ID VPS18_HUMAN Reviewed; 973 AA.
AC Q9P253; Q8TCG0; Q96DI3; Q9H268;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 24-JAN-2024, entry version 191.
DE RecName: Full=Vacuolar protein sorting-associated protein 18 homolog;
DE Short=hVPS18;
GN Name=VPS18 {ECO:0000312|HGNC:HGNC:15972}; Synonyms=KIAA1475;
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].
RX PubMed=11250079; DOI=10.1016/s0378-1119(01)00333-x;
RA Huizing M., Didier A., Walenta J., Anikster Y., Gahl W.A., Kraemer H.;
RT "Molecular cloning and characterization of human VPS18, VPS11, VPS16, and
RT VPS33.";
RL Gene 264:241-247(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
RC TISSUE=Lung;
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, SUBUNIT, INTERACTION WITH STX7; VPS33A AND VPS11, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11382755; DOI=10.1074/jbc.m101778200;
RA Kim B.Y., Kraemer H., Yamamoto A., Kominami E., Kohsaka S., Akazawa C.;
RT "Molecular characterization of mammalian homologues of class C Vps proteins
RT that interact with syntaxin-7.";
RL J. Biol. Chem. 276:29393-29402(2001).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Placenta;
RX PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H.,
RA Elsaesser H.-P., Mann M., Hasilik A.;
RT "Integral and associated lysosomal membrane proteins.";
RL Traffic 8:1676-1686(2007).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=18552835; DOI=10.1038/ncb1740;
RA Liang C., Lee J.S., Inn K.S., Gack M.U., Li Q., Roberts E.A., Vergne I.,
RA Deretic V., Feng P., Akazawa C., Jung J.U.;
RT "Beclin1-binding UVRAG targets the class C Vps complex to coordinate
RT autophagosome maturation and endocytic trafficking.";
RL Nat. Cell Biol. 10:776-787(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-689, 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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-362, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP INTERACTION WITH MON1B.
RX PubMed=20434987; DOI=10.1016/j.cell.2010.03.011;
RA Poteryaev D., Datta S., Ackema K., Zerial M., Spang A.;
RT "Identification of the switch in early-to-late endosome transition.";
RL Cell 141:497-508(2010).
RN [11]
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 [12]
RP SUBCELLULAR LOCATION.
RX PubMed=21802320; DOI=10.1016/j.immuni.2011.06.009;
RA Garg S., Sharma M., Ung C., Tuli A., Barral D.C., Hava D.L., Veerapen N.,
RA Besra G.S., Hacohen N., Brenner M.B.;
RT "Lysosomal trafficking, antigen presentation, and microbial killing are
RT controlled by the Arf-like GTPase Arl8b.";
RL Immunity 35:182-193(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP INTERACTION WITH SYNPO2.
RX PubMed=23434281; DOI=10.1016/j.cub.2013.01.064;
RA Ulbricht A., Eppler F.J., Tapia V.E., van der Ven P.F., Hampe N.,
RA Hersch N., Vakeel P., Stadel D., Haas A., Saftig P., Behrends C.,
RA Fuerst D.O., Volkmer R., Hoffmann B., Kolanus W., Hoehfeld J.;
RT "Cellular mechanotransduction relies on tension-induced and chaperone-
RT assisted autophagy.";
RL Curr. Biol. 23:430-435(2013).
RN [16]
RP REVIEW ON THE HOPS AND CORVET COMPLEXES.
RX PubMed=23351085; DOI=10.1111/febs.12151;
RA Solinger J.A., Spang A.;
RT "Tethering complexes in the endocytic pathway: CORVET and HOPS.";
RL FEBS J. 280:2743-2757(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-11; SER-13 AND
RP SER-912, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [18]
RP INTERACTION WITH VPS16 AND VPS41.
RX PubMed=23901104; DOI=10.1073/pnas.1307074110;
RA Graham S.C., Wartosch L., Gray S.R., Scourfield E.J., Deane J.E.,
RA Luzio J.P., Owen D.J.;
RT "Structural basis of Vps33A recruitment to the human HOPS complex by
RT Vps16.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:13345-13350(2013).
RN [19]
RP FUNCTION OF THE HOPS COMPLEX, AND INTERACTION WITH STX17.
RX PubMed=24554770; DOI=10.1091/mbc.e13-08-0447;
RA Jiang P., Nishimura T., Sakamaki Y., Itakura E., Hatta T., Natsume T.,
RA Mizushima N.;
RT "The HOPS complex mediates autophagosome-lysosome fusion through
RT interaction with syntaxin 17.";
RL Mol. Biol. Cell 25:1327-1337(2014).
RN [20]
RP FUNCTION, FUNCTION OF THE HOPS COMPLEX, AND INTERACTION WITH VPS33A AND
RP VPS16.
RX PubMed=25783203; DOI=10.1111/tra.12283;
RA Wartosch L., Guenesdogan U., Graham S.C., Luzio J.P.;
RT "Recruitment of VPS33A to HOPS by VPS16 Is Required for Lysosome Fusion
RT with Endosomes and Autophagosomes.";
RL Traffic 16:727-742(2015).
RN [21]
RP INTERACTION WITH PLEKHM1.
RX PubMed=28325809; DOI=10.1083/jcb.201607085;
RA Marwaha R., Arya S.B., Jagga D., Kaur H., Tuli A., Sharma M.;
RT "The Rab7 effector PLEKHM1 binds Arl8b to promote cargo traffic to
RT lysosomes.";
RL J. Cell Biol. 216:1051-1070(2017).
RN [22]
RP VARIANT [LARGE SCALE ANALYSIS] SER-913.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Plays a role in vesicle-mediated protein trafficking to
CC lysosomal compartments including the endocytic membrane transport and
CC autophagic pathways. Believed to act as a core component of the
CC putative HOPS and CORVET endosomal tethering complexes which are
CC proposed to be involved in the Rab5-to-Rab7 endosome conversion
CC probably implicating MON1A/B, and via binding SNAREs and SNARE
CC complexes to mediate tethering and docking events during SNARE-mediated
CC membrane fusion. The HOPS complex is proposed to be recruited to Rab7
CC on the late endosomal membrane and to regulate late endocytic,
CC phagocytic and autophagic traffic towards lysosomes. The CORVET complex
CC is proposed to function as a Rab5 effector to mediate early endosome
CC fusion probably in specific endosome subpopulations (PubMed:11382755,
CC PubMed:23351085, PubMed:24554770, PubMed:25783203). Required for fusion
CC of endosomes and autophagosomes with lysosomes (PubMed:25783203).
CC Involved in dendrite development of Pukinje cells (By similarity).
CC {ECO:0000250|UniProtKB:Q8R307, ECO:0000269|PubMed:25783203,
CC ECO:0000305|PubMed:11382755, ECO:0000305|PubMed:23351085,
CC ECO:0000305|PubMed:25783203}.
CC -!- SUBUNIT: Core component of at least two putative endosomal tethering
CC complexes, the homotypic fusion and vacuole protein sorting (HOPS)
CC complex and the class C core vacuole/endosome tethering (CORVET)
CC complex. Their common core is composed of the class C Vps proteins
CC VPS11, VPS16, VPS18 and VPS33A, which in HOPS further associates with
CC VPS39 and VPS41 and in CORVET with VPS8 and TGFBRAP1 (PubMed:23351085,
CC PubMed:25783203, PubMed:23901104). Interacts with RAB5C (By
CC similarity). Interacts with HOOK1 (By similarity). Interacts with STX7,
CC MON1B (PubMed:20434987, PubMed:24554770). Associates with adaptor
CC protein complex 3 (AP-3) and clathrin:AP-3 complexes (By similarity).
CC Interacts with SYNPO2 (PubMed:23434281). Interacts with PLEKHM1
CC (PubMed:28325809). {ECO:0000250|UniProtKB:Q8R307,
CC ECO:0000269|PubMed:11382755, ECO:0000269|PubMed:20434987,
CC ECO:0000269|PubMed:23434281, ECO:0000269|PubMed:23901104,
CC ECO:0000269|PubMed:24554770, ECO:0000269|PubMed:25783203,
CC ECO:0000269|PubMed:28325809, ECO:0000305|PubMed:23351085}.
CC -!- INTERACTION:
CC Q9P253; Q7L1V2: MON1B; NbExp=2; IntAct=EBI-1053363, EBI-2655311;
CC Q9P253; O15400: STX7; NbExp=2; IntAct=EBI-1053363, EBI-3221827;
CC Q9P253; Q9H270: VPS11; NbExp=9; IntAct=EBI-1053363, EBI-373380;
CC Q9P253; Q9H269: VPS16; NbExp=15; IntAct=EBI-1053363, EBI-2655929;
CC Q9P253; Q96AX1: VPS33A; NbExp=6; IntAct=EBI-1053363, EBI-2527283;
CC Q9P253; Q96JC1: VPS39; NbExp=2; IntAct=EBI-1053363, EBI-1050197;
CC Q9P253; P49754: VPS41; NbExp=4; IntAct=EBI-1053363, EBI-2130459;
CC Q9P253; Q63615: Vps33a; Xeno; NbExp=2; IntAct=EBI-1053363, EBI-918669;
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000269|PubMed:11382755}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11382755}; Cytoplasmic side {ECO:0000305}. Lysosome
CC membrane {ECO:0000269|PubMed:11382755, ECO:0000269|PubMed:21802320};
CC Peripheral membrane protein {ECO:0000269|PubMed:11382755}; Cytoplasmic
CC side {ECO:0000305}. Early endosome {ECO:0000269|PubMed:18552835}.
CC Cytoplasmic vesicle, autophagosome {ECO:0000305}. Cytoplasmic vesicle,
CC clathrin-coated vesicle {ECO:0000305}. Note=Cytoplasmic, peripheral
CC membrane protein associated with early endosomes and late
CC endosomes/lysosomes.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expression was highest in heart and low
CC in lung. {ECO:0000269|PubMed:11382755}.
CC -!- SIMILARITY: Belongs to the VPS18 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH01513.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
CC Sequence=BAA95999.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF308802; AAG34679.1; -; mRNA.
DR EMBL; AB040908; BAA95999.1; ALT_INIT; mRNA.
DR EMBL; AL713725; CAD28515.1; -; mRNA.
DR EMBL; BC001513; AAH01513.1; ALT_SEQ; mRNA.
DR CCDS; CCDS10069.1; -.
DR RefSeq; NP_065908.1; NM_020857.2.
DR AlphaFoldDB; Q9P253; -.
DR SMR; Q9P253; -.
DR BioGRID; 121664; 160.
DR ComplexPortal; CPX-6212; HOPS tethering complex.
DR ComplexPortal; CPX-6213; CORVET tethering complex.
DR CORUM; Q9P253; -.
DR IntAct; Q9P253; 59.
DR MINT; Q9P253; -.
DR STRING; 9606.ENSP00000220509; -.
DR GlyGen; Q9P253; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9P253; -.
DR PhosphoSitePlus; Q9P253; -.
DR SwissPalm; Q9P253; -.
DR BioMuta; VPS18; -.
DR DMDM; 23396938; -.
DR EPD; Q9P253; -.
DR jPOST; Q9P253; -.
DR MassIVE; Q9P253; -.
DR MaxQB; Q9P253; -.
DR PaxDb; 9606-ENSP00000220509; -.
DR PeptideAtlas; Q9P253; -.
DR ProteomicsDB; 83731; -.
DR Pumba; Q9P253; -.
DR Antibodypedia; 23197; 192 antibodies from 24 providers.
DR DNASU; 57617; -.
DR Ensembl; ENST00000220509.10; ENSP00000220509.5; ENSG00000104142.11.
DR GeneID; 57617; -.
DR KEGG; hsa:57617; -.
DR MANE-Select; ENST00000220509.10; ENSP00000220509.5; NM_020857.3; NP_065908.1.
DR UCSC; uc001zne.3; human.
DR AGR; HGNC:15972; -.
DR CTD; 57617; -.
DR DisGeNET; 57617; -.
DR GeneCards; VPS18; -.
DR HGNC; HGNC:15972; VPS18.
DR HPA; ENSG00000104142; Low tissue specificity.
DR MIM; 608551; gene.
DR neXtProt; NX_Q9P253; -.
DR OpenTargets; ENSG00000104142; -.
DR PharmGKB; PA38069; -.
DR VEuPathDB; HostDB:ENSG00000104142; -.
DR eggNOG; KOG2034; Eukaryota.
DR GeneTree; ENSGT00940000153635; -.
DR HOGENOM; CLU_003488_1_0_1; -.
DR InParanoid; Q9P253; -.
DR OMA; WIQREKW; -.
DR OrthoDB; 22879at2759; -.
DR PhylomeDB; Q9P253; -.
DR TreeFam; TF105704; -.
DR PathwayCommons; Q9P253; -.
DR Reactome; R-HSA-9754560; SARS-CoV-2 modulates autophagy.
DR SignaLink; Q9P253; -.
DR SIGNOR; Q9P253; -.
DR BioGRID-ORCS; 57617; 615 hits in 1206 CRISPR screens.
DR ChiTaRS; VPS18; human.
DR GeneWiki; VPS18; -.
DR GenomeRNAi; 57617; -.
DR Pharos; Q9P253; Tbio.
DR PRO; PR:Q9P253; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9P253; Protein.
DR Bgee; ENSG00000104142; Expressed in pancreatic ductal cell and 158 other cell types or tissues.
DR ExpressionAtlas; Q9P253; baseline and differential.
DR Genevisible; Q9P253; HS.
DR GO; GO:0005884; C:actin filament; IEA:Ensembl.
DR GO; GO:0030123; C:AP-3 adaptor complex; IEA:Ensembl.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0033263; C:CORVET complex; NAS:ComplexPortal.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030897; C:HOPS complex; IDA:UniProtKB.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:FlyBase.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0034058; P:endosomal vesicle fusion; NAS:ComplexPortal.
DR GO; GO:0007032; P:endosome organization; IDA:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0007040; P:lysosome organization; IDA:UniProtKB.
DR GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; IGI:FlyBase.
DR GO; GO:0048284; P:organelle fusion; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IMP:FlyBase.
DR GO; GO:0035542; P:regulation of SNARE complex assembly; NAS:ComplexPortal.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR GO; GO:0046718; P:viral entry into host cell; IEA:Ensembl.
DR CDD; cd16689; RING-H2_Vps18; 1.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR007810; Pep3_Vps18.
DR PANTHER; PTHR23323; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR23323:SF26; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 18 HOMOLOG; 1.
DR Pfam; PF05131; Pep3_Vps18; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50236; CHCR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Autophagy; Coiled coil; Cytoplasmic vesicle; Endosome;
KW Lysosome; Membrane; Metal-binding; Phosphoprotein; Protein transport;
KW Reference proteome; Transport; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..973
FT /note="Vacuolar protein sorting-associated protein 18
FT homolog"
FT /id="PRO_0000055906"
FT REPEAT 618..772
FT /note="CHCR"
FT ZN_FING 853..947
FT /note="RING-type"
FT REGION 903..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 454..481
FT /evidence="ECO:0000255"
FT COILED 802..848
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 362
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 912
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 913
FT /note="A -> S (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035950"
SQ SEQUENCE 973 AA; 110186 MW; 0008E21D66E8CFEC CRC64;
MASILDEYEN SLSRSAVLQP GCPSVGIPHS GYVNAQLEKE VPIFTKQRID FTPSERITSL
VVSSNQLCMS LGKDTLLRID LGKANEPNHV ELGRKDDAKV HKMFLDHTGS HLLIALSSTE
VLYVNRNGQK VRPLARWKGQ LVESVGWNKA LGTESSTGPI LVGTAQGHIF EAELSASEGG
LFGPAPDLYF RPLYVLNEEG GPAPVCSLEA ERGPDGRSFV IATTRQRLFQ FIGRAAEGAE
AQGFSGLFAA YTDHPPPFRE FPSNLGYSEL AFYTPKLRSA PRAFAWMMGD GVLYGALDCG
RPDSLLSEER VWEYPEGVGP GASPPLAIVL TQFHFLLLLA DRVEAVCTLT GQVVLRDHFL
EKFGPLKHMV KDSSTGQLWA YTERAVFRYH VQREARDVWR TYLDMNRFDL AKEYCRERPD
CLDTVLAREA DFCFRQRRYL ESARCYALTQ SYFEEIALKF LEARQEEALA EFLQRKLASL
KPAERTQATL LTTWLTELYL SRLGALQGDP EALTLYRETK ECFRTFLSSP RHKEWLFASR
ASIHELLASH GDTEHMVYFA VIMQDYERVV AYHCQHEAYE EALAVLARHR DPQLFYKFSP
ILIRHIPRQL VDAWIEMGSR LDARQLIPAL VNYSQGGEVQ QVSQAIRYME FCVNVLGETE
QAIHNYLLSL YARGRPDSLL AYLEQAGASP HRVHYDLKYA LRLCAEHGHH RACVHVYKVL
ELYEEAVDLA LQVDVDLAKQ CADLPEEDEE LRKKLWLKIA RHVVQEEEDV QTAMACLASC
PLLKIEDVLP FFPDFVTIDH FKEAICSSLK AYNHHIQELQ REMEEATASA QRIRRDLQEL
RGRYGTVEPQ DKCATCDFPL LNRPFYLFLC GHMFHADCLL QAVRPGLPAY KQARLEELQR
KLGAAPPPAK GSARAKEAEG GAATAGPSRE QLKADLDELV AAECVYCGEL MIRSIDRPFI
DPQRYEEEQL SWL
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