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Q9Y3E7 (CHMP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CHMP3
Synonyms:CGI149, NEDF, VPS24
ORF Names:CGI-149
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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. 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. Ref.2 Ref.4 Ref.10 Ref.20 Ref.27

Subunit structure

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. Ref.1 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.21 Ref.25 Ref.27 Ref.28

Subcellular location

Cytoplasmcytosol. Membrane; Lipid-anchor. Endosome. Late endosome membrane Probable. Note: Localizes to the midbody of dividing cells. Ref.2 Ref.14 Ref.20

Tissue specificity

Widely expressed. Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Ref.13

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.

Sequence similarities

Belongs to the SNF7 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

STAMBPO956305EBI-2118119,EBI-396676

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y3E7-1)

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.
Isoform 2 (identifier: Q9Y3E7-2)

Also known as: Vps24beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: Missing.
Isoform 3 (identifier: Q9Y3E7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MGLFGKTQEKPPKEL → MEGELYSALKEEEASESVSSTNFSGEMHFYELVEDTKDGIWLVQ
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9Y3E7-4)

The sequence of this isoform differs from the canonical sequence as follows:
     74-113: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Potential
Chain2 – 222221Charged multivesicular body protein 3
PRO_0000211479

Regions

Region2 – 113112Intramolecular interaction with C-terminus
Region59 – 646Important for autoinhibitory function
Region151 – 22272Interaction with VPS4A
Region151 – 22070Intramolecular interaction with N-terminus
Region168 – 1692Important for autoinhibitory function
Region203 – 2075Interaction with STAMBP
Region221 – 2222Interaction with STAMBP
Coiled coil22 – 5433 Potential
Coiled coil141 – 22282 Potential
Motif201 – 21111MIT-interacting motif

Sites

Binding site2161STAMBP
Site481Important for autoinhibitory function

Amino acid modifications

Modified residue2001Phosphoserine Ref.18 Ref.22 Ref.23 Ref.26
Lipidation21N-myristoyl glycine Potential
Cross-link179Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Natural variations

Alternative sequence1 – 6666Missing in isoform 2.
VSP_041076
Alternative sequence1 – 1515MGLFG…PPKEL → MEGELYSALKEEEASESVSS TNFSGEMHFYELVEDTKDGI WLVQ in isoform 3.
VSP_042124
Alternative sequence74 – 11340Missing in isoform 4.
VSP_042125

Experimental info

Mutagenesis24 – 252RK → SA: Impairs HIV-1 release; when associated with S-28.
Mutagenesis281R → S: Impairs HIV-1 release; when associated with 24-S-A-25. Ref.27
Mutagenesis481V → 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. Ref.28
Mutagenesis541K → S: Abolishes dimerization; when associated with N-56; E-59 and 62-D-E-63. Ref.27
Mutagenesis561Q → N: Abolishes dimerization; when associated with S-54; E-59 and 62-D-E-63. Ref.27
Mutagenesis591V → D: Abolishes interaction with CHMP2A and assembly into helical tubes in vitro; when associated with D-62; D-168 and D-169. Ref.27 Ref.28
Mutagenesis591V → E: Abolishes dimerization; when associated with S-54; N-56 and 62-D-E-63. Ref.27 Ref.28
Mutagenesis62 – 632VL → DE: Abolishes dimerization; when associated with S-54; N-56 and E-59. Ref.28
Mutagenesis621V → D: Abolishes interaction with CHMP2A and assembly into helical tubes in vitro; when associated with D-59; D-168 and D-169. Ref.28
Mutagenesis641A → D: Induces assembly with CHMP2A into helical tubes in vitro; when associated with D-48. Ref.28
Mutagenesis78 – 792YA → AE: Abolishes dimerization.
Mutagenesis168 – 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.
Mutagenesis179 – 22244Missing: Membrane association; releases autoinhibition. Ref.15 Ref.17
Mutagenesis216 – 2172RL → AA: Abolishes interaction with VPS4A and STAMBP.
Mutagenesis221 – 2222Missing: Abolishes interaction with VPS4A and STAMBP. Ref.15
Mutagenesis2221Missing: Impairs interaction with VPS4A and STAMBP. Ref.15
Sequence conflict2081E → D in AAF26737. Ref.1

Secondary structure

................ 222
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Vps24alpha) [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 7B1ACE5EA453E8C0

FASTA22225,073
        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 

« Hide

Isoform 2 (Vps24beta) [UniParc].

Checksum: 7B10B4D1FB7E1B62
Show »

FASTA15617,326
Isoform 3 [UniParc].

Checksum: 0BA3A646BBC05B51
Show »

FASTA25128,386
Isoform 4 [UniParc].

Checksum: E2951422F9E1A226
Show »

FASTA18220,770

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"The protein network of HIV budding."
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.
Cell 114:701-713(2003) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Helical structures of ESCRT-III are disassembled by VPS4."
Lata S., Schoehn G., Jain A., Pires R., Piehler J., Goettlinger H.G., Weissenhorn W.
Science 321:1354-1357(2008) [PubMed] [Europe PMC] [Abstract]
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]"Structural basis for autoinhibition of ESCRT-III CHMP3."
Lata S., Roessle M., Solomons J., Jamin M., Goettlinger H.G., Svergun D.I., Weissenhorn W.
J. Mol. Biol. 378:818-827(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Structural basis for budding by the ESCRT-III factor CHMP3."
Muziol T., Pineda-Molina E., Ravelli R.B., Zamborlini A., Usami Y., Goettlinger H., Weissenhorn W.
Dev. Cell 10:821-830(2006) [PubMed] [Europe PMC] [Abstract]
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]"Structural basis for ESCRT-III protein autoinhibition."
Bajorek M., Schubert H.L., McCullough J., Langelier C., Eckert D.M., Stubblefield W.M., Uter N.T., Myszka D.G., Hill C.P., Sundquist W.I.
Nat. Struct. Mol. Biol. 16:754-762(2009) [PubMed] [Europe PMC] [Abstract]
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]"Structural basis for Escrt-III Chmp3 recruitment of Amsh."
Solomons J., Sabin C., Poudevigne E., Usami Y., Hulsik D.L., Macheboeuf P., Hartlieb B., Gottlinger H., Weissenhorn W.
Structure 19:1149-1159(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 183-222 IN COMPLEX WITH STAMBP FRAGMENT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS33236.1. [Q9Y3E7-1]
CCDS42707.1. [Q9Y3E7-2]
CCDS54375.1. [Q9Y3E7-4]
RefSeqNP_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]
UniGeneHs.591582.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GD5X-ray2.80A/B/C/D9-183[»]
2XZEX-ray1.75Q/R183-222[»]
3FRTX-ray4.00A/B8-222[»]
3FRVX-ray3.70A1-150[»]
ProteinModelPortalQ9Y3E7.
SMRQ9Y3E7. Positions 5-181.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119660. 19 interactions.
DIPDIP-48532N.
IntActQ9Y3E7. 9 interactions.
MINTMINT-1185988.
STRING9606.ENSP00000263856.

PTM databases

PhosphoSiteQ9Y3E7.

Polymorphism databases

DMDM73917763.

Proteomic databases

MaxQBQ9Y3E7.
PaxDbQ9Y3E7.
PRIDEQ9Y3E7.

Protocols and materials databases

DNASU51652.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263856; ENSP00000263856; ENSG00000115561. [Q9Y3E7-1]
ENST00000409225; ENSP00000386590; ENSG00000115561. [Q9Y3E7-2]
ENST00000409727; ENSP00000387045; ENSG00000115561. [Q9Y3E7-4]
ENST00000439940; ENSP00000405575; ENSG00000115561. [Q9Y3E7-3]
GeneID100526767.
51652.
KEGGhsa:100526767.
hsa:51652.
UCSCuc002srj.3. human. [Q9Y3E7-1]
uc002srl.3. human. [Q9Y3E7-4]
uc010ytl.2. human. [Q9Y3E7-3]

Organism-specific databases

CTD100526767.
51652.
GeneCardsGC02M086730.
HGNCHGNC:29865. CHMP3.
HPAHPA015673.
MIM610052. gene.
neXtProtNX_Q9Y3E7.
PharmGKBPA134920495.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5491.
HOGENOMHOG000177219.
HOVERGENHBG107031.
KOK12193.
OMAMLDETMD.
OrthoDBEOG7D59Q2.
PhylomeDBQ9Y3E7.
TreeFamTF105848.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
REACT_116125. Disease.
SignaLinkQ9Y3E7.

Gene expression databases

BgeeQ9Y3E7.
CleanExHS_VPS24.
GenevestigatorQ9Y3E7.

Family and domain databases

InterProIPR005024. Snf7.
[Graphical view]
PfamPF03357. Snf7. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCHMP3. human.
EvolutionaryTraceQ9Y3E7.
GeneWikiVPS24.
NextBio55614.
PROQ9Y3E7.
SOURCESearch...

Entry information

Entry nameCHMP3_HUMAN
AccessionPrimary (citable) accession number: Q9Y3E7
Secondary accession number(s): A8K3W0 expand/collapse secondary AC list , B4DG34, B8ZZM0, B8ZZX5, Q3ZTS9, Q53S71, Q53SU5, Q9NZ51
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 115 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM