Full text data of CHMP4A
CHMP4A
(C14orf123, SHAX2)
[Confidence: low (only semi-automatic identification from reviews)]
Charged multivesicular body protein 4a (Chromatin-modifying protein 4a; CHMP4a; SNF7 homolog associated with Alix-2; SNF7-1; hSnf-1; Vacuolar protein sorting-associated protein 32-1; Vps32-1; hVps32-1)
Charged multivesicular body protein 4a (Chromatin-modifying protein 4a; CHMP4a; SNF7 homolog associated with Alix-2; SNF7-1; hSnf-1; Vacuolar protein sorting-associated protein 32-1; Vps32-1; hVps32-1)
UniProt
Q9BY43
ID CHM4A_HUMAN Reviewed; 222 AA.
AC Q9BY43; Q32Q79; Q86SZ8; Q96QJ9; Q9P026;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-FEB-2006, sequence version 3.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Charged multivesicular body protein 4a;
DE AltName: Full=Chromatin-modifying protein 4a;
DE Short=CHMP4a;
DE AltName: Full=SNF7 homolog associated with Alix-2;
DE AltName: Full=SNF7-1;
DE Short=hSnf-1;
DE AltName: Full=Vacuolar protein sorting-associated protein 32-1;
DE Short=Vps32-1;
DE Short=hVps32-1;
GN Name=CHMP4A; Synonyms=C14orf123, SHAX2; ORFNames=CDA04, HSPC134;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH PDCD6IP.
RC TISSUE=Cervix;
RX PubMed=12860994; DOI=10.1074/jbc.M301604200;
RA Katoh K., Shibata H., Suzuki H., Narai A., Ishidoh K., Kominami E.,
RA Yoshimori T., Maki M.;
RT "The ALG-2-interacting protein Alix associates with CHMP4b, a human
RT homologue of yeast Snf7 that is involved in multivesicular body
RT sorting.";
RL J. Biol. Chem. 278:39104-39113(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-153, FUNCTION, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH PDCD6IP.
RC TISSUE=Squamous cell carcinoma;
RX PubMed=14583093; DOI=10.1042/BJ20031347;
RA Peck J.W., Bowden E.T., Burbelo P.D.;
RT "Structure and function of human Vps20 and Snf7 proteins.";
RL Biochem. J. 377:693-700(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pheochromocytoma;
RA Li Y., Huang Q., Peng Y., Song H., Yu Y., Xu S., Ren S., Chen Z.,
RA Han Z.;
RT "A novel gene expressed in human pheochromocytoma.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-153.
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION IN HIV-1 BUDDING, AND INTERACTION WITH PDCD6IP.
RX PubMed=14505569; DOI=10.1016/S0092-8674(03)00653-6;
RA Strack B., Calistri A., Craig S., Popova E., Goettlinger H.G.;
RT "AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning
RT in virus budding.";
RL Cell 114:689-699(2003).
RN [9]
RP INTERACTION WITH CHMP4C; VPS4A AND PDCD6IP.
RX PubMed=14505570; DOI=10.1016/S0092-8674(03)00714-1;
RA von Schwedler U.K., Stuchell M., Mueller B., Ward D.M., Chung H.-Y.,
RA Morita E., Wang H.E., Davis T., He G.P., Cimbora D.M., Scott A.,
RA Kraeusslich H.-G., Kaplan J., Morham S.G., Sundquist W.I.;
RT "The protein network of HIV budding.";
RL Cell 114:701-713(2003).
RN [10]
RP FUNCTION IN HIV-1 BUDDING; SELF-ASSOCIATION, AND INTERACTION WITH
RP CHMP2A; CHMP4B; CHMP4C; CHMP6 AND PDCD6IP.
RX PubMed=14519844; DOI=10.1073/pnas.2133846100;
RA Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
RT "Divergent retroviral late-budding domains recruit vacuolar protein
RT sorting factors by using alternative adaptor proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003).
RN [11]
RP ERRATUM.
RA Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
RL Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003).
RN [12]
RP TISSUE SPECIFICITY, AND INTERACTION WITH PDCD6IP.
RX PubMed=14678797; DOI=10.1016/j.abb.2003.09.038;
RA Katoh K., Shibata H., Hatta K., Maki M.;
RT "CHMP4b is a major binding partner of the ALG-2-interacting protein
RT Alix among the three CHMP4 isoforms.";
RL Arch. Biochem. Biophys. 421:159-165(2004).
RN [13]
RP SUBCELLULAR LOCATION, AND LIPID-BINDING.
RX PubMed=15632132; DOI=10.1074/jbc.M413968200;
RA Lin Y., Kimpler L.A., Naismith T.V., Lauer J.M., Hanson P.I.;
RT "Interaction of the mammalian endosomal sorting complex required for
RT transport (ESCRT) III protein hSnf7-1 with itself, membranes, and the
RT AAA+ ATPase SKD1.";
RL J. Biol. Chem. 280:12799-12809(2005).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=17853893; DOI=10.1038/sj.emboj.7601850;
RA Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P.,
RA Rodesch C.K., Sundquist W.I.;
RT "Human ESCRT and ALIX proteins interact with proteins of the midbody
RT and function in cytokinesis.";
RL EMBO J. 26:4215-4227(2007).
RN [15]
RP AUTOINHIBITORY MECHANISM, INTERACTION WITH CHMP3, AND MUTAGENESIS OF
RP 182-ASP--SER-222.
RX PubMed=17547705; DOI=10.1111/j.1600-0854.2007.00584.x;
RA Shim S., Kimpler L.A., Hanson P.I.;
RT "Structure/function analysis of four core ESCRT-III proteins reveals
RT common regulatory role for extreme C-terminal domain.";
RL Traffic 8:1068-1079(2007).
RN [16]
RP FUNCTION, SELF-ASSOCIATION, AND STRUCTURE BY ELECTRON CRYOMICROSCOPY.
RX PubMed=18209100; DOI=10.1083/jcb.200707031;
RA Hanson P.I., Roth R., Lin Y., Heuser J.E.;
RT "Plasma membrane deformation by circular arrays of ESCRT-III protein
RT filaments.";
RL J. Cell Biol. 180:389-402(2008).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 210-222 IN COMPLEX WITH
RP PDCD6IP, AND MUTAGENESIS OF GLU-209; LEU-214; LEU-217 AND TRP-220.
RX PubMed=18511562; DOI=10.1073/pnas.0801567105;
RA McCullough J., Fisher R.D., Whitby F.G., Sundquist W.I., Hill C.P.;
RT "ALIX-CHMP4 interactions in the human ESCRT pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7687-7691(2008).
CC -!- FUNCTION: Probable core component of the endosomal sorting
CC required for transport complex III (ESCRT-III) which is involved
CC in multivesicular bodies (MVBs) formation and sorting of endosomal
CC cargo proteins into MVBs. MVBs contain intraluminal vesicles
CC (ILVs) that are generated by invagination and scission from the
CC limiting membrane of the endosome and mostly are delivered to
CC lysosomes enabling degradation of membrane proteins, such as
CC stimulated growth factor receptors, lysosomal enzymes and lipids.
CC The MVB pathway appears to require the sequential function of
CC ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly
CC dissociate from the invaginating membrane before the ILV is
CC released. The ESCRT machinery also functions in topologically
CC equivalent membrane fission events, such as the terminal stages of
CC cytokinesis and the budding of enveloped viruses (HIV-1 and other
CC lentiviruses). ESCRT-III proteins are believed to mediate the
CC necessary vesicle extrusion and/or membrane fission activities,
CC possibly in conjunction with the AAA ATPase VPS4. When
CC overexpressed, membrane-assembled circular arrays of CHMP4A
CC filaments can promote or stabilize negative curvature and outward
CC budding. Via its interaction with PDCD6IP involved in HIV-1 p6-
CC and p9-dependent virus release.
CC -!- SUBUNIT: Probable core component of the endosomal sorting required
CC for transport complex III (ESCRT-III). ESCRT-III components are
CC thought to multimerize to form a flat lattice on the perimeter
CC membrane of the endosome. Several assembly forms of ESCRT-III may
CC exist that interact and act sequentally. Self-associates;
CC overexpression leads to the assembly of filaments that curve and
CC associate to create circular rings. Interacts with CHMP2A.
CC Interacts with CHMP3; the interaction requires the release of
CC CHMP4A autoinhibition. Interacts with CHMP4B. Interacts with
CC CHMP4C. Interacts with CHMP6. Interacts with VPS4A. Interacts with
CC PDCD6IP; the interaction is direct.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane. Late endosome
CC membrane; Peripheral membrane protein (Probable). Note=Membrane-
CC associated. Localizes to large vesicle-like structures. Localizes
CC to the midbody of dividing cells. Localized in two distinct rings
CC on either side of the Fleming body.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
CC heart, kidney, liver and skeletal muscle. Also expressed in brain,
CC placenta, lung and pancreas.
CC -!- DOMAIN: The acidic C-terminus and the basic N-termminus are
CC thought to render the protein in a closed, soluble and inactive
CC conformation through an autoinhibitory intramolecular interaction.
CC The open and active conformation, which enables membrane binding
CC and oligomerization, is achieved by interaction with other
CC cellular binding partners, probably including other ESCRT
CC components (By similarity).
CC -!- SIMILARITY: Belongs to the SNF7 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH10893.2; Type=Erroneous initiation;
CC Sequence=AAI07700.1; Type=Erroneous initiation;
CC Sequence=CAD61949.1; Type=Erroneous initiation;
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DR EMBL; AB100262; BAC79376.2; -; mRNA.
DR EMBL; AY329084; AAQ91193.1; -; mRNA.
DR EMBL; AF212243; AAK14928.1; -; mRNA.
DR EMBL; AF161483; AAF29098.1; -; mRNA.
DR EMBL; BX161512; CAD61949.1; ALT_INIT; mRNA.
DR EMBL; AL096870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010893; AAH10893.2; ALT_INIT; mRNA.
DR EMBL; BC107699; AAI07700.1; ALT_INIT; mRNA.
DR RefSeq; NP_054888.2; NM_014169.3.
DR UniGene; Hs.279761; -.
DR PDB; 3C3O; X-ray; 2.15 A; B=210-222.
DR PDBsum; 3C3O; -.
DR ProteinModelPortal; Q9BY43; -.
DR SMR; Q9BY43; 20-94.
DR DIP; DIP-39082N; -.
DR IntAct; Q9BY43; 5.
DR MINT; MINT-3063754; -.
DR STRING; 9606.ENSP00000324205; -.
DR PhosphoSite; Q9BY43; -.
DR DMDM; 90152096; -.
DR PaxDb; Q9BY43; -.
DR PRIDE; Q9BY43; -.
DR DNASU; 29082; -.
DR GeneID; 29082; -.
DR KEGG; hsa:29082; -.
DR CTD; 29082; -.
DR GeneCards; GC14M024678; -.
DR HGNC; HGNC:20274; CHMP4A.
DR MIM; 610051; gene.
DR neXtProt; NX_Q9BY43; -.
DR PharmGKB; PA134888743; -.
DR eggNOG; NOG291419; -.
DR HOVERGEN; HBG050928; -.
DR InParanoid; Q9BY43; -.
DR KO; K12194; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR SignaLink; Q9BY43; -.
DR ChiTaRS; CHMP4A; human.
DR EvolutionaryTrace; Q9BY43; -.
DR GeneWiki; CHMP4A; -.
DR GenomeRNAi; 29082; -.
DR NextBio; 52058; -.
DR PRO; PR:Q9BY43; -.
DR ArrayExpress; Q9BY43; -.
DR Bgee; Q9BY43; -.
DR CleanEx; HS_CHMP4A; -.
DR Genevestigator; Q9BY43; -.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IDA:FlyBase.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR005024; Snf7.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Complete proteome; Cytoplasmic vesicle;
KW Endosome; Lipid-binding; Membrane; Polymorphism; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1 222 Charged multivesicular body protein 4a.
FT /FTId=PRO_0000211488.
FT REGION 1 150 Intramolecular interaction with C-
FT terminus (By similarity).
FT REGION 1 116 Interaction with phosphoinosides.
FT REGION 151 222 Intramolecular interaction with N-
FT terminus (By similarity).
FT COILED 20 105 Potential.
FT COILED 155 180 Potential.
FT VARIANT 153 153 G -> R (in dbSNP:rs2295322).
FT /FTId=VAR_023384.
FT MUTAGEN 182 222 Missing: Membrane association; releases
FT autoinhibition.
FT MUTAGEN 209 209 E->A: Reduces interaction with PDCD6IP.
FT MUTAGEN 214 214 L->A: Abolishes interaction with PDCD6IP.
FT MUTAGEN 217 217 L->A: Abolishes interaction with PDCD6IP.
FT MUTAGEN 220 220 W->A: Abolishes interaction with PDCD6IP.
FT CONFLICT 16 16 G -> R (in Ref. 4; AAF29098).
FT CONFLICT 66 66 L -> S (in Ref. 4; AAF29098).
FT CONFLICT 152 153 FG -> LLE (in Ref. 4; AAF29098).
FT HELIX 212 218
SQ SEQUENCE 222 AA; 25098 MW; 6712BA6AAA1D7CB7 CRC64;
MSGLGRLFGK GKKEKGPTPE EAIQKLKETE KILIKKQEFL EQKIQQELQT AKKYGTKNKR
AALQALRRKK RFEQQLAQTD GTLSTLEFQR EAIENATTNA EVLRTMELAA QSMKKAYQDM
DIDKVDELMT DITEQQEVAQ QISDAISRPM GFGDDVDEDE LLEELEELEQ EELAQELLNV
GDKEEEPSVK LPSVPSTHLP AGPAPKVDED EEALKQLAEW VS
//
ID CHM4A_HUMAN Reviewed; 222 AA.
AC Q9BY43; Q32Q79; Q86SZ8; Q96QJ9; Q9P026;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-FEB-2006, sequence version 3.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Charged multivesicular body protein 4a;
DE AltName: Full=Chromatin-modifying protein 4a;
DE Short=CHMP4a;
DE AltName: Full=SNF7 homolog associated with Alix-2;
DE AltName: Full=SNF7-1;
DE Short=hSnf-1;
DE AltName: Full=Vacuolar protein sorting-associated protein 32-1;
DE Short=Vps32-1;
DE Short=hVps32-1;
GN Name=CHMP4A; Synonyms=C14orf123, SHAX2; ORFNames=CDA04, HSPC134;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH PDCD6IP.
RC TISSUE=Cervix;
RX PubMed=12860994; DOI=10.1074/jbc.M301604200;
RA Katoh K., Shibata H., Suzuki H., Narai A., Ishidoh K., Kominami E.,
RA Yoshimori T., Maki M.;
RT "The ALG-2-interacting protein Alix associates with CHMP4b, a human
RT homologue of yeast Snf7 that is involved in multivesicular body
RT sorting.";
RL J. Biol. Chem. 278:39104-39113(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-153, FUNCTION, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH PDCD6IP.
RC TISSUE=Squamous cell carcinoma;
RX PubMed=14583093; DOI=10.1042/BJ20031347;
RA Peck J.W., Bowden E.T., Burbelo P.D.;
RT "Structure and function of human Vps20 and Snf7 proteins.";
RL Biochem. J. 377:693-700(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pheochromocytoma;
RA Li Y., Huang Q., Peng Y., Song H., Yu Y., Xu S., Ren S., Chen Z.,
RA Han Z.;
RT "A novel gene expressed in human pheochromocytoma.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-153.
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION IN HIV-1 BUDDING, AND INTERACTION WITH PDCD6IP.
RX PubMed=14505569; DOI=10.1016/S0092-8674(03)00653-6;
RA Strack B., Calistri A., Craig S., Popova E., Goettlinger H.G.;
RT "AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning
RT in virus budding.";
RL Cell 114:689-699(2003).
RN [9]
RP INTERACTION WITH CHMP4C; VPS4A AND PDCD6IP.
RX PubMed=14505570; DOI=10.1016/S0092-8674(03)00714-1;
RA von Schwedler U.K., Stuchell M., Mueller B., Ward D.M., Chung H.-Y.,
RA Morita E., Wang H.E., Davis T., He G.P., Cimbora D.M., Scott A.,
RA Kraeusslich H.-G., Kaplan J., Morham S.G., Sundquist W.I.;
RT "The protein network of HIV budding.";
RL Cell 114:701-713(2003).
RN [10]
RP FUNCTION IN HIV-1 BUDDING; SELF-ASSOCIATION, AND INTERACTION WITH
RP CHMP2A; CHMP4B; CHMP4C; CHMP6 AND PDCD6IP.
RX PubMed=14519844; DOI=10.1073/pnas.2133846100;
RA Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
RT "Divergent retroviral late-budding domains recruit vacuolar protein
RT sorting factors by using alternative adaptor proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003).
RN [11]
RP ERRATUM.
RA Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
RL Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003).
RN [12]
RP TISSUE SPECIFICITY, AND INTERACTION WITH PDCD6IP.
RX PubMed=14678797; DOI=10.1016/j.abb.2003.09.038;
RA Katoh K., Shibata H., Hatta K., Maki M.;
RT "CHMP4b is a major binding partner of the ALG-2-interacting protein
RT Alix among the three CHMP4 isoforms.";
RL Arch. Biochem. Biophys. 421:159-165(2004).
RN [13]
RP SUBCELLULAR LOCATION, AND LIPID-BINDING.
RX PubMed=15632132; DOI=10.1074/jbc.M413968200;
RA Lin Y., Kimpler L.A., Naismith T.V., Lauer J.M., Hanson P.I.;
RT "Interaction of the mammalian endosomal sorting complex required for
RT transport (ESCRT) III protein hSnf7-1 with itself, membranes, and the
RT AAA+ ATPase SKD1.";
RL J. Biol. Chem. 280:12799-12809(2005).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=17853893; DOI=10.1038/sj.emboj.7601850;
RA Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P.,
RA Rodesch C.K., Sundquist W.I.;
RT "Human ESCRT and ALIX proteins interact with proteins of the midbody
RT and function in cytokinesis.";
RL EMBO J. 26:4215-4227(2007).
RN [15]
RP AUTOINHIBITORY MECHANISM, INTERACTION WITH CHMP3, AND MUTAGENESIS OF
RP 182-ASP--SER-222.
RX PubMed=17547705; DOI=10.1111/j.1600-0854.2007.00584.x;
RA Shim S., Kimpler L.A., Hanson P.I.;
RT "Structure/function analysis of four core ESCRT-III proteins reveals
RT common regulatory role for extreme C-terminal domain.";
RL Traffic 8:1068-1079(2007).
RN [16]
RP FUNCTION, SELF-ASSOCIATION, AND STRUCTURE BY ELECTRON CRYOMICROSCOPY.
RX PubMed=18209100; DOI=10.1083/jcb.200707031;
RA Hanson P.I., Roth R., Lin Y., Heuser J.E.;
RT "Plasma membrane deformation by circular arrays of ESCRT-III protein
RT filaments.";
RL J. Cell Biol. 180:389-402(2008).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 210-222 IN COMPLEX WITH
RP PDCD6IP, AND MUTAGENESIS OF GLU-209; LEU-214; LEU-217 AND TRP-220.
RX PubMed=18511562; DOI=10.1073/pnas.0801567105;
RA McCullough J., Fisher R.D., Whitby F.G., Sundquist W.I., Hill C.P.;
RT "ALIX-CHMP4 interactions in the human ESCRT pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7687-7691(2008).
CC -!- FUNCTION: Probable core component of the endosomal sorting
CC required for transport complex III (ESCRT-III) which is involved
CC in multivesicular bodies (MVBs) formation and sorting of endosomal
CC cargo proteins into MVBs. MVBs contain intraluminal vesicles
CC (ILVs) that are generated by invagination and scission from the
CC limiting membrane of the endosome and mostly are delivered to
CC lysosomes enabling degradation of membrane proteins, such as
CC stimulated growth factor receptors, lysosomal enzymes and lipids.
CC The MVB pathway appears to require the sequential function of
CC ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly
CC dissociate from the invaginating membrane before the ILV is
CC released. The ESCRT machinery also functions in topologically
CC equivalent membrane fission events, such as the terminal stages of
CC cytokinesis and the budding of enveloped viruses (HIV-1 and other
CC lentiviruses). ESCRT-III proteins are believed to mediate the
CC necessary vesicle extrusion and/or membrane fission activities,
CC possibly in conjunction with the AAA ATPase VPS4. When
CC overexpressed, membrane-assembled circular arrays of CHMP4A
CC filaments can promote or stabilize negative curvature and outward
CC budding. Via its interaction with PDCD6IP involved in HIV-1 p6-
CC and p9-dependent virus release.
CC -!- SUBUNIT: Probable core component of the endosomal sorting required
CC for transport complex III (ESCRT-III). ESCRT-III components are
CC thought to multimerize to form a flat lattice on the perimeter
CC membrane of the endosome. Several assembly forms of ESCRT-III may
CC exist that interact and act sequentally. Self-associates;
CC overexpression leads to the assembly of filaments that curve and
CC associate to create circular rings. Interacts with CHMP2A.
CC Interacts with CHMP3; the interaction requires the release of
CC CHMP4A autoinhibition. Interacts with CHMP4B. Interacts with
CC CHMP4C. Interacts with CHMP6. Interacts with VPS4A. Interacts with
CC PDCD6IP; the interaction is direct.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane. Late endosome
CC membrane; Peripheral membrane protein (Probable). Note=Membrane-
CC associated. Localizes to large vesicle-like structures. Localizes
CC to the midbody of dividing cells. Localized in two distinct rings
CC on either side of the Fleming body.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
CC heart, kidney, liver and skeletal muscle. Also expressed in brain,
CC placenta, lung and pancreas.
CC -!- DOMAIN: The acidic C-terminus and the basic N-termminus are
CC thought to render the protein in a closed, soluble and inactive
CC conformation through an autoinhibitory intramolecular interaction.
CC The open and active conformation, which enables membrane binding
CC and oligomerization, is achieved by interaction with other
CC cellular binding partners, probably including other ESCRT
CC components (By similarity).
CC -!- SIMILARITY: Belongs to the SNF7 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH10893.2; Type=Erroneous initiation;
CC Sequence=AAI07700.1; Type=Erroneous initiation;
CC Sequence=CAD61949.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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DR EMBL; AB100262; BAC79376.2; -; mRNA.
DR EMBL; AY329084; AAQ91193.1; -; mRNA.
DR EMBL; AF212243; AAK14928.1; -; mRNA.
DR EMBL; AF161483; AAF29098.1; -; mRNA.
DR EMBL; BX161512; CAD61949.1; ALT_INIT; mRNA.
DR EMBL; AL096870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010893; AAH10893.2; ALT_INIT; mRNA.
DR EMBL; BC107699; AAI07700.1; ALT_INIT; mRNA.
DR RefSeq; NP_054888.2; NM_014169.3.
DR UniGene; Hs.279761; -.
DR PDB; 3C3O; X-ray; 2.15 A; B=210-222.
DR PDBsum; 3C3O; -.
DR ProteinModelPortal; Q9BY43; -.
DR SMR; Q9BY43; 20-94.
DR DIP; DIP-39082N; -.
DR IntAct; Q9BY43; 5.
DR MINT; MINT-3063754; -.
DR STRING; 9606.ENSP00000324205; -.
DR PhosphoSite; Q9BY43; -.
DR DMDM; 90152096; -.
DR PaxDb; Q9BY43; -.
DR PRIDE; Q9BY43; -.
DR DNASU; 29082; -.
DR GeneID; 29082; -.
DR KEGG; hsa:29082; -.
DR CTD; 29082; -.
DR GeneCards; GC14M024678; -.
DR HGNC; HGNC:20274; CHMP4A.
DR MIM; 610051; gene.
DR neXtProt; NX_Q9BY43; -.
DR PharmGKB; PA134888743; -.
DR eggNOG; NOG291419; -.
DR HOVERGEN; HBG050928; -.
DR InParanoid; Q9BY43; -.
DR KO; K12194; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR SignaLink; Q9BY43; -.
DR ChiTaRS; CHMP4A; human.
DR EvolutionaryTrace; Q9BY43; -.
DR GeneWiki; CHMP4A; -.
DR GenomeRNAi; 29082; -.
DR NextBio; 52058; -.
DR PRO; PR:Q9BY43; -.
DR ArrayExpress; Q9BY43; -.
DR Bgee; Q9BY43; -.
DR CleanEx; HS_CHMP4A; -.
DR Genevestigator; Q9BY43; -.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IDA:FlyBase.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR005024; Snf7.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Complete proteome; Cytoplasmic vesicle;
KW Endosome; Lipid-binding; Membrane; Polymorphism; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1 222 Charged multivesicular body protein 4a.
FT /FTId=PRO_0000211488.
FT REGION 1 150 Intramolecular interaction with C-
FT terminus (By similarity).
FT REGION 1 116 Interaction with phosphoinosides.
FT REGION 151 222 Intramolecular interaction with N-
FT terminus (By similarity).
FT COILED 20 105 Potential.
FT COILED 155 180 Potential.
FT VARIANT 153 153 G -> R (in dbSNP:rs2295322).
FT /FTId=VAR_023384.
FT MUTAGEN 182 222 Missing: Membrane association; releases
FT autoinhibition.
FT MUTAGEN 209 209 E->A: Reduces interaction with PDCD6IP.
FT MUTAGEN 214 214 L->A: Abolishes interaction with PDCD6IP.
FT MUTAGEN 217 217 L->A: Abolishes interaction with PDCD6IP.
FT MUTAGEN 220 220 W->A: Abolishes interaction with PDCD6IP.
FT CONFLICT 16 16 G -> R (in Ref. 4; AAF29098).
FT CONFLICT 66 66 L -> S (in Ref. 4; AAF29098).
FT CONFLICT 152 153 FG -> LLE (in Ref. 4; AAF29098).
FT HELIX 212 218
SQ SEQUENCE 222 AA; 25098 MW; 6712BA6AAA1D7CB7 CRC64;
MSGLGRLFGK GKKEKGPTPE EAIQKLKETE KILIKKQEFL EQKIQQELQT AKKYGTKNKR
AALQALRRKK RFEQQLAQTD GTLSTLEFQR EAIENATTNA EVLRTMELAA QSMKKAYQDM
DIDKVDELMT DITEQQEVAQ QISDAISRPM GFGDDVDEDE LLEELEELEQ EELAQELLNV
GDKEEEPSVK LPSVPSTHLP AGPAPKVDED EEALKQLAEW VS
//
MIM
610051
*RECORD*
*FIELD* NO
610051
*FIELD* TI
*610051 CHMP FAMILY, MEMBER 4A; CHMP4A
;;CHROMATIN-MODIFYING PROTEIN 4A;;
CHARGED MULTIVESICULAR BODY PROTEIN 4A;;
read moreCHMP4;;
SNF7, YEAST, HOMOLOG OF, 1;;
SNF7-1;;
HSPC134
*FIELD* TX
DESCRIPTION
CHMP4A belongs to the chromatin-modifying protein/charged multivesicular
body protein (CHMP) family. These proteins are components of ESCRT-III
(endosomal sorting complex required for transport III), a complex
involved in degradation of surface receptor proteins and formation of
endocytic multivesicular bodies (MVBs). Some CHMPs have both nuclear and
cytoplasmic/vesicular distributions, and one such CHMP, CHMP1A (164010),
is required for both MVB formation and regulation of cell cycle
progression (Tsang et al., 2006).
CLONING
Using the N-terminal region of ALIX (PDCD6IP; 608074) as bait in a yeast
2-hybrid screen of a HeLa cell cDNA library, Katoh et al. (2003) cloned
CHMP4A. The deduced 223-amino acid protein has 3 coiled-coil regions, a
basic N-terminal half, and an acidic C-terminal half.
By Northern blot analysis, Katoh et al. (2004) detected a 1-kb CHMP4A
transcript in all tissues examined, with highest expression in heart and
moderate expression in skeletal muscle, kidney, and liver.
By PCR of a human melanoma cDNA library, Lin et al. (2005) cloned
CHMP4A, which they designated SNF7-1. They identified 2 PxxP motifs near
the C terminus of CHMP4A. Northern blot analysis detected CHMP4A
expression in all tissues examined, with highest levels in kidney,
liver, skeletal muscle, and heart.
GENE FUNCTION
By yeast 2-hybrid analysis, Katoh et al. (2003) found that CHMP4A
interacted with ALIX.
Lin et al. (2005) found that overexpressed SNF7-1 associated with COS-7
cell membranes and perturbed normal multivesicular body biogenesis. The
N-terminal half of SNF7-1 localized to membranes and formed
detergent-resistant polymers, whereas the C-terminal half associated
with the ESCRT-III component SKD1 (VPS4B; 609983).
Tsang et al. (2006) performed a systematic yeast 2-hybrid analysis of
human ESCRT-III components, including CHMP4A. CHMP4A interacted with the
ESCRT-III protein VPS4A (609982) and with the signal transduction
molecule CC2D1A (610055).
In S. cerevisiae, ESCRT-III consists of Vps20 (610901), Snf7, Vps24
(610052), and Vps2 (610893), which assemble in that order and require
the ATPase Vps4 for their disassembly. Wollert et al. (2009)
reconstituted and visualized by fluorescence microscopy the
ESCRT-III-dependent budding and scission of intralumenal vesicles into
giant unilamellar vesicles. Wollert et al. (2009) showed that 3 subunits
of ESCRT-III, Vps20, Snf7, and Vps24, are sufficient to detach
intralumenal vesicles. Vps2, the ESCRT-III subunit responsible for
recruiting Vps4, and the ATPase activity of Vps4 were required for
ESCRT-III recycling and supported additional rounds of budding. The
minimum set of ESCRT-III and Vps4 proteins capable of multiple cycles of
vesicle detachment corresponds to the ancient set of ESCRT proteins
conserved from archaea to animals.
MAPPING
By genomic sequence analysis, Katoh et al. (2003) mapped the CHMP4A gene
to chromosome 14q11.2.
*FIELD* RF
1. Katoh, K.; Shibata, H.; Hatta, K.; Maki, M.: CHMP4b is a major
binding partner of the ALG-2-interacting protein Alix among the three
CHMP4 isoforms. Arch. Biochem. Biophys. 421: 159-165, 2004.
2. Katoh, K.; Shibata, H.; Suzuki, H.; Nara, A.; Ishidoh, K.; Kominami,
E.; Yoshimori, T.; Maki, M.: The ALG-2-interacting protein Alix associates
with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular
body sorting. J. Biol. Chem. 278: 39104-39113, 2003.
3. 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.
Note: Erratum: J. Biol. Chem. 281: 38966 only, 2006.
4. 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.
5. Wollert, T.; Wunder, C.; Lippincott-Schwartz, J.; Hurley, J. H.
: Membrane scission by the ESCRT-III complex. Nature 458: 172-177,
2009.
*FIELD* CN
Ada Hamosh - updated: 5/12/2009
Patricia A. Hartz - updated: 3/28/2007
*FIELD* CD
Patricia A. Hartz: 4/13/2006
*FIELD* ED
terry: 08/22/2012
alopez: 5/15/2009
terry: 5/12/2009
mgross: 3/28/2007
mgross: 4/13/2006
*RECORD*
*FIELD* NO
610051
*FIELD* TI
*610051 CHMP FAMILY, MEMBER 4A; CHMP4A
;;CHROMATIN-MODIFYING PROTEIN 4A;;
CHARGED MULTIVESICULAR BODY PROTEIN 4A;;
read moreCHMP4;;
SNF7, YEAST, HOMOLOG OF, 1;;
SNF7-1;;
HSPC134
*FIELD* TX
DESCRIPTION
CHMP4A belongs to the chromatin-modifying protein/charged multivesicular
body protein (CHMP) family. These proteins are components of ESCRT-III
(endosomal sorting complex required for transport III), a complex
involved in degradation of surface receptor proteins and formation of
endocytic multivesicular bodies (MVBs). Some CHMPs have both nuclear and
cytoplasmic/vesicular distributions, and one such CHMP, CHMP1A (164010),
is required for both MVB formation and regulation of cell cycle
progression (Tsang et al., 2006).
CLONING
Using the N-terminal region of ALIX (PDCD6IP; 608074) as bait in a yeast
2-hybrid screen of a HeLa cell cDNA library, Katoh et al. (2003) cloned
CHMP4A. The deduced 223-amino acid protein has 3 coiled-coil regions, a
basic N-terminal half, and an acidic C-terminal half.
By Northern blot analysis, Katoh et al. (2004) detected a 1-kb CHMP4A
transcript in all tissues examined, with highest expression in heart and
moderate expression in skeletal muscle, kidney, and liver.
By PCR of a human melanoma cDNA library, Lin et al. (2005) cloned
CHMP4A, which they designated SNF7-1. They identified 2 PxxP motifs near
the C terminus of CHMP4A. Northern blot analysis detected CHMP4A
expression in all tissues examined, with highest levels in kidney,
liver, skeletal muscle, and heart.
GENE FUNCTION
By yeast 2-hybrid analysis, Katoh et al. (2003) found that CHMP4A
interacted with ALIX.
Lin et al. (2005) found that overexpressed SNF7-1 associated with COS-7
cell membranes and perturbed normal multivesicular body biogenesis. The
N-terminal half of SNF7-1 localized to membranes and formed
detergent-resistant polymers, whereas the C-terminal half associated
with the ESCRT-III component SKD1 (VPS4B; 609983).
Tsang et al. (2006) performed a systematic yeast 2-hybrid analysis of
human ESCRT-III components, including CHMP4A. CHMP4A interacted with the
ESCRT-III protein VPS4A (609982) and with the signal transduction
molecule CC2D1A (610055).
In S. cerevisiae, ESCRT-III consists of Vps20 (610901), Snf7, Vps24
(610052), and Vps2 (610893), which assemble in that order and require
the ATPase Vps4 for their disassembly. Wollert et al. (2009)
reconstituted and visualized by fluorescence microscopy the
ESCRT-III-dependent budding and scission of intralumenal vesicles into
giant unilamellar vesicles. Wollert et al. (2009) showed that 3 subunits
of ESCRT-III, Vps20, Snf7, and Vps24, are sufficient to detach
intralumenal vesicles. Vps2, the ESCRT-III subunit responsible for
recruiting Vps4, and the ATPase activity of Vps4 were required for
ESCRT-III recycling and supported additional rounds of budding. The
minimum set of ESCRT-III and Vps4 proteins capable of multiple cycles of
vesicle detachment corresponds to the ancient set of ESCRT proteins
conserved from archaea to animals.
MAPPING
By genomic sequence analysis, Katoh et al. (2003) mapped the CHMP4A gene
to chromosome 14q11.2.
*FIELD* RF
1. Katoh, K.; Shibata, H.; Hatta, K.; Maki, M.: CHMP4b is a major
binding partner of the ALG-2-interacting protein Alix among the three
CHMP4 isoforms. Arch. Biochem. Biophys. 421: 159-165, 2004.
2. Katoh, K.; Shibata, H.; Suzuki, H.; Nara, A.; Ishidoh, K.; Kominami,
E.; Yoshimori, T.; Maki, M.: The ALG-2-interacting protein Alix associates
with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular
body sorting. J. Biol. Chem. 278: 39104-39113, 2003.
3. 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.
Note: Erratum: J. Biol. Chem. 281: 38966 only, 2006.
4. 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.
5. Wollert, T.; Wunder, C.; Lippincott-Schwartz, J.; Hurley, J. H.
: Membrane scission by the ESCRT-III complex. Nature 458: 172-177,
2009.
*FIELD* CN
Ada Hamosh - updated: 5/12/2009
Patricia A. Hartz - updated: 3/28/2007
*FIELD* CD
Patricia A. Hartz: 4/13/2006
*FIELD* ED
terry: 08/22/2012
alopez: 5/15/2009
terry: 5/12/2009
mgross: 3/28/2007
mgross: 4/13/2006