Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P62799

- H4_XENLA

UniProt

P62799 - H4_XENLA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Histone H4

Gene
N/A
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 4 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-KW

GO - Biological processi

  1. nucleosome assembly Source: InterPro
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H4
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6493984. hist1h4a.

Subcellular locationi

GO - Cellular componenti

  1. nucleosome Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 103102Histone H4PRO_0000158376Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei4 – 41Asymmetric dimethylarginine; by PRMT1; alternateBy similarity
Modified residuei4 – 41Citrulline; alternateBy similarity
Modified residuei4 – 41Omega-N-methylarginine; by PRMT1; alternateBy similarity
Modified residuei4 – 41Symmetric dimethylarginine; by PRMT5 and PRMT7; alternateBy similarity
Modified residuei6 – 61N6-acetyllysineBy similarity
Modified residuei9 – 91N6-acetyllysineBy similarity
Modified residuei13 – 131N6-acetyllysineBy similarity
Modified residuei17 – 171N6-acetyllysineBy similarity
Modified residuei21 – 211N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei21 – 211N6,N6-dimethyllysine; alternateBy similarity
Modified residuei21 – 211N6-methylated lysineBy similarity
Modified residuei21 – 211N6-methyllysine; alternateBy similarity
Modified residuei32 – 321N6-acetyllysineBy similarity
Modified residuei48 – 481Phosphoserine; by PAK2By similarity
Modified residuei52 – 521PhosphotyrosineBy similarity
Modified residuei60 – 601N6-acetyllysineBy similarity
Modified residuei80 – 801N6-acetyllysineBy similarity
Modified residuei89 – 891PhosphotyrosineBy similarity
Modified residuei92 – 921N6-acetyllysine; alternateBy similarity
Cross-linki92 – 92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity

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.By similarity
Citrullination at Arg-4 (H4R3ci) by PADI4 impairs methylation.By similarity
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 (By similarity).By similarity
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 (By similarity).By similarity
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 (By similarity).By similarity
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) (By similarity).By similarity
Sumoylated, which is associated with transcriptional repression.By similarity

Keywords - PTMi

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

Proteomic databases

PRIDEiP62799.

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
P842332EBI-302085,EBI-350041

Protein-protein interaction databases

BioGridi104647. 12 interactions.
DIPiDIP-37429N.
IntActiP62799. 4 interactions.

Structurei

Secondary structure

1
103
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 127Combined sources
Helixi23 – 264Combined sources
Helixi27 – 293Combined sources
Helixi32 – 4110Combined sources
Beta strandi45 – 473Combined sources
Helixi51 – 7626Combined sources
Beta strandi80 – 823Combined sources
Helixi84 – 907Combined sources
Turni91 – 944Combined sources
Beta strandi96 – 1005Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOIX-ray2.80B/F17-103[»]
1KX3X-ray2.00B/F2-103[»]
1KX4X-ray2.60B/F2-103[»]
1KX5X-ray1.94B/F2-103[»]
1M18X-ray2.45B/F2-103[»]
1M19X-ray2.30B/F2-103[»]
1M1AX-ray2.65B/F2-103[»]
1P34X-ray2.70B/F2-103[»]
1P3AX-ray3.00B/F2-103[»]
1P3BX-ray3.00B/F2-103[»]
1P3FX-ray2.90B/F2-103[»]
1P3GX-ray2.70B/F2-103[»]
1P3IX-ray2.30B/F2-103[»]
1P3KX-ray2.90B/F2-103[»]
1P3LX-ray2.40B/F2-103[»]
1P3MX-ray2.90B/F2-103[»]
1P3OX-ray2.75B/F2-103[»]
1P3PX-ray2.70B/F2-103[»]
1S32X-ray2.05B/F2-103[»]
1ZBBX-ray9.00B/F/b/f2-103[»]
1ZLAX-ray2.90B/F2-103[»]
2F8NX-ray2.90B/F1-103[»]
2FJ7X-ray3.20B/F2-103[»]
2HUEX-ray1.70C21-103[»]
2IO5X-ray2.70C2-103[»]
2NZDX-ray2.65B/F2-103[»]
3B6FX-ray3.45B/F2-103[»]
3B6GX-ray3.45B/F2-103[»]
3C1BX-ray2.20B/F2-103[»]
3C1CX-ray3.15B/F2-103[»]
3KUYX-ray2.90B/F2-103[»]
3KWQX-ray3.50B/F21-103[»]
3KXBX-ray3.20B/F2-103[»]
3LELX-ray2.95B/F/L/P2-103[»]
3LJAX-ray2.75B/F2-103[»]
3LZ0X-ray2.50B/F2-103[»]
3LZ1X-ray2.50B/F2-103[»]
3MGPX-ray2.44B/F2-103[»]
3MGQX-ray2.65B/F2-103[»]
3MGRX-ray2.30B/F2-103[»]
3MGSX-ray3.15B/F2-103[»]
3MNNX-ray2.50B/F2-103[»]
3MVDX-ray2.90B/F2-103[»]
3O62X-ray3.22B/F2-103[»]
3REHX-ray2.50B/F2-103[»]
3REIX-ray2.65B/F2-103[»]
3REJX-ray2.55B/F2-103[»]
3REKX-ray2.60B/F2-103[»]
3RELX-ray2.70B/F2-103[»]
3TU4X-ray3.00B/F2-103[»]
3UT9X-ray2.20B/F2-103[»]
3UTAX-ray2.07B/F2-103[»]
3UTBX-ray2.20B/F2-103[»]
4EO5X-ray2.35C21-103[»]
4J8UX-ray2.38B/F2-103[»]
4J8VX-ray2.58B/F2-103[»]
4J8WX-ray2.41B/F2-103[»]
4J8XX-ray2.87B/F2-103[»]
4KGCX-ray2.69B/F1-103[»]
4LD9X-ray3.31B/F1-103[»]
ProteinModelPortaliP62799.
SMRiP62799. Positions 21-102.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62799.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H4 family.Curated

Phylogenomic databases

HOVERGENiHBG051878.
KOiK11254.

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.

P62799-1 [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 databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00224 Genomic DNA. Translation: CAA25042.1.
X03017 Genomic DNA. Translation: CAA26809.1.
X03017 Genomic DNA. Translation: CAA26814.1.
X03018 Genomic DNA. Translation: CAA26819.1.
M21286 Genomic DNA. Translation: AAA49761.1.
M21286 Genomic DNA. Translation: AAA49766.1.
M21287 Genomic DNA. Translation: AAA49771.1.
BC078038 mRNA. Translation: AAH78038.1.
PIRiA02641. HSXL4.
RefSeqiNP_001087926.1. NM_001094457.1.
UniGeneiXl.85592.

Genome annotation databases

GeneIDi447787.
KEGGixla:447787.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00224 Genomic DNA. Translation: CAA25042.1 .
X03017 Genomic DNA. Translation: CAA26809.1 .
X03017 Genomic DNA. Translation: CAA26814.1 .
X03018 Genomic DNA. Translation: CAA26819.1 .
M21286 Genomic DNA. Translation: AAA49761.1 .
M21286 Genomic DNA. Translation: AAA49766.1 .
M21287 Genomic DNA. Translation: AAA49771.1 .
BC078038 mRNA. Translation: AAH78038.1 .
PIRi A02641. HSXL4.
RefSeqi NP_001087926.1. NM_001094457.1.
UniGenei Xl.85592.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AOI X-ray 2.80 B/F 17-103 [» ]
1KX3 X-ray 2.00 B/F 2-103 [» ]
1KX4 X-ray 2.60 B/F 2-103 [» ]
1KX5 X-ray 1.94 B/F 2-103 [» ]
1M18 X-ray 2.45 B/F 2-103 [» ]
1M19 X-ray 2.30 B/F 2-103 [» ]
1M1A X-ray 2.65 B/F 2-103 [» ]
1P34 X-ray 2.70 B/F 2-103 [» ]
1P3A X-ray 3.00 B/F 2-103 [» ]
1P3B X-ray 3.00 B/F 2-103 [» ]
1P3F X-ray 2.90 B/F 2-103 [» ]
1P3G X-ray 2.70 B/F 2-103 [» ]
1P3I X-ray 2.30 B/F 2-103 [» ]
1P3K X-ray 2.90 B/F 2-103 [» ]
1P3L X-ray 2.40 B/F 2-103 [» ]
1P3M X-ray 2.90 B/F 2-103 [» ]
1P3O X-ray 2.75 B/F 2-103 [» ]
1P3P X-ray 2.70 B/F 2-103 [» ]
1S32 X-ray 2.05 B/F 2-103 [» ]
1ZBB X-ray 9.00 B/F/b/f 2-103 [» ]
1ZLA X-ray 2.90 B/F 2-103 [» ]
2F8N X-ray 2.90 B/F 1-103 [» ]
2FJ7 X-ray 3.20 B/F 2-103 [» ]
2HUE X-ray 1.70 C 21-103 [» ]
2IO5 X-ray 2.70 C 2-103 [» ]
2NZD X-ray 2.65 B/F 2-103 [» ]
3B6F X-ray 3.45 B/F 2-103 [» ]
3B6G X-ray 3.45 B/F 2-103 [» ]
3C1B X-ray 2.20 B/F 2-103 [» ]
3C1C X-ray 3.15 B/F 2-103 [» ]
3KUY X-ray 2.90 B/F 2-103 [» ]
3KWQ X-ray 3.50 B/F 21-103 [» ]
3KXB X-ray 3.20 B/F 2-103 [» ]
3LEL X-ray 2.95 B/F/L/P 2-103 [» ]
3LJA X-ray 2.75 B/F 2-103 [» ]
3LZ0 X-ray 2.50 B/F 2-103 [» ]
3LZ1 X-ray 2.50 B/F 2-103 [» ]
3MGP X-ray 2.44 B/F 2-103 [» ]
3MGQ X-ray 2.65 B/F 2-103 [» ]
3MGR X-ray 2.30 B/F 2-103 [» ]
3MGS X-ray 3.15 B/F 2-103 [» ]
3MNN X-ray 2.50 B/F 2-103 [» ]
3MVD X-ray 2.90 B/F 2-103 [» ]
3O62 X-ray 3.22 B/F 2-103 [» ]
3REH X-ray 2.50 B/F 2-103 [» ]
3REI X-ray 2.65 B/F 2-103 [» ]
3REJ X-ray 2.55 B/F 2-103 [» ]
3REK X-ray 2.60 B/F 2-103 [» ]
3REL X-ray 2.70 B/F 2-103 [» ]
3TU4 X-ray 3.00 B/F 2-103 [» ]
3UT9 X-ray 2.20 B/F 2-103 [» ]
3UTA X-ray 2.07 B/F 2-103 [» ]
3UTB X-ray 2.20 B/F 2-103 [» ]
4EO5 X-ray 2.35 C 21-103 [» ]
4J8U X-ray 2.38 B/F 2-103 [» ]
4J8V X-ray 2.58 B/F 2-103 [» ]
4J8W X-ray 2.41 B/F 2-103 [» ]
4J8X X-ray 2.87 B/F 2-103 [» ]
4KGC X-ray 2.69 B/F 1-103 [» ]
4LD9 X-ray 3.31 B/F 1-103 [» ]
ProteinModelPortali P62799.
SMRi P62799. Positions 21-102.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 104647. 12 interactions.
DIPi DIP-37429N.
IntActi P62799. 4 interactions.

Chemistry

BindingDBi P62799.

Proteomic databases

PRIDEi P62799.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 447787.
KEGGi xla:447787.

Organism-specific databases

CTDi 8359.
Xenbasei XB-GENE-6493984. hist1h4a.

Phylogenomic databases

HOVERGENi HBG051878.
KOi K11254.

Miscellaneous databases

EvolutionaryTracei P62799.

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. "Primary structure of the histone H3 and H4 genes and their flanking sequences in a minor histone gene cluster of Xenopus laevis."
    Moorman A.F.M., de Boer P.A.J., de Laaf R.T.M., van Dongen W.M.A.M., Destree O.H.J.
    FEBS Lett. 136:45-52(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Transcription of a cloned Xenopus laevis H4 histone gene in the homologous frog oocyte system depends on an evolutionary conserved sequence motif in the -50 region."
    Clerc R.G., Bucher P., Strub K., Birnstiel M.L.
    Nucleic Acids Res. 11:8641-8657(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Genomic organization and nucleotide sequence of two distinct histone gene clusters from Xenopus laevis. Identification of novel conserved upstream sequence elements."
    Perry M., Thomsen G.H., Roeder R.G.
    J. Mol. Biol. 185:479-499(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. NIH - Xenopus Gene Collection (XGC) project
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.
  5. "Crystal structure of the nucleosome core particle at 2.8 A resolution."
    Luger K., Mader A.W., Richmond R.K., Sargent D.F., Richmond T.J.
    Nature 389:251-260(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 17-103.

Entry informationi

Entry nameiH4_XENLA
AccessioniPrimary (citable) accession number: P62799
Secondary accession number(s): P02304, P02305, Q6AZG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3