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Entry version 159 (08 May 2019)
Sequence version 1 (01 Jun 1998)
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Protein

Charged multivesicular body protein 2a

Gene

CHMP2A

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

Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis (PubMed:21310966). Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase (PubMed:26040712). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4.Curated2 Publications
(Microbial infection) The ESCRT machinery functions in topologically equivalent membrane fission events, such as the budding of enveloped viruses (HIV-1 and other lentiviruses). Involved in HIV-1 p6- and p9-dependent virus release.2 Publications

Miscellaneous

Its overexpression strongly inhibits HIV-1 release.

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

GO - Biological processi

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

Biological processProtein transport, Transport

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-162588 Budding and maturation of HIV virion
R-HSA-1632852 Macroautophagy
R-HSA-432720 Lysosome Vesicle Biogenesis
R-HSA-917729 Endosomal Sorting Complex Required For Transport (ESCRT)

<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:
Charged multivesicular body protein 2a
Alternative name(s):
Chromatin-modifying protein 2a
Short name:
CHMP2a
Putative breast adenocarcinoma marker BC-2
Vacuolar protein sorting-associated protein 2-1
Short name:
Vps2-1
Short name:
hVps2-1
<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:CHMP2A
Synonyms:BC2, CHMP2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:30216 CHMP2A

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
610893 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O43633

<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

Endosome, Membrane

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi169 – 170DE → AA: Diminishes interaction with VPS4B. 1 Publication2
Mutagenesisi181 – 222Missing : Membrane association; releases autoinhibition. 1 PublicationAdd BLAST42
Mutagenesisi216L → A: Diminishes interaction with VTA1. 1 Publication1
Mutagenesisi217 – 222Missing : Abolishes interaction with VTA1. 1 Publication6

Organism-specific databases

Open Targets

More...
OpenTargetsi
ENSG00000130724

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA142672111

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
CHMP2A

<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 ‘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_00002114621 – 222Charged multivesicular body protein 2aAdd BLAST222

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 residuei1N-acetylmethionine1 Publication1
Modified residuei184PhosphoserineCombined sources1
Modified residuei185PhosphothreonineCombined sources1
Modified residuei188PhosphoserineCombined sources1
Modified residuei190PhosphoserineCombined sources1
Modified residuei203PhosphoserineCombined sources1

<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

ISGylated in a CHMP5-dependent manner. Isgylation weakens and inhibits its interactions with VPS4A and VTA1 respectively.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
O43633

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
O43633

MaxQB - The MaxQuant DataBase

More...
MaxQBi
O43633

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

More...
PaxDbi
O43633

PeptideAtlas

More...
PeptideAtlasi
O43633

PRoteomics IDEntifications database

More...
PRIDEi
O43633

ProteomicsDB human proteome resource

More...
ProteomicsDBi
49086

2D gel databases

USC-OGP 2-DE database

More...
OGPi
O43633

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O43633

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

More...
PhosphoSitePlusi
O43633

<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
ENSG00000130724 Expressed in 227 organ(s), highest expression level in blood

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
O43633 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O43633 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA041153
HPA042031

<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

Probable core component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentially. In vitro, heteromerizes with CHMP3 (but not CHMP4) to form helical tubular structures that expose membrane-interacting sites on the outside whereas VPS4B can associate on the inside of the tubule. Interacts with CHMP1B, CHMP2B, CHMP3, CHMP4A, CHMP4B, CHMP4C and CHMP5. Interacts with VPS4A; the interaction is direct. Interacts with VPS4B; the interaction is direct. Interacts with MITD1. Interacts with VTA1; the interaction probably involves the open conformation of CHMP2A.7 Publications

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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
118091, 70 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-329 ESCRT-III complex

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
O43633

Database of interacting proteins

More...
DIPi
DIP-48533N

Protein interaction database and analysis system

More...
IntActi
O43633, 36 interactors

Molecular INTeraction database

More...
MINTi
O43633

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000469240

<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
O43633

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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

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>Regioni56 – 222Interaction with VPS4BAdd BLAST167
Regioni217 – 222Interaction with VTA16

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili12 – 53Sequence analysisAdd BLAST42
Coiled coili195 – 222Sequence analysisAdd BLAST28

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi210 – 220MIT-interacting motifAdd BLAST11

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The acidic C-terminus and the basic N-termminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components.

<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 SNF7 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3230 Eukaryota
COG5491 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000182832

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000177218

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O43633

KEGG Orthology (KO)

More...
KOi
K12191

Identification of Orthologs from Complete Genome Data

More...
OMAi
NMNRQLN

Database of Orthologous Groups

More...
OrthoDBi
1254120at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O43633

TreeFam database of animal gene trees

More...
TreeFami
TF300118

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005024 Snf7_fam

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03357 Snf7, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<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.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

O43633-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDLLFGRRKT PEELLRQNQR ALNRAMRELD RERQKLETQE KKIIADIKKM
60 70 80 90 100
AKQGQMDAVR IMAKDLVRTR RYVRKFVLMR ANIQAVSLKI QTLKSNNSMA
110 120 130 140 150
QAMKGVTKAM GTMNRQLKLP QIQKIMMEFE RQAEIMDMKE EMMNDAIDDA
160 170 180 190 200
MGDEEDEEES DAVVSQVLDE LGLSLTDELS NLPSTGGSLS VAAGGKKAEA
210 220
AASALADADA DLEERLKNLR RD
Length:222
Mass (Da):25,104
Last modified:June 1, 1998 - v1
<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:iF2B86C623829E32E
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
M0QXX8M0QXX8_HUMAN
Charged multivesicular body protein...
CHMP2A
55Annotation score:

Annotation score:1 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>
M0R1L7M0R1L7_HUMAN
Charged multivesicular body protein...
CHMP2A
159Annotation score:

Annotation score:1 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>
M0R1T5M0R1T5_HUMAN
Charged multivesicular body protein...
CHMP2A
227Annotation score:

Annotation score:1 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>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF042384 mRNA Translation: AAC00005.1
AJ277113 Genomic DNA Translation: CAC14310.1
AY364248 mRNA Translation: AAQ76807.1
BT007298 mRNA Translation: AAP35962.1
CR457002 mRNA Translation: CAG33283.1
AK311974 mRNA Translation: BAG34913.1
CH471135 Genomic DNA Translation: EAW72609.1
BC002502 mRNA Translation: AAH02502.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS12986.1

NCBI Reference Sequences

More...
RefSeqi
NP_055268.1, NM_014453.3
NP_940818.1, NM_198426.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000312547; ENSP00000310440; ENSG00000130724
ENST00000600118; ENSP00000469240; ENSG00000130724
ENST00000601220; ENSP00000472680; ENSG00000130724

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
27243

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:27243

UCSC genome browser

More...
UCSCi
uc002qti.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
AF042384 mRNA Translation: AAC00005.1
AJ277113 Genomic DNA Translation: CAC14310.1
AY364248 mRNA Translation: AAQ76807.1
BT007298 mRNA Translation: AAP35962.1
CR457002 mRNA Translation: CAG33283.1
AK311974 mRNA Translation: BAG34913.1
CH471135 Genomic DNA Translation: EAW72609.1
BC002502 mRNA Translation: AAH02502.1
CCDSiCCDS12986.1
RefSeqiNP_055268.1, NM_014453.3
NP_940818.1, NM_198426.2

3D structure databases

SMRiO43633
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118091, 70 interactors
ComplexPortaliCPX-329 ESCRT-III complex
CORUMiO43633
DIPiDIP-48533N
IntActiO43633, 36 interactors
MINTiO43633
STRINGi9606.ENSP00000469240

PTM databases

iPTMnetiO43633
PhosphoSitePlusiO43633

Polymorphism and mutation databases

BioMutaiCHMP2A

2D gel databases

OGPiO43633

Proteomic databases

EPDiO43633
jPOSTiO43633
MaxQBiO43633
PaxDbiO43633
PeptideAtlasiO43633
PRIDEiO43633
ProteomicsDBi49086

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
27243
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312547; ENSP00000310440; ENSG00000130724
ENST00000600118; ENSP00000469240; ENSG00000130724
ENST00000601220; ENSP00000472680; ENSG00000130724
GeneIDi27243
KEGGihsa:27243
UCSCiuc002qti.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
27243

GeneCards: human genes, protein and diseases

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GeneCardsi
CHMP2A
HGNCiHGNC:30216 CHMP2A
HPAiHPA041153
HPA042031
MIMi610893 gene
neXtProtiNX_O43633
OpenTargetsiENSG00000130724
PharmGKBiPA142672111

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3230 Eukaryota
COG5491 LUCA
GeneTreeiENSGT00950000182832
HOGENOMiHOG000177218
InParanoidiO43633
KOiK12191
OMAiNMNRQLN
OrthoDBi1254120at2759
PhylomeDBiO43633
TreeFamiTF300118

Enzyme and pathway databases

ReactomeiR-HSA-162588 Budding and maturation of HIV virion
R-HSA-1632852 Macroautophagy
R-HSA-432720 Lysosome Vesicle Biogenesis
R-HSA-917729 Endosomal Sorting Complex Required For Transport (ESCRT)

Miscellaneous databases

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

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ChiTaRSi
CHMP2A human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
CHMP2A

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

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GenomeRNAii
27243

Protein Ontology

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PROi
PR:O43633

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSG00000130724 Expressed in 227 organ(s), highest expression level in blood
ExpressionAtlasiO43633 baseline and differential
GenevisibleiO43633 HS

Family and domain databases

InterProiView protein in InterPro
IPR005024 Snf7_fam
PfamiView protein in Pfam
PF03357 Snf7, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiCHM2A_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: O43633
Secondary accession number(s): B2R4W6, Q3ZTT0
<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 30, 2005
Last sequence update: June 1, 1998
Last modified: May 8, 2019
This is version 159 of the entry and version 1 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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