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Entry version 163 (11 Dec 2019)
Sequence version 3 (23 Jan 2007)
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Protein

Charged multivesicular body protein 3

Gene

CHMP3

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 and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Selectively binds to phosphatidylinositol 3,5-bisphosphate PtdIns(3,5)P2 and PtdIns(3,4)P2 in preference to other phosphoinositides tested. Involved in late stages of cytokinesis. Plays a role in endosomal sorting/trafficking of EGF receptor. Isoform 2 prevents stress-mediated cell death and accumulation of reactive oxygen species when expressed in yeast cells.5 Publications

Miscellaneous

Its overexpression strongly inhibits HIV-1 release.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei48Important for autoinhibitory function1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei216STAMBP1

<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 processApoptosis, Cell cycle, Cell division, Protein 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-917729 Endosomal Sorting Complex Required For Transport (ESCRT)
R-HSA-9615710 Microautophagy

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
Q9Y3E7

<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 3
Alternative name(s):
Chromatin-modifying protein 3
Neuroendocrine differentiation factor
Vacuolar protein sorting-associated protein 24
Short name:
hVps24
<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:CHMP3
Synonyms:CGI149, NEDF, VPS24
ORF Names:CGI-149
<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 2

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000115561.15

Human Gene Nomenclature Database

More...
HGNCi
HGNC:29865 CHMP3

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
610052 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9Y3E7

<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

Cytoplasm, 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>Mutagenesisi24 – 25RK → SA: Impairs HIV-1 release; when associated with S-28. 1 Publication2
Mutagenesisi28R → S: Impairs HIV-1 release; when associated with 24-S-A-25. 1 Publication1
Mutagenesisi48V → D: Induces assembly with CHMP2A into helical tubes in vitro; when associated with D-64. Enhances inhibition of HIV-1 budding in vivo; when associated with D-168 and D-169. 1 Publication1
Mutagenesisi54K → S: Abolishes dimerization; when associated with N-56; E-59 and 62-D-E-63. 1 Publication1
Mutagenesisi56Q → N: Abolishes dimerization; when associated with S-54; E-59 and 62-D-E-63. 1 Publication1
Mutagenesisi59V → D: Abolishes interaction with CHMP2A and assembly into helical tubes in vitro; when associated with D-62; D-168 and D-169. 2 Publications1
Mutagenesisi59V → E: Abolishes dimerization; when associated with S-54; N-56 and 62-D-E-63. 2 Publications1
Mutagenesisi62 – 63VL → DE: Abolishes dimerization; when associated with S-54; N-56 and E-59. 1 Publication2
Mutagenesisi62V → D: Abolishes interaction with CHMP2A and assembly into helical tubes in vitro; when associated with D-59; D-168 and D-169. 1 Publication1
Mutagenesisi64A → D: Induces assembly with CHMP2A into helical tubes in vitro; when associated with D-48. 1 Publication1
Mutagenesisi78 – 79YA → AE: Abolishes dimerization. 1 Publication2
Mutagenesisi168 – 169IL → DD: Induces assembly with CHMP2A into helical tubes in vitro and slightly enhances inhibition of HIV-1 budding in vivo. Abolishes interaction with CHMP2A and assembly into helical tubes in vitro; when associated with D-59 and D-62. 1 Publication2
Mutagenesisi179 – 222Missing : Membrane association; releases autoinhibition. 1 PublicationAdd BLAST44
Mutagenesisi216 – 217RL → AA: Abolishes interaction with VPS4A and STAMBP. 1 Publication2
Mutagenesisi221 – 222Missing : Abolishes interaction with VPS4A and STAMBP. 1 Publication2
Mutagenesisi222Missing : Impairs interaction with VPS4A and STAMBP. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
100526767
51652

Open Targets

More...
OpenTargetsi
ENSG00000115561
ENSG00000249884

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA134920495

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q9Y3E7 Tbio

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
CHMP3

Domain mapping of disease mutations (DMDM)

More...
DMDMi
73917763

<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 methionineiRemovedSequence analysis
<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_00002114792 – 222Charged multivesicular body protein 3Add BLAST221

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Lipidationi2N-myristoyl glycineSequence analysis1
<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-linki179Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
<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 residuei200PhosphoserineCombined sources1

Keywords - PTMi

Isopeptide bond, Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q9Y3E7

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9Y3E7

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q9Y3E7

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

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PaxDbi
Q9Y3E7

PeptideAtlas

More...
PeptideAtlasi
Q9Y3E7

PRoteomics IDEntifications database

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PRIDEi
Q9Y3E7

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
86031 [Q9Y3E7-1]
86032 [Q9Y3E7-2]
86033 [Q9Y3E7-3]
86034 [Q9Y3E7-4]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9Y3E7

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

More...
PhosphoSitePlusi
Q9Y3E7

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

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

Widely expressed. Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000115561 Expressed in 232 organ(s), highest expression level in corpus callosum

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9Y3E7 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA015673
HPA073383

<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.

Forms a metastable monomer in solution; its core structure (without part of the putative autoinhibitory C-terminal acidic region) oligomerizes into a flat lattice via two different dimerization interfaces. In vitro, heteromerizes with CHMP2A (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. May interact with IGFBP7; the relevance of such interaction however remains unclear.

Interacts with CHMP2A.

Interacts with CHMP4A; the interaction requires the release of CHMP4A autoinhibition.

Interacts with VPS4A.

Interacts with STAMBP; the interaction appears to relieve the autoinhibition of CHMP3.

Interacts with VTA1.

11 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

Show more details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
119660, 33 interactors
1529307, 2 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-329 ESCRT-III complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q9Y3E7

Database of interacting proteins

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DIPi
DIP-48532N

Protein interaction database and analysis system

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IntActi
Q9Y3E7, 31 interactors

Molecular INTeraction database

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MINTi
Q9Y3E7

STRING: functional protein association networks

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STRINGi
9606.ENSP00000474823

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q9Y3E7 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

1222
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

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SMRi
Q9Y3E7

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9Y3E7

<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>Regioni2 – 113Intramolecular interaction with C-terminusAdd BLAST112
Regioni59 – 64Important for autoinhibitory function6
Regioni151 – 222Interaction with VPS4AAdd BLAST72
Regioni151 – 220Intramolecular interaction with N-terminusAdd BLAST70
Regioni168 – 169Important for autoinhibitory function2
Regioni203 – 207Interaction with STAMBP5
Regioni221 – 222Interaction with STAMBP2

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 coili22 – 54Sequence analysisAdd BLAST33
Coiled coili141 – 222Sequence analysisAdd BLAST82

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>Motifi201 – 211MIT-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
KOG0800 Eukaryota
KOG3229 Eukaryota
COG5491 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000182832

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000177219

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9Y3E7

KEGG Orthology (KO)

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KOi
K12193

Identification of Orthologs from Complete Genome Data

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OMAi
YASKAQM

Database of Orthologous Groups

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OrthoDBi
1418709at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9Y3E7

TreeFam database of animal gene trees

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TreeFami
TF105848

Family and domain databases

Database of protein disorder

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DisProti
DP01283

Integrated resource of protein families, domains and functional sites

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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>. 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>Sequences (4)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.

<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.

This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q9Y3E7-1) [UniParc]FASTAAdd to basket
Also known as: Vps24alpha

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MGLFGKTQEK PPKELVNEWS LKIRKEMRVV DRQIRDIQRE EEKVKRSVKD
60 70 80 90 100
AAKKGQKDVC IVLAKEMIRS RKAVSKLYAS KAHMNSVLMG MKNQLAVLRV
110 120 130 140 150
AGSLQKSTEV MKAMQSLVKI PEIQATMREL SKEMMKAGII EEMLEDTFES
160 170 180 190 200
MDDQEEMEEE AEMEIDRILF EITAGALGKA PSKVTDALPE PEPPGAMAAS
210 220
EDEEEEEEAL EAMQSRLATL RS
Length:222
Mass (Da):25,073
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:i7B1ACE5EA453E8C0
GO
Isoform 2 (identifier: Q9Y3E7-2) [UniParc]FASTAAdd to basket
Also known as: Vps24beta

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: Missing.

Show »
Length:156
Mass (Da):17,326
Checksum:i7B10B4D1FB7E1B62
GO
Isoform 3 (identifier: Q9Y3E7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MGLFGKTQEKPPKEL → MEGELYSALKEEEASESVSSTNFSGEMHFYELVEDTKDGIWLVQ

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Length:251
Mass (Da):28,386
Checksum:i0BA3A646BBC05B51
GO
Isoform 4 (identifier: Q9Y3E7-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     74-113: Missing.

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Length:182
Mass (Da):20,770
Checksum:iE2951422F9E1A226
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti208E → D in AAF26737 (PubMed:11549700).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0410761 – 66Missing in isoform 2. 2 PublicationsAdd BLAST66
Alternative sequenceiVSP_0421241 – 15MGLFG…PPKEL → MEGELYSALKEEEASESVSS TNFSGEMHFYELVEDTKDGI WLVQ in isoform 3. 1 PublicationAdd BLAST15
Alternative sequenceiVSP_04212574 – 113Missing in isoform 4. CuratedAdd BLAST40

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF219226 mRNA Translation: AAF26737.1
AY364249 mRNA Translation: AAQ76808.1
AF151907 mRNA Translation: AAD34144.1
AK290725 mRNA Translation: BAF83414.1
AK294389 mRNA Translation: BAG57645.1
AK312353 mRNA Translation: BAG35273.1
AK315835 mRNA Translation: BAF98726.1
AC015971 Genomic DNA Translation: AAX93078.1
AC064848 Genomic DNA No translation available.
AC068288 Genomic DNA Translation: AAY24211.1
CH471053 Genomic DNA Translation: EAW99448.1
CH471053 Genomic DNA Translation: EAW99449.1
CH471053 Genomic DNA Translation: EAW99450.1
CH471053 Genomic DNA Translation: EAW99451.1
BC004419 mRNA Translation: AAH04419.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS33236.1 [Q9Y3E7-1]
CCDS42707.1 [Q9Y3E7-2]
CCDS54375.1 [Q9Y3E7-4]

NCBI Reference Sequences

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RefSeqi
NP_001005753.1, NM_001005753.2 [Q9Y3E7-2]
NP_001180446.1, NM_001193517.1 [Q9Y3E7-4]
NP_001185883.1, NM_001198954.1 [Q9Y3E7-3]
NP_057163.1, NM_016079.3 [Q9Y3E7-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000263856; ENSP00000263856; ENSG00000115561 [Q9Y3E7-1]
ENST00000409225; ENSP00000386590; ENSG00000115561 [Q9Y3E7-2]
ENST00000409727; ENSP00000387045; ENSG00000115561 [Q9Y3E7-4]

Database of genes from NCBI RefSeq genomes

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GeneIDi
100526767
51652

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:100526767
hsa:51652

UCSC genome browser

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UCSCi
uc002srj.4 human [Q9Y3E7-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
AF219226 mRNA Translation: AAF26737.1
AY364249 mRNA Translation: AAQ76808.1
AF151907 mRNA Translation: AAD34144.1
AK290725 mRNA Translation: BAF83414.1
AK294389 mRNA Translation: BAG57645.1
AK312353 mRNA Translation: BAG35273.1
AK315835 mRNA Translation: BAF98726.1
AC015971 Genomic DNA Translation: AAX93078.1
AC064848 Genomic DNA No translation available.
AC068288 Genomic DNA Translation: AAY24211.1
CH471053 Genomic DNA Translation: EAW99448.1
CH471053 Genomic DNA Translation: EAW99449.1
CH471053 Genomic DNA Translation: EAW99450.1
CH471053 Genomic DNA Translation: EAW99451.1
BC004419 mRNA Translation: AAH04419.1
CCDSiCCDS33236.1 [Q9Y3E7-1]
CCDS42707.1 [Q9Y3E7-2]
CCDS54375.1 [Q9Y3E7-4]
RefSeqiNP_001005753.1, NM_001005753.2 [Q9Y3E7-2]
NP_001180446.1, NM_001193517.1 [Q9Y3E7-4]
NP_001185883.1, NM_001198954.1 [Q9Y3E7-3]
NP_057163.1, NM_016079.3 [Q9Y3E7-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GD5X-ray2.80A/B/C/D9-183[»]
2XZEX-ray1.75Q/R183-222[»]
3FRTX-ray4.00A/B8-222[»]
3FRVX-ray3.70A1-150[»]
SMRiQ9Y3E7
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi119660, 33 interactors
1529307, 2 interactors
ComplexPortaliCPX-329 ESCRT-III complex
CORUMiQ9Y3E7
DIPiDIP-48532N
IntActiQ9Y3E7, 31 interactors
MINTiQ9Y3E7
STRINGi9606.ENSP00000474823

PTM databases

iPTMnetiQ9Y3E7
PhosphoSitePlusiQ9Y3E7

Polymorphism and mutation databases

BioMutaiCHMP3
DMDMi73917763

Proteomic databases

EPDiQ9Y3E7
jPOSTiQ9Y3E7
MassIVEiQ9Y3E7
PaxDbiQ9Y3E7
PeptideAtlasiQ9Y3E7
PRIDEiQ9Y3E7
ProteomicsDBi86031 [Q9Y3E7-1]
86032 [Q9Y3E7-2]
86033 [Q9Y3E7-3]
86034 [Q9Y3E7-4]

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
51652

Genome annotation databases

EnsembliENST00000263856; ENSP00000263856; ENSG00000115561 [Q9Y3E7-1]
ENST00000409225; ENSP00000386590; ENSG00000115561 [Q9Y3E7-2]
ENST00000409727; ENSP00000387045; ENSG00000115561 [Q9Y3E7-4]
GeneIDi100526767
51652
KEGGihsa:100526767
hsa:51652
UCSCiuc002srj.4 human [Q9Y3E7-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
100526767
51652
DisGeNETi100526767
51652
EuPathDBiHostDB:ENSG00000115561.15

GeneCards: human genes, protein and diseases

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GeneCardsi
CHMP3
HGNCiHGNC:29865 CHMP3
HPAiHPA015673
HPA073383
MIMi610052 gene
neXtProtiNX_Q9Y3E7
OpenTargetsiENSG00000115561
ENSG00000249884
PharmGKBiPA134920495

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0800 Eukaryota
KOG3229 Eukaryota
COG5491 LUCA
GeneTreeiENSGT00950000182832
HOGENOMiHOG000177219
InParanoidiQ9Y3E7
KOiK12193
OMAiYASKAQM
OrthoDBi1418709at2759
PhylomeDBiQ9Y3E7
TreeFamiTF105848

Enzyme and pathway databases

ReactomeiR-HSA-162588 Budding and maturation of HIV virion
R-HSA-1632852 Macroautophagy
R-HSA-917729 Endosomal Sorting Complex Required For Transport (ESCRT)
R-HSA-9615710 Microautophagy
SignaLinkiQ9Y3E7

Miscellaneous databases

EvolutionaryTraceiQ9Y3E7

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
VPS24
PharosiQ9Y3E7 Tbio

Protein Ontology

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PROi
PR:Q9Y3E7
RNActiQ9Y3E7 protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000115561 Expressed in 232 organ(s), highest expression level in corpus callosum
GenevisibleiQ9Y3E7 HS

Family and domain databases

DisProtiDP01283
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
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiCHMP3_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: Q9Y3E7
Secondary accession number(s): A8K3W0
, B4DG34, B8ZZM0, B8ZZX5, Q3ZTS9, Q53S71, Q53SU5, Q9NZ51
<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: January 23, 2007
Last modified: December 11, 2019
This is version 163 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Reference proteome

Documents

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