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UniProtKB - P84227 (H32_BOVIN)

Entry version 127 (11 Dec 2019)
Sequence version 2 (23 Jan 2007)
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Protein

Histone H3.2

Gene
N/A
Organism
Bos taurus (Bovine)
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.

<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 ...

<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

More...Reactomei		R-BTA-1266695 Interleukin-7 signaling
R-BTA-201722 Formation of the beta-catenin:TCF transactivating complex
R-BTA-212300 PRC2 methylates histones and DNA
R-BTA-2299718 Condensation of Prophase Chromosomes
R-BTA-2559580 Oxidative Stress Induced Senescence
R-BTA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-BTA-3214841 PKMTs methylate histone lysines
R-BTA-3214842 HDMs demethylate histones
R-BTA-3214847 HATs acetylate histones
R-BTA-3214858 RMTs methylate histone arginines
R-BTA-3247509 Chromatin modifying enzymes
R-BTA-427359 SIRT1 negatively regulates rRNA expression
R-BTA-427413 NoRC negatively regulates rRNA expression
R-BTA-5250924 B-WICH complex positively regulates rRNA expression
R-BTA-5578749 Transcriptional regulation by small RNAs
R-BTA-5625886 Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3
R-BTA-73728 RNA Polymerase I Promoter Opening
R-BTA-73772 RNA Polymerase I Promoter Escape
R-BTA-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-BTA-9018519 Estrogen-dependent gene expression
R-BTA-983231 Factors involved in megakaryocyte development and platelet production

<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 H3.2
<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>OrganismiBos taurus (Bovine)
<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 identifieri9913 [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 › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos
<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
  • UP000009136 <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 3

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

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

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
<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_00002212572 – 136Histone H3.2Add BLAST135

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-crotonyllysine; alternateBy similarity1
Modified residuei5N6-methyllysine; 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-crotonyllysine; alternateBy similarity1
Modified residuei10N6-methyllysine; alternateBy similarity1
Modified residuei11ADP-ribosylserine; alternateBy similarity1
Modified residuei11Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA51 Publication1
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-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-crotonyllysine; alternateBy similarity1
Modified residuei19N6-glutaryllysine; 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-crotonyllysine; alternateBy similarity1
Modified residuei24N6-glutaryllysine; 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-crotonyllysine; alternateBy similarity1
Modified residuei28N6-glutaryllysine; alternateBy similarity1
Modified residuei28N6-methyllysine; alternateBy similarity1
Modified residuei29ADP-ribosylserine; alternateBy similarity1
Modified residuei29Phosphoserine; alternate; by AURKB, AURKC and RPS6KA51 Publication1
Modified residuei37N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei37N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei37N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei37N6-acetyllysine; alternateBy similarity1
Modified residuei37N6-methyllysine; alternateBy similarity1
Modified residuei38N6-methyllysineBy similarity1
Modified residuei42PhosphotyrosineBy similarity1
Modified residuei57N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei57N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei57N6-(beta-hydroxybutyryl)lysine; alternateBy similarity1
Modified residuei57N6-acetyllysine; alternateBy similarity1
Modified residuei57N6-crotonyllysine; alternateBy similarity1
Modified residuei57N6-glutaryllysine; alternateBy similarity1
Modified residuei57N6-methyllysine; by EHMT2; alternateBy similarity1
Modified residuei57N6-succinyllysine; alternateBy similarity1
Modified residuei58PhosphoserineBy similarity1
Modified residuei65N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei65N6-methyllysine; alternateBy similarity1
Modified residuei80N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei80N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei80N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei80N6-acetyllysine; alternateBy similarity1
Modified residuei80N6-glutaryllysine; alternateBy similarity1
Modified residuei80N6-methyllysine; alternateBy similarity1
Modified residuei80N6-succinyllysine; alternateBy similarity1
Modified residuei81PhosphothreonineBy similarity1
Modified residuei87PhosphoserineBy similarity1
Modified residuei108PhosphothreonineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi111S-palmitoyl cysteineBy similarity1
Modified residuei116N6-acetyllysine; alternateBy similarity1
Modified residuei116N6-glutaryllysine; alternateBy similarity1
Modified residuei123N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei123N6-acetyllysine; alternateBy similarity1
Modified residuei123N6-glutaryllysine; alternateBy similarity1
Modified residuei123N6-methyllysine; alternateBy similarity1
Modified residuei123N6-succinyllysine; alternateBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Acetylation 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-123 (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
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
Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. 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) and Lys-80 (H3K79me) require 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-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication.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-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin.By similarity
Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination (By similarity). Ubiquitinated by the CUL4-DDB-RBX1 complex in response to ultraviolet irradiation. This may weaken the interaction between histones and DNA and facilitate DNA accessibility to repair proteins (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
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.By similarity
Butyrylation of histones marks active promoters and competes with histone acetylation. It is present during late spermatogenesis.By similarity
Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a maximum frequency around the transcription start sites of genes. It gives a specific tag for epigenetic transcription activation. Desuccinylation at Lys-123 (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, Lipoprotein, Methylation, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...PaxDbi		P84227

PRoteomics IDEntifications database

More...PRIDEi		P84227

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P84227

<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 the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed during S phase, then expression strongly decreases as cell division slows down during the process of differentiation.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSBTAG00000032452 Expressed in 6 organ(s), highest expression level in heart

<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. During nucleosome assembly the chaperone ASF1A interacts with the histone H3-H4 heterodimer (By similarity).

By similarity

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

Protein interaction database and analysis system

More...IntActi		P84227, 1 interactor

STRING: functional protein association networks

More...STRINGi		9913.ENSBTAP00000053067

<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

3D structure databases

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

More...SMRi		P84227

Database of comparative protein structure models

More...ModBasei		Search...

<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
COG2036 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00960000186578

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000155290

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P84227

KEGG Orthology (KO)

More...KOi		K11253

Identification of Orthologs from Complete Genome Data

More...OMAi		FTTQMAR

Database of Orthologous Groups

More...OrthoDBi		1564596at2759

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_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.

P84227-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR 
        60         70         80         90        100
EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY 
       110        120        130 
LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA
Length:136
Mass (Da):15,388
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:i6FD8508EA50A0EEC
GO

Sequence databases

NCBI Reference Sequences

More...RefSeqi		NP_001160041.1, NM_001166569.1
XP_015318079.1, XM_015462593.1
XP_015318510.1, XM_015463024.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSBTAT00000066724; ENSBTAP00000065756; ENSBTAG00000050095
ENSBTAT00000069328; ENSBTAP00000062977; ENSBTAG00000051272
ENSBTAT00000071853; ENSBTAP00000072574; ENSBTAG00000050881
ENSBTAT00000078263; ENSBTAP00000066016; ENSBTAG00000054782
ENSBTAT00000079615; ENSBTAP00000063380; ENSBTAG00000054906

Database of genes from NCBI RefSeq genomes

More...GeneIDi		504599
788077

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		bta:504599
bta:788077

<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

RefSeqiNP_001160041.1, NM_001166569.1
XP_015318079.1, XM_015462593.1
XP_015318510.1, XM_015463024.1

3D structure databases

SMRiP84227
ModBaseiSearch...

Protein-protein interaction databases

IntActiP84227, 1 interactor
STRINGi9913.ENSBTAP00000053067

PTM databases

iPTMnetiP84227

Proteomic databases

PaxDbiP84227
PRIDEiP84227

Genome annotation databases

EnsembliENSBTAT00000066724; ENSBTAP00000065756; ENSBTAG00000050095
ENSBTAT00000069328; ENSBTAP00000062977; ENSBTAG00000051272
ENSBTAT00000071853; ENSBTAP00000072574; ENSBTAG00000050881
ENSBTAT00000078263; ENSBTAP00000066016; ENSBTAG00000054782
ENSBTAT00000079615; ENSBTAP00000063380; ENSBTAG00000054906
GeneIDi504599
788077
KEGGibta:504599
bta:788077

Phylogenomic databases

eggNOGiKOG1745 Eukaryota
COG2036 LUCA
GeneTreeiENSGT00960000186578
HOGENOMiHOG000155290
InParanoidiP84227
KOiK11253
OMAiFTTQMAR
OrthoDBi1564596at2759
TreeFamiTF314241

Enzyme and pathway databases

ReactomeiR-BTA-1266695 Interleukin-7 signaling
R-BTA-201722 Formation of the beta-catenin:TCF transactivating complex
R-BTA-212300 PRC2 methylates histones and DNA
R-BTA-2299718 Condensation of Prophase Chromosomes
R-BTA-2559580 Oxidative Stress Induced Senescence
R-BTA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-BTA-3214841 PKMTs methylate histone lysines
R-BTA-3214842 HDMs demethylate histones
R-BTA-3214847 HATs acetylate histones
R-BTA-3214858 RMTs methylate histone arginines
R-BTA-3247509 Chromatin modifying enzymes
R-BTA-427359 SIRT1 negatively regulates rRNA expression
R-BTA-427413 NoRC negatively regulates rRNA expression
R-BTA-5250924 B-WICH complex positively regulates rRNA expression
R-BTA-5578749 Transcriptional regulation by small RNAs
R-BTA-5625886 Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3
R-BTA-73728 RNA Polymerase I Promoter Opening
R-BTA-73772 RNA Polymerase I Promoter Escape
R-BTA-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-BTA-9018519 Estrogen-dependent gene expression
R-BTA-983231 Factors involved in megakaryocyte development and platelet production

Gene expression databases

BgeeiENSBTAG00000032452 Expressed in 6 organ(s), highest expression level in heart

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 nameiH32_BOVIN
<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: P84227
Secondary accession number(s): P02295
, P02297, P16105, P17269, P17320
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: December 11, 2019
This is version 127 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Keywords - Technical termi

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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