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P62805

- H4_HUMAN

UniProt

P62805 - H4_HUMAN

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Protein

Histone H4

Gene

HIST1H4A

more
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. DNA binding Source: UniProtKB
  2. histone demethylase activity (H4-K20 specific) Source: Reactome
  3. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. CENP-A containing nucleosome assembly Source: Reactome
  2. chromatin organization Source: Reactome
  3. DNA replication-dependent nucleosome assembly Source: UniProt
  4. DNA replication-independent nucleosome assembly Source: UniProt
  5. histone H4-K20 demethylation Source: GOC
  6. mitotic cell cycle Source: Reactome
  7. negative regulation of megakaryocyte differentiation Source: UniProtKB
  8. nucleosome assembly Source: Reactome
  9. telomere maintenance Source: Reactome
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_172610. HATs acetylate histones.
REACT_172744. Condensation of Prophase Chromosomes.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.
REACT_200808. PRC2 methylates histones and DNA.
REACT_200827. SIRT1 negatively regulates rRNA Expression.
REACT_200856. NoRC negatively regulates rRNA expression.
REACT_2204. RNA Polymerase I Chain Elongation.
REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_2232. RNA Polymerase I Promoter Opening.
REACT_27271. Meiotic recombination.
REACT_75792. Meiotic synapsis.
REACT_75925. Amyloids.
REACT_7963. Packaging Of Telomere Ends.

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
ProteomesiUP000005640: 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

  1. extracellular region Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
  3. membrane Source: UniProtKB
  4. nuclear chromosome Source: UniProt
  5. nucleoplasm Source: Reactome
  6. nucleosome Source: UniProtKB
  7. nucleus Source: UniProtKB
  8. protein complex Source: UniProt
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 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; alternate3 Publications
Modified residuei6 – 61N6-crotonyllysine; alternate1 Publication
Modified residuei9 – 91N6-acetyllysine; alternate3 Publications
Modified residuei9 – 91N6-crotonyllysine; alternate1 Publication
Modified residuei13 – 131N6-acetyllysine; alternate4 Publications
Modified residuei13 – 131N6-crotonyllysine; alternate1 Publication
Modified residuei17 – 171N6-acetyllysine; alternate4 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-acetyllysine1 Publication
Modified residuei48 – 481Phosphoserine; by PAK26 Publications
Modified residuei52 – 521Phosphotyrosine2 Publications
Modified residuei89 – 891PhosphotyrosineBy similarity
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.4 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.4 Publications
Monomethylated, dimethylated or trimethylated at Lys-21 (H4K20me1, H4K20me2, H4K20me3). Monomethylation is performed by SET8. Trimethylation is performed by SUV420H1 and SUV420H2 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-H4.8 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

MaxQBiP62805.
PaxDbiP62805.
PeptideAtlasiP62805.
PRIDEiP62805.

2D gel databases

SWISS-2DPAGEP62805.

PTM databases

PhosphoSiteiP62805.

Expressioni

Gene expression databases

BgeeiP62805.
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.
GenevestigatoriP62805.

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
BPTFQ128303EBI-302023,EBI-1560273
BPTFQ12830-416EBI-302023,EBI-4288838
BRD2P254405EBI-302023,EBI-2874802
CENPAP494504EBI-302023,EBI-1751979
COPRSQ9NQ923EBI-302023,EBI-1642558
CrebbpP454812EBI-302023,EBI-296306From a different organism.
H3F3BP842433EBI-302023,EBI-120658
HAT1O149294EBI-302023,EBI-2339359
HDAC1Q135472EBI-302023,EBI-301834
JMJD4Q9H9V93EBI-302023,EBI-2866290
KDM4AO751647EBI-302023,EBI-936709
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
SETD8Q9NQR15EBI-302023,EBI-1268946
SfmbtQ9VK3310EBI-302023,EBI-117801From a different organism.
SMARCA5O602642EBI-302023,EBI-352588
TLE1Q047246EBI-302023,EBI-711424
TP53BP1Q128888EBI-302023,EBI-396540
YWHAZP631043EBI-302023,EBI-347088

Protein-protein interaction databases

BioGridi113899. 21 interactions.
113955. 150 interactions.
113956. 17 interactions.
113957. 29 interactions.
113958. 16 interactions.
113959. 18 interactions.
113960. 16 interactions.
113961. 20 interactions.
113962. 17 interactions.
113963. 18 interactions.
113964. 16 interactions.
113966. 42 interactions.
125732. 74 interactions.
299853. 17 interactions.
DIPiDIP-33079N.
IntActiP62805. 96 interactions.
MINTiMINT-276350.
STRINGi9606.ENSP00000289352.

Structurei

Secondary structure

1
103
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 94Combined 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:
PDBe
RCSB PDB
PDBj
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[»]
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[»]
ProteinModelPortaliP62805.
SMRiP62805. Positions 21-102.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62805.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H4 family.Curated

Phylogenomic databases

eggNOGiCOG2036.
GeneTreeiENSGT00760000119019.
HOGENOMiHOG000234654.
HOVERGENiHBG051878.
InParanoidiP62805.
KOiK11254.
OMAiYEEVRVV.
OrthoDBiEOG77T174.
PhylomeDBiP62805.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR001951. Histone_H4.
IPR019809. Histone_H4_CS.
[Graphical view]
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00623. HISTONEH4.
SMARTiSM00417. H4. 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 AAI28106.1 differs from that shown. Reason: Frameshift at position 3.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711V → A in AAH67496. (PubMed:15489334)Curated
Sequence conflicti77 – 771A → P in CAG46986. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti64 – 641E → Q in a breast cancer sample; somatic mutation. 1 Publication
VAR_036206

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
ENST00000579512; ENSP00000462355; ENSG00000270276.
ENST00000611927; ENSP00000479794; ENSG00000273542.
ENST00000612061; ENSP00000482412; ENSG00000270276.
ENST00000614247; ENSP00000479461; ENSG00000277157.
ENST00000615164; ENSP00000484789; ENSG00000276966.
ENST00000617569; ENSP00000479106; ENSG00000278637.
ENST00000618305; ENSP00000480960; ENSG00000275126.
ENST00000621520; ENSP00000481507; ENSG00000270276.
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.3. human.

Polymorphism databases

DMDMi51317339.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS30847.1.
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.
PIRi D40335. HSHU4.
RefSeqi NP_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.
UniGenei Hs.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:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZKK X-ray 1.45 E/F/G/H 16-25 [» ]
2BQZ X-ray 1.50 B/F 18-26 [» ]
2CV5 X-ray 2.50 B/F 1-103 [» ]
2IG0 X-ray 1.70 B 17-26 [» ]
2KWN NMR - B 10-24 [» ]
2KWO NMR - B 2-21 [» ]
2LVM NMR - B 15-28 [» ]
2QQS X-ray 2.82 C/D 17-26 [» ]
2RJE X-ray 1.86 P/Q 16-26 [» ]
2RNY NMR - B 14-28 [» ]
2RS9 NMR - A 2-11 [» ]
3A6N X-ray 2.70 B/F 1-103 [» ]
3AFA X-ray 2.50 B/F 1-103 [» ]
3AN2 X-ray 3.60 B/F 1-103 [» ]
3AV1 X-ray 2.50 B/F 1-103 [» ]
3AV2 X-ray 2.80 B/F 1-103 [» ]
3AYW X-ray 2.90 B/F 1-103 [» ]
3AZE X-ray 3.00 B/F 1-103 [» ]
3AZF X-ray 2.70 B/F 1-103 [» ]
3AZG X-ray 2.40 B/F 1-103 [» ]
3AZH X-ray 3.49 B/F 1-103 [» ]
3AZI X-ray 2.70 B/F 1-103 [» ]
3AZJ X-ray 2.89 B/F 1-103 [» ]
3AZK X-ray 3.20 B/F 1-103 [» ]
3AZL X-ray 2.70 B/F 1-103 [» ]
3AZM X-ray 2.89 B/F 1-103 [» ]
3AZN X-ray 3.00 B/F 1-103 [» ]
3CFS X-ray 2.40 E 28-42 [» ]
3CFV X-ray 2.60 E/F 25-42 [» ]
3F9W X-ray 1.60 E/F/G/H 16-25 [» ]
3F9X X-ray 1.25 E/F/G/H 16-25 [» ]
3F9Y X-ray 1.50 E/F 16-25 [» ]
3F9Z X-ray 1.60 E/F/G/H 16-25 [» ]
3IJ1 X-ray 2.10 B 16-26 [» ]
3JPX X-ray 2.05 B 14-28 [» ]
3NQJ X-ray 2.10 B 21-103 [» ]
3NQU X-ray 2.50 B 1-103 [» ]
3O36 X-ray 1.70 D/E 15-20 [» ]
3QBY X-ray 1.95 H 16-26 [» ]
3QZS X-ray 1.80 C/D 13-22 [» ]
3QZT X-ray 1.50 B 13-22 [» ]
3QZV X-ray 2.00 C 8-18 [» ]
3R45 X-ray 2.60 B 1-103 [» ]
3UVW X-ray 1.37 B 2-12 [» ]
3UVX X-ray 1.91 B 12-22 [» ]
3UVY X-ray 2.02 B 16-26 [» ]
3UW9 X-ray 2.30 E/F 8-18 [» ]
3W96 X-ray 3.00 B/F 1-103 [» ]
3W97 X-ray 3.20 B/F 1-103 [» ]
3W98 X-ray 3.42 B/F 1-103 [» ]
3W99 X-ray 3.00 B/F 17-103 [» ]
3WA9 X-ray 3.07 B/F 1-103 [» ]
3WAA X-ray 3.20 B/F 1-103 [» ]
3WKJ X-ray 2.80 B/F 1-103 [» ]
4GQB X-ray 2.06 C 2-22 [» ]
4H9N X-ray 1.95 B 2-103 [» ]
4H9O X-ray 2.05 B 2-103 [» ]
4H9P X-ray 2.20 B 2-103 [» ]
4H9Q X-ray 1.95 B 2-103 [» ]
4H9R X-ray 2.20 B 2-103 [» ]
4H9S X-ray 2.60 C/D 21-103 [» ]
4HGA X-ray 2.80 C 1-103 [» ]
4M38 X-ray 2.20 E/F 2-22 [» ]
4N3W X-ray 1.90 C 14-28 [» ]
4N4F X-ray 1.83 C 6-26 [» ]
4QUT X-ray 1.70 B 10-16 [» ]
4QUU X-ray 1.80 B 4-16 [» ]
ProteinModelPortali P62805.
SMRi P62805. Positions 21-102.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113899. 21 interactions.
113955. 150 interactions.
113956. 17 interactions.
113957. 29 interactions.
113958. 16 interactions.
113959. 18 interactions.
113960. 16 interactions.
113961. 20 interactions.
113962. 17 interactions.
113963. 18 interactions.
113964. 16 interactions.
113966. 42 interactions.
125732. 74 interactions.
299853. 17 interactions.
DIPi DIP-33079N.
IntActi P62805. 96 interactions.
MINTi MINT-276350.
STRINGi 9606.ENSP00000289352.

Chemistry

ChEMBLi CHEMBL5876.

PTM databases

PhosphoSitei P62805.

Polymorphism databases

DMDMi 51317339.

2D gel databases

SWISS-2DPAGE P62805.

Proteomic databases

MaxQBi P62805.
PaxDbi P62805.
PeptideAtlasi P62805.
PRIDEi P62805.

Protocols and materials databases

DNASUi 8294.
8360.
8362.
8363.
8364.
8365.
8366.
8367.
8368.
8370.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000244537 ; ENSP00000244537 ; ENSG00000274618 .
ENST00000355057 ; ENSP00000347168 ; ENSG00000197238 .
ENST00000358064 ; ENSP00000350767 ; ENSG00000197837 .
ENST00000377727 ; ENSP00000366956 ; ENSG00000158406 .
ENST00000377745 ; ENSP00000366974 ; ENSG00000278705 .
ENST00000377803 ; ENSP00000367034 ; ENSG00000197061 .
ENST00000539745 ; ENSP00000443017 ; ENSG00000197837 .
ENST00000579512 ; ENSP00000462355 ; ENSG00000270276 .
ENST00000611927 ; ENSP00000479794 ; ENSG00000273542 .
ENST00000612061 ; ENSP00000482412 ; ENSG00000270276 .
ENST00000614247 ; ENSP00000479461 ; ENSG00000277157 .
ENST00000615164 ; ENSP00000484789 ; ENSG00000276966 .
ENST00000617569 ; ENSP00000479106 ; ENSG00000278637 .
ENST00000618305 ; ENSP00000480960 ; ENSG00000275126 .
ENST00000621520 ; ENSP00000481507 ; ENSG00000270276 .
GeneIDi 121504.
554313.
8294.
8359.
8360.
8361.
8362.
8363.
8364.
8365.
8366.
8367.
8368.
8370.
KEGGi hsa: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.
UCSCi uc001ess.3. human.

Organism-specific databases

CTDi 121504.
554313.
8294.
8359.
8360.
8361.
8362.
8363.
8364.
8365.
8366.
8367.
8368.
8370.
HGNCi HGNC: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.
HPAi CAB011503.
CAB021887.
CAB037279.
HPA042201.
MIMi 142750. 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.
neXtProti NX_P62805.
PharmGKBi PA29169.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2036.
GeneTreei ENSGT00760000119019.
HOGENOMi HOG000234654.
HOVERGENi HBG051878.
InParanoidi P62805.
KOi K11254.
OMAi YEEVRVV.
OrthoDBi EOG77T174.
PhylomeDBi P62805.

Enzyme and pathway databases

Reactomei REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_172610. HATs acetylate histones.
REACT_172744. Condensation of Prophase Chromosomes.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.
REACT_200808. PRC2 methylates histones and DNA.
REACT_200827. SIRT1 negatively regulates rRNA Expression.
REACT_200856. NoRC negatively regulates rRNA expression.
REACT_2204. RNA Polymerase I Chain Elongation.
REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_2232. RNA Polymerase I Promoter Opening.
REACT_27271. Meiotic recombination.
REACT_75792. Meiotic synapsis.
REACT_75925. Amyloids.
REACT_7963. Packaging Of Telomere Ends.

Miscellaneous databases

EvolutionaryTracei P62805.
GeneWikii HIST1H4A.
HIST1H4B.
HIST1H4C.
HIST1H4D.
HIST1H4E.
HIST1H4F.
HIST1H4H.
HIST1H4I.
HIST1H4J.
HIST1H4K.
HIST1H4L.
HIST2H4A.
HIST4H4.
NextBioi 31093.
PROi P62805.
SOURCEi Search...

Gene expression databases

Bgeei P62805.
CleanExi HS_HIST1H4A.
HS_HIST1H4B.
HS_HIST1H4C.
HS_HIST1H4D.
HS_HIST1H4E.
HS_HIST1H4F.
HS_HIST1H4H.
HS_HIST1H4I.
HS_HIST1H4L.
HS_HIST2H4A.
HS_HIST2H4B.
HS_HIST4H4.
ExpressionAtlasi P62805. baseline and differential.
Genevestigatori P62805.

Family and domain databases

Gene3Di 1.10.20.10. 1 hit.
InterProi IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR001951. Histone_H4.
IPR019809. Histone_H4_CS.
[Graphical view ]
Pfami PF00125. Histone. 1 hit.
[Graphical view ]
PRINTSi PR00623. HISTONEH4.
SMARTi SM00417. H4. 1 hit.
[Graphical view ]
SUPFAMi SSF47113. SSF47113. 1 hit.
PROSITEi PS00047. HISTONE_H4. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and in vitro transcription of a human H4 histone gene."
    Sierra F., Stein G., Stein J.
    Nucleic Acids Res. 11:7069-7086(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Protein-DNA interactions in vivo upstream of a cell cycle-regulated human H4 histone gene."
    Pauli U., Chrysogelos S., Stein G., Stein J., Nick H.
    Science 236:1308-1311(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Isolation and characterization of two human H1 histone genes within clusters of core histone genes."
    Albig W., Kardalinou E., Drabent B., Zimmer A., Doenecke D.
    Genomics 10:940-948(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  4. "Association of histone H4 genes with the mammalian testis-specific H1t histone gene."
    Drabent B., Kardalinou E., Bode C., Doenecke D.
    DNA Cell Biol. 14:591-597(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Characterization of the H1.5 gene completes the set of human H1 subtype genes."
    Albig W., Meergans T., Doenecke D.
    Gene 184:141-148(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "The human histone gene cluster at the D6S105 locus."
    Albig W., Doenecke D.
    Hum. Genet. 101:284-294(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "Human histone gene organization: nonregular arrangement within a large cluster."
    Albig W., Kioschis P., Poustka A., Meergans K., Doenecke D.
    Genomics 40:314-322(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  8. "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] (HIST1H4A; HIST1H4B; HIST1H4C; HIST1H4D; HIST1H4E; HIST1H4F; HIST1H4H; HIST1H4I; HIST1H4J; HIST1H4K; HIST1H4L; HIST2H4A AND HIST4H4).
  9. "A recurring translocation, t(3;6)(q27;p21), in non-Hodgkin's lymphoma results in replacement of the 5' regulatory region of BCL6 with a novel H4 histone gene."
    Akasaka T., Miura I., Takahashi N., Akasaka H., Yonetani N., Ohno H., Fukuhara S., Okuma M.
    Cancer Res. 57:7-12(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  10. "Functional characterization of a human histone gene cluster duplication."
    Braastad C.D., Hovhannisyan H., van Wijnen A.J., Stein J.L., Stein G.S.
    Gene 342:35-40(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  11. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (HIST1H4F; HIST1H4H AND HIST2H4A).
  12. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HIST1H4A; HIST1H4B; HIST1H4C; HIST1H4D; HIST1H4E; HIST1H4F; HIST1H4H; HIST1H4I; HIST1H4J; HIST1H4K AND HIST1H4L).
  13. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  14. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cerebellum, Eye and Placenta.
  15. Bienvenut W.V.
    Submitted (MAR-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 25-36; 47-56; 61-78 AND 81-93, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  16. "Histone H4 acetylation distinguishes coding regions of the human genome from heterochromatin in a differentiation-dependent but transcription-independent manner."
    O'Neill L.P., Turner B.M.
    EMBO J. 14:3946-3957(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-6; LYS-9; LYS-13 AND LYS-17.
  17. "A highly basic histone H4 domain bound to the sharply bent region of nucleosomal DNA."
    Ebralidse K.K., Grachev S.A., Mirzabekov A.D.
    Nature 331:365-367(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING REGION.
  18. "Histone H4 acetylation in human cells. Frequency of acetylation at different sites defined by immunolabeling with site-specific antibodies."
    Turner B.M., O'Neill L.P., Allan I.M.
    FEBS Lett. 253:141-145(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-6; LYS-9; LYS-13 AND LYS-17.
  19. "Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1."
    Strahl B.D., Briggs S.D., Brame C.J., Caldwell J.A., Koh S.S., Ma H., Cook R.G., Shabanowitz J., Hunt D.F., Stallcup M.R., Allis C.D.
    Curr. Biol. 11:996-1000(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-4.
  20. "Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor."
    Wang H., Huang Z.-Q., Xia L., Feng Q., Erdjument-Bromage H., Strahl B.D., Briggs S.D., Allis C.D., Wong J., Tempst P., Zhang Y.
    Science 293:853-857(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT ARG-4.
  21. "Characterization of t(3;6)(q27;p21) breakpoints in B-cell non-Hodgkin's lymphoma and construction of the histone H4/BCL6 fusion gene, leading to altered expression of Bcl-6."
    Kurata M., Maesako Y., Ueda C., Nishikori M., Akasaka T., Uchiyama T., Ohno H.
    Cancer Res. 62:6224-6230(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN B-CELL NON-HODGKIN LYMPHOMA, CHROMOSOMAL TRANSLOCATION WITH BCL6.
  22. "PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin."
    Nishioka K., Rice J.C., Sarma K., Erdjument-Bromage H., Werner J., Wang Y., Chuikov S., Valenzuela P., Tempst P., Steward R., Lis J.T., Allis C.D., Reinberg D.
    Mol. Cell 9:1201-1213(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-21.
  23. "Histone sumoylation is associated with transcriptional repression."
    Shiio Y., Eisenman R.N.
    Proc. Natl. Acad. Sci. U.S.A. 100:13225-13230(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION.
  24. Cited for: CITRULLINATION AT ARG-4, METHYLATION AT ARG-4.
  25. "SET8 recognizes the sequence RHRK20VLRDN within the N terminus of histone H4 and mono-methylates lysine 20."
    Yin Y., Liu C., Tsai S.N., Zhou B., Ngai S.M., Zhu G.
    J. Biol. Chem. 280:30025-30031(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-21.
  26. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  28. "Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage."
    Wang H., Zhai L., Xu J., Joo H.-Y., Jackson S., Erdjument-Bromage H., Tempst P., Xiong Y., Zhang Y.
    Mol. Cell 22:383-394(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  29. "Structural basis for histone N-terminal recognition by human peptidylarginine deiminase 4."
    Arita K., Shimizu T., Hashimoto H., Hidaka Y., Yamada M., Sato M.
    Proc. Natl. Acad. Sci. U.S.A. 103:5291-5296(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: CITRULLINATION AT ARG-4.
  30. "Certain and progressive methylation of histone H4 at lysine 20 during the cell cycle."
    Pesavento J.J., Yang H., Kelleher N.L., Mizzen C.A.
    Mol. Cell. Biol. 28:468-486(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT SER-2; LYS-13 AND LYS-17, PHOSPHORYLATION AT SER-2, METHYLATION AT LYS-21.
  31. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  32. "BBAP monoubiquitylates histone H4 at lysine 91 and selectively modulates the DNA damage response."
    Yan Q., Dutt S., Xu R., Graves K., Juszczynski P., Manis J.P., Shipp M.A.
    Mol. Cell 36:110-120(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-92, UBIQUITINATION AT LYS-92.
  33. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  34. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9; LYS-13; LYS-17 AND LYS-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND TYR-52, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  36. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  37. "Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification."
    Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T., Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.
    Cell 146:1016-1028(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROTONYLATION AT LYS-6; LYS-9 AND LYS-13.
  38. "Phosphorylation of H4 Ser 47 promotes HIRA-mediated nucleosome assembly."
    Kang B., Pu M., Hu G., Wen W., Dong Z., Zhao K., Stillman B., Zhang Z.
    Genes Dev. 25:1359-1364(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-48.
  39. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  40. "Alteration of the nucleosomal DNA path in the crystal structure of a human nucleosome core particle."
    Tsunaka Y., Kajimura N., Tate S., Morikawa K.
    Nucleic Acids Res. 33:3424-3434(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  41. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-64.

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: October 29, 2014
This is version 141 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

External Data

Dasty 3