VPS53_HUMAN
ID VPS53_HUMAN Reviewed; 832 AA.
AC Q5VIR6; A8K2S8; B3FH42; Q8WYW3; Q9BRR2; Q9BY02; Q9NV25;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Vacuolar protein sorting-associated protein 53 homolog;
GN Name=VPS53; ORFNames=PP13624;
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] (ISOFORM 2), FUNCTION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15878329; DOI=10.1016/j.yexcr.2005.01.022;
RA Liewen H., Meinhold-Heerlein I., Oliveira V., Schwarzenbacher R., Luo G.,
RA Wadle A., Jung M., Pfreundschuh M., Stenner-Liewen F.;
RT "Characterization of the human GARP (Golgi associated retrograde protein)
RT complex.";
RL Exp. Cell Res. 306:24-34(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RX PubMed=12565177; DOI=10.1016/s0304-3835(02)00622-5;
RA Zhao X., He M., Wan D., Ye Y., He Y., Han L., Guo M., Huang Y., Qin W.,
RA Wang M.W., Chong W., Chen J., Zhang L., Yang N., Xu B., Wu M., Zuo L.,
RA Gu J.;
RT "The minimum LOH region defined on chromosome 17p13.3 in human
RT hepatocellular carcinoma with gene content analysis.";
RL Cancer Lett. 190:221-232(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=18367545; DOI=10.1091/mbc.e07-11-1189;
RA Perez-Victoria F.J., Mardones G.A., Bonifacino J.S.;
RT "Requirement of the human GARP complex for mannose 6-phosphate-receptor-
RT dependent sorting of cathepsin D to lysosomes.";
RL Mol. Biol. Cell 19:2350-2362(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Placenta, and Tongue;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Placenta;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-657 (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 AND THR-391, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-110 AND LYS-360, AND
RP IDENTIFICATION BY MASS 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 [11]
RP INTERACTION WITH VPS51.
RX PubMed=20685960; DOI=10.1091/mbc.e10-05-0392;
RA Perez-Victoria F.J., Schindler C., Magadan J.G., Mardones G.A.,
RA Delevoye C., Romao M., Raposo G., Bonifacino J.S.;
RT "Ang2/fat-free is a conserved subunit of the Golgi-associated retrograde
RT protein complex.";
RL Mol. Biol. Cell 21:3386-3395(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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 [14]
RP INVOLVEMENT IN PCH2E, AND VARIANT PCH2E ARG-695.
RX PubMed=24577744; DOI=10.1136/jmedgenet-2013-101823;
RA Feinstein M., Flusser H., Lerman-Sagie T., Ben-Zeev B., Lev D., Agamy O.,
RA Cohen I., Kadir R., Sivan S., Leshinsky-Silver E., Markus B., Birk O.S.;
RT "VPS53 mutations cause progressive cerebello-cerebral atrophy type 2
RT (PCCA2).";
RL J. Med. Genet. 51:303-308(2014).
RN [15]
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).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE EARP COMPLEX.
RX PubMed=25799061; DOI=10.1038/ncb3129;
RA Schindler C., Chen Y., Pu J., Guo X., Bonifacino J.S.;
RT "EARP is a multisubunit tethering complex involved in endocytic
RT recycling.";
RL Nat. Cell Biol. 17:639-650(2015).
RN [17]
RP INTERACTION WITH EIPR1, IDENTIFICATION IN THE EARP COMPLEX, AND
RP IDENTIFICATION IN THE GARP COMPLEX.
RX PubMed=27440922; DOI=10.1091/mbc.e16-04-0209;
RA Gershlick D.C., Schindler C., Chen Y., Bonifacino J.S.;
RT "TSSC1 is novel component of the endosomal retrieval machinery.";
RL Mol. Biol. Cell 27:2867-2878(2016).
RN [18]
RP INTERACTION WITH VPS50.
RX PubMed=31721635; DOI=10.1091/mbc.e18-07-0469;
RA Topalidou I., Cattin-Ortola J., Hummer B., Asensio C.S., Ailion M.;
RT "EIPR1 controls dense-core vesicle cargo retention and EARP complex
RT localization in insulin-secreting cells.";
RL Mol. Biol. Cell 31:59-79(2020).
CC -!- FUNCTION: Acts as component of the GARP complex that is involved in
CC retrograde transport from early and late endosomes to the trans-Golgi
CC network (TGN). The GARP complex is required for the maintenance of the
CC cycling of mannose 6-phosphate receptors between the TGN and endosomes,
CC this cycling is necessary for proper lysosomal sorting of acid
CC hydrolases such as CTSD (PubMed:15878329, PubMed:18367545). Acts as
CC component of the EARP complex that is involved in endocytic recycling.
CC The EARP complex associates with Rab4-positive endosomes and promotes
CC recycling of internalized transferrin receptor (TFRC) to the plasma
CC membrane (PubMed:25799061). {ECO:0000269|PubMed:15878329,
CC ECO:0000269|PubMed:18367545, ECO:0000269|PubMed:25799061}.
CC -!- SUBUNIT: Component of the Golgi-associated retrograde protein (GARP)
CC complex, also called VFT (VPS fifty-three) complex, composed of VPS51,
CC VPS52, VPS53 and VPS54 (PubMed:27440922, PubMed:15878329). Component of
CC the endosome-associated retrograde protein (EARP) complex, composed of
CC VPS51, VPS52, VPS53 and VPS50/Syndetin (PubMed:25799061,
CC PubMed:27440922). EIPR1 interacts with both EARP and GARP complexes and
CC mediates the recruitment of the GARP complex to the trans-Golgi network
CC (PubMed:27440922). Interacts with VPS50 in an EIPR1-independent manner
CC (PubMed:31721635). {ECO:0000269|PubMed:15878329,
CC ECO:0000269|PubMed:25799061, ECO:0000269|PubMed:27440922,
CC ECO:0000269|PubMed:31721635}.
CC -!- INTERACTION:
CC Q5VIR6; Q96JG6: VPS50; NbExp=8; IntAct=EBI-2850511, EBI-11044388;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:15878329, ECO:0000269|PubMed:18367545}; Peripheral
CC membrane protein. Endosome membrane {ECO:0000269|PubMed:18367545};
CC Peripheral membrane protein. Recycling endosome
CC {ECO:0000269|PubMed:25799061}. Note=Localizes to the trans-Golgi
CC network as part of the GARP complex, while it localizes to recycling
CC endosomes as part of the EARP complex (PubMed:25799061).
CC {ECO:0000269|PubMed:25799061}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5VIR6-4; Sequence=Displayed;
CC Name=2; Synonyms=long;
CC IsoId=Q5VIR6-1; Sequence=VSP_060664, VSP_060665;
CC Name=3; Synonyms=short;
CC IsoId=Q5VIR6-2; Sequence=VSP_060662, VSP_060664, VSP_060665;
CC Name=4;
CC IsoId=Q5VIR6-3; Sequence=VSP_060787, VSP_060663;
CC -!- DISEASE: Pontocerebellar hypoplasia 2E (PCH2E) [MIM:615851]: An
CC autosomal recessive neurodegenerative disorder characterized by
CC progressive cerebello-cerebral atrophy, profound intellectual
CC disability, progressive microcephaly, spasticity, and early-onset
CC epilepsy. {ECO:0000269|PubMed:24577744}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the VPS53 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL55842.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=BAA91935.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY444797; AAS20944.1; -; mRNA.
DR EMBL; AF246287; AAK27973.1; -; mRNA.
DR EMBL; EU021218; ABW03005.1; -; mRNA.
DR EMBL; AK001841; BAA91935.1; ALT_INIT; mRNA.
DR EMBL; AK290343; BAF83032.1; -; mRNA.
DR EMBL; AC015853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC027455; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471108; EAW90661.1; -; Genomic_DNA.
DR EMBL; BC006116; AAH06116.1; -; mRNA.
DR EMBL; AF318335; AAL55842.1; ALT_SEQ; mRNA.
DR CCDS; CCDS10995.1; -. [Q5VIR6-2]
DR CCDS; CCDS45558.1; -. [Q5VIR6-4]
DR RefSeq; NP_001121631.1; NM_001128159.2. [Q5VIR6-4]
DR RefSeq; NP_060759.2; NM_018289.3. [Q5VIR6-2]
DR AlphaFoldDB; Q5VIR6; -.
DR SMR; Q5VIR6; -.
DR BioGRID; 120563; 136.
DR ComplexPortal; CPX-6207; EARP tethering complex.
DR ComplexPortal; CPX-6208; GARP tethering complex.
DR CORUM; Q5VIR6; -.
DR DIP; DIP-59352N; -.
DR IntAct; Q5VIR6; 22.
DR MINT; Q5VIR6; -.
DR STRING; 9606.ENSP00000401435; -.
DR iPTMnet; Q5VIR6; -.
DR PhosphoSitePlus; Q5VIR6; -.
DR BioMuta; VPS53; -.
DR DMDM; 74746777; -.
DR EPD; Q5VIR6; -.
DR jPOST; Q5VIR6; -.
DR MassIVE; Q5VIR6; -.
DR MaxQB; Q5VIR6; -.
DR PaxDb; Q5VIR6; -.
DR PeptideAtlas; Q5VIR6; -.
DR PRIDE; Q5VIR6; -.
DR ProteomicsDB; 65251; -. [Q5VIR6-1]
DR ProteomicsDB; 65252; -. [Q5VIR6-2]
DR ProteomicsDB; 65253; -. [Q5VIR6-3]
DR ProteomicsDB; 65254; -. [Q5VIR6-4]
DR Antibodypedia; 10256; 134 antibodies from 26 providers.
DR DNASU; 55275; -.
DR Ensembl; ENST00000291074.10; ENSP00000291074.5; ENSG00000141252.21. [Q5VIR6-2]
DR Ensembl; ENST00000437048.7; ENSP00000401435.2; ENSG00000141252.21. [Q5VIR6-4]
DR Ensembl; ENST00000571805.6; ENSP00000459312.1; ENSG00000141252.21. [Q5VIR6-1]
DR Ensembl; ENST00000638350.1; ENSP00000492070.1; ENSG00000283883.2. [Q5VIR6-2]
DR Ensembl; ENST00000639801.2; ENSP00000492761.1; ENSG00000283883.2. [Q5VIR6-4]
DR Ensembl; ENST00000639896.1; ENSP00000492119.1; ENSG00000283883.2. [Q5VIR6-1]
DR Ensembl; ENST00000680069.1; ENSP00000505145.1; ENSG00000141252.21. [Q5VIR6-3]
DR Ensembl; ENST00000680465.1; ENSP00000505997.1; ENSG00000141252.21. [Q5VIR6-4]
DR GeneID; 55275; -.
DR KEGG; hsa:55275; -.
DR MANE-Select; ENST00000437048.7; ENSP00000401435.2; NM_001128159.3; NP_001121631.1.
DR UCSC; uc002frm.3; human. [Q5VIR6-4]
DR CTD; 55275; -.
DR DisGeNET; 55275; -.
DR GeneCards; VPS53; -.
DR HGNC; HGNC:25608; VPS53.
DR HPA; ENSG00000141252; Low tissue specificity.
DR MalaCards; VPS53; -.
DR MIM; 615850; gene.
DR MIM; 615851; phenotype.
DR neXtProt; NX_Q5VIR6; -.
DR OpenTargets; ENSG00000141252; -.
DR Orphanet; 247198; Progressive cerebello-cerebral atrophy.
DR PharmGKB; PA142670618; -.
DR VEuPathDB; HostDB:ENSG00000141252; -.
DR eggNOG; KOG2180; Eukaryota.
DR GeneTree; ENSGT00390000015165; -.
DR HOGENOM; CLU_007339_0_0_1; -.
DR InParanoid; Q5VIR6; -.
DR OMA; YKFAEAK; -.
DR PhylomeDB; Q5VIR6; -.
DR TreeFam; TF106150; -.
DR PathwayCommons; Q5VIR6; -.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR SignaLink; Q5VIR6; -.
DR BioGRID-ORCS; 55275; 134 hits in 1088 CRISPR screens.
DR ChiTaRS; VPS53; human.
DR GenomeRNAi; 55275; -.
DR Pharos; Q5VIR6; Tbio.
DR PRO; PR:Q5VIR6; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q5VIR6; protein.
DR Bgee; ENSG00000141252; Expressed in sural nerve and 105 other tissues.
DR ExpressionAtlas; Q5VIR6; baseline and differential.
DR Genevisible; Q5VIR6; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:1990745; C:EARP complex; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000938; C:GARP complex; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR GO; GO:0007041; P:lysosomal transport; IMP:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR Gene3D; 1.10.357.110; -; 1.
DR InterPro; IPR039766; Vps53.
DR InterPro; IPR038260; Vps53_C_sf.
DR InterPro; IPR007234; Vps53_N.
DR PANTHER; PTHR12820; PTHR12820; 1.
DR Pfam; PF04100; Vps53_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Disease variant; Endosome;
KW Epilepsy; Golgi apparatus; Intellectual disability; Membrane;
KW Neurodegeneration; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..832
FT /note="Vacuolar protein sorting-associated protein 53
FT homolog"
FT /id="PRO_0000215189"
FT REGION 373..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 97..138
FT /evidence="ECO:0000255"
FT COMPBIAS 395..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 110
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 360
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 391
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 96..124
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305|PubMed:14702039,
FT ECO:0000305|PubMed:15489334"
FT /id="VSP_060662"
FT VAR_SEQ 672
FT /note="N -> K (in isoform 4)"
FT /evidence="ECO:0000305|PubMed:12565177"
FT /id="VSP_060787"
FT VAR_SEQ 673..832
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305|PubMed:12565177"
FT /id="VSP_060663"
FT VAR_SEQ 696..699
FT /note="LLLD -> VRWT (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000305|PubMed:14702039,
FT ECO:0000305|PubMed:15489334, ECO:0000305|PubMed:15878329"
FT /id="VSP_060664"
FT VAR_SEQ 700..832
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000305|PubMed:14702039,
FT ECO:0000305|PubMed:15489334, ECO:0000305|PubMed:15878329"
FT /id="VSP_060665"
FT VARIANT 328
FT /note="L -> I (in dbSNP:rs16954056)"
FT /id="VAR_059959"
FT VARIANT 375
FT /note="L -> R (in dbSNP:rs61644407)"
FT /id="VAR_066561"
FT VARIANT 695
FT /note="Q -> R (in PCH2E; dbSNP:rs587777465)"
FT /evidence="ECO:0000269|PubMed:24577744"
FT /id="VAR_071803"
FT CONFLICT 27
FT /note="I -> V (in Ref. 3; ABW03005)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="K -> N (in Ref. 3; ABW03005)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="A -> T (in Ref. 2; AAK27973)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="T -> P (in Ref. 2; AAK27973)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="G -> E (in Ref. 2; AAK27973)"
FT /evidence="ECO:0000305"
FT CONFLICT 656
FT /note="L -> PV (in Ref. 2; AAK27973)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="F -> L (in Ref. 2; AAK27973)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 832 AA; 94405 MW; EA71D35158E9419E CRC64;
MMEEEELEFV EELEAVLQLT PEVQLAIEQV FPSQDPLDRA DFNAVEYINT LFPTEQSLAN
IDEVVNKIRL KIRRLDDNIR TVVRGQTNVG QDGRQALEEA QKAIQQLFGK IKDIKDKAEK
SEQMVKEITR DIKQLDHAKR HLTTSITTLN HLHMLAGGVD SLEAMTRRRQ YGEVANLLQG
VMNVLEHFHK YMGIPQIRQL SERVKAAQTE LGQQILADFE EAFPSQGTKR PGGPSNVLRD
ACLVANILDP RIKQEIIKKF IKQHLSEYLV LFQENQDVAW LDKIDRRYAW IKRQLVDYEE
KYGRMFPREW CMAERIAVEF CHVTRAELAK IMRTRAKEIE VKLLLFAIQR TTNFEGFLAK
RFSGCTLTDG TLKKLESPPP STNPFLEDEP TPEMEELATE KGDLDQPKKP KAPDNPFHGI
VSKCFEPHLY VYIESQDKNL GELIDRFVAD FKAQGPPKPN TDEGGAVLPS CADLFVYYKK
CMVQCSQLST GEPMIALTTI FQKYLREYAW KILSGNLPKT TTSSGGLTIS SLLKEKEGSE
VAKFTLEELC LICNILSTAE YCLATTQQLE EKLKEKVDVS LIERINLTGE MDTFSTVISS
SIQLLVQDLD AACDPALTAM SKMQWQNVEH VGDQSPYVTS VILHIKQNVP IIRDNLASTR
KYFTQFCVKF ANSFIPKFIT HLFKCKPISM VGAEQLLLDT HSLKMVLLDL PSISSQVVRK
APASYTKIVV KGMTRAEMIL KVVMAPHEPL VVFVDNYIKL LTDCNTETFQ KILDMKGLKR
SEQSSMLELL RQRLPAPPSG AESSGSLSLT APTPEQESSR IRKLEKLIKK RL
