[1]	NUCLEOTIDE SEQUENCE [MRNA], AND POSSIBLE INTERACTION WITH IGFBP7. DOI=10.1210/jc.86.9.4504; PubMed=11549700 [NCBI, ExPASy, EBI, Israel, Japan] Wilson E.M., Oh Y., Hwa V., Rosenfeld R.G.; "Interaction of IGF-binding protein-related protein 1 with a novel protein, neuroendocrine differentiation factor, results in neuroendocrine differentiation of prostate cancer cells."; J. Clin. Endocrinol. Metab. 86:4504-4511(2001).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1101/gr.10.5.703; PubMed=10810093 [NCBI, ExPASy, EBI, Israel, Japan] Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."; Genome Res. 10:703-713(2000).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."; Nature 434:724-731(2005).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Uterus; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	FUNCTION IN HIV-1 BUDDING, AND INTERACTION WITH CHMP4A. DOI=10.1016/S0092-8674(03)00714-1; PubMed=14505570 [NCBI, ExPASy, EBI, Israel, Japan] von Schwedler U.K., Stuchell M., Mueller B., Ward D.M., Chung H.-Y., Morita E., Wang H.E., Davis T., He G.P., Cimbora D.M., Scott A., Kraeusslich H.-G., Kaplan J., Morham S.G., Sundquist W.I.; "The protein network of HIV budding."; Cell 114:701-713(2003).
[6]	INTERACTION WITH CHMP2A AND VPS4A. DOI=10.1073/pnas.2133846100; PubMed=14519844 [NCBI, ExPASy, EBI, Israel, Japan] Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.; "Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins."; Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003).
[7]	ERRATUM. Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.; Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003).
[8]	FUNCTION, AND SUBCELLULAR LOCATION. DOI=10.1016/j.yexcr.2004.11.003; PubMed=15707591 [NCBI, ExPASy, EBI, Israel, Japan] Yan Q., Hunt P.R., Frelin L., Vida T.A., Pevsner J., Bean A.J.; "mVps24p functions in EGF receptor sorting/trafficking from the early endosome."; Exp. Cell Res. 304:265-273(2005).
[9]	TISSUE SPECIFICITY. DOI=10.1074/jbc.M413968200; PubMed=15632132 [NCBI, ExPASy, EBI, Israel, Japan] Lin Y., Kimpler L.A., Naismith T.V., Lauer J.M., Hanson P.I.; "Interaction of the mammalian endosomal sorting complex required for transport (ESCRT) III protein hSnf7-1 with itself, membranes, and the AAA+ ATPase SKD1."; J. Biol. Chem. 280:12799-12809(2005).
[10]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[11]	SUBCELLULAR LOCATION, AND INTERACTION WITH STAMBP. DOI=10.1016/j.ygeno.2006.04.003; PubMed=16730941 [NCBI, ExPASy, EBI, Israel, Japan] Tsang H.T.H., Connell J.W., Brown S.E., Thompson A., Reid E., Sanderson C.M.; "A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex."; Genomics 88:333-346(2006).
[12]	AUTOINHIBITORY MECHANISM, INTRAMOLECULAR INTERACTION, INTERACTION WITH STAMBP AND VPS4A, AND MUTAGENESIS OF 221-ARG-SER-222. DOI=10.1073/pnas.0603788103; PubMed=17146056 [NCBI, ExPASy, EBI, Israel, Japan] Zamborlini A., Usami Y., Radoshitzky S.R., Popova E., Palu G., Goettlinger H.; "Release of autoinhibition converts ESCRT-III components into potent inhibitors of HIV-1 budding."; Proc. Natl. Acad. Sci. U.S.A. 103:19140-19145(2006).
[13]	AUTOINHIBITORY MECHANSIM, INTERACTION WITH CHMP4A, AND MUTAGENESIS OF 179-LYS--SER-222. DOI=10.1111/j.1600-0854.2007.00584.x; PubMed=17547705 [NCBI, ExPASy, EBI, Israel, Japan] Shim S., Kimpler L.A., Hanson P.I.; "Structure/function analysis of four core ESCRT-III proteins reveals common regulatory role for extreme C-terminal domain."; Traffic 8:1068-1079(2007).
[14]	UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-179, AND MASS SPECTROMETRY. DOI=10.1021/pr800468j; PubMed=18781797 [NCBI, ExPASy, EBI, Israel, Japan] Meierhofer D., Wang X., Huang L., Kaiser P.; "Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry."; J. Proteome Res. 7:4566-4576(2008).
[15]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.; "A quantitative atlas of mitotic phosphorylation."; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]	POLYMERIZATION WITH CHMP2A, AND ELECTRON MICROSCOPY. DOI=10.1126/science.1161070; PubMed=18687924 [NCBI, ExPASy, EBI, Israel, Japan] Lata S., Schoehn G., Jain A., Pires R., Piehler J., Goettlinger H.G., Weissenhorn W.; "Helical structures of ESCRT-III are disassembled by VPS4."; Science 321:1354-1357(2008).
[17]	INTERACTION WITH STAMBP, AND MASS SPECTROMETRY. DOI=10.1074/jbc.M611635200; PubMed=17261583 [NCBI, ExPASy, EBI, Israel, Japan] Ma Y.M., Boucrot E., Villen J., Affar el B., Gygi S.P., Goettlinger H.G., Kirchhausen T.; "Targeting of AMSH to endosomes is required for epidermal growth factor receptor degradation."; J. Biol. Chem. 282:9805-9812(2007).
[18]	FUNCTION IN CYTOKINESIS, AND SUBCELLULAR LOCATION. DOI=10.1042/BJ20071296; PubMed=18076377 [NCBI, ExPASy, EBI, Israel, Japan] Dukes J.D., Richardson J.D., Simmons R., Whitley P.; "A dominant-negative ESCRT-III protein perturbs cytokinesis and trafficking to lysosomes."; Biochem. J. 411:233-239(2008).
[19]	AUTOINHIBITORY MECHANSIM, AND INTERACTION WITH STAMBP. DOI=10.1016/j.jmb.2008.03.030; PubMed=18395747 [NCBI, ExPASy, EBI, Israel, Japan] Lata S., Roessle M., Solomons J., Jamin M., Goettlinger H.G., Svergun D.I., Weissenhorn W.; "Structural basis for autoinhibition of ESCRT-III CHMP3."; J. Mol. Biol. 378:818-827(2008).
[20]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[21]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 5-183, SUBUNIT, FUNCTION IN HIV-1 BUDDING, AND MUTAGENESIS OF 24-ARG-LYS-25; ARG-28; LYS-54; GLN-56; VAL-59; 62-VAL-LEU-63 AND 78-TYR-ALA-79. DOI=10.1016/j.devcel.2006.03.013; PubMed=16740483 [NCBI, ExPASy, EBI, Israel, Japan] Muziol T., Pineda-Molina E., Ravelli R.B., Zamborlini A., Usami Y., Goettlinger H., Weissenhorn W.; "Structural basis for budding by the ESCRT-III factor CHMP3."; Dev. Cell 10:821-830(2006).

Comments

FUNCTION: 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. Required for sorting/trafficking of EGF receptor (By similarity).
SUBUNIT: 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.
INTERACTION:
O95630:STAMBP; NbExp=2; IntAct=EBI-2118119, EBI-396676;
SUBCELLULAR LOCATION: Cytoplasm, cytosol. Membrane; Lipid-anchor. Endosome. Late endosome membrane (Probable). Note=Localizes to the midbody of dividing cells.
TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.
DOMAIN: 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.
MISCELLANEOUS: Its overexpression strongly inhibits HIV-1 release.
SIMILARITY: Belongs to the SNF7 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF219226; AAF26737.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF151907; AAD34144.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC015971; AAX93078.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC068288; AAY24211.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004419; AAH04419.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00100673; -.

RefSeq

NP_001005753.1; -.
NP_057163.1; -.

UniGene

Hs.591582

3D structure databases

PDB

2GD5; X-ray; 2.80 A; A/B/C/D=9-183.

[ExPASy / RCSB / EBI]

PDBsum

2GD5; -.

SMR

Q9Y3E7; 4-159, 5-160.

ModBase

Q9Y3E7.

Protein-protein interaction databases

IntAct

Q9Y3E7; 1.

PTM databases

PhosphoSite

Q9Y3E7; -.

Organism-specific databases

GC02M086642; -.

HIX0002239; -.

HGNC:29865; VPS24.

HPA015673; -.

610052; gene. [NCBI / EBI]

PharmGKB

PA134920495; -.

Gene expression databases

Q9Y3E7; -.

Q9Y3E7; -.

HS_VPS24; -.

ENSG00000115561; Homo sapiens.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from electronic annotation from UniProtKB-SubCell).
GO:0031902;	Cellular component: late endosome membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0007049;	Biological process: cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0051301;	Biological process: cell division (inferred from electronic annotation from UniProtKB-KW).
GO:0015031;	Biological process: protein transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR005024; Snf7.
Graphical view of domain structure.

Pfam

PF03357; Snf7; 1.
Pfam graphical view of domain structure.

Proteomic databases

PRIDE

Q9Y3E7; -.

Genome annotation databases

Ensembl

ENSG00000115561; Homo sapiens. [Contig view]

GeneID

51652; -.

KEGG

hsa:51652; -.

Phylogenomic databases

HOGENOM

Q9Y3E7; -.

HOVERGEN

Q9Y3E7; -.

OMA

Q9Y3E7; CVILAKE.

Other

55614; -.

VPS24; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cell cycle; Cell division; Coiled coil; Cytoplasm; Endosome; Isopeptide bond; Lipoprotein; Membrane; Myristate; Phosphoprotein; Protein transport; Transport; Ubl conjugation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (Potential).`
`CHAIN`	`2 222`	`221`	`Charged multivesicular body protein 3.`	`PRO_0000211479`
`REGION`	`2 113`	`112`	`Intramolecular interaction with C-terminus.`
`REGION`	`151 222`	`72`	`Interaction with VPS4A.`
`REGION`	`151 220`	`70`	`Intramolecular interaction with N-terminus.`
`REGION`	`196 222`	`27`	`Interaction with STAMBP.`
`COILED`	`22 54`	`33`	`Potential.`
`COILED`	`141 222`	`82`	`Potential.`
`MOTIF`	`201 211`	`11`	`MIT-interacting motif.`
`MOD_RES`	`116 116`		`Phosphoserine (By similarity).`
`MOD_RES`	`126 126`		`Phosphothreonine (By similarity).`
`MOD_RES`	`200 200`		`Phosphoserine.`
`LIPID`	`2 2`		`N-myristoyl glycine (Potential).`
`CROSSLNK`	`179 179`		`Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin).`
`MUTAGEN`	`24 25`		`RK->SA: Impairs HIV-1 release; when associated with S-28.`
`MUTAGEN`	`28 28`		`R->S: Impairs HIV-1 relase; when associated with 24-S-A-25.`
`MUTAGEN`	`54 54`		`K->S: Abolishes dimerization; when associated with N-56, E-59 and 62-D-E-63.`
`MUTAGEN`	`56 56`		`Q->N: Abolishes dimerization; when associated with S-54, E-59 and 62-D-E-63.`
`MUTAGEN`	`59 59`		`V->E: Abolishes dimerization; when associated with S-54, N-56 and 62-D-E-63.`
`MUTAGEN`	`62 63`		`VL->DE: Abolishes dimerization; when associated with S-54, N-56 and E-59.`
`MUTAGEN`	`78 79`		`YA->AE: Abolishes dimerization.`
`MUTAGEN`	`179 222`		`Missing: Membrane association; releases autoinhibition.`
`MUTAGEN`	`221 222`		`RS->AA: Abolishes interaction with VPS4A and STAMBP.`
`MUTAGEN`	`221 222`		`Missing: Abolishes interaction with VPS4A and STAMBP.`
`CONFLICT`	`208 208`		`E -> D (in Ref. 1; AAF26737).`
`HELIX`	`15 53`	`39`
`HELIX`	`57 100`	`44`
`HELIX`	`109 112`	`4`
`TURN`	`113 115`	`3`
`STRAND`	`120 122`	`3`
`HELIX`	`125 137`	`13`
`HELIX`	`164 167`	`4`

Sequence information

Length: 222 AA [This is the length of the unprocessed precursor]

Molecular weight: 25073 Da [This is the MW of the unprocessed precursor]

CRC64: 7B1ACE5EA453E8C0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGLFGKTQEK PPKELVNEWS LKIRKEMRVV DRQIRDIQRE EEKVKRSVKD AAKKGQKDVC 

        70         80         90        100        110        120 
IVLAKEMIRS RKAVSKLYAS KAHMNSVLMG MKNQLAVLRV AGSLQKSTEV MKAMQSLVKI 

       130        140        150        160        170        180 
PEIQATMREL SKEMMKAGII EEMLEDTFES MDDQEEMEEE AEMEIDRILF EITAGALGKA 

       190        200        210        220 
PSKVTDALPE PEPPGAMAAS EDEEEEEEAL EAMQSRLATL RS

Q9Y3E7 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools