ID   VP37C_HUMAN             Reviewed;         355 AA.
AC   A5D8V6; Q8N3K4;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   28-JAN-2026, entry version 140.
DE   RecName: Full=Vacuolar protein sorting-associated protein 37C;
DE            Short=hVps37C;
DE   AltName: Full=ESCRT-I complex subunit VPS37C;
GN   Name=VPS37C; Synonyms=PML39;
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], AND VARIANT ASP-182.
RC   TISSUE=Amygdala;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-198.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-198.
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   FUNCTION, INTERACTION WITH HGS; STAM2 AND TSG101, AND SUBCELLULAR LOCATION.
RX   PubMed=15509564; DOI=10.1074/jbc.m410384200;
RA   Eastman S.W., Martin-Serrano J., Chung W., Zang T., Bieniasz P.D.;
RT   "Identification of human VPS37C, a component of endosomal sorting complex
RT   required for transport-I important for viral budding.";
RL   J. Biol. Chem. 280:628-636(2005).
RN   [6]
RP   INTERACTION WITH TSG101; VPS28; MVB12A AND MVB12B, AND IDENTIFICATION BY
RP   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   [7]
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   [8]
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   [9]
RP   PHOSPHORYLATION BY TBK1.
RX   PubMed=21270402; DOI=10.4049/jimmunol.1000262;
RA   Da Q., Yang X., Xu Y., Gao G., Cheng G., Tang H.;
RT   "TANK-binding kinase 1 attenuates PTAP-dependent retroviral budding through
RT   targeting endosomal sorting complex required for transport-I.";
RL   J. Immunol. 186:3023-3030(2011).
RN   [10]
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 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:15509564}.
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 HGS and STAM2.
CC       Interacts with CEP55. {ECO:0000269|PubMed:15509564,
CC       ECO:0000269|PubMed:17853893, ECO:0000269|PubMed:18005716,
CC       ECO:0000269|PubMed:22405001}.
CC   -!- INTERACTION:
CC       A5D8V6; Q4LEZ3: AARD; NbExp=3; IntAct=EBI-2559305, EBI-5463075;
CC       A5D8V6; Q8NFV4-4: ABHD11; NbExp=3; IntAct=EBI-2559305, EBI-12318443;
CC       A5D8V6; Q9NQ33: ASCL3; NbExp=3; IntAct=EBI-2559305, EBI-12108222;
CC       A5D8V6; O95429: BAG4; NbExp=3; IntAct=EBI-2559305, EBI-2949658;
CC       A5D8V6; Q96CA5: BIRC7; NbExp=3; IntAct=EBI-2559305, EBI-517623;
CC       A5D8V6; Q6P1W5: C1orf94; NbExp=6; IntAct=EBI-2559305, EBI-946029;
CC       A5D8V6; Q53EZ4: CEP55; NbExp=8; IntAct=EBI-2559305, EBI-747776;
CC       A5D8V6; O43186: CRX; NbExp=3; IntAct=EBI-2559305, EBI-748171;
CC       A5D8V6; Q15038: DAZAP2; NbExp=6; IntAct=EBI-2559305, EBI-724310;
CC       A5D8V6; O75935-2: DCTN3; NbExp=3; IntAct=EBI-2559305, EBI-12091947;
CC       A5D8V6; P35638: DDIT3; NbExp=3; IntAct=EBI-2559305, EBI-742651;
CC       A5D8V6; P35638-2: DDIT3; NbExp=3; IntAct=EBI-2559305, EBI-10173632;
CC       A5D8V6; Q8WWB3: DYDC1; NbExp=3; IntAct=EBI-2559305, EBI-740680;
CC       A5D8V6; O00167-2: EYA2; NbExp=3; IntAct=EBI-2559305, EBI-12807776;
CC       A5D8V6; Q92567: FAM168A; NbExp=3; IntAct=EBI-2559305, EBI-7957930;
CC       A5D8V6; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-2559305, EBI-12193763;
CC       A5D8V6; B7ZLH0: FAM22F; NbExp=3; IntAct=EBI-2559305, EBI-10220102;
CC       A5D8V6; O94868-3: FCHSD2; NbExp=3; IntAct=EBI-2559305, EBI-11958845;
CC       A5D8V6; Q12951-2: FOXI1; NbExp=6; IntAct=EBI-2559305, EBI-12018822;
CC       A5D8V6; Q96AE4-2: FUBP1; NbExp=3; IntAct=EBI-2559305, EBI-12121668;
CC       A5D8V6; Q08379: GOLGA2; NbExp=3; IntAct=EBI-2559305, EBI-618309;
CC       A5D8V6; Q13227: GPS2; NbExp=3; IntAct=EBI-2559305, EBI-713355;
CC       A5D8V6; P62993: GRB2; NbExp=3; IntAct=EBI-2559305, EBI-401755;
CC       A5D8V6; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-2559305, EBI-2514791;
CC       A5D8V6; A0A087WSW0: HELT; NbExp=3; IntAct=EBI-2559305, EBI-12057631;
CC       A5D8V6; O14964: HGS; NbExp=3; IntAct=EBI-2559305, EBI-740220;
CC       A5D8V6; P52597: HNRNPF; NbExp=3; IntAct=EBI-2559305, EBI-352986;
CC       A5D8V6; Q9BUJ2: HNRNPUL1; NbExp=3; IntAct=EBI-2559305, EBI-1018153;
CC       A5D8V6; Q12906-6: ILF3; NbExp=3; IntAct=EBI-2559305, EBI-12904528;
CC       A5D8V6; Q13351: KLF1; NbExp=3; IntAct=EBI-2559305, EBI-8284732;
CC       A5D8V6; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-2559305, EBI-3044087;
CC       A5D8V6; Q14525: KRT33B; NbExp=3; IntAct=EBI-2559305, EBI-1049638;
CC       A5D8V6; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-2559305, EBI-11992140;
CC       A5D8V6; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-2559305, EBI-1048945;
CC       A5D8V6; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-2559305, EBI-12805508;
CC       A5D8V6; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-2559305, EBI-10241353;
CC       A5D8V6; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-2559305, EBI-12111050;
CC       A5D8V6; Q3LI66: KRTAP6-2; NbExp=5; IntAct=EBI-2559305, EBI-11962084;
CC       A5D8V6; Q8IUC3: KRTAP7-1; NbExp=3; IntAct=EBI-2559305, EBI-18394498;
CC       A5D8V6; Q14657: LAGE3; NbExp=3; IntAct=EBI-2559305, EBI-1052105;
CC       A5D8V6; Q14847-2: LASP1; NbExp=3; IntAct=EBI-2559305, EBI-9088686;
CC       A5D8V6; Q8NDC0: MAPK1IP1L; NbExp=6; IntAct=EBI-2559305, EBI-741424;
CC       A5D8V6; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-2559305, EBI-8487781;
CC       A5D8V6; Q96HA8: NTAQ1; NbExp=6; IntAct=EBI-2559305, EBI-741158;
CC       A5D8V6; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-2559305, EBI-741048;
CC       A5D8V6; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-2559305, EBI-10181968;
CC       A5D8V6; P55771: PAX9; NbExp=3; IntAct=EBI-2559305, EBI-12111000;
CC       A5D8V6; O75340: PDCD6; NbExp=6; IntAct=EBI-2559305, EBI-352915;
CC       A5D8V6; Q9UBV8: PEF1; NbExp=3; IntAct=EBI-2559305, EBI-724639;
CC       A5D8V6; P55347: PKNOX1; NbExp=4; IntAct=EBI-2559305, EBI-1373569;
CC       A5D8V6; Q96I87: PKNOX1; NbExp=3; IntAct=EBI-2559305, EBI-10173774;
CC       A5D8V6; Q96KN3: PKNOX2; NbExp=5; IntAct=EBI-2559305, EBI-2692890;
CC       A5D8V6; O15496: PLA2G10; NbExp=3; IntAct=EBI-2559305, EBI-726466;
CC       A5D8V6; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-2559305, EBI-949255;
CC       A5D8V6; O15162: PLSCR1; NbExp=3; IntAct=EBI-2559305, EBI-740019;
CC       A5D8V6; P52435: POLR2J; NbExp=3; IntAct=EBI-2559305, EBI-394753;
CC       A5D8V6; Q9H1A7: POLR2J3; NbExp=3; IntAct=EBI-2559305, EBI-12818681;
CC       A5D8V6; Q16633: POU2AF1; NbExp=3; IntAct=EBI-2559305, EBI-943588;
CC       A5D8V6; P86480: PRR20D; NbExp=3; IntAct=EBI-2559305, EBI-12754095;
CC       A5D8V6; P25788: PSMA3; NbExp=3; IntAct=EBI-2559305, EBI-348380;
CC       A5D8V6; Q9BTL3: RAMAC; NbExp=3; IntAct=EBI-2559305, EBI-744023;
CC       A5D8V6; Q93062: RBPMS; NbExp=3; IntAct=EBI-2559305, EBI-740322;
CC       A5D8V6; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-2559305, EBI-740343;
CC       A5D8V6; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-2559305, EBI-11987469;
CC       A5D8V6; Q8HWS3: RFX6; NbExp=3; IntAct=EBI-2559305, EBI-746118;
CC       A5D8V6; Q8N443: RIBC1; NbExp=6; IntAct=EBI-2559305, EBI-10265323;
CC       A5D8V6; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-2559305, EBI-726876;
CC       A5D8V6; Q9NQG5: RPRD1B; NbExp=3; IntAct=EBI-2559305, EBI-747925;
CC       A5D8V6; Q01196-8: RUNX1; NbExp=3; IntAct=EBI-2559305, EBI-12001422;
CC       A5D8V6; Q6FGM0: SH3GL1; NbExp=3; IntAct=EBI-2559305, EBI-10173690;
CC       A5D8V6; Q99961: SH3GL1; NbExp=3; IntAct=EBI-2559305, EBI-697911;
CC       A5D8V6; Q8TEC5: SH3RF2; NbExp=3; IntAct=EBI-2559305, EBI-2130111;
CC       A5D8V6; O94875: SORBS2; NbExp=3; IntAct=EBI-2559305, EBI-311323;
CC       A5D8V6; O94875-10: SORBS2; NbExp=3; IntAct=EBI-2559305, EBI-12037893;
CC       A5D8V6; O60504: SORBS3; NbExp=6; IntAct=EBI-2559305, EBI-741237;
CC       A5D8V6; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-2559305, EBI-11959123;
CC       A5D8V6; O75886: STAM2; NbExp=6; IntAct=EBI-2559305, EBI-373258;
CC       A5D8V6; Q8IWL8: STH; NbExp=3; IntAct=EBI-2559305, EBI-12843506;
CC       A5D8V6; Q9Y6A5: TACC3; NbExp=3; IntAct=EBI-2559305, EBI-2554984;
CC       A5D8V6; Q7Z6R9: TFAP2D; NbExp=3; IntAct=EBI-2559305, EBI-11952651;
CC       A5D8V6; Q92734: TFG; NbExp=6; IntAct=EBI-2559305, EBI-357061;
CC       A5D8V6; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-2559305, EBI-1105213;
CC       A5D8V6; Q01085-2: TIAL1; NbExp=3; IntAct=EBI-2559305, EBI-11064654;
CC       A5D8V6; Q08117: TLE5; NbExp=3; IntAct=EBI-2559305, EBI-717810;
CC       A5D8V6; Q08117-2: TLE5; NbExp=3; IntAct=EBI-2559305, EBI-11741437;
CC       A5D8V6; Q86WV8: TSC1; NbExp=3; IntAct=EBI-2559305, EBI-12806590;
CC       A5D8V6; Q99816: TSG101; NbExp=7; IntAct=EBI-2559305, EBI-346882;
CC       A5D8V6; Q5T6F2: UBAP2; NbExp=3; IntAct=EBI-2559305, EBI-2514383;
CC       A5D8V6; Q6NVU6: UFSP1; NbExp=3; IntAct=EBI-2559305, EBI-12068150;
CC       A5D8V6; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-2559305, EBI-12040603;
CC       A5D8V6; O00308: WWP2; NbExp=6; IntAct=EBI-2559305, EBI-743923;
CC       A5D8V6; P98170: XIAP; NbExp=7; IntAct=EBI-2559305, EBI-517127;
CC       A5D8V6; Q9BYJ9: YTHDF1; NbExp=3; IntAct=EBI-2559305, EBI-1051237;
CC       A5D8V6; Q9UDW3: ZMAT5; NbExp=3; IntAct=EBI-2559305, EBI-7850213;
CC       A5D8V6; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-2559305, EBI-12030590;
CC       A5D8V6; G4XUV3; NbExp=3; IntAct=EBI-2559305, EBI-10177989;
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane
CC       {ECO:0000305|PubMed:15509564}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:15509564}. Note=Probably associates with membranes.
CC       Recruited to the plasma membrane by HIV-1.
CC   -!- PTM: Phosphorylated by TBK1. {ECO:0000269|PubMed:21270402}.
CC   -!- SIMILARITY: Belongs to the VPS37 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD38936.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL834261; CAD38936.1; ALT_INIT; mRNA.
DR   EMBL; AP000437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471076; EAW73925.1; -; Genomic_DNA.
DR   EMBL; BC141827; AAI41828.1; -; mRNA.
DR   EMBL; BC142702; AAI42703.1; -; mRNA.
DR   CCDS; CCDS31573.1; -.
DR   RefSeq; NP_060436.4; NM_017966.4.
DR   RefSeq; XP_005274134.1; XM_005274077.4.
DR   AlphaFoldDB; A5D8V6; -.
DR   SMR; A5D8V6; -.
DR   BioGRID; 120371; 147.
DR   ComplexPortal; CPX-7147; ESCRT-I complex, VPS37C-MVB12A variant.
DR   ComplexPortal; CPX-7166; ESCRT-I complex, VPS37C-MVB12B variant.
DR   ComplexPortal; CPX-7202; ESCRT-I complex, VPS37C-UBAP1 variant.
DR   CORUM; A5D8V6; -.
DR   FunCoup; A5D8V6; 576.
DR   IntAct; A5D8V6; 124.
DR   MINT; A5D8V6; -.
DR   STRING; 9606.ENSP00000301765; -.
DR   MoonDB; A5D8V6; Predicted.
DR   GlyGen; A5D8V6; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; A5D8V6; -.
DR   PhosphoSitePlus; A5D8V6; -.
DR   BioMuta; VPS37C; -.
DR   jPOST; A5D8V6; -.
DR   MassIVE; A5D8V6; -.
DR   PaxDb; 9606-ENSP00000301765; -.
DR   PeptideAtlas; A5D8V6; -.
DR   ProteomicsDB; 712; -.
DR   Pumba; A5D8V6; -.
DR   Antibodypedia; 28060; 143 antibodies from 28 providers.
DR   DNASU; 55048; -.
DR   Ensembl; ENST00000301765.10; ENSP00000301765.5; ENSG00000167987.12.
DR   GeneID; 55048; -.
DR   KEGG; hsa:55048; -.
DR   MANE-Select; ENST00000301765.10; ENSP00000301765.5; NM_017966.5; NP_060436.4.
DR   UCSC; uc001nqv.2; human.
DR   AGR; HGNC:26097; -.
DR   ClinPGx; PA142670617; -.
DR   CTD; 55048; -.
DR   DisGeNET; 55048; -.
DR   GeneCards; VPS37C; -.
DR   HGNC; HGNC:26097; VPS37C.
DR   HPA; ENSG00000167987; Low tissue specificity.
DR   MIM; 610038; gene.
DR   OpenTargets; ENSG00000167987; -.
DR   VEuPathDB; HostDB:ENSG00000167987; -.
DR   eggNOG; KOG3270; Eukaryota.
DR   GeneTree; ENSGT00950000183012; -.
DR   HOGENOM; CLU_067118_0_0_1; -.
DR   InParanoid; A5D8V6; -.
DR   OMA; PMYRAGY; -.
DR   OrthoDB; 10004364at2759; -.
DR   PAN-GO; A5D8V6; 4 GO annotations based on evolutionary models.
DR   PhylomeDB; A5D8V6; -.
DR   PathwayCommons; A5D8V6; -.
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; A5D8V6; -.
DR   SIGNOR; A5D8V6; -.
DR   Agora; ENSG00000167987; -.
DR   BioGRID-ORCS; 55048; 96 hits in 1159 CRISPR screens.
DR   ChiTaRS; VPS37C; human.
DR   GenomeRNAi; 55048; -.
DR   Pharos; A5D8V6; Tbio.
DR   PRO; PR:A5D8V6; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; A5D8V6; protein.
DR   Bgee; ENSG00000167987; Expressed in secondary oocyte and 200 other cell types or tissues.
DR   ExpressionAtlas; A5D8V6; baseline and differential.
DR   GO; GO:0005929; C:cilium; IDA:HPA.
DR   GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR   GO; GO:0000813; C:ESCRT I complex; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; NAS: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; NAS: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   FunFam; 1.10.287.660:FF:000003; vacuolar protein sorting-associated protein 37B; 1.
DR   Gene3D; 1.10.287.660; Helix hairpin bin; 1.
DR   InterPro; IPR037202; ESCRT_assembly_dom.
DR   InterPro; IPR029012; Helix_hairpin_bin_sf.
DR   InterPro; IPR009851; Mod_r.
DR   PANTHER; PTHR13678; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 37; 1.
DR   PANTHER; PTHR13678:SF8; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 37C; 1.
DR   Pfam; PF07200; Mod_r; 1.
DR   SUPFAM; SSF140111; Endosomal sorting complex assembly domain; 1.
DR   PROSITE; PS51314; VPS37_C; 1.
PE   1: Evidence at protein level;
KW   Endosome; Membrane; Phosphoprotein; Protein transport;
KW   Proteomics identification; Reference proteome; Transport.
FT   CHAIN           1..355
FT                   /note="Vacuolar protein sorting-associated protein 37C"
FT                   /id="PRO_0000312198"
FT   DOMAIN          78..167
FT                   /note="VPS37 C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00646"
FT   REGION          159..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..186
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..214
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..304
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..355
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         29
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8R105"
FT   VARIANT         182
FT                   /note="V -> D (in dbSNP:rs2232142)"
FT                   /evidence="ECO:0000269|PubMed:17974005"
FT                   /id="VAR_037451"
FT   VARIANT         198
FT                   /note="L -> S (in dbSNP:rs754382)"
FT                   /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT                   /id="VAR_037452"
SQ   SEQUENCE   355 AA;  38659 MW;  1DE18F0E4C7C7E2E CRC64;
     METLKDKTLQ ELEELQNDSE AIDQLALESP EVQDLQLERE MALATNRSLA ERNLEFQGPL
     EISRSNLSDR YQELRKLVER CQEQKAKLEK FSSALQPGTL LDLLQVEGMK IEEESEAMAE
     KFLEGEVPLE TFLENFSSMR MLSHLRRVRV EKLQEVVRKP RASQELAGDA PPPRPPPPVR
     PVPQGTPPVV EEQPQPPLAM PPYPLPYSPS PSLPVGPTAH GALPPAPFPV VSQPSFYSGP
     LGPTYPAAQL GPRGAAGYSW SPQRSMPPRP GYPGTPMGAS GPGYPLRGGR APSPGYPQQS
     PYPATGGKPP YPIQPQLPSF PGQPQPSVPL QPPYPPGPAP PYGFPPPPGP AWPGY
//