Full text data of VPS37B
VPS37B
[Confidence: low (only semi-automatic identification from reviews)]
Vacuolar protein sorting-associated protein 37B; hVps37B (ESCRT-I complex subunit VPS37B)
Vacuolar protein sorting-associated protein 37B; hVps37B (ESCRT-I complex subunit VPS37B)
UniProt
Q9H9H4
ID VP37B_HUMAN Reviewed; 285 AA.
AC Q9H9H4;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Vacuolar protein sorting-associated protein 37B;
DE Short=hVps37B;
DE AltName: Full=ESCRT-I complex subunit VPS37B;
GN Name=VPS37B;
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].
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=Muscle;
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 [3]
RP FUNCTION, INTERACTION WITH TSG101, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15218037; DOI=10.1074/jbc.M405226200;
RA Stuchell M.D., Garrus J.E., Mueller B., Stray K.M., Ghaffarian S.,
RA McKinnon R., Kraeusslich H.-G., Morham S.G., Sundquist W.I.;
RT "The human endosomal sorting complex required for transport (ESCRT-I)
RT and its role in HIV-1 budding.";
RL J. Biol. Chem. 279:36059-36071(2004).
RN [4]
RP INTERACTION WITH TSG101; VPS28; MVB12A AND MVB12B, RECONSTITUTION OF
RP THE ESCRT-I COMPLEX, AND MASS SPECTROMETRY.
RX PubMed=18005716; DOI=10.1016/j.chom.2007.06.003;
RA Morita E., Sandrin V., Alam S.L., Eckert D.M., Gygi S.P.,
RA Sundquist W.I.;
RT "Identification of human MVB12 proteins as ESCRT-I subunits that
RT function in HIV budding.";
RL Cell Host Microbe 2:41-53(2007).
RN [5]
RP INTERACTION WITH CEP55.
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 [6]
RP INTERACTION WITH IST1.
RX PubMed=19129479; DOI=10.1091/mbc.E08-05-0475;
RA Bajorek M., Morita E., Skalicky J.J., Morham S.G., Babst M.,
RA Sundquist W.I.;
RT "Biochemical analyses of human IST1 and its function in cytokinesis.";
RL Mol. Biol. Cell 20:1360-1373(2009).
RN [7]
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 [8]
RP IDENTIFICATION IN AN ESCRT-I COMPLEX WITH UBAP1, AND SUBUNIT.
RX PubMed=22405001; DOI=10.1016/j.str.2011.12.013;
RA Agromayor M., Soler N., Caballe A., Kueck T., Freund S.M., Allen M.D.,
RA Bycroft M., Perisic O., Ye Y., McDonald B., Scheel H., Hofmann K.,
RA Neil S.J., Martin-Serrano J., Williams R.L.;
RT "The UBAP1 subunit of ESCRT-I interacts with ubiquitin via a SOUBA
RT domain.";
RL Structure 20:414-428(2012).
CC -!- FUNCTION: Component of the ESCRT-I complex, a regulator of
CC vesicular trafficking process. Required for the sorting of
CC endocytic ubiquitinated cargos into multivesicular bodies. May be
CC involved in cell growth and differentiation.
CC -!- SUBUNIT: Component of the ESCRT-I complex (endosomal sorting
CC complex required for transport I) which consists of TSG101, VPS28,
CC a VPS37 protein (VPS37A to -D) and MVB12A or MVB12B in a 1:1:1:1
CC stoechiometry. Interacts with TSG101, VPS28, MVB12A and MVB12B.
CC Component of the ESCRT-I complex (endosomal sorting complex
CC required for transport I) which consists of TSG101, VPS28, a VPS37
CC protein (VPS37A to -D) and UBAP1 in a 1:1:1:1 stoechiometry.
CC Interacts with CEP55. Interacts with IST1.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane; Peripheral membrane
CC protein. Note=Recruited to the endosomal membrane in a VPS4A-
CC dependent fashion.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in macrophages and
CC lymphocytes.
CC -!- SIMILARITY: Belongs to the VPS37 family.
CC -!- SIMILARITY: Contains 1 VPS37 C-terminal domain.
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; AK022812; BAB14255.1; -; mRNA.
DR EMBL; BC005882; AAH05882.1; -; mRNA.
DR RefSeq; NP_078943.1; NM_024667.2.
DR UniGene; Hs.507162; -.
DR ProteinModelPortal; Q9H9H4; -.
DR SMR; Q9H9H4; 108-156.
DR IntAct; Q9H9H4; 6.
DR MINT; MINT-6173622; -.
DR STRING; 9606.ENSP00000267202; -.
DR PhosphoSite; Q9H9H4; -.
DR DMDM; 74734015; -.
DR PaxDb; Q9H9H4; -.
DR PeptideAtlas; Q9H9H4; -.
DR PRIDE; Q9H9H4; -.
DR DNASU; 79720; -.
DR Ensembl; ENST00000267202; ENSP00000267202; ENSG00000139722.
DR GeneID; 79720; -.
DR KEGG; hsa:79720; -.
DR UCSC; uc001udl.3; human.
DR CTD; 79720; -.
DR GeneCards; GC12M123349; -.
DR HGNC; HGNC:25754; VPS37B.
DR HPA; HPA038217; -.
DR MIM; 610037; gene.
DR neXtProt; NX_Q9H9H4; -.
DR PharmGKB; PA142670616; -.
DR eggNOG; NOG329947; -.
DR HOGENOM; HOG000234744; -.
DR HOVERGEN; HBG073355; -.
DR InParanoid; Q9H9H4; -.
DR KO; K12185; -.
DR OMA; PSVMPRR; -.
DR OrthoDB; EOG7KQ22B; -.
DR PhylomeDB; Q9H9H4; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR ChiTaRS; VPS37B; human.
DR GenomeRNAi; 79720; -.
DR NextBio; 69072; -.
DR PRO; PR:Q9H9H4; -.
DR ArrayExpress; Q9H9H4; -.
DR Bgee; Q9H9H4; -.
DR CleanEx; HS_VPS37B; -.
DR Genevestigator; Q9H9H4; -.
DR GO; GO:0000813; C:ESCRT I complex; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR GO; GO:0019068; P:virion assembly; TAS:Reactome.
DR InterPro; IPR009851; Mod_r.
DR Pfam; PF07200; Mod_r; 1.
DR PROSITE; PS51314; VPS37_C; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Endosome; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1 285 Vacuolar protein sorting-associated
FT protein 37B.
FT /FTId=PRO_0000287200.
FT DOMAIN 84 173 VPS37 C-terminal.
FT REGION 50 170 Interaction with IST1.
FT COMPBIAS 170 280 Pro-rich.
SQ SEQUENCE 285 AA; 31307 MW; 43E70924AFA5DCE5 CRC64;
MAGAGSEARF AGLSLVQLNE LLEDEGQLTE MVQKMEETQN VQLNKEMTLA SNRSLAEGNL
LYQPQLDTLK ARLTQKYQEL QVLFEAYQIK KTKLDRQSSS ASLETLLALL QAEGAKIEED
TENMAEKFLD GELPLDSFID VYQSKRKLAH MRRVKIEKLQ EMVLKGQRLP QALAPLPPRL
PELAPTAPLP YPAPEASGPP AVAPRRIPPP PPPVPAGRLA TPFTAAMSSG QAVPYPGLQC
PPLPPRVGLP TQQGFSSQFV SPYPPPLPQR PPPRLPPHQP GFILQ
//
ID VP37B_HUMAN Reviewed; 285 AA.
AC Q9H9H4;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Vacuolar protein sorting-associated protein 37B;
DE Short=hVps37B;
DE AltName: Full=ESCRT-I complex subunit VPS37B;
GN Name=VPS37B;
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].
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=Muscle;
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 [3]
RP FUNCTION, INTERACTION WITH TSG101, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15218037; DOI=10.1074/jbc.M405226200;
RA Stuchell M.D., Garrus J.E., Mueller B., Stray K.M., Ghaffarian S.,
RA McKinnon R., Kraeusslich H.-G., Morham S.G., Sundquist W.I.;
RT "The human endosomal sorting complex required for transport (ESCRT-I)
RT and its role in HIV-1 budding.";
RL J. Biol. Chem. 279:36059-36071(2004).
RN [4]
RP INTERACTION WITH TSG101; VPS28; MVB12A AND MVB12B, RECONSTITUTION OF
RP THE ESCRT-I COMPLEX, AND MASS SPECTROMETRY.
RX PubMed=18005716; DOI=10.1016/j.chom.2007.06.003;
RA Morita E., Sandrin V., Alam S.L., Eckert D.M., Gygi S.P.,
RA Sundquist W.I.;
RT "Identification of human MVB12 proteins as ESCRT-I subunits that
RT function in HIV budding.";
RL Cell Host Microbe 2:41-53(2007).
RN [5]
RP INTERACTION WITH CEP55.
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 [6]
RP INTERACTION WITH IST1.
RX PubMed=19129479; DOI=10.1091/mbc.E08-05-0475;
RA Bajorek M., Morita E., Skalicky J.J., Morham S.G., Babst M.,
RA Sundquist W.I.;
RT "Biochemical analyses of human IST1 and its function in cytokinesis.";
RL Mol. Biol. Cell 20:1360-1373(2009).
RN [7]
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 [8]
RP IDENTIFICATION IN AN ESCRT-I COMPLEX WITH UBAP1, AND SUBUNIT.
RX PubMed=22405001; DOI=10.1016/j.str.2011.12.013;
RA Agromayor M., Soler N., Caballe A., Kueck T., Freund S.M., Allen M.D.,
RA Bycroft M., Perisic O., Ye Y., McDonald B., Scheel H., Hofmann K.,
RA Neil S.J., Martin-Serrano J., Williams R.L.;
RT "The UBAP1 subunit of ESCRT-I interacts with ubiquitin via a SOUBA
RT domain.";
RL Structure 20:414-428(2012).
CC -!- FUNCTION: Component of the ESCRT-I complex, a regulator of
CC vesicular trafficking process. Required for the sorting of
CC endocytic ubiquitinated cargos into multivesicular bodies. May be
CC involved in cell growth and differentiation.
CC -!- SUBUNIT: Component of the ESCRT-I complex (endosomal sorting
CC complex required for transport I) which consists of TSG101, VPS28,
CC a VPS37 protein (VPS37A to -D) and MVB12A or MVB12B in a 1:1:1:1
CC stoechiometry. Interacts with TSG101, VPS28, MVB12A and MVB12B.
CC Component of the ESCRT-I complex (endosomal sorting complex
CC required for transport I) which consists of TSG101, VPS28, a VPS37
CC protein (VPS37A to -D) and UBAP1 in a 1:1:1:1 stoechiometry.
CC Interacts with CEP55. Interacts with IST1.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane; Peripheral membrane
CC protein. Note=Recruited to the endosomal membrane in a VPS4A-
CC dependent fashion.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in macrophages and
CC lymphocytes.
CC -!- SIMILARITY: Belongs to the VPS37 family.
CC -!- SIMILARITY: Contains 1 VPS37 C-terminal domain.
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; AK022812; BAB14255.1; -; mRNA.
DR EMBL; BC005882; AAH05882.1; -; mRNA.
DR RefSeq; NP_078943.1; NM_024667.2.
DR UniGene; Hs.507162; -.
DR ProteinModelPortal; Q9H9H4; -.
DR SMR; Q9H9H4; 108-156.
DR IntAct; Q9H9H4; 6.
DR MINT; MINT-6173622; -.
DR STRING; 9606.ENSP00000267202; -.
DR PhosphoSite; Q9H9H4; -.
DR DMDM; 74734015; -.
DR PaxDb; Q9H9H4; -.
DR PeptideAtlas; Q9H9H4; -.
DR PRIDE; Q9H9H4; -.
DR DNASU; 79720; -.
DR Ensembl; ENST00000267202; ENSP00000267202; ENSG00000139722.
DR GeneID; 79720; -.
DR KEGG; hsa:79720; -.
DR UCSC; uc001udl.3; human.
DR CTD; 79720; -.
DR GeneCards; GC12M123349; -.
DR HGNC; HGNC:25754; VPS37B.
DR HPA; HPA038217; -.
DR MIM; 610037; gene.
DR neXtProt; NX_Q9H9H4; -.
DR PharmGKB; PA142670616; -.
DR eggNOG; NOG329947; -.
DR HOGENOM; HOG000234744; -.
DR HOVERGEN; HBG073355; -.
DR InParanoid; Q9H9H4; -.
DR KO; K12185; -.
DR OMA; PSVMPRR; -.
DR OrthoDB; EOG7KQ22B; -.
DR PhylomeDB; Q9H9H4; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_116125; Disease.
DR ChiTaRS; VPS37B; human.
DR GenomeRNAi; 79720; -.
DR NextBio; 69072; -.
DR PRO; PR:Q9H9H4; -.
DR ArrayExpress; Q9H9H4; -.
DR Bgee; Q9H9H4; -.
DR CleanEx; HS_VPS37B; -.
DR Genevestigator; Q9H9H4; -.
DR GO; GO:0000813; C:ESCRT I complex; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; TAS:Reactome.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR GO; GO:0019068; P:virion assembly; TAS:Reactome.
DR InterPro; IPR009851; Mod_r.
DR Pfam; PF07200; Mod_r; 1.
DR PROSITE; PS51314; VPS37_C; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Endosome; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1 285 Vacuolar protein sorting-associated
FT protein 37B.
FT /FTId=PRO_0000287200.
FT DOMAIN 84 173 VPS37 C-terminal.
FT REGION 50 170 Interaction with IST1.
FT COMPBIAS 170 280 Pro-rich.
SQ SEQUENCE 285 AA; 31307 MW; 43E70924AFA5DCE5 CRC64;
MAGAGSEARF AGLSLVQLNE LLEDEGQLTE MVQKMEETQN VQLNKEMTLA SNRSLAEGNL
LYQPQLDTLK ARLTQKYQEL QVLFEAYQIK KTKLDRQSSS ASLETLLALL QAEGAKIEED
TENMAEKFLD GELPLDSFID VYQSKRKLAH MRRVKIEKLQ EMVLKGQRLP QALAPLPPRL
PELAPTAPLP YPAPEASGPP AVAPRRIPPP PPPVPAGRLA TPFTAAMSSG QAVPYPGLQC
PPLPPRVGLP TQQGFSSQFV SPYPPPLPQR PPPRLPPHQP GFILQ
//
MIM
610037
*RECORD*
*FIELD* NO
610037
*FIELD* TI
*610037 VACUOLAR PROTEIN SORTING 37, YEAST, HOMOLOG OF, B; VPS37B
*FIELD* TX
CLONING
read more
By searching a database for sequences homologous to yeast Vps37,
Stuchell et al. (2004) identified human VPS37B. The deduced 285-amino
acid protein has an N-terminal mod(r) (modifier of rudimentary) domain
that contains 2 coiled-coil motifs.
GENE FUNCTION
Using yeast 2-hybrid analysis, Stuchell et al. (2004) showed that VPS37B
bound TSG101 (601387), which functions in vacuolar protein sorting.
TSG101 bound to several different sites on VPS37B, including a putative
coiled-coil region and a PTAP motif. In transfected human embryonic
kidney cells, TSG101 and VPS28 (601387) coimmunoprecipitated with
VPS37B, and the 3 proteins comigrated in a size-exclusion gel as a
350-kD complex, the size expected for ESCRT-I (endosomal sorting complex
required for transport I). Like TSG101, VPS37B became trapped on
aberrant endosomal compartments in the presence of mutant VPS4A (609982)
lacking ATPase activity. VPS37B could recruit TSG101/ESCRT-I activity
and thereby rescue budding of mutant human immunodeficiency virus
(HIV)-1 Gag proteins or HIV-1 viruses lacking native late domains.
Stuchell et al. (2004) concluded that VPS37B is a component of the human
ESCRT-I complex required for HIV-1 budding and infectivity.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the VPS37B
gene to chromosome 12 (TMAP RH98647).
*FIELD* RF
1. Stuchell, M. D.; Garrus, J. E.; Muller, B.; Stray, K. M.; Ghaffarian,
S.; McKinnon, R.; Krausslich, H.-G.; Morham, S. G.; Sundquist, W.
I.: The human endosomal sorting complex required for transport (ESCRT-I)
and its role in HIV-1 budding. J. Biol. Chem. 279: 36059-36071,
2004.
*FIELD* CD
Patricia A. Hartz: 4/10/2006
*FIELD* ED
mgross: 04/14/2008
mgross: 4/10/2006
*RECORD*
*FIELD* NO
610037
*FIELD* TI
*610037 VACUOLAR PROTEIN SORTING 37, YEAST, HOMOLOG OF, B; VPS37B
*FIELD* TX
CLONING
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By searching a database for sequences homologous to yeast Vps37,
Stuchell et al. (2004) identified human VPS37B. The deduced 285-amino
acid protein has an N-terminal mod(r) (modifier of rudimentary) domain
that contains 2 coiled-coil motifs.
GENE FUNCTION
Using yeast 2-hybrid analysis, Stuchell et al. (2004) showed that VPS37B
bound TSG101 (601387), which functions in vacuolar protein sorting.
TSG101 bound to several different sites on VPS37B, including a putative
coiled-coil region and a PTAP motif. In transfected human embryonic
kidney cells, TSG101 and VPS28 (601387) coimmunoprecipitated with
VPS37B, and the 3 proteins comigrated in a size-exclusion gel as a
350-kD complex, the size expected for ESCRT-I (endosomal sorting complex
required for transport I). Like TSG101, VPS37B became trapped on
aberrant endosomal compartments in the presence of mutant VPS4A (609982)
lacking ATPase activity. VPS37B could recruit TSG101/ESCRT-I activity
and thereby rescue budding of mutant human immunodeficiency virus
(HIV)-1 Gag proteins or HIV-1 viruses lacking native late domains.
Stuchell et al. (2004) concluded that VPS37B is a component of the human
ESCRT-I complex required for HIV-1 budding and infectivity.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the VPS37B
gene to chromosome 12 (TMAP RH98647).
*FIELD* RF
1. Stuchell, M. D.; Garrus, J. E.; Muller, B.; Stray, K. M.; Ghaffarian,
S.; McKinnon, R.; Krausslich, H.-G.; Morham, S. G.; Sundquist, W.
I.: The human endosomal sorting complex required for transport (ESCRT-I)
and its role in HIV-1 budding. J. Biol. Chem. 279: 36059-36071,
2004.
*FIELD* CD
Patricia A. Hartz: 4/10/2006
*FIELD* ED
mgross: 04/14/2008
mgross: 4/10/2006