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Protein

Histone H2A.Z

Gene

H2AFZ

Organism
Homo sapiens (Human)
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

Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division.1 Publication

<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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1221632 Meiotic synapsis
R-HSA-171306 Packaging Of Telomere Ends
R-HSA-1912408 Pre-NOTCH Transcription and Translation
R-HSA-201722 Formation of the beta-catenin:TCF transactivating complex
R-HSA-212300 PRC2 methylates histones and DNA
R-HSA-2299718 Condensation of Prophase Chromosomes
R-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-HSA-2559586 DNA Damage/Telomere Stress Induced Senescence
R-HSA-3214858 RMTs methylate histone arginines
R-HSA-427359 SIRT1 negatively regulates rRNA expression
R-HSA-427389 ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression
R-HSA-427413 NoRC negatively regulates rRNA expression
R-HSA-5250924 B-WICH complex positively regulates rRNA expression
R-HSA-5334118 DNA methylation
R-HSA-5578749 Transcriptional regulation by small RNAs
R-HSA-5617472 Activation of anterior HOX genes in hindbrain development during early embryogenesis
R-HSA-5625886 Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3
R-HSA-606279 Deposition of new CENPA-containing nucleosomes at the centromere
R-HSA-73728 RNA Polymerase I Promoter Opening
R-HSA-73777 RNA Polymerase I Chain Elongation
R-HSA-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-9018519 Estrogen-dependent gene expression
R-HSA-912446 Meiotic recombination
R-HSA-977225 Amyloid fiber formation

SIGNOR Signaling Network Open Resource

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SIGNORi
P0C0S5

<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 H2A.Z
Short name:
H2A/z
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:H2AFZ
Synonyms:H2AZ
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000164032.11

Human Gene Nomenclature Database

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HGNCi
HGNC:4741 H2AFZ

Online Mendelian Inheritance in Man (OMIM)

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MIMi
142763 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P0C0S5

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi83T → I: Decreases interaction with VPS72. Almost abolishes interaction with VPS72; when associated with N-93. Abolishes interaction with VPS72; when associated with N-93 and IG-101. 1 Publication1
Mutagenesisi93G → N: Decreases interaction with VPS72. Almost abolishes interaction with VPS72; when associated with I-83. Abolishes interaction with VPS72; when associated with I-83 and IG-101. 1 Publication1
Mutagenesisi98D → N: No effect on interaction with VPS72. 1 Publication1
Mutagenesisi101I → IG: Abolishes interaction with VPS72; when associated with I-83 and N-93. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
3015

Open Targets

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OpenTargetsi
ENSG00000164032

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA29119

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
H2AFZ

Domain mapping of disease mutations (DMDM)

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DMDMi
83288408

<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 methionineiRemovedCurated
<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_00000552972 – 128Histone H2A.ZAdd BLAST127

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 residuei5N6-acetyllysine; alternateCombined sources1 Publication1
Modified residuei5N6-methyllysine; alternate1 Publication1
Modified residuei8N6-acetyllysine; alternateCombined sources1 Publication1
Modified residuei8N6-methyllysine; alternate1 Publication1
Modified residuei12N6-acetyllysineCombined sources1 Publication1
Modified residuei14N6-acetyllysineCombined sources1
<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-linki122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

<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

Monoubiquitination of Lys-122 gives a specific tag for epigenetic transcriptional repression.1 Publication
Acetylated on Lys-5, Lys-8 and Lys-12 during interphase. Acetylation disappears at mitosis (By similarity).By similarity
Monomethylated on Lys-5 and Lys-8 by SETD6. SETD6 predominantly methylates Lys-8, lys-5 being a possible secondary site.1 Publication
Not phosphorylated.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P0C0S5

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P0C0S5

MaxQB - The MaxQuant DataBase

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MaxQBi
P0C0S5

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P0C0S5

PeptideAtlas

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PeptideAtlasi
P0C0S5

PRoteomics IDEntifications database

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PRIDEi
P0C0S5

ProteomicsDB human proteome resource

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ProteomicsDBi
52295

Consortium for Top Down Proteomics

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TopDownProteomicsi
P0C0S5

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P0C0S5

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P0C0S5

SwissPalm database of S-palmitoylation events

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SwissPalmi
P0C0S5

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P0C0S5

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000164032 Expressed in 239 organ(s), highest expression level in myometrium

CleanEx database of gene expression profiles

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CleanExi
HS_H2AFZ

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P0C0S5 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB022549
HPA057236

<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. H2A or its variant H2AFZ forms a heterodimer with H2B. H2AFZ interacts with INCENP (By similarity). Interacts (via M6 cassette) with ANP32E; leading to removal of H2A.Z/H2AFZ from the nucleosome. Heterodimer HIST1H2BJ and H2AFZ interacts with VPS72 (via N-terminal domain) (PubMed:26974126). Interacts with PWWP2A (PubMed:28645917).By similarity4 Publications

<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
109269, 97 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P0C0S5

Database of interacting proteins

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DIPi
DIP-38593N

Protein interaction database and analysis system

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IntActi
P0C0S5, 12 interactors

Molecular INTeraction database

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MINTi
P0C0S5

STRING: functional protein association networks

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STRINGi
9606.ENSP00000296417

<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

1128
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F66X-ray2.60C/G1-128[»]
3WA9X-ray3.07C/G1-128[»]
4CAYX-ray1.48A19-128[»]
4NFTX-ray2.61A/B/C/D16-114[»]
5B31X-ray2.20G1-128[»]
5B32X-ray2.35G1-128[»]
5B33X-ray2.92C/G1-128[»]
5CHLX-ray1.89B22-113[»]
5FUGX-ray2.70A/D/G/J19-128[»]
5Z30X-ray2.45C/G1-128[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P0C0S5

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

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SMRi
P0C0S5

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P0C0S5

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 17Required for interaction with INCENPBy similarityAdd BLAST17
Regioni89 – 100M6 cassetteAdd BLAST12
Regioni93 – 103Required for interaction with INCENPBy similarityAdd BLAST11
Regioni120 – 128Required for interaction with PWWP2A1 Publication9

<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 H2A family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1757 Eukaryota
COG5262 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00900000140979

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000234652

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG009342

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P0C0S5

KEGG Orthology (KO)

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KOi
K11251

Identification of Orthologs from Complete Genome Data

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OMAi
DKDKGKM

Database of Orthologous Groups

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OrthoDBi
1504122at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P0C0S5

TreeFam database of animal gene trees

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TreeFami
TF354232

Family and domain databases

Conserved Domains Database

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CDDi
cd00074 H2A, 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
IPR009072 Histone-fold
IPR002119 Histone_H2A
IPR007125 Histone_H2A/H2B/H3
IPR032454 Histone_H2A_C
IPR032458 Histone_H2A_CS

Pfam protein domain database

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Pfami
View protein in Pfam
PF00125 Histone, 1 hit
PF16211 Histone_H2A_C, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00620 HISTONEH2A

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00414 H2A, 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
PS00046 HISTONE_H2A, 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>.<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.

P0C0S5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAGGKAGKDS GKAKTKAVSR SQRAGLQFPV GRIHRHLKSR TTSHGRVGAT
60 70 80 90 100
AAVYSAAILE YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL
110 120
IKATIAGGGV IPHIHKSLIG KKGQQKTV
Length:128
Mass (Da):13,553
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:iE024E53818230371
GO

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 13413.4 Da from positions 2 - 128. Determined by ESI. Monoisotopic, not modified.1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X52317 mRNA Translation: CAA36553.1
M37583 mRNA Translation: AAA35984.1
L10138 Genomic DNA Translation: AAC61625.1
CR457415 mRNA Translation: CAG33696.1
AK315413 mRNA Translation: BAG37803.1
AC097460 Genomic DNA Translation: AAY41013.1
CH471057 Genomic DNA Translation: EAX06118.1
BC018002 mRNA Translation: AAH18002.1
BC020936 mRNA Translation: AAH20936.1
BC103743 mRNA Translation: AAI03744.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS3654.1

Protein sequence database of the Protein Information Resource

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PIRi
A35881

NCBI Reference Sequences

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RefSeqi
NP_002097.1, NM_002106.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.119192

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000296417; ENSP00000296417; ENSG00000164032

Database of genes from NCBI RefSeq genomes

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GeneIDi
3015

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:3015

UCSC genome browser

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UCSCi
uc003hvo.2 human

<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
X52317 mRNA Translation: CAA36553.1
M37583 mRNA Translation: AAA35984.1
L10138 Genomic DNA Translation: AAC61625.1
CR457415 mRNA Translation: CAG33696.1
AK315413 mRNA Translation: BAG37803.1
AC097460 Genomic DNA Translation: AAY41013.1
CH471057 Genomic DNA Translation: EAX06118.1
BC018002 mRNA Translation: AAH18002.1
BC020936 mRNA Translation: AAH20936.1
BC103743 mRNA Translation: AAI03744.1
CCDSiCCDS3654.1
PIRiA35881
RefSeqiNP_002097.1, NM_002106.3
UniGeneiHs.119192

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F66X-ray2.60C/G1-128[»]
3WA9X-ray3.07C/G1-128[»]
4CAYX-ray1.48A19-128[»]
4NFTX-ray2.61A/B/C/D16-114[»]
5B31X-ray2.20G1-128[»]
5B32X-ray2.35G1-128[»]
5B33X-ray2.92C/G1-128[»]
5CHLX-ray1.89B22-113[»]
5FUGX-ray2.70A/D/G/J19-128[»]
5Z30X-ray2.45C/G1-128[»]
ProteinModelPortaliP0C0S5
SMRiP0C0S5
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109269, 97 interactors
CORUMiP0C0S5
DIPiDIP-38593N
IntActiP0C0S5, 12 interactors
MINTiP0C0S5
STRINGi9606.ENSP00000296417

PTM databases

iPTMnetiP0C0S5
PhosphoSitePlusiP0C0S5
SwissPalmiP0C0S5

Polymorphism and mutation databases

BioMutaiH2AFZ
DMDMi83288408

Proteomic databases

EPDiP0C0S5
jPOSTiP0C0S5
MaxQBiP0C0S5
PaxDbiP0C0S5
PeptideAtlasiP0C0S5
PRIDEiP0C0S5
ProteomicsDBi52295
TopDownProteomicsiP0C0S5

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
3015
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296417; ENSP00000296417; ENSG00000164032
GeneIDi3015
KEGGihsa:3015
UCSCiuc003hvo.2 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
3015
DisGeNETi3015
EuPathDBiHostDB:ENSG00000164032.11

GeneCards: human genes, protein and diseases

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GeneCardsi
H2AFZ
HGNCiHGNC:4741 H2AFZ
HPAiCAB022549
HPA057236
MIMi142763 gene
neXtProtiNX_P0C0S5
OpenTargetsiENSG00000164032
PharmGKBiPA29119

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1757 Eukaryota
COG5262 LUCA
GeneTreeiENSGT00900000140979
HOGENOMiHOG000234652
HOVERGENiHBG009342
InParanoidiP0C0S5
KOiK11251
OMAiDKDKGKM
OrthoDBi1504122at2759
PhylomeDBiP0C0S5
TreeFamiTF354232

Enzyme and pathway databases

ReactomeiR-HSA-1221632 Meiotic synapsis
R-HSA-171306 Packaging Of Telomere Ends
R-HSA-1912408 Pre-NOTCH Transcription and Translation
R-HSA-201722 Formation of the beta-catenin:TCF transactivating complex
R-HSA-212300 PRC2 methylates histones and DNA
R-HSA-2299718 Condensation of Prophase Chromosomes
R-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-HSA-2559586 DNA Damage/Telomere Stress Induced Senescence
R-HSA-3214858 RMTs methylate histone arginines
R-HSA-427359 SIRT1 negatively regulates rRNA expression
R-HSA-427389 ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression
R-HSA-427413 NoRC negatively regulates rRNA expression
R-HSA-5250924 B-WICH complex positively regulates rRNA expression
R-HSA-5334118 DNA methylation
R-HSA-5578749 Transcriptional regulation by small RNAs
R-HSA-5617472 Activation of anterior HOX genes in hindbrain development during early embryogenesis
R-HSA-5625886 Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3
R-HSA-606279 Deposition of new CENPA-containing nucleosomes at the centromere
R-HSA-73728 RNA Polymerase I Promoter Opening
R-HSA-73777 RNA Polymerase I Chain Elongation
R-HSA-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-9018519 Estrogen-dependent gene expression
R-HSA-912446 Meiotic recombination
R-HSA-977225 Amyloid fiber formation
SIGNORiP0C0S5

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
H2AFZ human
EvolutionaryTraceiP0C0S5

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
H2AFZ

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
3015
PMAP-CutDBiP0C0S5

Protein Ontology

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PROi
PR:P0C0S5

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000164032 Expressed in 239 organ(s), highest expression level in myometrium
CleanExiHS_H2AFZ
GenevisibleiP0C0S5 HS

Family and domain databases

CDDicd00074 H2A, 1 hit
Gene3Di1.10.20.10, 1 hit
InterProiView protein in InterPro
IPR009072 Histone-fold
IPR002119 Histone_H2A
IPR007125 Histone_H2A/H2B/H3
IPR032454 Histone_H2A_C
IPR032458 Histone_H2A_CS
PfamiView protein in Pfam
PF00125 Histone, 1 hit
PF16211 Histone_H2A_C, 1 hit
PRINTSiPR00620 HISTONEH2A
SMARTiView protein in SMART
SM00414 H2A, 1 hit
SUPFAMiSSF47113 SSF47113, 1 hit
PROSITEiView protein in PROSITE
PS00046 HISTONE_H2A, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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 nameiH2AZ_HUMAN
<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: P0C0S5
Secondary accession number(s): B2RD56, P17317, Q6I9U0
<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: December 6, 2005
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 139 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
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.

<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, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
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