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UniProtKB - Q6NXT2 (H3C_HUMAN)

Entry version 153 (07 Apr 2021)
Sequence version 3 (23 Jan 2007)
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Protein

Histone H3.3C

Gene

H3-5

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

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. Hominid-specific H3.5/H3F3C preferentially colocalizes with euchromatin, and it is associated with actively transcribed genes.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

Complete GO annotation on QuickGO ...

GO - Biological processi

  • positive regulation of cell growth Source: UniProtKB
Complete GO annotation on QuickGO ...

<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

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q6NXT2

<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%5Fand%5Ftaxonomy%5Fsection">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 H3.3C
Alternative name(s):
Histone H3.5Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:H3-5Imported
Synonyms:H3F3CImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 12

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:33164, H3-5

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		616134, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q6NXT2

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000188375.4

<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

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

Organism-specific databases

DisGeNET

More...DisGeNETi		440093

Open Targets

More...OpenTargetsi		ENSG00000188375

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA165512903

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q6NXT2, Tbio

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		H3F3C

Domain mapping of disease mutations (DMDM)

More...DMDMi		116248097

<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%5Fprocessing%5Fsection">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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002539602 – 135Histone H3.3CAdd BLAST134

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 residuei3Asymmetric dimethylarginine; by PRMT6; alternateBy similarity1
Modified residuei3Citrulline; alternateBy similarity1
Modified residuei4Phosphothreonine; by HASPINBy similarity1
Modified residuei5Allysine; alternateBy similarity1
Modified residuei5N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei5N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei5N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei5N6-(beta-hydroxybutyryl)lysine; alternateBy similarity1
Modified residuei5N6-acetyllysine; alternateBy similarity1
Modified residuei5N6-methyllysine; alternateBy similarity1
Modified residuei65-glutamyl dopamine; alternateBy similarity1
Modified residuei65-glutamyl serotonin; alternateBy similarity1
Modified residuei7Phosphothreonine; by PKCBy similarity1
Modified residuei9Citrulline; alternateBy similarity1
Modified residuei9Symmetric dimethylarginine; by PRMT5; alternateBy similarity1
Modified residuei10N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei10N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei10N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei10N6-(beta-hydroxybutyryl)lysine; alternateBy similarity1
Modified residuei10N6-acetyllysine; alternateBy similarity1
Modified residuei10N6-lactoyllysine; alternateBy similarity1
Modified residuei10N6-methyllysine; alternateBy similarity1
Modified residuei11ADP-ribosylserine; alternateBy similarity1
Modified residuei11Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5By similarity1
Modified residuei12Phosphothreonine; by PKCBy similarity1
Modified residuei15N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei15N6-(beta-hydroxybutyryl)lysine; alternateBy similarity1
Modified residuei15N6-acetyllysine; alternateBy similarity1
Modified residuei15N6-glutaryllysine; alternateBy similarity1
Modified residuei15N6-lactoyllysine; alternateBy similarity1
Modified residuei15N6-succinyllysine; alternateBy similarity1
Modified residuei18Asymmetric dimethylarginine; by CARM1; alternateBy similarity1
Modified residuei18Citrulline; alternateBy similarity1
Modified residuei19N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei19N6-(beta-hydroxybutyryl)lysine; alternateBy similarity1
Modified residuei19N6-acetyllysine; alternateBy similarity1
Modified residuei19N6-butyryllysine; alternateBy similarity1
Modified residuei19N6-glutaryllysine; alternateBy similarity1
Modified residuei19N6-lactoyllysine; alternateBy similarity1
Modified residuei19N6-methyllysine; alternateBy similarity1
Modified residuei24N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei24N6-(beta-hydroxybutyryl)lysine; alternateBy similarity1
Modified residuei24N6-acetyllysine; alternateBy similarity1
Modified residuei24N6-butyryllysine; alternateBy similarity1
Modified residuei24N6-glutaryllysine; alternateBy similarity1
Modified residuei24N6-lactoyllysine; alternateBy similarity1
Modified residuei24N6-methyllysine; alternateBy similarity1
Modified residuei27CitrullineBy similarity1
Modified residuei28N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei28N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei28N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei28N6-acetyllysine; alternateBy similarity1
Modified residuei28N6-glutaryllysine; alternateBy similarity1
Modified residuei28N6-lactoyllysine; alternateBy similarity1
Modified residuei28N6-methyllysine; alternateBy similarity1
Modified residuei29ADP-ribosylserine; alternateBy similarity1
Modified residuei29Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5By similarity1
Modified residuei32PhosphoserineBy similarity1
Modified residuei37N6-methyllysineBy similarity1
Modified residuei41PhosphotyrosineBy similarity1
Modified residuei56N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei56N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei56N6-(beta-hydroxybutyryl)lysine; alternateBy similarity1
Modified residuei56N6-acetyllysine; alternateBy similarity1
Modified residuei56N6-glutaryllysine; alternateBy similarity1
Modified residuei56N6-lactoyllysine; alternateBy similarity1
Modified residuei56N6-methyllysine; by EHMT2; alternateBy similarity1
Modified residuei56N6-succinyllysine; alternateBy similarity1
Modified residuei57Phosphoserine1 Publication1
Modified residuei64N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei64N6-methyllysine; alternateBy similarity1
Modified residuei80Phosphothreonine1 Publication1
Modified residuei86PhosphoserineBy similarity1
Modified residuei107PhosphothreonineBy similarity1
Modified residuei115N6-acetyllysineBy similarity1
Modified residuei115N6-glutaryllysine; alternateBy similarity1
Modified residuei122N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei122N6-acetyllysine; alternateBy similarity1
Modified residuei122N6-glutaryllysine; alternateBy similarity1
Modified residuei122N6-methyllysine; alternateBy similarity1
Modified residuei122N6-succinyllysine; alternateBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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 is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). Acetylation at Lys-122 (H3K122ac) by EP300/p300 plays a central role in chromatin structure: localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability (By similarity).By similarity
Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.By similarity
Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes regardless of their transcription state and is enriched on inactive promoters, while it is absent on active promoters (By similarity).By similarity
Methylation at Lys-5 (H3K4me) is linked to gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) requires preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin. Monomethylation at Lys-56 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication (By similarity).By similarity
Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase and dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylated at Ser-29 (H3S28ph) by MAP3K20 isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph) by PKN1 is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. Phosphorylation at Tyr-41 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin (By similarity).By similarity
Lysine deamination at Lys-5 (H3K4all) to form allysine is mediated by LOXL2. Allysine formation by LOXL2 only takes place on H3K4me3 and results in gene repression (By similarity).By similarity
Butyrylation of histones marks active promoters and competes with histone acetylation. It is present during late spermatogenesis.By similarity
Succinylated. Desuccinylation at Lys-122 (H3K122succ) by SIRT7 in response to DNA damage promotes chromatin condensation and double-strand breaks (DSBs) repair.By similarity
Serine ADP-ribosylation constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Serine ADP-ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive with phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac).By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Citrullination, Hydroxylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q6NXT2

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q6NXT2

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q6NXT2

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q6NXT2

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

More...PaxDbi		Q6NXT2

PeptideAtlas

More...PeptideAtlasi		Q6NXT2

PRoteomics IDEntifications database

More...PRIDEi		Q6NXT2

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		66771

Consortium for Top Down Proteomics

More...TopDownProteomicsi		Q6NXT2

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q6NXT2

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

More...PhosphoSitePlusi		Q6NXT2

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q6NXT2

<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

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Specifically expressed in the seminiferous tubules of testis.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000188375, Expressed in testis and 75 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q6NXT2, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000188375, Group enriched (blood, testis)

<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%5Fsection">'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%5Fsection">'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%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		136289, 53 interactors

Protein interaction database and analysis system

More...IntActi		Q6NXT2, 43 interactors

Molecular INTeraction database

More...MINTi		Q6NXT2

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000339835

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q6NXT2, protein

<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

1135
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

More...SMRi		Q6NXT2

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q6NXT2

<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 H3 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1745, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT01020000230443

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_078295_4_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q6NXT2

Identification of Orthologs from Complete Genome Data

More...OMAi		PKMARTK

Database of Orthologous Groups

More...OrthoDBi		1564596at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q6NXT2

TreeFam database of animal gene trees

More...TreeFami		TF314241

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.20.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR009072, Histone-fold
IPR007125, Histone_H2A/H2B/H3
IPR000164, Histone_H3/CENP-A

The PANTHER Classification System

More...PANTHERi		PTHR11426, PTHR11426, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00125, Histone, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00622, HISTONEH3

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00428, H3, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47113, SSF47113, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00322, HISTONE_H3_1, 1 hit
PS00959, HISTONE_H3_2, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q6NXT2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MARTKQTARK STGGKAPRKQ LATKAARKST PSTCGVKPHR YRPGTVALRE 
        60         70         80         90        100
IRRYQKSTEL LIRKLPFQRL VREIAQDFNT DLRFQSAAVG ALQEASEAYL 
       110        120        130 
VGLLEDTNLC AIHAKRVTIM PKDIQLARRI RGERA
Length:135
Mass (Da):15,214
Last modified:January 23, 2007 - v3
<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:iF2941F8A9BC61BB5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti88A → V in ADW85800 (PubMed:21274551).Curated1
Sequence conflicti88A → V in AAH66906 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_06816439H → R. Corresponds to variant dbSNP:rs3759295Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
HQ873957 mRNA Translation: ADW85800.1
AC023050 Genomic DNA No translation available.
BC066906 mRNA Translation: AAH66906.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS31769.1

NCBI Reference Sequences

More...RefSeqi		NP_001013721.2, NM_001013699.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000340398; ENSP00000339835; ENSG00000188375

Database of genes from NCBI RefSeq genomes

More...GeneIDi		440093

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:440093

UCSC genome browser

More...UCSCi		uc001rkr.3, 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
HQ873957 mRNA Translation: ADW85800.1
AC023050 Genomic DNA No translation available.
BC066906 mRNA Translation: AAH66906.1
CCDSiCCDS31769.1
RefSeqiNP_001013721.2, NM_001013699.2

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
2PUYX-ray1.43E2-11[»]
3KV4X-ray2.19B2-25[»]
4Z5TX-ray2.80A/E1-135[»]
5BWNX-ray1.94B6-14[»]
5BWOX-ray2.38B6-14[»]
5F6KX-ray2.41M2-10[»]
5I3LX-ray1.85C2-21[»]
6OI3X-ray1.66B2-22[»]
SMRiQ6NXT2
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi136289, 53 interactors
IntActiQ6NXT2, 43 interactors
MINTiQ6NXT2
STRINGi9606.ENSP00000339835

PTM databases

iPTMnetiQ6NXT2
PhosphoSitePlusiQ6NXT2
SwissPalmiQ6NXT2

Genetic variation databases

BioMutaiH3F3C
DMDMi116248097

Proteomic databases

EPDiQ6NXT2
jPOSTiQ6NXT2
MassIVEiQ6NXT2
MaxQBiQ6NXT2
PaxDbiQ6NXT2
PeptideAtlasiQ6NXT2
PRIDEiQ6NXT2
ProteomicsDBi66771
TopDownProteomicsiQ6NXT2

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		55173, 31 antibodies

Genome annotation databases

EnsembliENST00000340398; ENSP00000339835; ENSG00000188375
GeneIDi440093
KEGGihsa:440093
UCSCiuc001rkr.3, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		440093
DisGeNETi440093

GeneCards: human genes, protein and diseases

More...GeneCardsi		H3-5
HGNCiHGNC:33164, H3-5
HPAiENSG00000188375, Group enriched (blood, testis)
MIMi616134, gene
neXtProtiNX_Q6NXT2
OpenTargetsiENSG00000188375
PharmGKBiPA165512903
VEuPathDBiHostDB:ENSG00000188375.4

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1745, Eukaryota
GeneTreeiENSGT01020000230443
HOGENOMiCLU_078295_4_0_1
InParanoidiQ6NXT2
OMAiPKMARTK
OrthoDBi1564596at2759
PhylomeDBiQ6NXT2
TreeFamiTF314241

Enzyme and pathway databases

PathwayCommonsiQ6NXT2

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		440093, 47 hits in 923 CRISPR screens

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

More...ChiTaRSi		H3F3C, human
EvolutionaryTraceiQ6NXT2

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

More...GenomeRNAii		440093
PharosiQ6NXT2, Tbio

Protein Ontology

More...PROi		PR:Q6NXT2
RNActiQ6NXT2, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000188375, Expressed in testis and 75 other tissues
GenevisibleiQ6NXT2, HS

Family and domain databases

Gene3Di1.10.20.10, 1 hit
InterProiView protein in InterPro
IPR009072, Histone-fold
IPR007125, Histone_H2A/H2B/H3
IPR000164, Histone_H3/CENP-A
PANTHERiPTHR11426, PTHR11426, 1 hit
PfamiView protein in Pfam
PF00125, Histone, 1 hit
PRINTSiPR00622, HISTONEH3
SMARTiView protein in SMART
SM00428, H3, 1 hit
SUPFAMiSSF47113, SSF47113, 1 hit
PROSITEiView protein in PROSITE
PS00322, HISTONE_H3_1, 1 hit
PS00959, HISTONE_H3_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...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 nameiH3C_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: Q6NXT2
Secondary accession number(s): E9P281
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: January 23, 2007
Last modified: April 7, 2021
This is version 153 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families
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