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Entry version 138 (16 Oct 2019)
Sequence version 2 (23 Jan 2007)
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Protein

Histone H4

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi17 – 215

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Histone H4
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiXenopus laevis (African clawed frog)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri8355 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

Xenopus laevis and tropicalis biology and genomics resource

More...
Xenbasei
XB-GENE-6493984 h4c1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001583762 – 103Histone H4Add BLAST102

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineBy similarity1
Modified residuei2PhosphoserineBy similarity1
Modified residuei4Asymmetric dimethylarginine; by PRMT1; alternateBy similarity1
Modified residuei4Citrulline; alternateBy similarity1
Modified residuei4Omega-N-methylarginine; by PRMT1; alternateBy similarity1
Modified residuei4Symmetric dimethylarginine; by PRMT5 and PRMT7; alternateBy similarity1
Modified residuei6N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei6N6-acetyllysineBy similarity1
Modified residuei6N6-butyryllysine; alternateBy similarity1
Modified residuei9N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei9N6-acetyllysineBy similarity1
Modified residuei9N6-butyryllysine; alternateBy similarity1
Modified residuei9N6-propionyllysine; alternateBy similarity1
Modified residuei13N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei13N6-acetyllysineBy similarity1
Modified residuei13N6-butyryllysine; alternateBy similarity1
Modified residuei17N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei17N6-acetyllysineBy similarity1
Modified residuei17N6-butyryllysine; alternateBy similarity1
Modified residuei17N6-propionyllysine; alternateBy similarity1
Modified residuei21N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei21N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei21N6-methylated lysineBy similarity1
Modified residuei21N6-methyllysine; alternateBy similarity1
Modified residuei32N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei32N6-acetyllysineBy similarity1
Modified residuei32N6-butyryllysine; alternateBy similarity1
Modified residuei32N6-propionyllysine; alternateBy similarity1
Modified residuei32N6-succinyllysine; alternateBy similarity1
Modified residuei45N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei45N6-butyryllysine; alternateBy similarity1
Modified residuei45N6-propionyllysine; alternateBy similarity1
Modified residuei48Phosphoserine; by PAK2By similarity1
Modified residuei52PhosphotyrosineBy similarity1
Modified residuei60N6-(2-hydroxyisobutyryl)lysineBy similarity1
Modified residuei60N6-acetyllysineBy similarity1
Modified residuei78N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei78N6-butyryllysine; alternateBy similarity1
Modified residuei78N6-propionyllysine; alternateBy similarity1
Modified residuei78N6-succinyllysineBy similarity1
Modified residuei80N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei80N6-acetyllysineBy similarity1
Modified residuei80N6-butyryllysine; alternateBy similarity1
Modified residuei80N6-propionyllysine; alternateBy similarity1
Modified residuei89PhosphotyrosineBy similarity1
Modified residuei92N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei92N6-acetyllysine; alternateBy similarity1
Modified residuei92N6-butyryllysine; alternateBy similarity1
Modified residuei92N6-propionyllysine; alternateBy similarity1
Modified residuei92N6-succinyllysine; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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 KMT5B and KMT5C 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
Butyrylation of histones marks active promoters and competes with histone acetylation.By similarity

Keywords - PTMi

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

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P62799

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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.

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
104647, 13 interactors

Database of interacting proteins

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DIPi
DIP-37429N

Protein interaction database and analysis system

More...
IntActi
P62799, 10 interactors

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1103
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P62799

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P62799

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the histone H4 family.Curated

Phylogenomic databases

KEGG Orthology (KO)

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KOi
K11254

Database of Orthologous Groups

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OrthoDBi
1564596at2759

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00076 H4, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.20.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR035425 CENP-T/H4_C
IPR009072 Histone-fold
IPR001951 Histone_H4
IPR019809 Histone_H4_CS
IPR004823 TAF_TATA-bd

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF15511 CENP-T_C, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00623 HISTONEH4

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00417 H4, 1 hit
SM00803 TAF, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47113 SSF47113, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00047 HISTONE_H4, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA9E5DFD3F8B97598
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

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PIRi
A02641 HSXL4

NCBI Reference Sequences

More...
RefSeqi
NP_001087926.1, NM_001094457.1
XP_018095104.1, XM_018239615.1
XP_018095605.1, XM_018240116.1
XP_018095606.1, XM_018240117.1
XP_018096302.1, XM_018240813.1
XP_018097458.1, XM_018241969.1
XP_018098137.1, XM_018242648.1
XP_018118237.1, XM_018262748.1
XP_018120359.1, XM_018264870.1
XP_018120360.1, XM_018264871.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
108703479
108703798
108703799
108704306
108705162
108705878
108716550
108717647
108717648
447787

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
xla:108703479
xla:108703798
xla:108703799
xla:108704306
xla:108705162
xla:108705878
xla:108716550
xla:108717647
xla:108717648
xla:447787

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
PIRiA02641 HSXL4
RefSeqiNP_001087926.1, NM_001094457.1
XP_018095104.1, XM_018239615.1
XP_018095605.1, XM_018240116.1
XP_018095606.1, XM_018240117.1
XP_018096302.1, XM_018240813.1
XP_018097458.1, XM_018241969.1
XP_018098137.1, XM_018242648.1
XP_018118237.1, XM_018262748.1
XP_018120359.1, XM_018264870.1
XP_018120360.1, XM_018264871.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB 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[»]
4R8PX-ray3.28B/F2-103[»]
4WU8X-ray2.45B/F2-103[»]
4WU9X-ray2.60B/F2-103[»]
4XUJX-ray3.18B/F2-103[»]
4XZQX-ray2.40B/F25-103[»]
4YS3X-ray3.00B/F25-103[»]
4Z66X-ray2.50B/F22-103[»]
4ZBJX-ray2.25C21-103[»]
4ZUXX-ray3.82B/F/L/P1-103[»]
5BS7X-ray3.30C/D2-103[»]
5BSAX-ray4.61C/D2-103[»]
5CP6X-ray2.60B/F2-103[»]
5DNMX-ray2.81B/F2-103[»]
5DNNX-ray2.80B/F2-103[»]
5E5AX-ray2.81B/F1-103[»]
5F99X-ray2.63B/F1-103[»]
5HQ2X-ray4.50B2-103[»]
5KGFelectron microscopy4.54B/F1-103[»]
5MLUX-ray2.80B/F20-103[»]
5NL0X-ray5.40B/F/L2-103[»]
5O9Gelectron microscopy4.80B/F1-103[»]
5OMXX-ray2.32B/F1-103[»]
5ONGX-ray2.80B/F1-103[»]
5ONWX-ray2.80B/F1-103[»]
5OXVX-ray6.72B/F/L/P2-103[»]
5OY7X-ray5.77B/F/J/N/R/V/Z/d2-103[»]
5X0Xelectron microscopy3.97B/F1-103[»]
5X0Yelectron microscopy3.97B/F2-103[»]
5XF6X-ray2.63B/F2-103[»]
5Z3Lelectron microscopy4.31B/F2-103[»]
5Z3Oelectron microscopy3.62B/F2-103[»]
5Z3Telectron microscopy4.06B/F2-103[»]
5Z3Uelectron microscopy4.31B/F2-103[»]
5Z3Velectron microscopy4.22B/F2-103[»]
6ESFelectron microscopy3.70B/F2-103[»]
6ESGelectron microscopy5.40B/F2-103[»]
6ESHelectron microscopy5.10B/F2-103[»]
6ESIelectron microscopy6.30B/F2-103[»]
6FQ5electron microscopy3.80B19-102[»]
F19-103[»]
6FQ6electron microscopy4.00B/F19-103[»]
6FQ8electron microscopy4.80B/F18-103[»]
6FTXelectron microscopy4.50B/F1-103[»]
6G0Lelectron microscopy4.50B/F1-103[»]
6GYTX-ray2.50C10-17[»]
6I84electron microscopy4.40O/U1-103[»]
6IROelectron microscopy3.40B/F2-103[»]
6IY2electron microscopy3.47B/F16-103[»]
6IY3electron microscopy3.67B/F16-103[»]
6J99electron microscopy4.10B/F1-103[»]
6JM9electron microscopy7.30B/F17-103[»]
6JMAelectron microscopy6.80B/F17-103[»]
6JYLelectron microscopy3.37B/F2-103[»]
6K1Pelectron microscopy3.87B/F2-103[»]
6NE3electron microscopy3.90B/F1-103[»]
6NJ9electron microscopy2.96B/F2-103[»]
6NN6electron microscopy3.90B/F2-103[»]
6NOGelectron microscopy3.90B/F2-103[»]
6NQAelectron microscopy3.54B/F2-103[»]
6NZOelectron microscopy3.80B/F1-103[»]
6O22Other-F1-103[»]
6O96electron microscopy3.50B/F1-103[»]
6OM3X-ray3.30B/F/N/R1-103[»]
6PX1electron microscopy3.30B/F1-103[»]
6PX3electron microscopy4.10B/F1-103[»]
6R1Telectron microscopy3.70B/F17-103[»]
6R1Uelectron microscopy4.36B/F2-103[»]
6R25electron microscopy4.61B/F2-103[»]
SMRiP62799
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi104647, 13 interactors
DIPiDIP-37429N
IntActiP62799, 10 interactors

Proteomic databases

PRIDEiP62799

Genome annotation databases

GeneIDi108703479
108703798
108703799
108704306
108705162
108705878
108716550
108717647
108717648
447787
KEGGixla:108703479
xla:108703798
xla:108703799
xla:108704306
xla:108705162
xla:108705878
xla:108716550
xla:108717647
xla:108717648
xla:447787

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
447787
XenbaseiXB-GENE-6493984 h4c1

Phylogenomic databases

KOiK11254
OrthoDBi1564596at2759

Miscellaneous databases

EvolutionaryTraceiP62799

Family and domain databases

CDDicd00076 H4, 1 hit
Gene3Di1.10.20.10, 1 hit
InterProiView protein in InterPro
IPR035425 CENP-T/H4_C
IPR009072 Histone-fold
IPR001951 Histone_H4
IPR019809 Histone_H4_CS
IPR004823 TAF_TATA-bd
PfamiView protein in Pfam
PF15511 CENP-T_C, 1 hit
PRINTSiPR00623 HISTONEH4
SMARTiView protein in SMART
SM00417 H4, 1 hit
SM00803 TAF, 1 hit
SUPFAMiSSF47113 SSF47113, 1 hit
PROSITEiView protein in PROSITE
PS00047 HISTONE_H4, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiH4_XENLA
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P62799
Secondary accession number(s): P02304, P02305, Q6AZG5
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 16, 2019
This is version 138 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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
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