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Q9Y3E7

- CHMP3_HUMAN

UniProt

Q9Y3E7 - CHMP3_HUMAN

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Protein
Charged multivesicular body protein 3
Gene
CHMP3, CGI149, NEDF, VPS24, CGI-149
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei48 – 481Important for autoinhibitory function
Binding sitei216 – 2161STAMBP

GO - Molecular functioni

  1. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cell cycle Source: UniProtKB-KW
  3. cell division Source: UniProtKB-KW
  4. endosomal transport Source: Reactome
  5. membrane organization Source: Reactome
  6. positive regulation of viral release from host cell Source: UniProt
  7. protein transport Source: UniProtKB-KW
  8. regulation of viral process Source: UniProt
  9. viral life cycle Source: Reactome
  10. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Cell cycle, Cell division, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_27258. Endosomal Sorting Complex Required For Transport (ESCRT).
REACT_6359. Budding and maturation of HIV virion.
SignaLinkiQ9Y3E7.

Names & Taxonomyi

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
Gene namesi
Name:CHMP3
Synonyms:CGI149, NEDF, VPS24
ORF Names:CGI-149
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:29865. CHMP3.

Subcellular locationi

Cytoplasmcytosol. Membrane; Lipid-anchor. Endosome. Late endosome membrane Inferred
Note: Localizes to the midbody of dividing cells.3 Publications

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  3. late endosome membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi24 – 252RK → SA: Impairs HIV-1 release; when associated with S-28.
Mutagenesisi28 – 281R → S: Impairs HIV-1 release; when associated with 24-S-A-25. 1 Publication
Mutagenesisi48 – 481V → 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 Publication
Mutagenesisi54 – 541K → S: Abolishes dimerization; when associated with N-56; E-59 and 62-D-E-63. 1 Publication
Mutagenesisi56 – 561Q → N: Abolishes dimerization; when associated with S-54; E-59 and 62-D-E-63. 1 Publication
Mutagenesisi59 – 591V → D: Abolishes interaction with CHMP2A and assembly into helical tubes in vitro; when associated with D-62; D-168 and D-169. 2 Publications
Mutagenesisi59 – 591V → E: Abolishes dimerization; when associated with S-54; N-56 and 62-D-E-63. 2 Publications
Mutagenesisi62 – 632VL → DE: Abolishes dimerization; when associated with S-54; N-56 and E-59. 1 Publication
Mutagenesisi62 – 621V → D: Abolishes interaction with CHMP2A and assembly into helical tubes in vitro; when associated with D-59; D-168 and D-169. 1 Publication
Mutagenesisi64 – 641A → D: Induces assembly with CHMP2A into helical tubes in vitro; when associated with D-48. 1 Publication
Mutagenesisi78 – 792YA → AE: Abolishes dimerization.
Mutagenesisi168 – 1692IL → 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.
Mutagenesisi179 – 22244Missing: Membrane association; releases autoinhibition. 2 Publications
Add
BLAST
Mutagenesisi216 – 2172RL → AA: Abolishes interaction with VPS4A and STAMBP.
Mutagenesisi221 – 2222Missing: Abolishes interaction with VPS4A and STAMBP. 1 Publication
Mutagenesisi222 – 2221Missing: Impairs interaction with VPS4A and STAMBP. 1 Publication

Organism-specific databases

PharmGKBiPA134920495.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed Reviewed prediction
Chaini2 – 222221Charged multivesicular body protein 3
PRO_0000211479Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine Reviewed prediction
Cross-linki179 – 179Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei200 – 2001Phosphoserine4 Publications

Keywords - PTMi

Isopeptide bond, Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9Y3E7.
PaxDbiQ9Y3E7.
PRIDEiQ9Y3E7.

PTM databases

PhosphoSiteiQ9Y3E7.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9Y3E7.
CleanExiHS_VPS24.
GenevestigatoriQ9Y3E7.

Organism-specific databases

HPAiHPA015673.

Interactioni

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 sequentally. 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 VTA1.12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
STAMBPO956305EBI-2118119,EBI-396676

Protein-protein interaction databases

BioGridi119660. 19 interactions.
DIPiDIP-48532N.
IntActiQ9Y3E7. 9 interactions.
MINTiMINT-1185988.
STRINGi9606.ENSP00000263856.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 5339
Helixi57 – 10044
Helixi109 – 1124
Turni113 – 1153
Beta strandi120 – 1223
Helixi125 – 13713
Helixi164 – 1674
Helixi201 – 22020

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GD5X-ray2.80A/B/C/D9-183[»]
2XZEX-ray1.75Q/R183-222[»]
3FRTX-ray4.00A/B8-222[»]
3FRVX-ray3.70A1-150[»]
ProteinModelPortaliQ9Y3E7.
SMRiQ9Y3E7. Positions 5-181.

Miscellaneous databases

EvolutionaryTraceiQ9Y3E7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 113112Intramolecular interaction with C-terminus
Add
BLAST
Regioni59 – 646Important for autoinhibitory function
Regioni151 – 22272Interaction with VPS4A
Add
BLAST
Regioni151 – 22070Intramolecular interaction with N-terminus
Add
BLAST
Regioni168 – 1692Important for autoinhibitory function
Regioni203 – 2075Interaction with STAMBP
Regioni221 – 2222Interaction with STAMBP

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili22 – 5433 Reviewed prediction
Add
BLAST
Coiled coili141 – 22282 Reviewed prediction
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi201 – 21111MIT-interacting motif
Add
BLAST

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.

Sequence similaritiesi

Belongs to the SNF7 family.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5491.
HOGENOMiHOG000177219.
HOVERGENiHBG107031.
KOiK12193.
OMAiMLDETMD.
OrthoDBiEOG7D59Q2.
PhylomeDBiQ9Y3E7.
TreeFamiTF105848.

Family and domain databases

InterProiIPR005024. Snf7.
[Graphical view]
PfamiPF03357. Snf7. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y3E7-1) [UniParc]FASTAAdd to Basket

Also known as: Vps24alpha

This isoform has been chosen as the 'canonical' 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

MGLFGKTQEK PPKELVNEWS LKIRKEMRVV DRQIRDIQRE EEKVKRSVKD    50
AAKKGQKDVC IVLAKEMIRS RKAVSKLYAS KAHMNSVLMG MKNQLAVLRV 100
AGSLQKSTEV MKAMQSLVKI PEIQATMREL SKEMMKAGII EEMLEDTFES 150
MDDQEEMEEE AEMEIDRILF EITAGALGKA PSKVTDALPE PEPPGAMAAS 200
EDEEEEEEAL EAMQSRLATL RS 222
Length:222
Mass (Da):25,073
Last modified:January 23, 2007 - v3
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

Note: No experimental confirmation available.

Show »
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.

Note: No experimental confirmation available.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6666Missing in isoform 2.
VSP_041076Add
BLAST
Alternative sequencei1 – 1515MGLFG…PPKEL → MEGELYSALKEEEASESVSS TNFSGEMHFYELVEDTKDGI WLVQ in isoform 3.
VSP_042124Add
BLAST
Alternative sequencei74 – 11340Missing in isoform 4.
VSP_042125Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti208 – 2081E → D in AAF26737. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
UniGeneiHs.591582.

Genome annotation databases

EnsembliENST00000263856; ENSP00000263856; ENSG00000115561. [Q9Y3E7-1]
ENST00000409225; ENSP00000386590; ENSG00000115561. [Q9Y3E7-2]
ENST00000409727; ENSP00000387045; ENSG00000115561. [Q9Y3E7-4]
ENST00000439940; ENSP00000405575; ENSG00000115561. [Q9Y3E7-3]
GeneIDi100526767.
51652.
KEGGihsa:100526767.
hsa:51652.
UCSCiuc002srj.3. human. [Q9Y3E7-1]
uc002srl.3. human. [Q9Y3E7-4]
uc010ytl.2. human. [Q9Y3E7-3]

Polymorphism databases

DMDMi73917763.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS33236.1. [Q9Y3E7-1 ]
CCDS42707.1. [Q9Y3E7-2 ]
CCDS54375.1. [Q9Y3E7-4 ]
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 ]
UniGenei Hs.591582.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2GD5 X-ray 2.80 A/B/C/D 9-183 [» ]
2XZE X-ray 1.75 Q/R 183-222 [» ]
3FRT X-ray 4.00 A/B 8-222 [» ]
3FRV X-ray 3.70 A 1-150 [» ]
ProteinModelPortali Q9Y3E7.
SMRi Q9Y3E7. Positions 5-181.
ModBasei Search...

Protein-protein interaction databases

BioGridi 119660. 19 interactions.
DIPi DIP-48532N.
IntActi Q9Y3E7. 9 interactions.
MINTi MINT-1185988.
STRINGi 9606.ENSP00000263856.

PTM databases

PhosphoSitei Q9Y3E7.

Polymorphism databases

DMDMi 73917763.

Proteomic databases

MaxQBi Q9Y3E7.
PaxDbi Q9Y3E7.
PRIDEi Q9Y3E7.

Protocols and materials databases

DNASUi 51652.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263856 ; ENSP00000263856 ; ENSG00000115561 . [Q9Y3E7-1 ]
ENST00000409225 ; ENSP00000386590 ; ENSG00000115561 . [Q9Y3E7-2 ]
ENST00000409727 ; ENSP00000387045 ; ENSG00000115561 . [Q9Y3E7-4 ]
ENST00000439940 ; ENSP00000405575 ; ENSG00000115561 . [Q9Y3E7-3 ]
GeneIDi 100526767.
51652.
KEGGi hsa:100526767.
hsa:51652.
UCSCi uc002srj.3. human. [Q9Y3E7-1 ]
uc002srl.3. human. [Q9Y3E7-4 ]
uc010ytl.2. human. [Q9Y3E7-3 ]

Organism-specific databases

CTDi 100526767.
51652.
GeneCardsi GC02M086730.
HGNCi HGNC:29865. CHMP3.
HPAi HPA015673.
MIMi 610052. gene.
neXtProti NX_Q9Y3E7.
PharmGKBi PA134920495.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5491.
HOGENOMi HOG000177219.
HOVERGENi HBG107031.
KOi K12193.
OMAi MLDETMD.
OrthoDBi EOG7D59Q2.
PhylomeDBi Q9Y3E7.
TreeFami TF105848.

Enzyme and pathway databases

Reactomei REACT_27258. Endosomal Sorting Complex Required For Transport (ESCRT).
REACT_6359. Budding and maturation of HIV virion.
SignaLinki Q9Y3E7.

Miscellaneous databases

ChiTaRSi CHMP3. human.
EvolutionaryTracei Q9Y3E7.
GeneWikii VPS24.
NextBioi 55614.
PROi Q9Y3E7.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y3E7.
CleanExi HS_VPS24.
Genevestigatori Q9Y3E7.

Family and domain databases

InterProi IPR005024. Snf7.
[Graphical view ]
Pfami PF03357. Snf7. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Interaction of IGF-binding protein-related protein 1 with a novel protein, neuroendocrine differentiation factor, results in neuroendocrine differentiation of prostate cancer cells."
    Wilson E.M., Oh Y., Hwa V., Rosenfeld R.G.
    J. Clin. Endocrinol. Metab. 86:4504-4511(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), POSSIBLE INTERACTION WITH IGFBP7.
  2. "mVps24p functions in EGF receptor sorting/trafficking from the early endosome."
    Yan Q., Hunt P.R., Frelin L., Vida T.A., Pevsner J., Bean A.J.
    Exp. Cell Res. 304:265-273(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
    Tissue: Heart.
  3. "NovelFam3000 -- uncharacterized human protein domains conserved across model organisms."
    Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P., Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.
    BMC Genomics 7:48-48(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Characterization of a novel alternatively spliced human transcript encoding an N-terminally truncated Vps24 protein that suppresses the effects of Bax in an ESCRT independent manner in yeast."
    Khoury C.M., Yang Z., Ismail S., Greenwood M.T.
    Gene 391:233-241(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION.
    Tissue: Heart.
  5. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
    Tissue: Amygdala, Pericardium and Synovial cell.
  7. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Uterus.
  10. Cited for: FUNCTION IN HIV-1 BUDDING, INTERACTION WITH CHMP4A.
  11. "Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins."
    Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
    Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHMP2A AND VPS4A.
  12. Erratum
    Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
    Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003)
  13. "Interaction of the mammalian endosomal sorting complex required for transport (ESCRT) III protein hSnf7-1 with itself, membranes, and the AAA+ ATPase SKD1."
    Lin Y., Kimpler L.A., Naismith T.V., Lauer J.M., Hanson P.I.
    J. Biol. Chem. 280:12799-12809(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  14. "A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex."
    Tsang H.T.H., Connell J.W., Brown S.E., Thompson A., Reid E., Sanderson C.M.
    Genomics 88:333-346(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH STAMBP.
  15. "Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding."
    Zamborlini A., Usami Y., Radoshitzky S.R., Popova E., Palu G., Goettlinger H.
    Proc. Natl. Acad. Sci. U.S.A. 103:19140-19145(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOINHIBITORY MECHANISM, INTRAMOLECULAR INTERACTION, INTERACTION WITH STAMBP AND VPS4A, MUTAGENESIS OF 216-ARG-LEU-217; 221-ARG-SER-222 AND SER-222.
  16. "Targeting of AMSH to endosomes is required for epidermal growth factor receptor degradation."
    Ma Y.M., Boucrot E., Villen J., Affar el B., Gygi S.P., Goettlinger H.G., Kirchhausen T.
    J. Biol. Chem. 282:9805-9812(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STAMBP, IDENTIFICATION BY MASS SPECTROMETRY.
  17. "Structure/function analysis of four core ESCRT-III proteins reveals common regulatory role for extreme C-terminal domain."
    Shim S., Kimpler L.A., Hanson P.I.
    Traffic 8:1068-1079(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOINHIBITORY MECHANISM, INTERACTION WITH CHMP4A, MUTAGENESIS OF 179-LYS--SER-222.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: POLYMERIZATION WITH CHMP2A, ELECTRON MICROSCOPY.
  20. "A dominant-negative ESCRT-III protein perturbs cytokinesis and trafficking to lysosomes."
    Dukes J.D., Richardson J.D., Simmons R., Whitley P.
    Biochem. J. 411:233-239(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CYTOKINESIS, SUBCELLULAR LOCATION.
  21. Cited for: AUTOINHIBITORY MECHANISM, INTERACTION WITH STAMBP.
  22. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  23. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Mechanism of inhibition of retrovirus release from cells by interferon-induced gene ISG15."
    Kuang Z., Seo E.J., Leis J.
    J. Virol. 85:7153-7161(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VTA1 AND VPS4A.
  26. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 5-183, SUBUNIT, FUNCTION IN HIV-1 BUDDING, MUTAGENESIS OF 24-ARG-LYS-25; ARG-28; LYS-54; GLN-56; VAL-59; 62-VAL-LEU-63 AND 78-TYR-ALA-79.
  28. Cited for: X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) OF 1-222, INTERACTION WITH CHMP2A, MUTAGENESIS OF VAL-48; VAL-59; VAL-62; ALA-64 AND 168-ILE-LEU-169.
  29. Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 183-222 IN COMPLEX WITH STAMBP FRAGMENT.

Entry informationi

Entry nameiCHMP3_HUMAN
AccessioniPrimary (citable) accession number: Q9Y3E7
Secondary accession number(s): A8K3W0
, B4DG34, B8ZZM0, B8ZZX5, Q3ZTS9, Q53S71, Q53SU5, Q9NZ51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 116 of the entry and version 3 of the sequence. [Complete history]
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.

Miscellaneousi

Miscellaneous

Its overexpression strongly inhibits HIV-1 release.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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