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Protein

Histone H1.5

Gene

Hist1h1b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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).By similarity

GO - Molecular functioni

  1. DNA binding Source: MGI

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 – 11Removed2 Publications
Chaini2 – 223222Histone H1.5PRO_0000195918Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei17 – 171N6-acetyllysine1 Publication
Modified residuei18 – 181Phosphoserine1 Publication
Modified residuei26 – 261N6-acetyllysine; alternateBy similarity
Modified residuei26 – 261N6-methyllysine; alternateBy similarity
Modified residuei27 – 271N6-methyllysineBy similarity
Modified residuei34 – 341N6-methyllysine; alternateBy similarity
Modified residuei34 – 341N6-succinyllysine; alternate1 Publication
Modified residuei46 – 461N6-acetyllysine1 Publication
Modified residuei54 – 541Citrulline1 Publication
Modified residuei75 – 751N6-acetyllysine1 Publication
Modified residuei90 – 901N6-acetyllysineBy similarity
Modified residuei97 – 971N6-succinyllysineBy similarity
Modified residuei104 – 1041PhosphoserineBy similarity
Modified residuei152 – 1521PhosphothreonineBy similarity
Modified residuei165 – 1651N6-acetyllysineBy similarity
Modified residuei170 – 1701PhosphoserineBy similarity
Modified residuei185 – 1851N6-methyllysineBy similarity
Modified residuei186 – 1861PhosphoserineBy 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.1 Publication

Keywords - PTMi

Acetylation, Citrullination, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP43276.
PRIDEiP43276.

PTM databases

PhosphoSiteiP43276.

Expressioni

Gene expression databases

BgeeiP43276.
CleanExiMM_HIST1H1B.
ExpressionAtlasiP43276. baseline and differential.
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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 10974H15PROSITE-ProRule annotationAdd
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.PROSITE-ProRule annotation
Contains 1 H15 (linker histone H1/H5 globular) domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00670000097781.
HOGENOMiHOG000251627.
HOVERGENiHBG009035.
InParanoidiP43276.
KOiK11275.
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

        10         20         30         40         50
MSETAPAETA APAPVEKSPA KKKTTKKAGA AKRKATGPPV SELITKAVSA
60 70 80 90 100
SKERGGVSLP ALKKALAAGG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG
110 120 130 140 150
ASGSFKLNKK AASGEAKPKA KKTGAAKAKK PAGATPKKPK KTAGAKKTVK
160 170 180 190 200
KTPKKAKKPA AAGVKKVAKS PKKAKAAAKP KKAAKSPAKP KAVKSKASKP
210 220
KVTKPKTAKP KAAKAKKAVS KKK
Length:223
Mass (Da):22,576
Last modified:January 23, 2007 - v2
Checksum:iB9C26AC31C2716B6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611A → T in BAB32001 (PubMed:12408966).Curated
Sequence conflicti120 – 1201A → V in BAB32001 (PubMed:12408966).Curated
Sequence conflicti137 – 1371K → N in BAB32001 (PubMed:12408966).Curated
Sequence conflicti195 – 1951S → F in BAB32001 (PubMed:12408966).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP43276.
SMRiP43276. Positions 37-109.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiP43276.

Proteomic databases

MaxQBiP43276.
PRIDEiP43276.

Protocols and materials databases

DNASUi56702.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3009.
MGIiMGI:1861461. Hist1h1b.

Phylogenomic databases

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

Miscellaneous databases

NextBioi313147.
PROiP43276.
SOURCEiSearch...

Gene expression databases

BgeeiP43276.
CleanExiMM_HIST1H1B.
ExpressionAtlasiP43276. baseline and differential.
GenevestigatoriP43276.

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]
ProtoNetiSearch...

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. "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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  7. Cited for: CITRULLINATION AT ARG-54.

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: March 4, 2015
This is version 124 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.