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UniProtKB - O60814 (H2B1K_HUMAN)

Entry version 191 (29 Sep 2021)
Sequence version 3 (23 Jan 2007)
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Protein

Histone H2B type 1-K

Gene

H2BC12

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.

Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid.

<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

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 functionAntibiotic, Antimicrobial, DNA-binding

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		O60814

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-110328, Recognition and association of DNA glycosylase with site containing an affected pyrimidine
R-HSA-110329, Cleavage of the damaged pyrimidine
R-HSA-110330, Recognition and association of DNA glycosylase with site containing an affected purine
R-HSA-110331, Cleavage of the damaged purine
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-3214815, HDACs deacetylate histones
R-HSA-3214847, HATs acetylate histones
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-5689880, Ub-specific processing proteases
R-HSA-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-HSA-5693571, Nonhomologous End-Joining (NHEJ)
R-HSA-5693607, Processing of DNA double-strand break ends
R-HSA-606279, Deposition of new CENPA-containing nucleosomes at the centromere
R-HSA-69473, G2/M DNA damage checkpoint
R-HSA-73728, RNA Polymerase I Promoter Opening
R-HSA-73772, RNA Polymerase I Promoter Escape
R-HSA-8866654, E3 ubiquitin ligases ubiquitinate target proteins
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-9609690, HCMV Early Events
R-HSA-9610379, HCMV Late Events
R-HSA-9616222, Transcriptional regulation of granulopoiesis
R-HSA-9670095, Inhibition of DNA recombination at telomere
R-HSA-9710421, Defective pyroptosis
R-HSA-977225, Amyloid fiber formation

<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 H2B type 1-K
Short name:
H2B K
Alternative name(s):
HIRA-interacting protein 1
<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:H2BC12Imported
Synonyms:H2BFTImported, HIRIP1, HIST1H2BKImported
<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 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_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 6

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:13954, H2BC12

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		615045, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_O60814

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000197903

<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		85236

Open Targets

More...OpenTargetsi		ENSG00000197903

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA134955134

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		O60814, Tbio

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		HIST1H2BK

<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 similarity4 Publications
<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_00000718282 – 126Histone H2B type 1-KAdd BLAST125

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-acetylprolineBy similarity1
Modified residuei6N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei6N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei6N6-acetyllysine; alternate2 Publications1
Modified residuei6N6-butyryllysine; alternate1 Publication1
Modified residuei6N6-crotonyllysine; alternate1 Publication1
Modified residuei6N6-lactoyllysine; alternate1 Publication1
<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-linki6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei12N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei12N6-acetyllysine; alternate1 Publication1
Modified residuei12N6-crotonyllysine; alternate1 Publication1
Modified residuei12N6-lactoyllysine; alternate1 Publication1
Modified residuei13N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei13N6-acetyllysine; alternate2 Publications1
Modified residuei13N6-crotonyllysine; alternate1 Publication1
Modified residuei15Phosphoserine; by STK4/MST11 Publication1
Modified residuei16N6-acetyllysine; alternate2 Publications1
Modified residuei16N6-crotonyllysine; alternate1 Publication1
Modified residuei16N6-lactoyllysine; alternate1 Publication1
Modified residuei17N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei17N6-acetyllysine; alternate1 Publication1
Modified residuei17N6-crotonyllysine; alternate1 Publication1
Modified residuei17N6-glutaryllysine; alternate1 Publication1
Modified residuei17N6-lactoyllysine; alternate1 Publication1
Modified residuei21N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei21N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei21N6-acetyllysine; alternate2 Publications1
Modified residuei21N6-butyryllysine; alternate1 Publication1
Modified residuei21N6-crotonyllysine; alternate1 Publication1
Modified residuei21N6-lactoyllysine; alternate1 Publication1
Cross-linki21Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei24N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei24N6-acetyllysine; alternateBy similarity1
Modified residuei24N6-crotonyllysine; alternate1 Publication1
Modified residuei24N6-lactoyllysine; alternate1 Publication1
Modified residuei25N6-(2-hydroxyisobutyryl)lysine1 Publication1
Modified residuei35N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei35N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei35N6-crotonyllysine; alternate1 Publication1
Modified residuei35N6-glutaryllysine; alternate1 Publication1
Modified residuei35N6-succinyllysine; alternate1 Publication1
Cross-linki35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei37Phosphoserine; by AMPKBy similarity1
Modified residuei44N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei44N6-glutaryllysine; alternate1 Publication1
Modified residuei44N6-lactoyllysine; alternate1 Publication1
Modified residuei47N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei47N6-glutaryllysine; alternate1 Publication1
Modified residuei47N6-methyllysine; alternate1 Publication1
Modified residuei58N6,N6-dimethyllysine; alternate1 Publication1
Modified residuei58N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei80Dimethylated arginineBy similarity1
Modified residuei86N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei86N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei86N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei86N6-acetyllysine; alternateBy similarity1
Modified residuei86N6-lactoyllysine; alternate1 Publication1
Modified residuei87Omega-N-methylarginineBy similarity1
Modified residuei93Omega-N-methylarginineBy similarity1
Modified residuei109N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei109N6-glutaryllysine; alternate1 Publication1
Modified residuei109N6-lactoyllysine; alternate1 Publication1
Modified residuei109N6-methyllysine; alternate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi113O-linked (GlcNAc) serineBy similarity1
Modified residuei116PhosphothreonineBy similarity1
Modified residuei117N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei117N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei117N6-glutaryllysine; alternate1 Publication1
Modified residuei117N6-lactoyllysine; alternate1 Publication1
Modified residuei117N6-malonyllysine; alternate1 Publication1
Modified residuei117N6-methylated lysine; alternateBy similarity1
Modified residuei117N6-succinyllysine; alternate1 Publication1
Modified residuei121N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei121N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei121N6-glutaryllysine; alternate1 Publication1
Modified residuei121N6-lactoyllysine; alternate1 Publication1
Modified residuei121N6-succinyllysine; alternate1 Publication1
Cross-linki121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate3 Publications

<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 at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons.1 Publication
Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription (By similarity). Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination.By similarity1 Publication
GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes (By similarity).By similarity
Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes.1 Publication
Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription.1 Publication

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		O60814

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		O60814

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		O60814

MaxQB - The MaxQuant DataBase

More...MaxQBi		O60814

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

More...PaxDbi		O60814

PeptideAtlas

More...PeptideAtlasi		O60814

PRoteomics IDEntifications database

More...PRIDEi		O60814

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		49607

Consortium for Top Down Proteomics

More...TopDownProteomicsi		O60814

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		O60814, 1 site

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O60814

MetOSite database of methionine sulfoxide sites

More...MetOSitei		O60814

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

More...PhosphoSitePlusi		O60814

SwissPalm database of S-palmitoylation events

More...SwissPalmi		O60814

<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

More...Bgeei		ENSG00000197903, Expressed in stomach and 117 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		O60814, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O60814, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000197903, Tissue enriched (lymphoid)

<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">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		124439, 66 interactors

Database of interacting proteins

More...DIPi		DIP-48935N

Protein interaction database and analysis system

More...IntActi		O60814, 36 interactors

Molecular INTeraction database

More...MINTi		O60814

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000349430

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		O60814, 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

1126
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		O60814

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		O60814

<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 – 36DisorderedSequence analysisAdd BLAST36

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi17 – 35Basic residuesSequence analysisAdd BLAST19

<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 H2B family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1744, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT01030000234651

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_075666_2_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O60814

Identification of Orthologs from Complete Genome Data

More...OMAi		YTSANIM

Database of Orthologous Groups

More...OrthoDBi		1536672at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		O60814

TreeFam database of animal gene trees

More...TreeFami		TF300212

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.20.10, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID00010

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR009072, Histone-fold
IPR007125, Histone_H2A/H2B/H3
IPR000558, Histone_H2B

The PANTHER Classification System

More...PANTHERi		PTHR23428, PTHR23428, 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		PR00621, HISTONEH2B

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00427, H2B, 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
PS00357, HISTONE_H2B, 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.

O60814-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH 
        60         70         80         90        100
PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR 
       110        120 
LLLPGELAKH AVSEGTKAVT KYTSAK
Length:126
Mass (Da):13,890
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:iFAF9279F44BE703D
GO

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
AJ223352 mRNA Translation: CAA11276.1
AF531294 Genomic DNA Translation: AAN06694.1
AK292062 mRNA Translation: BAF84751.1
AL021807 Genomic DNA No translation available.
CH471081 Genomic DNA Translation: EAX03084.1
BC000893 mRNA Translation: AAH00893.1
BC051872 mRNA Translation: AAH51872.1
BC064959 mRNA Translation: AAH64959.1
BC108737 mRNA Translation: AAI08738.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS4621.1

Protein sequence database of the Protein Information Resource

More...PIRi		S65409

NCBI Reference Sequences

More...RefSeqi		NP_001299582.1, NM_001312653.1
NP_542160.1, NM_080593.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000356950; ENSP00000349430; ENSG00000197903

Database of genes from NCBI RefSeq genomes

More...GeneIDi		85236

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:85236

UCSC genome browser

More...UCSCi		uc063mja.1, 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
AJ223352 mRNA Translation: CAA11276.1
AF531294 Genomic DNA Translation: AAN06694.1
AK292062 mRNA Translation: BAF84751.1
AL021807 Genomic DNA No translation available.
CH471081 Genomic DNA Translation: EAX03084.1
BC000893 mRNA Translation: AAH00893.1
BC051872 mRNA Translation: AAH51872.1
BC064959 mRNA Translation: AAH64959.1
BC108737 mRNA Translation: AAI08738.1
CCDSiCCDS4621.1
PIRiS65409
RefSeqiNP_001299582.1, NM_001312653.1
NP_542160.1, NM_080593.2

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
2CV5X-ray2.50D/H1-126[»]
6KE9X-ray2.22D/H32-126[»]
6L9HX-ray2.60D/H32-126[»]
6LE9X-ray2.60D/H32-126[»]
6T79electron microscopy3.20D/H1-126[»]
6T7Aelectron microscopy3.70D/H1-126[»]
6T7Belectron microscopy5.10D/H1-126[»]
6T7Celectron microscopy4.00D/H1-126[»]
6T7Delectron microscopy4.40D/H1-126[»]
6V92electron microscopy20.00d/h1-126[»]
6Y5Delectron microscopy4.10D/H/P/T1-126[»]
7BWDelectron microscopy4.32D/H2-126[»]
7DBPelectron microscopy4.50D/H1-126[»]
7JZVelectron microscopy3.90O/o2-126[»]
SMRiO60814
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi124439, 66 interactors
DIPiDIP-48935N
IntActiO60814, 36 interactors
MINTiO60814
STRINGi9606.ENSP00000349430

PTM databases

GlyGeniO60814, 1 site
iPTMnetiO60814
MetOSiteiO60814
PhosphoSitePlusiO60814
SwissPalmiO60814

Genetic variation databases

BioMutaiHIST1H2BK

Proteomic databases

EPDiO60814
jPOSTiO60814
MassIVEiO60814
MaxQBiO60814
PaxDbiO60814
PeptideAtlasiO60814
PRIDEiO60814
ProteomicsDBi49607
TopDownProteomicsiO60814

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		25744, 71 antibodies

The DNASU plasmid repository

More...DNASUi		85236

Genome annotation databases

EnsembliENST00000356950; ENSP00000349430; ENSG00000197903
GeneIDi85236
KEGGihsa:85236
UCSCiuc063mja.1, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		85236
DisGeNETi85236

GeneCards: human genes, protein and diseases

More...GeneCardsi		H2BC12
HGNCiHGNC:13954, H2BC12
HPAiENSG00000197903, Tissue enriched (lymphoid)
MIMi615045, gene
neXtProtiNX_O60814
OpenTargetsiENSG00000197903
PharmGKBiPA134955134
VEuPathDBiHostDB:ENSG00000197903

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1744, Eukaryota
GeneTreeiENSGT01030000234651
HOGENOMiCLU_075666_2_1_1
InParanoidiO60814
OMAiYTSANIM
OrthoDBi1536672at2759
PhylomeDBiO60814
TreeFamiTF300212

Enzyme and pathway databases

PathwayCommonsiO60814
ReactomeiR-HSA-110328, Recognition and association of DNA glycosylase with site containing an affected pyrimidine
R-HSA-110329, Cleavage of the damaged pyrimidine
R-HSA-110330, Recognition and association of DNA glycosylase with site containing an affected purine
R-HSA-110331, Cleavage of the damaged purine
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-3214815, HDACs deacetylate histones
R-HSA-3214847, HATs acetylate histones
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-5689880, Ub-specific processing proteases
R-HSA-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-HSA-5693571, Nonhomologous End-Joining (NHEJ)
R-HSA-5693607, Processing of DNA double-strand break ends
R-HSA-606279, Deposition of new CENPA-containing nucleosomes at the centromere
R-HSA-69473, G2/M DNA damage checkpoint
R-HSA-73728, RNA Polymerase I Promoter Opening
R-HSA-73772, RNA Polymerase I Promoter Escape
R-HSA-8866654, E3 ubiquitin ligases ubiquitinate target proteins
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-9609690, HCMV Early Events
R-HSA-9610379, HCMV Late Events
R-HSA-9616222, Transcriptional regulation of granulopoiesis
R-HSA-9670095, Inhibition of DNA recombination at telomere
R-HSA-9710421, Defective pyroptosis
R-HSA-977225, Amyloid fiber formation

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		85236, 105 hits in 986 CRISPR screens

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

More...ChiTaRSi		HIST1H2BK, human
EvolutionaryTraceiO60814

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		HIST1H2BK

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

More...GenomeRNAii		85236
PharosiO60814, Tbio

Protein Ontology

More...PROi		PR:O60814
RNActiO60814, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000197903, Expressed in stomach and 117 other tissues
ExpressionAtlasiO60814, baseline and differential
GenevisibleiO60814, HS

Family and domain databases

Gene3Di1.10.20.10, 1 hit
IDEALiIID00010
InterProiView protein in InterPro
IPR009072, Histone-fold
IPR007125, Histone_H2A/H2B/H3
IPR000558, Histone_H2B
PANTHERiPTHR23428, PTHR23428, 1 hit
PfamiView protein in Pfam
PF00125, Histone, 1 hit
PRINTSiPR00621, HISTONEH2B
SMARTiView protein in SMART
SM00427, H2B, 1 hit
SUPFAMiSSF47113, SSF47113, 1 hit
PROSITEiView protein in PROSITE
PS00357, HISTONE_H2B, 1 hit

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 nameiH2B1K_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: O60814
Secondary accession number(s): A8K7P7, Q2VPI7
<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: August 31, 2004
Last sequence update: January 23, 2007
Last modified: September 29, 2021
This is version 191 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  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. SIMILARITY comments
    Index of protein domains and families
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