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Protein

Histone H4

Gene

HIST1H4A

more
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi17 – 215

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • histone binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • protein domain specific binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-1221632. Meiotic synapsis.
R-HSA-171306. Packaging Of Telomere Ends.
R-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-212300. PRC2 methylates histones and DNA.
R-HSA-2299718. Condensation of Prophase Chromosomes.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-HSA-3214815. HDACs deacetylate histones.
R-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-3214842. HDMs demethylate histones.
R-HSA-3214847. HATs acetylate histones.
R-HSA-3214858. RMTs methylate histone arginines.
R-HSA-427359. SIRT1 negatively regulates rRNA Expression.
R-HSA-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-5250924. B-WICH complex positively regulates rRNA expression.
R-HSA-5334118. DNA methylation.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-HSA-5625886. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-606279. Deposition of new CENPA-containing nucleosomes at the centromere.
R-HSA-69473. G2/M DNA damage checkpoint.
R-HSA-73728. RNA Polymerase I Promoter Opening.
R-HSA-73777. RNA Polymerase I Chain Elongation.
R-HSA-912446. Meiotic recombination.
R-HSA-977225. Amyloid fiber formation.
SIGNORiP62805.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H4
Gene namesi
Name:HIST1H4A
Synonyms:H4/A, H4FA
AND
Name:HIST1H4B
Synonyms:H4/I, H4FI
AND
Name:HIST1H4C
Synonyms:H4/G, H4FG
AND
Name:HIST1H4D
Synonyms:H4/B, H4FB
AND
Name:HIST1H4E
Synonyms:H4/J, H4FJ
AND
Name:HIST1H4F
Synonyms:H4/C, H4FC
AND
Name:HIST1H4H
Synonyms:H4/H, H4FH
AND
Name:HIST1H4I
Synonyms:H4/M, H4FM
AND
Name:HIST1H4J
Synonyms:H4/E, H4FE
AND
Name:HIST1H4K
Synonyms:H4/D, H4FD
AND
Name:HIST1H4L
Synonyms:H4/K, H4FK
AND
Name:HIST2H4A
Synonyms:H4/N, H4F2, H4FN, HIST2H4
AND
Name:HIST2H4B
Synonyms:H4/O, H4FO
AND
Name:HIST4H4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componentsi: Chromosome 1, Chromosome 12, Chromosome 6

Organism-specific databases

HGNCiHGNC:4781. HIST1H4A.
HGNC:4789. HIST1H4B.
HGNC:4787. HIST1H4C.
HGNC:4782. HIST1H4D.
HGNC:4790. HIST1H4E.
HGNC:4783. HIST1H4F.
HGNC:4788. HIST1H4H.
HGNC:4793. HIST1H4I.
HGNC:4785. HIST1H4J.
HGNC:4784. HIST1H4K.
HGNC:4791. HIST1H4L.
HGNC:4794. HIST2H4A.
HGNC:29607. HIST2H4B.
HGNC:20510. HIST4H4.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • extracellular region Source: Reactome
  • membrane Source: UniProtKB
  • nuclear chromosome Source: UniProtKB
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nucleoplasm Source: Reactome
  • nucleosome Source: UniProtKB
  • nucleus Source: UniProtKB
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechi

Involvement in diseasei

Chromosomal aberrations involving HISTONE H4 is a cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation t(3;6)(q27;p21), with BCL6.

Organism-specific databases

PharmGKBiPA29169.

Chemistry

ChEMBLiCHEMBL5876.

Polymorphism and mutation databases

BioMutaiHIST1H4A.
DMDMi51317339.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 103102Histone H4PRO_0000158320Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei2 – 21Phosphoserine1 Publication
Modified residuei4 – 41Asymmetric dimethylarginine; by PRMT1; alternate3 Publications
Modified residuei4 – 41Citrulline; alternate2 Publications
Modified residuei4 – 41Omega-N-methylarginine; by PRMT1; alternate3 Publications
Modified residuei4 – 41Symmetric dimethylarginine; by PRMT5 and PRMT7; alternateBy similarity
Modified residuei6 – 61N6-acetyllysine; alternateCombined sources2 Publications
Modified residuei6 – 61N6-crotonyllysine; alternate1 Publication
Modified residuei9 – 91N6-acetyllysine; alternateCombined sources2 Publications
Modified residuei9 – 91N6-crotonyllysine; alternate1 Publication
Modified residuei13 – 131N6-acetyllysine; alternateCombined sources3 Publications
Modified residuei13 – 131N6-crotonyllysine; alternate1 Publication
Cross-linki13 – 13Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei17 – 171N6-acetyllysine; alternateCombined sources3 Publications
Modified residuei17 – 171N6-crotonyllysine; alternateBy similarity
Modified residuei21 – 211N6,N6,N6-trimethyllysine; alternate3 Publications
Modified residuei21 – 211N6,N6-dimethyllysine; alternate3 Publications
Modified residuei21 – 211N6-methyllysine; alternate3 Publications
Modified residuei32 – 321N6-acetyllysineCombined sources
Modified residuei48 – 481Phosphoserine; by PAK2Combined sources1 Publication
Modified residuei52 – 521PhosphotyrosineCombined sources
Modified residuei81 – 811PhosphothreonineBy similarity
Modified residuei89 – 891PhosphotyrosineCombined sources
Modified residuei92 – 921N6-acetyllysine; alternate1 Publication
Modified residuei92 – 921N6-succinyllysine; alternateBy similarity
Cross-linki92 – 92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication

Post-translational modificationi

Acetylation at Lys-6 (H4K5ac), Lys-9 (H4K8ac), Lys-13 (H4K12ac) and Lys-17 (H4K16ac) occurs in coding regions of the genome but not in heterochromatin.3 Publications
Citrullination at Arg-4 (H4R3ci) by PADI4 impairs methylation.4 Publications
Monomethylation and asymmetric dimethylation at Arg-4 (H4R3me1 and H4R3me2a, respectively) by PRMT1 favors acetylation at Lys-9 (H4K8ac) and Lys-13 (H4K12ac). Demethylation is performed by JMJD6. Symmetric dimethylation on Arg-4 (H4R3me2s) by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage.3 Publications
Monomethylated, dimethylated or trimethylated at Lys-21 (H4K20me1, H4K20me2, H4K20me3). Monomethylation is performed by SET8. Trimethylation is performed by KMT5B and KMT5C and induces gene silencing.
Phosphorylated by PAK2 at Ser-48 (H4S47ph). This phosphorylation increases the association of H3.3-H4 with the histone chaperone HIRA, thus promoting nucleosome assembly of H3.3-H4 and inhibiting nucleosome assembly of H3.1-H4.2 Publications
Ubiquitinated by the CUL4-DDB-RBX1 complex in response to ultraviolet irradiation. This may weaken the interaction between histones and DNA and facilitate DNA accessibility to repair proteins. Monoubiquitinated at Lys-92 of histone H4 (H4K91ub1) in response to DNA damage. The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post-translational modifications such as H4 Lys-21 methylation (H4K20me).5 Publications
Sumoylated, which is associated with transcriptional repression.1 Publication
Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes.1 Publication

Keywords - PTMi

Acetylation, Citrullination, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP62805.
MaxQBiP62805.
PaxDbiP62805.
PeptideAtlasiP62805.
PRIDEiP62805.
TopDownProteomicsiP62805.

2D gel databases

SWISS-2DPAGEP62805.

PTM databases

iPTMnetiP62805.
PhosphoSiteiP62805.
SwissPalmiP62805.

Expressioni

Gene expression databases

BgeeiENSG00000124529.
CleanExiHS_HIST1H4A.
HS_HIST1H4B.
HS_HIST1H4C.
HS_HIST1H4D.
HS_HIST1H4E.
HS_HIST1H4F.
HS_HIST1H4H.
HS_HIST1H4I.
HS_HIST1H4L.
HS_HIST2H4A.
HS_HIST2H4B.
HS_HIST4H4.
ExpressionAtlasiP62805. baseline and differential.
GenevisibleiP62805. HS.

Organism-specific databases

HPAiCAB011503.
CAB021887.
CAB037279.
HPA042201.

Interactioni

Subunit structurei

The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.

Binary interactionsi

WithEntry#Exp.IntActNotes
ASF1AQ9Y2944EBI-302023,EBI-749553
BPTFQ128303EBI-302023,EBI-1560273
BPTFQ12830-416EBI-302023,EBI-4288838
BRD2P254405EBI-302023,EBI-2874802
BRD4O60885-17EBI-302023,EBI-9345088
BRPF1P552018EBI-302023,EBI-2837428
CENPAP494504EBI-302023,EBI-1751979
COPRSQ9NQ923EBI-302023,EBI-1642558
CrebbpP454812EBI-302023,EBI-296306From a different organism.
H3F3BP842433EBI-302023,EBI-120658
HAT1O149294EBI-302023,EBI-2339359
HDAC1Q135473EBI-302023,EBI-301834
HIST1H3DP684313EBI-302023,EBI-79722
JMJD4Q9H9V93EBI-302023,EBI-2866290
KDM4AO751647EBI-302023,EBI-936709
KMT5AQ9NQR15EBI-302023,EBI-1268946
L3MBTL1Q9Y4684EBI-302023,EBI-1265089
MCM2P497363EBI-302023,EBI-374819
MCM3P252052EBI-302023,EBI-355153
MCM5P339922EBI-302023,EBI-359410
PHF20Q9BVI03EBI-302023,EBI-2560802
PHF20L1A8MW922EBI-302023,EBI-2560834
PRMT5O147443EBI-302023,EBI-351098
RBBP7Q165764EBI-302023,EBI-352227
SfmbtQ9VK3310EBI-302023,EBI-117801From a different organism.
SIAH1Q8IUQ43EBI-302023,EBI-747107
SMARCA5O602642EBI-302023,EBI-352588
TLE1Q047246EBI-302023,EBI-711424
TP53BP1Q128888EBI-302023,EBI-396540
YWHAZP631043EBI-302023,EBI-347088

GO - Molecular functioni

  • histone binding Source: UniProtKB
  • protein domain specific binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113899. 23 interactions.
113955. 172 interactions.
113956. 17 interactions.
113957. 30 interactions.
113958. 16 interactions.
113959. 18 interactions.
113960. 16 interactions.
113961. 20 interactions.
113962. 16 interactions.
113963. 21 interactions.
113964. 18 interactions.
113966. 48 interactions.
125732. 87 interactions.
299853. 18 interactions.
DIPiDIP-33079N.
IntActiP62805. 112 interactions.
MINTiMINT-276350.
STRINGi9606.ENSP00000367034.

Chemistry

BindingDBiP62805.

Structurei

Secondary structure

1
103
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni7 – 104Combined sources
Beta strandi21 – 233Combined sources
Beta strandi28 – 303Combined sources
Helixi32 – 4110Combined sources
Beta strandi45 – 473Combined sources
Helixi49 – 7628Combined sources
Beta strandi80 – 823Combined sources
Helixi84 – 918Combined sources
Beta strandi94 – 963Combined sources
Turni97 – 1026Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZKKX-ray1.45E/F/G/H16-25[»]
2BQZX-ray1.50B/F18-26[»]
2CV5X-ray2.50B/F1-103[»]
2IG0X-ray1.70B17-26[»]
2KWNNMR-B10-24[»]
2KWONMR-B2-21[»]
2LVMNMR-B15-28[»]
2QQSX-ray2.82C/D17-26[»]
2RJEX-ray1.86P/Q16-26[»]
2RNYNMR-B14-28[»]
2RS9NMR-A2-11[»]
3A6NX-ray2.70B/F1-103[»]
3AFAX-ray2.50B/F1-103[»]
3AN2X-ray3.60B/F1-103[»]
3AV1X-ray2.50B/F1-103[»]
3AV2X-ray2.80B/F1-103[»]
3AYWX-ray2.90B/F1-103[»]
3AZEX-ray3.00B/F1-103[»]
3AZFX-ray2.70B/F1-103[»]
3AZGX-ray2.40B/F1-103[»]
3AZHX-ray3.49B/F1-103[»]
3AZIX-ray2.70B/F1-103[»]
3AZJX-ray2.89B/F1-103[»]
3AZKX-ray3.20B/F1-103[»]
3AZLX-ray2.70B/F1-103[»]
3AZMX-ray2.89B/F1-103[»]
3AZNX-ray3.00B/F1-103[»]
3CFSX-ray2.40E28-42[»]
3CFVX-ray2.60E/F25-42[»]
3F9WX-ray1.60E/F/G/H16-25[»]
3F9XX-ray1.25E/F/G/H16-25[»]
3F9YX-ray1.50E/F16-25[»]
3F9ZX-ray1.60E/F/G/H16-25[»]
3IJ1X-ray2.10B16-26[»]
3JPXX-ray2.05B14-28[»]
3NQJX-ray2.10B21-103[»]
3NQUX-ray2.50B1-103[»]
3O36X-ray1.70D/E15-20[»]
3QBYX-ray1.95H16-26[»]
3QZSX-ray1.80C/D13-22[»]
3QZTX-ray1.50B13-22[»]
3QZVX-ray2.00C8-18[»]
3R45X-ray2.60B1-103[»]
3UVWX-ray1.37B2-12[»]
3UVXX-ray1.91B12-22[»]
3UVYX-ray2.02B16-26[»]
3UW9X-ray2.30E/F8-18[»]
3W96X-ray3.00B/F1-103[»]
3W97X-ray3.20B/F1-103[»]
3W98X-ray3.42B/F1-103[»]
3W99X-ray3.00B/F17-103[»]
3WA9X-ray3.07B/F1-103[»]
3WAAX-ray3.20B/F1-103[»]
3WKJX-ray2.80B/F1-103[»]
3WTPX-ray2.67B/F1-103[»]
3X1SX-ray2.81B/F2-103[»]
3X1TX-ray2.81B/F2-103[»]
3X1UX-ray3.25B/F2-103[»]
3X1VX-ray2.92B/F2-103[»]
4GQBX-ray2.06C2-22[»]
4H9NX-ray1.95B2-103[»]
4H9OX-ray2.05B2-103[»]
4H9PX-ray2.20B2-103[»]
4H9QX-ray1.95B2-103[»]
4H9RX-ray2.20B2-103[»]
4H9SX-ray2.60C/D21-103[»]
4HGAX-ray2.80C1-103[»]
4M38X-ray2.20E/F2-22[»]
4N3WX-ray1.90C14-28[»]
4N4FX-ray1.83C6-26[»]
4QUTX-ray1.70B10-16[»]
4QUUX-ray1.80B4-16[»]
4QYDX-ray1.94B5-18[»]
4U9WX-ray2.49E/F/G/H2-6[»]
4YM5X-ray4.00B/F1-103[»]
4YM6X-ray3.51B/F1-103[»]
4YY6X-ray1.45Z2-12[»]
4YYDX-ray1.52Z2-12[»]
4YYGX-ray2.10B2-12[»]
4YYHX-ray1.74Y/Z2-12[»]
4YYIX-ray1.50C/F2-12[»]
4YYJX-ray1.85C/F2-12[»]
4YYKX-ray1.79C/F2-12[»]
4YYMX-ray1.50Z2-12[»]
4YYNX-ray1.85Z2-12[»]
4Z2MX-ray2.98H/J1-103[»]
4Z5TX-ray2.80B/F1-103[»]
5AV5X-ray2.40B/F1-103[»]
5AV6X-ray2.20B/F1-103[»]
5AV8X-ray2.20B/F1-103[»]
5AV9X-ray2.20B/F1-103[»]
5AVBX-ray2.40B/F1-103[»]
5AVCX-ray2.40B/F1-103[»]
5AY8X-ray2.80B/F1-103[»]
5B0YX-ray2.56B/F1-103[»]
5B0ZX-ray1.99B/F1-103[»]
5B24X-ray3.60B/F1-103[»]
5B2IX-ray3.00B/F1-103[»]
5B2JX-ray2.60B/F1-103[»]
5B40X-ray3.33B/F1-103[»]
5BNVX-ray2.79B/E2-103[»]
5BNXX-ray2.31B2-103[»]
5BO0X-ray2.91B2-103[»]
5C3IX-ray3.50C/G/K/O/S/W1-103[»]
5CPIX-ray2.90B/F1-103[»]
5CPJX-ray3.15B/F1-103[»]
5CPKX-ray2.63B/F1-103[»]
5FA5X-ray2.34C2-21[»]
5FFWX-ray1.50C2-11[»]
5FWEX-ray2.05C/D2-16[»]
5JA4X-ray2.42B2-103[»]
ProteinModelPortaliP62805.
SMRiP62805. Positions 21-102.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62805.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H4 family.Curated

Phylogenomic databases

eggNOGiKOG3467. Eukaryota.
COG2036. LUCA.
GeneTreeiENSGT00760000119019.
HOGENOMiHOG000234654.
HOVERGENiHBG051878.
InParanoidiP62805.
KOiK11254.
OMAiSTHNERI.
OrthoDBiEOG091G0XGD.
PhylomeDBiP62805.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR001951. Histone_H4.
IPR019809. Histone_H4_CS.
IPR004823. TAF_TATA-bd.
[Graphical view]
PRINTSiPR00623. HISTONEH4.
SMARTiSM00417. H4. 1 hit.
SM00803. TAF. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00047. HISTONE_H4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P62805-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL
60 70 80 90 100
IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG

FGG
Length:103
Mass (Da):11,367
Last modified:January 23, 2007 - v2
Checksum:iA9E5DFD3F8B97598
GO

Sequence cautioni

The sequence AAI28106 differs from that shown. Reason: Frameshift at position 3. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711V → A in AAH67496 (PubMed:15489334).Curated
Sequence conflicti77 – 771A → P in CAG46986 (Ref. 11) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti64 – 641E → Q in a breast cancer sample; somatic mutation. 1 Publication
Corresponds to variant rs747622981 [ dbSNP | Ensembl ].
VAR_036206

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00038 Genomic DNA. Translation: CAA24918.1. Sequence problems.
M16707 Genomic DNA. Translation: AAA52652.1.
M60749 Genomic DNA. Translation: AAA63188.1.
X60481 Genomic DNA. Translation: CAA43011.1.
X60482 Genomic DNA. Translation: CAA43012.1.
X60483 Genomic DNA. Translation: CAA43013.1.
X60484 Genomic DNA. Translation: CAA43014.1.
X60486 Genomic DNA. Translation: CAA43016.1.
X60487 Genomic DNA. Translation: CAA43017.1.
X67081 Genomic DNA. Translation: CAA47464.1.
Z80787 Genomic DNA. Translation: CAB02549.1.
X83548 Genomic DNA. Translation: CAA58538.1.
AF525682 Genomic DNA. Translation: AAM83108.1.
AY128653 Genomic DNA. Translation: AAN01438.1.
AY128654 Genomic DNA. Translation: AAN01439.1.
AY128655 Genomic DNA. Translation: AAN01440.1.
AY128656 Genomic DNA. Translation: AAN01441.1.
AY128657 Genomic DNA. Translation: AAN01442.1.
AY128658 Genomic DNA. Translation: AAN01443.1.
AY128659 Genomic DNA. Translation: AAN01444.1.
AY128661 Genomic DNA. Translation: AAN01446.1.
AY128662 Genomic DNA. Translation: AAN01447.1.
AY128663 Genomic DNA. Translation: AAN01448.1.
AY128664 Genomic DNA. Translation: AAN01449.1.
AY128665 Genomic DNA. Translation: AAN01450.1.
AB000905 Genomic DNA. Translation: BAA19208.1.
AY648850 Genomic DNA. Translation: AAT68253.1.
CR542169 mRNA. Translation: CAG46966.1.
CR542172 mRNA. Translation: CAG46969.1.
CR542180 mRNA. Translation: CAG46977.1.
CR542187 mRNA. Translation: CAG46984.1.
CR542189 mRNA. Translation: CAG46986.1.
AL021807 Genomic DNA. Translation: CAA16946.1.
AL021917 Genomic DNA. Translation: CAC69642.1.
AL031777 Genomic DNA. Translation: CAC03414.1.
AL031777 Genomic DNA. Translation: CAC03418.1.
AL049822 Genomic DNA. Translation: CAC03426.1.
AL049822 Genomic DNA. Translation: CAC03427.1.
AL353759 Genomic DNA. Translation: CAC04128.1.
Z98744 Genomic DNA. Translation: CAD24074.1.
AL591493 Genomic DNA. Translation: CAI12560.1.
AL591493 Genomic DNA. Translation: CAI12567.1.
CH471087 Genomic DNA. Translation: EAW55509.1.
CH471087 Genomic DNA. Translation: EAW55510.1.
CH471087 Genomic DNA. Translation: EAW55538.1.
CH471087 Genomic DNA. Translation: EAW55549.1.
CH471087 Genomic DNA. Translation: EAW55555.1.
CH471094 Genomic DNA. Translation: EAW96325.1.
CH471081 Genomic DNA. Translation: EAX03086.1.
CH471081 Genomic DNA. Translation: EAX03111.1.
CH471081 Genomic DNA. Translation: EAX03112.1.
CH471081 Genomic DNA. Translation: EAX03121.1.
BC017361 mRNA. Translation: AAH17361.1.
BC054014 mRNA. Translation: AAH54014.1.
BC066248 mRNA. Translation: AAH66248.1.
BC066249 mRNA. Translation: AAH66249.1.
BC066250 mRNA. Translation: AAH66250.1.
BC067495 mRNA. Translation: AAH67495.1.
BC067496 mRNA. Translation: AAH67496.1.
BC067497 mRNA. Translation: AAH67497.1.
BC069288 mRNA. Translation: AAH69288.1.
BC069392 mRNA. Translation: AAH69392.1.
BC069467 mRNA. Translation: AAH69467.1.
BC069654 mRNA. Translation: AAH69654.1.
BC093763 mRNA. Translation: AAH93763.1.
BC093765 mRNA. Translation: AAH93765.1.
BC093969 mRNA. Translation: AAH93969.1.
BC111093 mRNA. Translation: AAI11094.1.
BC111434 mRNA. Translation: AAI11435.1.
BC112193 mRNA. Translation: AAI12194.1.
BC120939 mRNA. Translation: AAI20940.1.
BC128104 mRNA. Translation: AAI28105.1.
BC128105 mRNA. Translation: AAI28106.1. Frameshift.
BC130558 mRNA. Translation: AAI30559.1.
BC130560 mRNA. Translation: AAI30561.1.
BC143045 mRNA. Translation: AAI43046.1.
CCDSiCCDS30847.1.
CCDS30851.1.
CCDS4571.1.
CCDS4572.1.
CCDS4583.1.
CCDS4589.1.
CCDS4593.1.
CCDS4598.1.
CCDS4604.1.
CCDS4620.1.
CCDS4630.1.
CCDS4631.1.
CCDS4637.1.
CCDS8665.1.
PIRiD40335. HSHU4.
RefSeqiNP_001029249.1. NM_001034077.4.
NP_003486.1. NM_003495.2.
NP_003529.1. NM_003538.3.
NP_003530.1. NM_003539.3.
NP_003531.1. NM_003540.3.
NP_003532.1. NM_003541.2.
NP_003533.1. NM_003542.3.
NP_003534.1. NM_003543.3.
NP_003535.1. NM_003544.2.
NP_003536.1. NM_003545.3.
NP_003537.1. NM_003546.2.
NP_003539.1. NM_003548.2.
NP_068803.1. NM_021968.3.
NP_778224.1. NM_175054.2.
UniGeneiHs.143080.
Hs.247816.
Hs.248172.
Hs.248178.
Hs.248179.
Hs.278483.
Hs.46423.
Hs.528055.
Hs.533295.
Hs.55468.
Hs.591790.
Hs.655235.
Hs.662174.
Hs.706635.
Hs.745457.

Genome annotation databases

EnsembliENST00000244537; ENSP00000244537; ENSG00000274618.
ENST00000355057; ENSP00000347168; ENSG00000197238.
ENST00000358064; ENSP00000350767; ENSG00000197837.
ENST00000377727; ENSP00000366956; ENSG00000158406.
ENST00000377745; ENSP00000366974; ENSG00000278705.
ENST00000377803; ENSP00000367034; ENSG00000197061.
ENST00000539745; ENSP00000443017; ENSG00000197837.
ENST00000578186; ENSP00000462667; ENSG00000270882.
ENST00000579512; ENSP00000462355; ENSG00000270276.
ENST00000611927; ENSP00000479794; ENSG00000273542.
ENST00000612061; ENSP00000482412; ENSG00000270276.
ENST00000613412; ENSP00000481343; ENSG00000270882.
ENST00000614247; ENSP00000479461; ENSG00000277157.
ENST00000614272; ENSP00000478519; ENSG00000270882.
ENST00000615164; ENSP00000484789; ENSG00000276966.
ENST00000615353; ENSP00000481486; ENSG00000276180.
ENST00000617569; ENSP00000479106; ENSG00000278637.
ENST00000618193; ENSP00000478786; ENSG00000270882.
ENST00000618305; ENSP00000480960; ENSG00000275126.
ENST00000621520; ENSP00000481507; ENSG00000270276.
ENST00000634560; ENSP00000489319; ENSG00000158406.
ENST00000634956; ENSP00000489567; ENSG00000158406.
ENST00000635491; ENSP00000489236; ENSG00000158406.
GeneIDi121504.
554313.
8294.
8359.
8360.
8361.
8362.
8363.
8364.
8365.
8366.
8367.
8368.
8370.
KEGGihsa:121504.
hsa:554313.
hsa:8294.
hsa:8359.
hsa:8360.
hsa:8361.
hsa:8362.
hsa:8363.
hsa:8364.
hsa:8365.
hsa:8366.
hsa:8367.
hsa:8368.
hsa:8370.
UCSCiuc001ess.4. human.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00038 Genomic DNA. Translation: CAA24918.1. Sequence problems.
M16707 Genomic DNA. Translation: AAA52652.1.
M60749 Genomic DNA. Translation: AAA63188.1.
X60481 Genomic DNA. Translation: CAA43011.1.
X60482 Genomic DNA. Translation: CAA43012.1.
X60483 Genomic DNA. Translation: CAA43013.1.
X60484 Genomic DNA. Translation: CAA43014.1.
X60486 Genomic DNA. Translation: CAA43016.1.
X60487 Genomic DNA. Translation: CAA43017.1.
X67081 Genomic DNA. Translation: CAA47464.1.
Z80787 Genomic DNA. Translation: CAB02549.1.
X83548 Genomic DNA. Translation: CAA58538.1.
AF525682 Genomic DNA. Translation: AAM83108.1.
AY128653 Genomic DNA. Translation: AAN01438.1.
AY128654 Genomic DNA. Translation: AAN01439.1.
AY128655 Genomic DNA. Translation: AAN01440.1.
AY128656 Genomic DNA. Translation: AAN01441.1.
AY128657 Genomic DNA. Translation: AAN01442.1.
AY128658 Genomic DNA. Translation: AAN01443.1.
AY128659 Genomic DNA. Translation: AAN01444.1.
AY128661 Genomic DNA. Translation: AAN01446.1.
AY128662 Genomic DNA. Translation: AAN01447.1.
AY128663 Genomic DNA. Translation: AAN01448.1.
AY128664 Genomic DNA. Translation: AAN01449.1.
AY128665 Genomic DNA. Translation: AAN01450.1.
AB000905 Genomic DNA. Translation: BAA19208.1.
AY648850 Genomic DNA. Translation: AAT68253.1.
CR542169 mRNA. Translation: CAG46966.1.
CR542172 mRNA. Translation: CAG46969.1.
CR542180 mRNA. Translation: CAG46977.1.
CR542187 mRNA. Translation: CAG46984.1.
CR542189 mRNA. Translation: CAG46986.1.
AL021807 Genomic DNA. Translation: CAA16946.1.
AL021917 Genomic DNA. Translation: CAC69642.1.
AL031777 Genomic DNA. Translation: CAC03414.1.
AL031777 Genomic DNA. Translation: CAC03418.1.
AL049822 Genomic DNA. Translation: CAC03426.1.
AL049822 Genomic DNA. Translation: CAC03427.1.
AL353759 Genomic DNA. Translation: CAC04128.1.
Z98744 Genomic DNA. Translation: CAD24074.1.
AL591493 Genomic DNA. Translation: CAI12560.1.
AL591493 Genomic DNA. Translation: CAI12567.1.
CH471087 Genomic DNA. Translation: EAW55509.1.
CH471087 Genomic DNA. Translation: EAW55510.1.
CH471087 Genomic DNA. Translation: EAW55538.1.
CH471087 Genomic DNA. Translation: EAW55549.1.
CH471087 Genomic DNA. Translation: EAW55555.1.
CH471094 Genomic DNA. Translation: EAW96325.1.
CH471081 Genomic DNA. Translation: EAX03086.1.
CH471081 Genomic DNA. Translation: EAX03111.1.
CH471081 Genomic DNA. Translation: EAX03112.1.
CH471081 Genomic DNA. Translation: EAX03121.1.
BC017361 mRNA. Translation: AAH17361.1.
BC054014 mRNA. Translation: AAH54014.1.
BC066248 mRNA. Translation: AAH66248.1.
BC066249 mRNA. Translation: AAH66249.1.
BC066250 mRNA. Translation: AAH66250.1.
BC067495 mRNA. Translation: AAH67495.1.
BC067496 mRNA. Translation: AAH67496.1.
BC067497 mRNA. Translation: AAH67497.1.
BC069288 mRNA. Translation: AAH69288.1.
BC069392 mRNA. Translation: AAH69392.1.
BC069467 mRNA. Translation: AAH69467.1.
BC069654 mRNA. Translation: AAH69654.1.
BC093763 mRNA. Translation: AAH93763.1.
BC093765 mRNA. Translation: AAH93765.1.
BC093969 mRNA. Translation: AAH93969.1.
BC111093 mRNA. Translation: AAI11094.1.
BC111434 mRNA. Translation: AAI11435.1.
BC112193 mRNA. Translation: AAI12194.1.
BC120939 mRNA. Translation: AAI20940.1.
BC128104 mRNA. Translation: AAI28105.1.
BC128105 mRNA. Translation: AAI28106.1. Frameshift.
BC130558 mRNA. Translation: AAI30559.1.
BC130560 mRNA. Translation: AAI30561.1.
BC143045 mRNA. Translation: AAI43046.1.
CCDSiCCDS30847.1.
CCDS30851.1.
CCDS4571.1.
CCDS4572.1.
CCDS4583.1.
CCDS4589.1.
CCDS4593.1.
CCDS4598.1.
CCDS4604.1.
CCDS4620.1.
CCDS4630.1.
CCDS4631.1.
CCDS4637.1.
CCDS8665.1.
PIRiD40335. HSHU4.
RefSeqiNP_001029249.1. NM_001034077.4.
NP_003486.1. NM_003495.2.
NP_003529.1. NM_003538.3.
NP_003530.1. NM_003539.3.
NP_003531.1. NM_003540.3.
NP_003532.1. NM_003541.2.
NP_003533.1. NM_003542.3.
NP_003534.1. NM_003543.3.
NP_003535.1. NM_003544.2.
NP_003536.1. NM_003545.3.
NP_003537.1. NM_003546.2.
NP_003539.1. NM_003548.2.
NP_068803.1. NM_021968.3.
NP_778224.1. NM_175054.2.
UniGeneiHs.143080.
Hs.247816.
Hs.248172.
Hs.248178.
Hs.248179.
Hs.278483.
Hs.46423.
Hs.528055.
Hs.533295.
Hs.55468.
Hs.591790.
Hs.655235.
Hs.662174.
Hs.706635.
Hs.745457.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZKKX-ray1.45E/F/G/H16-25[»]
2BQZX-ray1.50B/F18-26[»]
2CV5X-ray2.50B/F1-103[»]
2IG0X-ray1.70B17-26[»]
2KWNNMR-B10-24[»]
2KWONMR-B2-21[»]
2LVMNMR-B15-28[»]
2QQSX-ray2.82C/D17-26[»]
2RJEX-ray1.86P/Q16-26[»]
2RNYNMR-B14-28[»]
2RS9NMR-A2-11[»]
3A6NX-ray2.70B/F1-103[»]
3AFAX-ray2.50B/F1-103[»]
3AN2X-ray3.60B/F1-103[»]
3AV1X-ray2.50B/F1-103[»]
3AV2X-ray2.80B/F1-103[»]
3AYWX-ray2.90B/F1-103[»]
3AZEX-ray3.00B/F1-103[»]
3AZFX-ray2.70B/F1-103[»]
3AZGX-ray2.40B/F1-103[»]
3AZHX-ray3.49B/F1-103[»]
3AZIX-ray2.70B/F1-103[»]
3AZJX-ray2.89B/F1-103[»]
3AZKX-ray3.20B/F1-103[»]
3AZLX-ray2.70B/F1-103[»]
3AZMX-ray2.89B/F1-103[»]
3AZNX-ray3.00B/F1-103[»]
3CFSX-ray2.40E28-42[»]
3CFVX-ray2.60E/F25-42[»]
3F9WX-ray1.60E/F/G/H16-25[»]
3F9XX-ray1.25E/F/G/H16-25[»]
3F9YX-ray1.50E/F16-25[»]
3F9ZX-ray1.60E/F/G/H16-25[»]
3IJ1X-ray2.10B16-26[»]
3JPXX-ray2.05B14-28[»]
3NQJX-ray2.10B21-103[»]
3NQUX-ray2.50B1-103[»]
3O36X-ray1.70D/E15-20[»]
3QBYX-ray1.95H16-26[»]
3QZSX-ray1.80C/D13-22[»]
3QZTX-ray1.50B13-22[»]
3QZVX-ray2.00C8-18[»]
3R45X-ray2.60B1-103[»]
3UVWX-ray1.37B2-12[»]
3UVXX-ray1.91B12-22[»]
3UVYX-ray2.02B16-26[»]
3UW9X-ray2.30E/F8-18[»]
3W96X-ray3.00B/F1-103[»]
3W97X-ray3.20B/F1-103[»]
3W98X-ray3.42B/F1-103[»]
3W99X-ray3.00B/F17-103[»]
3WA9X-ray3.07B/F1-103[»]
3WAAX-ray3.20B/F1-103[»]
3WKJX-ray2.80B/F1-103[»]
3WTPX-ray2.67B/F1-103[»]
3X1SX-ray2.81B/F2-103[»]
3X1TX-ray2.81B/F2-103[»]
3X1UX-ray3.25B/F2-103[»]
3X1VX-ray2.92B/F2-103[»]
4GQBX-ray2.06C2-22[»]
4H9NX-ray1.95B2-103[»]
4H9OX-ray2.05B2-103[»]
4H9PX-ray2.20B2-103[»]
4H9QX-ray1.95B2-103[»]
4H9RX-ray2.20B2-103[»]
4H9SX-ray2.60C/D21-103[»]
4HGAX-ray2.80C1-103[»]
4M38X-ray2.20E/F2-22[»]
4N3WX-ray1.90C14-28[»]
4N4FX-ray1.83C6-26[»]
4QUTX-ray1.70B10-16[»]
4QUUX-ray1.80B4-16[»]
4QYDX-ray1.94B5-18[»]
4U9WX-ray2.49E/F/G/H2-6[»]
4YM5X-ray4.00B/F1-103[»]
4YM6X-ray3.51B/F1-103[»]
4YY6X-ray1.45Z2-12[»]
4YYDX-ray1.52Z2-12[»]
4YYGX-ray2.10B2-12[»]
4YYHX-ray1.74Y/Z2-12[»]
4YYIX-ray1.50C/F2-12[»]
4YYJX-ray1.85C/F2-12[»]
4YYKX-ray1.79C/F2-12[»]
4YYMX-ray1.50Z2-12[»]
4YYNX-ray1.85Z2-12[»]
4Z2MX-ray2.98H/J1-103[»]
4Z5TX-ray2.80B/F1-103[»]
5AV5X-ray2.40B/F1-103[»]
5AV6X-ray2.20B/F1-103[»]
5AV8X-ray2.20B/F1-103[»]
5AV9X-ray2.20B/F1-103[»]
5AVBX-ray2.40B/F1-103[»]
5AVCX-ray2.40B/F1-103[»]
5AY8X-ray2.80B/F1-103[»]
5B0YX-ray2.56B/F1-103[»]
5B0ZX-ray1.99B/F1-103[»]
5B24X-ray3.60B/F1-103[»]
5B2IX-ray3.00B/F1-103[»]
5B2JX-ray2.60B/F1-103[»]
5B40X-ray3.33B/F1-103[»]
5BNVX-ray2.79B/E2-103[»]
5BNXX-ray2.31B2-103[»]
5BO0X-ray2.91B2-103[»]
5C3IX-ray3.50C/G/K/O/S/W1-103[»]
5CPIX-ray2.90B/F1-103[»]
5CPJX-ray3.15B/F1-103[»]
5CPKX-ray2.63B/F1-103[»]
5FA5X-ray2.34C2-21[»]
5FFWX-ray1.50C2-11[»]
5FWEX-ray2.05C/D2-16[»]
5JA4X-ray2.42B2-103[»]
ProteinModelPortaliP62805.
SMRiP62805. Positions 21-102.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113899. 23 interactions.
113955. 172 interactions.
113956. 17 interactions.
113957. 30 interactions.
113958. 16 interactions.
113959. 18 interactions.
113960. 16 interactions.
113961. 20 interactions.
113962. 16 interactions.
113963. 21 interactions.
113964. 18 interactions.
113966. 48 interactions.
125732. 87 interactions.
299853. 18 interactions.
DIPiDIP-33079N.
IntActiP62805. 112 interactions.
MINTiMINT-276350.
STRINGi9606.ENSP00000367034.

Chemistry

BindingDBiP62805.
ChEMBLiCHEMBL5876.

PTM databases

iPTMnetiP62805.
PhosphoSiteiP62805.
SwissPalmiP62805.

Polymorphism and mutation databases

BioMutaiHIST1H4A.
DMDMi51317339.

2D gel databases

SWISS-2DPAGEP62805.

Proteomic databases

EPDiP62805.
MaxQBiP62805.
PaxDbiP62805.
PeptideAtlasiP62805.
PRIDEiP62805.
TopDownProteomicsiP62805.

Protocols and materials databases

DNASUi8294.
8360.
8362.
8363.
8364.
8365.
8366.
8367.
8368.
8370.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000244537; ENSP00000244537; ENSG00000274618.
ENST00000355057; ENSP00000347168; ENSG00000197238.
ENST00000358064; ENSP00000350767; ENSG00000197837.
ENST00000377727; ENSP00000366956; ENSG00000158406.
ENST00000377745; ENSP00000366974; ENSG00000278705.
ENST00000377803; ENSP00000367034; ENSG00000197061.
ENST00000539745; ENSP00000443017; ENSG00000197837.
ENST00000578186; ENSP00000462667; ENSG00000270882.
ENST00000579512; ENSP00000462355; ENSG00000270276.
ENST00000611927; ENSP00000479794; ENSG00000273542.
ENST00000612061; ENSP00000482412; ENSG00000270276.
ENST00000613412; ENSP00000481343; ENSG00000270882.
ENST00000614247; ENSP00000479461; ENSG00000277157.
ENST00000614272; ENSP00000478519; ENSG00000270882.
ENST00000615164; ENSP00000484789; ENSG00000276966.
ENST00000615353; ENSP00000481486; ENSG00000276180.
ENST00000617569; ENSP00000479106; ENSG00000278637.
ENST00000618193; ENSP00000478786; ENSG00000270882.
ENST00000618305; ENSP00000480960; ENSG00000275126.
ENST00000621520; ENSP00000481507; ENSG00000270276.
ENST00000634560; ENSP00000489319; ENSG00000158406.
ENST00000634956; ENSP00000489567; ENSG00000158406.
ENST00000635491; ENSP00000489236; ENSG00000158406.
GeneIDi121504.
554313.
8294.
8359.
8360.
8361.
8362.
8363.
8364.
8365.
8366.
8367.
8368.
8370.
KEGGihsa:121504.
hsa:554313.
hsa:8294.
hsa:8359.
hsa:8360.
hsa:8361.
hsa:8362.
hsa:8363.
hsa:8364.
hsa:8365.
hsa:8366.
hsa:8367.
hsa:8368.
hsa:8370.
UCSCiuc001ess.4. human.

Organism-specific databases

CTDi121504.
554313.
8294.
8359.
8360.
8361.
8362.
8363.
8364.
8365.
8366.
8367.
8368.
8370.
GeneCardsiHIST1H4A.
HIST1H4B.
HIST1H4C.
HIST1H4D.
HIST1H4E.
HIST1H4F.
HIST1H4H.
HIST1H4I.
HIST1H4J.
HIST1H4K.
HIST1H4L.
HIST2H4A.
HIST2H4B.
HIST4H4.
HGNCiHGNC:4781. HIST1H4A.
HGNC:4789. HIST1H4B.
HGNC:4787. HIST1H4C.
HGNC:4782. HIST1H4D.
HGNC:4790. HIST1H4E.
HGNC:4783. HIST1H4F.
HGNC:4788. HIST1H4H.
HGNC:4793. HIST1H4I.
HGNC:4785. HIST1H4J.
HGNC:4784. HIST1H4K.
HGNC:4791. HIST1H4L.
HGNC:4794. HIST2H4A.
HGNC:29607. HIST2H4B.
HGNC:20510. HIST4H4.
HPAiCAB011503.
CAB021887.
CAB037279.
HPA042201.
MIMi142750. gene.
602822. gene.
602823. gene.
602824. gene.
602825. gene.
602826. gene.
602827. gene.
602828. gene.
602829. gene.
602830. gene.
602831. gene.
602833. gene.
615069. gene.
neXtProtiNX_P62805.
PharmGKBiPA29169.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3467. Eukaryota.
COG2036. LUCA.
GeneTreeiENSGT00760000119019.
HOGENOMiHOG000234654.
HOVERGENiHBG051878.
InParanoidiP62805.
KOiK11254.
OMAiSTHNERI.
OrthoDBiEOG091G0XGD.
PhylomeDBiP62805.

Enzyme and pathway databases

ReactomeiR-HSA-1221632. Meiotic synapsis.
R-HSA-171306. Packaging Of Telomere Ends.
R-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-212300. PRC2 methylates histones and DNA.
R-HSA-2299718. Condensation of Prophase Chromosomes.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-HSA-3214815. HDACs deacetylate histones.
R-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-3214842. HDMs demethylate histones.
R-HSA-3214847. HATs acetylate histones.
R-HSA-3214858. RMTs methylate histone arginines.
R-HSA-427359. SIRT1 negatively regulates rRNA Expression.
R-HSA-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-5250924. B-WICH complex positively regulates rRNA expression.
R-HSA-5334118. DNA methylation.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-HSA-5625886. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-606279. Deposition of new CENPA-containing nucleosomes at the centromere.
R-HSA-69473. G2/M DNA damage checkpoint.
R-HSA-73728. RNA Polymerase I Promoter Opening.
R-HSA-73777. RNA Polymerase I Chain Elongation.
R-HSA-912446. Meiotic recombination.
R-HSA-977225. Amyloid fiber formation.
SIGNORiP62805.

Miscellaneous databases

ChiTaRSiHIST1H4A. human.
EvolutionaryTraceiP62805.
GeneWikiiHIST1H4A.
HIST1H4B.
HIST1H4C.
HIST1H4D.
HIST1H4E.
HIST1H4F.
HIST1H4H.
HIST1H4I.
HIST1H4J.
HIST1H4K.
HIST1H4L.
HIST2H4A.
HIST4H4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000124529.
CleanExiHS_HIST1H4A.
HS_HIST1H4B.
HS_HIST1H4C.
HS_HIST1H4D.
HS_HIST1H4E.
HS_HIST1H4F.
HS_HIST1H4H.
HS_HIST1H4I.
HS_HIST1H4L.
HS_HIST2H4A.
HS_HIST2H4B.
HS_HIST4H4.
ExpressionAtlasiP62805. baseline and differential.
GenevisibleiP62805. HS.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR001951. Histone_H4.
IPR019809. Histone_H4_CS.
IPR004823. TAF_TATA-bd.
[Graphical view]
PRINTSiPR00623. HISTONEH4.
SMARTiSM00417. H4. 1 hit.
SM00803. TAF. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00047. HISTONE_H4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiH4_HUMAN
AccessioniPrimary (citable) accession number: P62805
Secondary accession number(s): A2VCL0
, P02304, P02305, Q6DRA9, Q6FGB8, Q6NWP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 162 of the entry and version 2 of the sequence. [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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  3. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  8. 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.