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Protein

Histone H1.1

Gene

Hist1h1a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

H1 histones bind to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. H1 histones 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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H1.1
Alternative name(s):
Histone H1a
Gene namesi
Name:Hist1h1a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi1305706. Hist1h1a.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation
  • Chromosome PROSITE-ProRule annotation

  • Note: Mainly localizes in euchromatin.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 214213Histone H1.1PRO_0000419132Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineCombined sources
Modified residuei12 – 121PhosphoserineCombined sources
Modified residuei17 – 171N6-acetyllysineBy similarity
Modified residuei43 – 431PhosphoserineCombined sources
Modified residuei56 – 561CitrullineBy similarity
Modified residuei67 – 671PhosphoserineCombined sources
Modified residuei77 – 771N6-acetyllysineBy similarity
Modified residuei92 – 921N6-acetyllysineBy similarity
Modified residuei106 – 1061PhosphoserineBy similarity
Modified residuei121 – 1211N6-acetyllysineBy similarity
Modified residuei202 – 2021PhosphothreonineBy 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-56 (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.By similarity

Keywords - PTMi

Acetylation, Citrullination, Phosphoprotein

Proteomic databases

PaxDbiD4A3K5.
PeptideAtlasiD4A3K5.
PRIDEiD4A3K5.

PTM databases

iPTMnetiD4A3K5.

Interactioni

Subunit structurei

Interacts with DFFB.By similarity

Protein-protein interaction databases

BioGridi253432. 8 interactions.
STRINGi10116.ENSRNOP00000023054.

Structurei

3D structure databases

ProteinModelPortaliD4A3K5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 11174H15PROSITE-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

eggNOGiKOG4012. Eukaryota.
ENOG4112541. LUCA.
GeneTreeiENSGT00670000097781.
InParanoidiD4A3K5.
KOiK11275.
OMAiNIHSHNV.
OrthoDBiEOG74TX2T.
PhylomeDBiD4A3K5.
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]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS51504. H15. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

D4A3K5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSETAPVPQP ASVAPEKPAA TKKTRKPAKA AVPRKKPAGP SVSELIVQAV
60 70 80 90 100
SSSKERSGVS LAALKKSLAA AGYDVEKNNS RIKLGLKSLV NKGTLVQTKG
110 120 130 140 150
TGAAGSFKLN KKAESKASTT KVTVKAKASG AAKKPKKTAG AAAKKTVKTP
160 170 180 190 200
KKPKKPAVSK KTSSKSPKKP KVVKAKKVAK SPAKAKAVKP KAAKVKVTKP
210
KTPAKPKKAA PKKK
Length:214
Mass (Da):22,004
Last modified:April 20, 2010 - v1
Checksum:i154211E35249E239
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06091665 Genomic DNA. No translation available.
CH474064 Genomic DNA. Translation: EDL86563.1.
RefSeqiNP_001099583.1. NM_001106113.1.
UniGeneiRn.218709.

Genome annotation databases

EnsembliENSRNOT00000023054; ENSRNOP00000023054; ENSRNOG00000017175.
GeneIDi291145.
KEGGirno:291145.
UCSCiRGD:1305706. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06091665 Genomic DNA. No translation available.
CH474064 Genomic DNA. Translation: EDL86563.1.
RefSeqiNP_001099583.1. NM_001106113.1.
UniGeneiRn.218709.

3D structure databases

ProteinModelPortaliD4A3K5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi253432. 8 interactions.
STRINGi10116.ENSRNOP00000023054.

PTM databases

iPTMnetiD4A3K5.

Proteomic databases

PaxDbiD4A3K5.
PeptideAtlasiD4A3K5.
PRIDEiD4A3K5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000023054; ENSRNOP00000023054; ENSRNOG00000017175.
GeneIDi291145.
KEGGirno:291145.
UCSCiRGD:1305706. rat.

Organism-specific databases

CTDi3024.
RGDi1305706. Hist1h1a.

Phylogenomic databases

eggNOGiKOG4012. Eukaryota.
ENOG4112541. LUCA.
GeneTreeiENSGT00670000097781.
InParanoidiD4A3K5.
KOiK11275.
OMAiNIHSHNV.
OrthoDBiEOG74TX2T.
PhylomeDBiD4A3K5.
TreeFamiTF313664.

Miscellaneous databases

PROiD4A3K5.

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]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS51504. H15. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-12; SER-43 AND SER-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiH11_RAT
AccessioniPrimary (citable) accession number: D4A3K5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: April 20, 2010
Last modified: July 6, 2016
This is version 50 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.