VP37A_HUMAN
ID VP37A_HUMAN Reviewed; 397 AA.
AC Q8NEZ2; Q336D5; Q6NW27; Q8N3D7; Q8TBL7; Q96DL9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Vacuolar protein sorting-associated protein 37A;
DE Short=hVps37A;
DE AltName: Full=ESCRT-I complex subunit VPS37A;
DE AltName: Full=Hepatocellular carcinoma-related protein 1;
GN Name=VPS37A; Synonyms=HCRP1;
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 [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=14623289; DOI=10.1016/j.bbrc.2003.10.109;
RA Xu Z., Liang L., Wang H., Li T., Zhao M.;
RT "HCRP1, a novel gene that is downregulated in hepatocellular carcinoma,
RT encodes a growth-inhibitory protein.";
RL Biochem. Biophys. Res. Commun. 311:1057-1066(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Synovium;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Melanoma;
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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH TSG101.
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TSG101; VPS28 AND HGS.
RX PubMed=15240819; DOI=10.1091/mbc.e04-03-0250;
RA Bache K.G., Slagsvold T., Cabezas A., Rosendal K.R., Raiborg C.,
RA Stenmark H.;
RT "The growth-regulatory protein HCRP1/hVps37A is a subunit of mammalian
RT ESCRT-I and mediates receptor down-regulation.";
RL Mol. Biol. Cell 15:4337-4346(2004).
RN [7]
RP INTERACTION WITH TSG101, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
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., 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 [11]
RP IDENTIFICATION IN AN ESCRT-I COMPLEX WITH UBAP1, AND SUBUNIT.
RX PubMed=21757351; DOI=10.1016/j.cub.2011.06.028;
RA Stefani F., Zhang L., Taylor S., Donovan J., Rollinson S., Doyotte A.,
RA Brownhill K., Bennion J., Pickering-Brown S., Woodman P.;
RT "UBAP1 is a component of an endosome-specific ESCRT-I complex that is
RT essential for MVB sorting.";
RL Curr. Biol. 21:1245-1250(2011).
RN [12]
RP TISSUE SPECIFICITY, VARIANT SPG53 ASN-382, AND CHARACTERIZATION OF VARIANT
RP SPG53 ASN-382.
RX PubMed=22717650; DOI=10.1136/jmedgenet-2012-100742;
RA Zivony-Elboum Y., Westbroek W., Kfir N., Savitzki D., Shoval Y., Bloom A.,
RA Rod R., Khayat M., Gross B., Samri W., Cohen H., Sonkin V., Freidman T.,
RA Geiger D., Fattal-Valevski A., Anikster Y., Waters A.M., Kleta R.,
RA Falik-Zaccai T.C.;
RT "A founder mutation in Vps37A causes autosomal recessive complex hereditary
RT spastic paraparesis.";
RL J. Med. Genet. 49:462-472(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(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:15240819}.
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 and HGS. Component of an ESCRT-I complex
CC (endosomal sorting complex required for transport I) which consists of
CC TSG101, VPS28, VPS37A and UBAP1 in a 1:1:1:1 stoichiometry.
CC {ECO:0000269|PubMed:15218037, ECO:0000269|PubMed:15240819,
CC ECO:0000269|PubMed:18005716, ECO:0000269|PubMed:21757351}.
CC -!- INTERACTION:
CC Q8NEZ2; P54252: ATXN3; NbExp=3; IntAct=EBI-2850578, EBI-946046;
CC Q8NEZ2; G5E9A7: DMWD; NbExp=3; IntAct=EBI-2850578, EBI-10976677;
CC Q8NEZ2; P22607: FGFR3; NbExp=3; IntAct=EBI-2850578, EBI-348399;
CC Q8NEZ2; Q8TB36: GDAP1; NbExp=3; IntAct=EBI-2850578, EBI-11110431;
CC Q8NEZ2; P28799: GRN; NbExp=3; IntAct=EBI-2850578, EBI-747754;
CC Q8NEZ2; P06396: GSN; NbExp=3; IntAct=EBI-2850578, EBI-351506;
CC Q8NEZ2; P01112: HRAS; NbExp=3; IntAct=EBI-2850578, EBI-350145;
CC Q8NEZ2; O43464: HTRA2; NbExp=3; IntAct=EBI-2850578, EBI-517086;
CC Q8NEZ2; P42858: HTT; NbExp=6; IntAct=EBI-2850578, EBI-466029;
CC Q8NEZ2; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-2850578, EBI-1055254;
CC Q8NEZ2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-2850578, EBI-10975473;
CC Q8NEZ2; O14901: KLF11; NbExp=3; IntAct=EBI-2850578, EBI-948266;
CC Q8NEZ2; P35240: NF2; NbExp=3; IntAct=EBI-2850578, EBI-1014472;
CC Q8NEZ2; P35240-4: NF2; NbExp=3; IntAct=EBI-2850578, EBI-1014514;
CC Q8NEZ2; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-2850578, EBI-2811583;
CC Q8NEZ2; P60891: PRPS1; NbExp=3; IntAct=EBI-2850578, EBI-749195;
CC Q8NEZ2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-2850578, EBI-396669;
CC Q8NEZ2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2850578, EBI-5235340;
CC Q8NEZ2; Q13148: TARDBP; NbExp=3; IntAct=EBI-2850578, EBI-372899;
CC Q8NEZ2; Q86WV8: TSC1; NbExp=3; IntAct=EBI-2850578, EBI-12806590;
CC Q8NEZ2; Q99816: TSG101; NbExp=6; IntAct=EBI-2850578, EBI-346882;
CC Q8NEZ2; O76024: WFS1; NbExp=3; IntAct=EBI-2850578, EBI-720609;
CC Q8NEZ2-2; G5E9A7: DMWD; NbExp=3; IntAct=EBI-10270911, EBI-10976677;
CC Q8NEZ2-2; P28799: GRN; NbExp=3; IntAct=EBI-10270911, EBI-747754;
CC Q8NEZ2-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-10270911, EBI-5235340;
CC Q8NEZ2-2; Q13148: TARDBP; NbExp=3; IntAct=EBI-10270911, EBI-372899;
CC Q8NEZ2-2; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-10270911, EBI-5235829;
CC Q8NEZ2-2; Q99816: TSG101; NbExp=5; IntAct=EBI-10270911, EBI-346882;
CC -!- SUBCELLULAR LOCATION: Late endosome membrane; Peripheral membrane
CC protein. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NEZ2-1; Sequence=Displayed;
CC Name=2; Synonyms=beta;
CC IsoId=Q8NEZ2-2; Sequence=VSP_025367;
CC Name=3;
CC IsoId=Q8NEZ2-3; Sequence=VSP_025368, VSP_025369;
CC -!- TISSUE SPECIFICITY: Widely expressed. Examined tissues include heart,
CC brain, placenta, liver, skeletal muscle, kidney and pancreas. More
CC abundant in liver. Strongly decreased or undetected in hepatomas.
CC {ECO:0000269|PubMed:14623289, ECO:0000269|PubMed:22717650}.
CC -!- DISEASE: Spastic paraplegia 53, autosomal recessive (SPG53)
CC [MIM:614898]: A form of spastic paraplegia, a neurodegenerative
CC disorder characterized by a slow, gradual, progressive weakness and
CC spasticity of the lower limbs. Rate of progression and the severity of
CC symptoms are quite variable. Initial symptoms may include difficulty
CC with balance, weakness and stiffness in the legs, muscle spasms, and
CC dragging the toes when walking. Complicated forms are recognized by
CC additional variable features including spastic quadriparesis, seizures,
CC dementia, amyotrophy, extrapyramidal disturbance, cerebral or
CC cerebellar atrophy, optic atrophy, and peripheral neuropathy, as well
CC as by extra neurological manifestations. SPG53 is characterized by
CC pronounced early onset spastic paraparesis of upper and lower limbs,
CC mild intellectual disability, kyphosis, pectus carinatum and
CC hypertrichosis. {ECO:0000269|PubMed:22717650}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the VPS37 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22363.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AY033079; AAK54349.1; -; mRNA.
DR EMBL; AF547097; AAQ12067.1; -; mRNA.
DR EMBL; AK057204; BAB71381.1; -; mRNA.
DR EMBL; AL834189; CAD38883.1; -; mRNA.
DR EMBL; BC022363; AAH22363.1; ALT_INIT; mRNA.
DR EMBL; BC067754; AAH67754.1; -; mRNA.
DR CCDS; CCDS47811.1; -. [Q8NEZ2-2]
DR CCDS; CCDS6001.1; -. [Q8NEZ2-1]
DR RefSeq; NP_001138624.1; NM_001145152.1. [Q8NEZ2-2]
DR RefSeq; NP_689628.2; NM_152415.2. [Q8NEZ2-1]
DR RefSeq; XP_016868510.1; XM_017013021.1. [Q8NEZ2-1]
DR RefSeq; XP_016868511.1; XM_017013022.1.
DR RefSeq; XP_016868515.1; XM_017013026.1.
DR AlphaFoldDB; Q8NEZ2; -.
DR SMR; Q8NEZ2; -.
DR BioGRID; 126479; 29.
DR ComplexPortal; CPX-7146; ESCRT-I complex, VPS37A-MVB12B variant.
DR ComplexPortal; CPX-7162; ESCRT-I complex, VPS37A-MVB12A variant.
DR ComplexPortal; CPX-7181; ESCRT-I complex, VPS37A-UBAP1 variant.
DR IntAct; Q8NEZ2; 36.
DR MINT; Q8NEZ2; -.
DR STRING; 9606.ENSP00000318629; -.
DR GlyGen; Q8NEZ2; 10 sites, 2 O-linked glycans (10 sites).
DR iPTMnet; Q8NEZ2; -.
DR PhosphoSitePlus; Q8NEZ2; -.
DR BioMuta; VPS37A; -.
DR DMDM; 74715446; -.
DR EPD; Q8NEZ2; -.
DR jPOST; Q8NEZ2; -.
DR MassIVE; Q8NEZ2; -.
DR MaxQB; Q8NEZ2; -.
DR PaxDb; Q8NEZ2; -.
DR PeptideAtlas; Q8NEZ2; -.
DR PRIDE; Q8NEZ2; -.
DR ProteomicsDB; 73247; -. [Q8NEZ2-1]
DR ProteomicsDB; 73248; -. [Q8NEZ2-2]
DR ProteomicsDB; 73249; -. [Q8NEZ2-3]
DR Antibodypedia; 22259; 153 antibodies from 24 providers.
DR DNASU; 137492; -.
DR Ensembl; ENST00000324849.9; ENSP00000318629.4; ENSG00000155975.10. [Q8NEZ2-1]
DR Ensembl; ENST00000425020.6; ENSP00000412824.2; ENSG00000155975.10. [Q8NEZ2-3]
DR Ensembl; ENST00000521829.5; ENSP00000429680.1; ENSG00000155975.10. [Q8NEZ2-2]
DR GeneID; 137492; -.
DR KEGG; hsa:137492; -.
DR MANE-Select; ENST00000324849.9; ENSP00000318629.4; NM_152415.3; NP_689628.2.
DR UCSC; uc003wxj.4; human. [Q8NEZ2-1]
DR CTD; 137492; -.
DR DisGeNET; 137492; -.
DR GeneCards; VPS37A; -.
DR HGNC; HGNC:24928; VPS37A.
DR HPA; ENSG00000155975; Low tissue specificity.
DR MalaCards; VPS37A; -.
DR MIM; 609927; gene.
DR MIM; 614898; phenotype.
DR neXtProt; NX_Q8NEZ2; -.
DR OpenTargets; ENSG00000155975; -.
DR Orphanet; 319199; Autosomal recessive spastic paraplegia type 53.
DR PharmGKB; PA142670615; -.
DR VEuPathDB; HostDB:ENSG00000155975; -.
DR eggNOG; KOG3270; Eukaryota.
DR GeneTree; ENSGT00950000183012; -.
DR HOGENOM; CLU_062319_0_0_1; -.
DR InParanoid; Q8NEZ2; -.
DR OMA; HIKECLR; -.
DR OrthoDB; 1573421at2759; -.
DR PhylomeDB; Q8NEZ2; -.
DR TreeFam; TF332146; -.
DR PathwayCommons; Q8NEZ2; -.
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; Q8NEZ2; -.
DR BioGRID-ORCS; 137492; 379 hits in 1085 CRISPR screens.
DR ChiTaRS; VPS37A; human.
DR GeneWiki; VPS37A; -.
DR GenomeRNAi; 137492; -.
DR Pharos; Q8NEZ2; Tbio.
DR PRO; PR:Q8NEZ2; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q8NEZ2; protein.
DR Bgee; ENSG00000155975; Expressed in islet of Langerhans and 179 other tissues.
DR ExpressionAtlas; Q8NEZ2; baseline and differential.
DR Genevisible; Q8NEZ2; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0000813; C:ESCRT I complex; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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: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; IMP:UniProtKB.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; TAS:ParkinsonsUK-UCL.
DR Gene3D; 1.10.287.660; -; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR037202; ESCRT_assembly_dom.
DR InterPro; IPR029012; Helix_hairpin_bin_sf.
DR InterPro; IPR009851; Mod_r.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF07200; Mod_r; 1.
DR SUPFAM; SSF140111; SSF140111; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS51314; VPS37_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Endosome;
KW Hereditary spastic paraplegia; Membrane; Neurodegeneration; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..397
FT /note="Vacuolar protein sorting-associated protein 37A"
FT /id="PRO_0000287198"
FT DOMAIN 308..397
FT /note="VPS37 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00646"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 42..67
FT /note="SIAEIQKDVEYRLPFTINNLTININI -> R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14623289"
FT /id="VSP_025367"
FT VAR_SEQ 140..185
FT /note="LYSNPSGMSPYASQGFPFLPPYPPQEANRSITSLSVADTVSSSTTS -> QL
FT EIRWHHPHCLEISLARSSNSLGFSISSSISSTRSKQEYHFFICC (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_025368"
FT VAR_SEQ 186..397
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_025369"
FT VARIANT 206
FT /note="I -> F (in dbSNP:rs17502618)"
FT /id="VAR_032287"
FT VARIANT 213
FT /note="I -> V (in dbSNP:rs17687375)"
FT /id="VAR_032288"
FT VARIANT 382
FT /note="K -> N (in SPG53; found in patients with complex
FT hereditary spastic paraparesis; hypomorphic mutation; does
FT not affect interaction with TSG101 and VPS28;
FT dbSNP:rs211694394)"
FT /evidence="ECO:0000269|PubMed:22717650"
FT /id="VAR_068424"
FT CONFLICT 313
FT /note="K -> R (in Ref. 2; BAB71381)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="S -> I (in Ref. 4; AAH67754)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 44314 MW; 96EBB670F04A0923 CRC64;
MSWLFPLTKS ASSSAAGSPG GLTSLQQQKQ RLIESLRNSH SSIAEIQKDV EYRLPFTINN
LTININILLP PQFPQEKPVI SVYPPIRHHL MDKQGVYVTS PLVNNFTMHS DLGKIIQSLL
DEFWKNPPVL APTSTAFPYL YSNPSGMSPY ASQGFPFLPP YPPQEANRSI TSLSVADTVS
SSTTSHTTAK PAAPSFGVLS NLPLPIPTVD ASIPTSQNGF GYKMPDVPDA FPELSELSVS
QLTDMNEQEE VLLEQFLTLP QLKQIITDKD DLVKSIEELA RKNLLLEPSL EAKRQTVLDK
YELLTQMKST FEKKMQRQHE LSESCSASAL QARLKVAAHE AEEESDNIAE DFLEGKMEID
DFLSSFMEKR TICHCRRAKE EKLQQAIAMH SQFHAPL
