNA. Translation: BAB32001.1.
CCDSiCCDS26295.1.
PIRiA35245.
S49492.
RefSeqiNP_064418.1. NM_020034.2.
UniGeneiMm.221314.

Genome annotation databases

EnsembliENSMUST00000080511; ENSMUSP00000079356; ENSMUSG00000058773.
GeneIDi56702.
KEGGimmu:56702.
UCSCiuc007pri.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z46227 Genomic DNA. Translation: CAA86299.1 .
U62922 Genomic DNA. Translation: AAB05798.1 .
AY158904 Genomic DNA. Translation: AAO06215.1 .
AK020117 mRNA. Translation: BAB32001.1 .
CCDSi CCDS26295.1.
PIRi A35245.
S49492.
RefSeqi NP_064418.1. NM_020034.2.
UniGenei Mm.221314.

3D structure databases

ProteinModelPortali P43276.
SMRi P43276. Positions 37-109.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 208131. 1 interaction.
IntActi P43276. 3 interactions.
MINTi MINT-1868570.

PTM databases

PhosphoSitei P43276.

Proteomic databases

MaxQBi P43276.
PRIDEi P43276.

Protocols and materials databases

DNASUi 56702.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000080511 ; ENSMUSP00000079356 ; ENSMUSG00000058773 .
GeneIDi 56702.
KEGGi mmu:56702.
UCSCi uc007pri.1. mouse.

Organism-specific databases

CTDi 3009.
MGIi MGI:1861461. Hist1h1b.

Phylogenomic databases

GeneTreei ENSGT00670000097781.
HOGENOMi HOG000251627.
HOVERGENi HBG009035.
InParanoidi P43276.
KOi K11275.
OMAi FIRKGMD.
OrthoDBi EOG74TX2T.
TreeFami TF313664.

Miscellaneous databases

NextBioi 313147.
PROi P43276.
SOURCEi Search...

Gene expression databases

ArrayExpressi P43276.
Bgeei P43276.
CleanExi MM_HIST1H1B.
Genevestigatori P43276.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
InterProi IPR005818. Histone_H1/H5_H15.
IPR005819. Histone_H5.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00538. Linker_histone. 1 hit.
[Graphical view ]
PRINTSi PR00624. HISTONEH5.
SMARTi SM00526. H15. 1 hit.
[Graphical view ]
PROSITEi PS51504. H15. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiH15_MOUSE
AccessioniPrimary (citable) accession number: P43276
Secondary accession number(s): Q9CRM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi