Full text data of CHMP7
CHMP7
[Confidence: low (only semi-automatic identification from reviews)]
Charged multivesicular body protein 7 (Chromatin-modifying protein 7)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Charged multivesicular body protein 7 (Chromatin-modifying protein 7)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q8WUX9
ID CHMP7_HUMAN Reviewed; 453 AA.
AC Q8WUX9; B2RDT3; D3DSS1; Q8NDM1; Q9BT50;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2002, sequence version 1.
DT 22-JAN-2014, entry version 96.
DE RecName: Full=Charged multivesicular body protein 7;
DE AltName: Full=Chromatin-modifying protein 7;
GN Name=CHMP7;
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 [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph, and Ovary;
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CHMP4B.
RX PubMed=16856878; DOI=10.1042/BJ20060897;
RA Horii M., Shibata H., Kobayashi R., Katoh K., Yorikawa C., Yasuda J.,
RA Maki M.;
RT "CHMP7, a novel ESCRT-III-related protein, associates with CHMP4b and
RT functions in the endosomal sorting pathway.";
RL Biochem. J. 400:23-32(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Plays a role in the endosomal sorting pathway.
CC -!- SUBUNIT: Interacts with CHMP4B, but not with VPS25.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Diffused localization, with
CC some punctate distribution, especially in the perinuclear area.
CC -!- SIMILARITY: Belongs to the SNF7 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK315664; BAG38030.1; -; mRNA.
DR EMBL; AL833843; CAD38703.2; -; mRNA.
DR EMBL; CH471080; EAW63632.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63634.1; -; Genomic_DNA.
DR EMBL; BC004344; AAH04344.1; -; mRNA.
DR EMBL; BC019110; AAH19110.1; -; mRNA.
DR EMBL; BC042050; AAH42050.1; -; mRNA.
DR RefSeq; NP_689485.1; NM_152272.3.
DR UniGene; Hs.5019; -.
DR ProteinModelPortal; Q8WUX9; -.
DR IntAct; Q8WUX9; 1.
DR MINT; MINT-1460844; -.
DR STRING; 9606.ENSP00000324491; -.
DR PhosphoSite; Q8WUX9; -.
DR DMDM; 73917782; -.
DR PaxDb; Q8WUX9; -.
DR PRIDE; Q8WUX9; -.
DR Ensembl; ENST00000313219; ENSP00000324491; ENSG00000147457.
DR Ensembl; ENST00000397677; ENSP00000380794; ENSG00000147457.
DR GeneID; 91782; -.
DR KEGG; hsa:91782; -.
DR UCSC; uc003xdc.2; human.
DR CTD; 91782; -.
DR GeneCards; GC08P023101; -.
DR HGNC; HGNC:28439; CHMP7.
DR HPA; HPA036119; -.
DR MIM; 611130; gene.
DR neXtProt; NX_Q8WUX9; -.
DR PharmGKB; PA142672115; -.
DR eggNOG; NOG272120; -.
DR HOGENOM; HOG000290682; -.
DR HOVERGEN; HBG081151; -.
DR InParanoid; Q8WUX9; -.
DR KO; K15053; -.
DR OMA; DESTLCM; -.
DR OrthoDB; EOG7M3J0G; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR GenomeRNAi; 91782; -.
DR NextBio; 77457; -.
DR PRO; PR:Q8WUX9; -.
DR ArrayExpress; Q8WUX9; -.
DR Bgee; Q8WUX9; -.
DR CleanEx; HS_CHMP7; -.
DR Genevestigator; Q8WUX9; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000815; C:ESCRT III complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0008565; F:protein transporter activity; IMP:UniProtKB.
DR GO; GO:0045324; P:late endosome to vacuole transport; IMP:UniProtKB.
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 Coiled coil; Complete proteome; Cytoplasm; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1 453 Charged multivesicular body protein 7.
FT /FTId=PRO_0000211516.
FT COILED 243 312 Potential.
FT MOD_RES 232 232 Phosphoserine (By similarity).
FT MOD_RES 417 417 Phosphoserine.
FT CONFLICT 433 434 GG -> E (in Ref. 2; CAD38703).
FT CONFLICT 440 442 KSP -> NLQ (in Ref. 2; CAD38703).
SQ SEQUENCE 453 AA; 50911 MW; CF91D562B918AEA1 CRC64;
MWSPEREAEA PAGGDPAGLL PPEWEEDEER MSFLFSAFKR SREVNSTDWD SKMGFWAPLV
LSHSRRQGVV RLRLRDLQEA FQRKGSVPLG LATVLQDLLR RGELQRESDF MASVDSSWIS
WGVGVFLLKP LKWTLSNMLG DNKVPAEEVL VAVELLKEKA EEVYRLYQNS PLSSHPVVAL
SELSTLCANS CPDERTFYLV LLQLQKEKRV TVLEQNGEKI VKFARGPRAK VSPVNDVDVG
VYQLMQSEQL LSRKVESLSQ EAERCKEEAR RACRAGKKQL ALRSLKAKQR TEKRIEALHA
KLDTVQGILD RIYASQTDQM VFNAYQAGVG ALKLSMKDVT VEKAESLVDQ IQELCDTQDE
VSQTLAGGVT NGLDFDSEEL EKELDILLQD TTKEPLDLPD NPRNRHFTNS VPNPRISDAE
LEAELEKLSL SEGGLVPSSK SPKRQLEPTL KPL
//
ID CHMP7_HUMAN Reviewed; 453 AA.
AC Q8WUX9; B2RDT3; D3DSS1; Q8NDM1; Q9BT50;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2002, sequence version 1.
DT 22-JAN-2014, entry version 96.
DE RecName: Full=Charged multivesicular body protein 7;
DE AltName: Full=Chromatin-modifying protein 7;
GN Name=CHMP7;
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 [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph, and Ovary;
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CHMP4B.
RX PubMed=16856878; DOI=10.1042/BJ20060897;
RA Horii M., Shibata H., Kobayashi R., Katoh K., Yorikawa C., Yasuda J.,
RA Maki M.;
RT "CHMP7, a novel ESCRT-III-related protein, associates with CHMP4b and
RT functions in the endosomal sorting pathway.";
RL Biochem. J. 400:23-32(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Plays a role in the endosomal sorting pathway.
CC -!- SUBUNIT: Interacts with CHMP4B, but not with VPS25.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Diffused localization, with
CC some punctate distribution, especially in the perinuclear area.
CC -!- SIMILARITY: Belongs to the SNF7 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK315664; BAG38030.1; -; mRNA.
DR EMBL; AL833843; CAD38703.2; -; mRNA.
DR EMBL; CH471080; EAW63632.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63634.1; -; Genomic_DNA.
DR EMBL; BC004344; AAH04344.1; -; mRNA.
DR EMBL; BC019110; AAH19110.1; -; mRNA.
DR EMBL; BC042050; AAH42050.1; -; mRNA.
DR RefSeq; NP_689485.1; NM_152272.3.
DR UniGene; Hs.5019; -.
DR ProteinModelPortal; Q8WUX9; -.
DR IntAct; Q8WUX9; 1.
DR MINT; MINT-1460844; -.
DR STRING; 9606.ENSP00000324491; -.
DR PhosphoSite; Q8WUX9; -.
DR DMDM; 73917782; -.
DR PaxDb; Q8WUX9; -.
DR PRIDE; Q8WUX9; -.
DR Ensembl; ENST00000313219; ENSP00000324491; ENSG00000147457.
DR Ensembl; ENST00000397677; ENSP00000380794; ENSG00000147457.
DR GeneID; 91782; -.
DR KEGG; hsa:91782; -.
DR UCSC; uc003xdc.2; human.
DR CTD; 91782; -.
DR GeneCards; GC08P023101; -.
DR HGNC; HGNC:28439; CHMP7.
DR HPA; HPA036119; -.
DR MIM; 611130; gene.
DR neXtProt; NX_Q8WUX9; -.
DR PharmGKB; PA142672115; -.
DR eggNOG; NOG272120; -.
DR HOGENOM; HOG000290682; -.
DR HOVERGEN; HBG081151; -.
DR InParanoid; Q8WUX9; -.
DR KO; K15053; -.
DR OMA; DESTLCM; -.
DR OrthoDB; EOG7M3J0G; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR GenomeRNAi; 91782; -.
DR NextBio; 77457; -.
DR PRO; PR:Q8WUX9; -.
DR ArrayExpress; Q8WUX9; -.
DR Bgee; Q8WUX9; -.
DR CleanEx; HS_CHMP7; -.
DR Genevestigator; Q8WUX9; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000815; C:ESCRT III complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0008565; F:protein transporter activity; IMP:UniProtKB.
DR GO; GO:0045324; P:late endosome to vacuole transport; IMP:UniProtKB.
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 Coiled coil; Complete proteome; Cytoplasm; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1 453 Charged multivesicular body protein 7.
FT /FTId=PRO_0000211516.
FT COILED 243 312 Potential.
FT MOD_RES 232 232 Phosphoserine (By similarity).
FT MOD_RES 417 417 Phosphoserine.
FT CONFLICT 433 434 GG -> E (in Ref. 2; CAD38703).
FT CONFLICT 440 442 KSP -> NLQ (in Ref. 2; CAD38703).
SQ SEQUENCE 453 AA; 50911 MW; CF91D562B918AEA1 CRC64;
MWSPEREAEA PAGGDPAGLL PPEWEEDEER MSFLFSAFKR SREVNSTDWD SKMGFWAPLV
LSHSRRQGVV RLRLRDLQEA FQRKGSVPLG LATVLQDLLR RGELQRESDF MASVDSSWIS
WGVGVFLLKP LKWTLSNMLG DNKVPAEEVL VAVELLKEKA EEVYRLYQNS PLSSHPVVAL
SELSTLCANS CPDERTFYLV LLQLQKEKRV TVLEQNGEKI VKFARGPRAK VSPVNDVDVG
VYQLMQSEQL LSRKVESLSQ EAERCKEEAR RACRAGKKQL ALRSLKAKQR TEKRIEALHA
KLDTVQGILD RIYASQTDQM VFNAYQAGVG ALKLSMKDVT VEKAESLVDQ IQELCDTQDE
VSQTLAGGVT NGLDFDSEEL EKELDILLQD TTKEPLDLPD NPRNRHFTNS VPNPRISDAE
LEAELEKLSL SEGGLVPSSK SPKRQLEPTL KPL
//
MIM
611130
*RECORD*
*FIELD* NO
611130
*FIELD* TI
*611130 CHMP FAMILY, MEMBER 7; CHMP7
;;CHARGED MULTIVESICULAR BODY PROTEIN 7;;
CHROMATIN-MODIFYING PROTEIN 7
read more*FIELD* TX
CLONING
By searching a database for sequences similar to CHMP family members,
followed by PCR of a human embryonic kidney cell line cDNA library,
Horii et al. (2006) cloned CHMP7. The deduced 453-amino acid protein
contains an SNF7 (CHMP4A; 610051)-related domain with a coiled-coil
region in its N-terminal half and an SNF7 domain with 2 coiled-coil
regions in its C-terminal half. The N-terminal half of CHMP7 also has 2
putative calmodulin (see CALM1; 114180)-binding IQ motifs and a clathrin
(see CLTC; 118955)-binding motif. Epitope-tagged CHMP7 showed diffuse
cytoplasmic staining and a punctate pattern, especially in the
perinuclear area.
GENE FUNCTION
Using pull-down assays with human embryonic kidney cells, Horii et al.
(2006) showed that CHMP7 interacted with CHMP4B (610897), but not with
EAP20 (VPS25; 610907). Overexpression of fluorescence-tagged CHMP7
impaired transport of endocytosed EGF (131530) in the endosome-lysosome
pathway. Moreover, overexpression of CHMP7 suppressed release of
virus-like particles into the culture medium of cotransfected cells.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the CHMP7
gene to chromosome 8 (TMAP STS-W49732).
*FIELD* RF
1. Horii, M.; Shibata, H.; Kobayashi, R.; Katoh, K.; Yorikawa, C.;
Yasuda, J.; Maki, M.: CHMP7, a novel ESCRT-III-related protein, associates
with CHMP4b and functions in the endosomal sorting pathway. Biochem.
J. 400: 23-32, 2006.
*FIELD* CD
Patricia A. Hartz: 6/21/2007
*FIELD* ED
mgross: 06/21/2007
*RECORD*
*FIELD* NO
611130
*FIELD* TI
*611130 CHMP FAMILY, MEMBER 7; CHMP7
;;CHARGED MULTIVESICULAR BODY PROTEIN 7;;
CHROMATIN-MODIFYING PROTEIN 7
read more*FIELD* TX
CLONING
By searching a database for sequences similar to CHMP family members,
followed by PCR of a human embryonic kidney cell line cDNA library,
Horii et al. (2006) cloned CHMP7. The deduced 453-amino acid protein
contains an SNF7 (CHMP4A; 610051)-related domain with a coiled-coil
region in its N-terminal half and an SNF7 domain with 2 coiled-coil
regions in its C-terminal half. The N-terminal half of CHMP7 also has 2
putative calmodulin (see CALM1; 114180)-binding IQ motifs and a clathrin
(see CLTC; 118955)-binding motif. Epitope-tagged CHMP7 showed diffuse
cytoplasmic staining and a punctate pattern, especially in the
perinuclear area.
GENE FUNCTION
Using pull-down assays with human embryonic kidney cells, Horii et al.
(2006) showed that CHMP7 interacted with CHMP4B (610897), but not with
EAP20 (VPS25; 610907). Overexpression of fluorescence-tagged CHMP7
impaired transport of endocytosed EGF (131530) in the endosome-lysosome
pathway. Moreover, overexpression of CHMP7 suppressed release of
virus-like particles into the culture medium of cotransfected cells.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the CHMP7
gene to chromosome 8 (TMAP STS-W49732).
*FIELD* RF
1. Horii, M.; Shibata, H.; Kobayashi, R.; Katoh, K.; Yorikawa, C.;
Yasuda, J.; Maki, M.: CHMP7, a novel ESCRT-III-related protein, associates
with CHMP4b and functions in the endosomal sorting pathway. Biochem.
J. 400: 23-32, 2006.
*FIELD* CD
Patricia A. Hartz: 6/21/2007
*FIELD* ED
mgross: 06/21/2007