VP37B_HUMAN
ID VP37B_HUMAN Reviewed; 285 AA.
AC Q9H9H4;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 project:
RT 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) and
RT 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 THE
RP ESCRT-I COMPLEX, AND IDENTIFICATION BY 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., Sundquist W.I.;
RT "Identification of human MVB12 proteins as ESCRT-I subunits that function
RT 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., Rodesch C.K.,
RA Sundquist W.I.;
RT "Human ESCRT and ALIX proteins interact with proteins of the midbody and
RT 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., Buerckstuemmer T.,
RA 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).
RN [9]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-218, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular
CC trafficking process. Required for the sorting of endocytic
CC ubiquitinated cargos into multivesicular bodies. May be involved in
CC cell growth and differentiation. {ECO:0000269|PubMed:15218037}.
CC -!- SUBUNIT: 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 MVB12A or MVB12B in a 1:1:1:1 stoichiometry.
CC Interacts with TSG101, VPS28, MVB12A and MVB12B. Component of the
CC ESCRT-I complex (endosomal sorting complex required for transport I)
CC which consists of TSG101, VPS28, a VPS37 protein (VPS37A to -D) and
CC UBAP1 in a 1:1:1:1 stoichiometry. Interacts with CEP55. Interacts with
CC IST1. {ECO:0000269|PubMed:15218037, ECO:0000269|PubMed:17853893,
CC ECO:0000269|PubMed:18005716, ECO:0000269|PubMed:19129479,
CC ECO:0000269|PubMed:22405001}.
CC -!- INTERACTION:
CC Q9H9H4; O95817: BAG3; NbExp=3; IntAct=EBI-4400866, EBI-747185;
CC Q9H9H4; Q13895: BYSL; NbExp=8; IntAct=EBI-4400866, EBI-358049;
CC Q9H9H4; Q6P1J9: CDC73; NbExp=3; IntAct=EBI-4400866, EBI-930143;
CC Q9H9H4; Q96GG9: DCUN1D1; NbExp=3; IntAct=EBI-4400866, EBI-740086;
CC Q9H9H4; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-4400866, EBI-744099;
CC Q9H9H4; P07992: ERCC1; NbExp=4; IntAct=EBI-4400866, EBI-750962;
CC Q9H9H4; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-4400866, EBI-742102;
CC Q9H9H4; Q8TES7-6: FBF1; NbExp=3; IntAct=EBI-4400866, EBI-10244131;
CC Q9H9H4; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-4400866, EBI-739467;
CC Q9H9H4; O14964: HGS; NbExp=6; IntAct=EBI-4400866, EBI-740220;
CC Q9H9H4; O60341: KDM1A; NbExp=3; IntAct=EBI-4400866, EBI-710124;
CC Q9H9H4; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-4400866, EBI-739832;
CC Q9H9H4; O43639: NCK2; NbExp=6; IntAct=EBI-4400866, EBI-713635;
CC Q9H9H4; Q13131: PRKAA1; NbExp=3; IntAct=EBI-4400866, EBI-1181405;
CC Q9H9H4; P54646: PRKAA2; NbExp=3; IntAct=EBI-4400866, EBI-1383852;
CC Q9H9H4; P47897: QARS1; NbExp=3; IntAct=EBI-4400866, EBI-347462;
CC Q9H9H4; P47897-2: QARS1; NbExp=3; IntAct=EBI-4400866, EBI-10209725;
CC Q9H9H4; Q96HL8: SH3YL1; NbExp=7; IntAct=EBI-4400866, EBI-722667;
CC Q9H9H4; Q96GM5: SMARCD1; NbExp=7; IntAct=EBI-4400866, EBI-358489;
CC Q9H9H4; O60504: SORBS3; NbExp=3; IntAct=EBI-4400866, EBI-741237;
CC Q9H9H4; Q08117: TLE5; NbExp=3; IntAct=EBI-4400866, EBI-717810;
CC Q9H9H4; Q08117-2: TLE5; NbExp=3; IntAct=EBI-4400866, EBI-11741437;
CC Q9H9H4; Q99816: TSG101; NbExp=3; IntAct=EBI-4400866, EBI-346882;
CC Q9H9H4; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-4400866, EBI-7353612;
CC Q9H9H4; Q8TF42: UBASH3B; NbExp=6; IntAct=EBI-4400866, EBI-1380492;
CC Q9H9H4; Q548N1: VPS28; NbExp=3; IntAct=EBI-4400866, EBI-10243107;
CC Q9H9H4; Q9UK41: VPS28; NbExp=6; IntAct=EBI-4400866, EBI-727424;
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000269|PubMed:15218037}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15218037}. Note=Recruited to the endosomal membrane
CC in a VPS4A-dependent fashion.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in macrophages and
CC lymphocytes. {ECO:0000269|PubMed:15218037}.
CC -!- SIMILARITY: Belongs to the VPS37 family. {ECO:0000305}.
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DR EMBL; AK022812; BAB14255.1; -; mRNA.
DR EMBL; BC005882; AAH05882.1; -; mRNA.
DR CCDS; CCDS9239.1; -.
DR RefSeq; NP_078943.1; NM_024667.2.
DR PDB; 6VME; X-ray; 2.19 A; C/K/L/M/N/O=97-167.
DR PDBsum; 6VME; -.
DR AlphaFoldDB; Q9H9H4; -.
DR SMR; Q9H9H4; -.
DR BioGRID; 122836; 57.
DR ComplexPortal; CPX-2505; ESCRT-I complex, VPS37B-MVB12A variant.
DR ComplexPortal; CPX-7164; ESCRT-I complex, VPS37B-MVB12B variant.
DR ComplexPortal; CPX-7201; ESCRT-I complex, VPS37B-UBAP1 variant.
DR CORUM; Q9H9H4; -.
DR ELM; Q9H9H4; -.
DR IntAct; Q9H9H4; 37.
DR MINT; Q9H9H4; -.
DR STRING; 9606.ENSP00000267202; -.
DR GlyGen; Q9H9H4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H9H4; -.
DR MetOSite; Q9H9H4; -.
DR PhosphoSitePlus; Q9H9H4; -.
DR BioMuta; VPS37B; -.
DR DMDM; 74734015; -.
DR EPD; Q9H9H4; -.
DR jPOST; Q9H9H4; -.
DR MassIVE; Q9H9H4; -.
DR MaxQB; Q9H9H4; -.
DR PaxDb; Q9H9H4; -.
DR PeptideAtlas; Q9H9H4; -.
DR PRIDE; Q9H9H4; -.
DR ProteomicsDB; 81322; -.
DR Antibodypedia; 52311; 75 antibodies from 17 providers.
DR DNASU; 79720; -.
DR Ensembl; ENST00000267202.7; ENSP00000267202.2; ENSG00000139722.7.
DR GeneID; 79720; -.
DR KEGG; hsa:79720; -.
DR MANE-Select; ENST00000267202.7; ENSP00000267202.2; NM_024667.3; NP_078943.1.
DR UCSC; uc001udl.4; human.
DR CTD; 79720; -.
DR DisGeNET; 79720; -.
DR GeneCards; VPS37B; -.
DR HGNC; HGNC:25754; VPS37B.
DR HPA; ENSG00000139722; Low tissue specificity.
DR MIM; 610037; gene.
DR neXtProt; NX_Q9H9H4; -.
DR OpenTargets; ENSG00000139722; -.
DR PharmGKB; PA142670616; -.
DR VEuPathDB; HostDB:ENSG00000139722; -.
DR eggNOG; KOG3270; Eukaryota.
DR GeneTree; ENSGT00950000183012; -.
DR HOGENOM; CLU_067118_1_0_1; -.
DR InParanoid; Q9H9H4; -.
DR OMA; QRAPPRM; -.
DR OrthoDB; 1197293at2759; -.
DR PhylomeDB; Q9H9H4; -.
DR TreeFam; TF321840; -.
DR PathwayCommons; Q9H9H4; -.
DR Reactome; R-HSA-162588; Budding and maturation of HIV virion.
DR Reactome; R-HSA-174490; Membrane binding and targetting of GAG proteins.
DR Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Reactome; R-HSA-9615710; Late endosomal microautophagy.
DR SignaLink; Q9H9H4; -.
DR BioGRID-ORCS; 79720; 20 hits in 1077 CRISPR screens.
DR ChiTaRS; VPS37B; human.
DR GenomeRNAi; 79720; -.
DR Pharos; Q9H9H4; Tbio.
DR PRO; PR:Q9H9H4; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9H9H4; protein.
DR Bgee; ENSG00000139722; Expressed in lower esophagus mucosa and 183 other tissues.
DR ExpressionAtlas; Q9H9H4; baseline and differential.
DR Genevisible; Q9H9H4; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0000813; C:ESCRT I complex; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; TAS:ParkinsonsUK-UCL.
DR GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0036258; P:multivesicular body assembly; TAS:ParkinsonsUK-UCL.
DR GO; GO:1903774; P:positive regulation of viral budding via host ESCRT complex; IMP:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IC:ComplexPortal.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; TAS:ParkinsonsUK-UCL.
DR GO; GO:0019076; P:viral release from host cell; IMP:UniProtKB.
DR Gene3D; 1.10.287.660; -; 1.
DR InterPro; IPR037202; ESCRT_assembly_dom.
DR InterPro; IPR029012; Helix_hairpin_bin_sf.
DR InterPro; IPR009851; Mod_r.
DR Pfam; PF07200; Mod_r; 1.
DR SUPFAM; SSF140111; SSF140111; 1.
DR PROSITE; PS51314; VPS37_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endosome; Membrane; Methylation; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..285
FT /note="Vacuolar protein sorting-associated protein 37B"
FT /id="PRO_0000287200"
FT DOMAIN 84..173
FT /note="VPS37 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00646"
FT REGION 50..170
FT /note="Interaction with IST1"
FT /evidence="ECO:0000269|PubMed:19129479"
FT REGION 175..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..279
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 218
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT HELIX 103..129
FT /evidence="ECO:0007829|PDB:6VME"
FT HELIX 135..162
FT /evidence="ECO:0007829|PDB:6VME"
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
