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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //