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Protein

Histone H1.3

Gene

HIST1H1D

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

  • chromatin DNA binding Source: UniProtKB
  • RNA binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionDNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-211227 Activation of DNA fragmentation factor
R-HSA-2559584 Formation of Senescence-Associated Heterochromatin Foci (SAHF)

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H1.3
Alternative name(s):
Histone H1c
Histone H1s-2
Gene namesi
Name:HIST1H1D
Synonyms:H1F3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000124575.6
HGNCiHGNC:4717 HIST1H1D
MIMi142210 gene
neXtProtiNX_P16402

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi3007
OpenTargetsiENSG00000124575
PharmGKBiPA29095

Polymorphism and mutation databases

BioMutaiHIST1H1D
DMDMi121925

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001959072 – 221Histone H1.3Add BLAST220

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei2PhosphoserineCombined sources1
Modified residuei17N6-acetyllysineBy similarity1
Modified residuei18PhosphothreonineCombined sources1
Modified residuei35N6-(beta-hydroxybutyryl)lysine1 Publication1
Modified residuei47N6-(beta-hydroxybutyryl)lysine1 Publication1
Modified residuei53N6-(beta-hydroxybutyryl)lysine1 Publication1
Modified residuei55CitrullineBy similarity1
Modified residuei65N6-(beta-hydroxybutyryl)lysine1 Publication1
Modified residuei76N6-(beta-hydroxybutyryl)lysine1 Publication1
Modified residuei86N6-(beta-hydroxybutyryl)lysine1 Publication1
Modified residuei91N6-(beta-hydroxybutyryl)lysine1 Publication1
Modified residuei105Phosphoserine; by PKCBy similarity1
Modified residuei107N6-(beta-hydroxybutyryl)lysine1 Publication1
Modified residuei170N6-(beta-hydroxybutyryl)lysine1 Publication1

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-55 (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, Hydroxylation, Phosphoprotein

Proteomic databases

EPDiP16402
MaxQBiP16402
PaxDbiP16402
PeptideAtlasiP16402
PRIDEiP16402

PTM databases

iPTMnetiP16402
PhosphoSitePlusiP16402
SwissPalmiP16402

Expressioni

Gene expression databases

BgeeiENSG00000124575
CleanExiHS_HIST1H1D
GenevisibleiP16402 HS

Organism-specific databases

HPAiHPA055907

Interactioni

Protein-protein interaction databases

BioGridi109262, 46 interactors
CORUMiP16402
IntActiP16402, 8 interactors
MINTiP16402
STRINGi9606.ENSP00000244534

Structurei

3D structure databases

ProteinModelPortaliP16402
SMRiP16402
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini37 – 110H15PROSITE-ProRule annotationAdd BLAST74

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

Phylogenomic databases

eggNOGiKOG4012 Eukaryota
ENOG4112541 LUCA
GeneTreeiENSGT00670000097781
HOGENOMiHOG000251627
HOVERGENiHBG009035
InParanoidiP16402
KOiK11275
OMAiNSAITHG
OrthoDBiEOG091G0XGD
PhylomeDBiP16402
TreeFamiTF313664

Family and domain databases

Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR005818 Histone_H1/H5_H15
IPR005819 Histone_H5
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF00538 Linker_histone, 1 hit
PRINTSiPR00624 HISTONEH5
SMARTiView protein in SMART
SM00526 H15, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
PROSITEiView protein in PROSITE
PS51504 H15, 1 hit

Sequencei

Sequence statusi: Complete.

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

P16402-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSETAPLAPT IPAPAEKTPV KKKAKKAGAT AGKRKASGPP VSELITKAVA
60 70 80 90 100
ASKERSGVSL AALKKALAAA GYDVEKNNSR IKLGLKSLVS KGTLVQTKGT
110 120 130 140 150
GASGSFKLNK KAASGEGKPK AKKAGAAKPR KPAGAAKKPK KVAGAATPKK
160 170 180 190 200
SIKKTPKKVK KPATAAGTKK VAKSAKKVKT PQPKKAAKSP AKAKAPKPKA
210 220
AKPKSGKPKV TKAKKAAPKK K
Length:221
Mass (Da):22,350
Last modified:January 23, 2007 - v2
Checksum:iDB987FE8DE034D12
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04930675E → K. Corresponds to variant dbSNP:rs2050949Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60747 Genomic DNA Translation: AAA63186.1
AF531303 Genomic DNA Translation: AAN06703.1
AK312845 mRNA Translation: BAG35698.1
AL031777 Genomic DNA No translation available.
CH471087 Genomic DNA Translation: EAW55548.1
BC104874 mRNA Translation: AAI04875.1
BC111971 mRNA Translation: AAI11972.1
CCDSiCCDS4597.1
PIRiB40335
RefSeqiNP_005311.1, NM_005320.2
UniGeneiHs.136857

Genome annotation databases

EnsembliENST00000244534; ENSP00000244534; ENSG00000124575
GeneIDi3007
KEGGihsa:3007
UCSCiuc003nhd.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiH13_HUMAN
AccessioniPrimary (citable) accession number: P16402
Secondary accession number(s): B2R751, Q2M2I2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 166 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health