VPS52_HUMAN
ID VPS52_HUMAN Reviewed; 723 AA.
AC Q8N1B4; A2BF38; B0UZZ4; B4DNI9; Q53GR4; Q5JPA0; Q5SQW1; Q8IUN6; Q9NPT5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Vacuolar protein sorting-associated protein 52 homolog;
DE AltName: Full=SAC2 suppressor of actin mutations 2-like protein;
GN Name=VPS52; Synonyms=SACM2L;
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] (ISOFORM 2).
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] (ISOFORM 1).
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Colon;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 255-723 (ISOFORM 1).
RC TISSUE=Brain;
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 [7]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND INTERACTION WITH RAB6A AND
RP STX10.
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 [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [9]
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 [10]
RP INTERACTION WITH UHRF1BP1L.
RX PubMed=20163565; DOI=10.1111/j.1600-0854.2010.01049.x;
RA Otto G.P., Razi M., Morvan J., Stenner F., Tooze S.A.;
RT "A novel syntaxin 6-interacting protein, SHIP164, regulates syntaxin 6-
RT dependent sorting from early endosomes.";
RL Traffic 11:688-705(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 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 [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=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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, AND IDENTIFICATION BY
RP 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 [15]
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 [16]
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).
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,
CC PubMed:20685960). Component of the endosome-associated retrograde
CC protein (EARP) complex, composed of VPS51, VPS52, VPS53 and
CC VPS50/Syndetin (PubMed:25799061, PubMed:27440922). EIPR1 interacts with
CC both EARP and GARP complexes and mediates the recruitment of the GARP
CC complex to the trans-Golgi network (PubMed:27440922). Interacts with
CC RAB6A and STX10 (PubMed:15878329, PubMed:20685960). Interacts with
CC UHRF1BP1L (PubMed:20163565). {ECO:0000269|PubMed:15878329,
CC ECO:0000269|PubMed:20163565, ECO:0000269|PubMed:20685960,
CC ECO:0000269|PubMed:25799061, ECO:0000269|PubMed:27440922}.
CC -!- INTERACTION:
CC Q8N1B4; C9JG97: AAMP; NbExp=3; IntAct=EBI-2799833, EBI-10176499;
CC Q8N1B4; Q6PJ05: ATP6V1D; NbExp=3; IntAct=EBI-2799833, EBI-10253919;
CC Q8N1B4; Q8N5Z9: ATP6V1D; NbExp=3; IntAct=EBI-2799833, EBI-10266952;
CC Q8N1B4; Q9Y5K8: ATP6V1D; NbExp=6; IntAct=EBI-2799833, EBI-2684998;
CC Q8N1B4; Q96GS4: BORCS6; NbExp=3; IntAct=EBI-2799833, EBI-10193358;
CC Q8N1B4; Q13895: BYSL; NbExp=3; IntAct=EBI-2799833, EBI-358049;
CC Q8N1B4; Q9NX04: C1orf109; NbExp=6; IntAct=EBI-2799833, EBI-8643161;
CC Q8N1B4; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-2799833, EBI-747505;
CC Q8N1B4; Q53TS8: C2CD6; NbExp=3; IntAct=EBI-2799833, EBI-739879;
CC Q8N1B4; Q9NP86: CABP5; NbExp=3; IntAct=EBI-2799833, EBI-10311131;
CC Q8N1B4; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-2799833, EBI-10171570;
CC Q8N1B4; Q8IYE1: CCDC13; NbExp=3; IntAct=EBI-2799833, EBI-10961312;
CC Q8N1B4; Q8IYE0: CCDC146; NbExp=3; IntAct=EBI-2799833, EBI-10749669;
CC Q8N1B4; Q8IYE0-2: CCDC146; NbExp=3; IntAct=EBI-2799833, EBI-10247802;
CC Q8N1B4; Q8N715: CCDC185; NbExp=3; IntAct=EBI-2799833, EBI-740814;
CC Q8N1B4; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-2799833, EBI-10961624;
CC Q8N1B4; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-2799833, EBI-10175300;
CC Q8N1B4; Q86Y33-5: CDC20B; NbExp=3; IntAct=EBI-2799833, EBI-11983537;
CC Q8N1B4; Q99459: CDC5L; NbExp=3; IntAct=EBI-2799833, EBI-374880;
CC Q8N1B4; Q07002: CDK18; NbExp=3; IntAct=EBI-2799833, EBI-746238;
CC Q8N1B4; Q96LK0: CEP19; NbExp=3; IntAct=EBI-2799833, EBI-741885;
CC Q8N1B4; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-2799833, EBI-749051;
CC Q8N1B4; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-2799833, EBI-5453285;
CC Q8N1B4; O43602-2: DCX; NbExp=3; IntAct=EBI-2799833, EBI-14148644;
CC Q8N1B4; P26196: DDX6; NbExp=6; IntAct=EBI-2799833, EBI-351257;
CC Q8N1B4; Q9NVH1: DNAJC11; NbExp=3; IntAct=EBI-2799833, EBI-1055336;
CC Q8N1B4; O60941-5: DTNB; NbExp=3; IntAct=EBI-2799833, EBI-11984733;
CC Q8N1B4; Q7L775: EPM2AIP1; NbExp=6; IntAct=EBI-2799833, EBI-6255981;
CC Q8N1B4; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-2799833, EBI-1752811;
CC Q8N1B4; Q3B820: FAM161A; NbExp=3; IntAct=EBI-2799833, EBI-719941;
CC Q8N1B4; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-2799833, EBI-7225287;
CC Q8N1B4; Q6P9G8: FAM184A; NbExp=3; IntAct=EBI-2799833, EBI-10253239;
CC Q8N1B4; Q9Y247: FAM50B; NbExp=3; IntAct=EBI-2799833, EBI-742802;
CC Q8N1B4; P55040: GEM; NbExp=3; IntAct=EBI-2799833, EBI-744104;
CC Q8N1B4; Q969S9: GFM2; NbExp=3; IntAct=EBI-2799833, EBI-2371750;
CC Q8N1B4; Q92805: GOLGA1; NbExp=6; IntAct=EBI-2799833, EBI-6164177;
CC Q8N1B4; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-2799833, EBI-739467;
CC Q8N1B4; Q92917: GPKOW; NbExp=3; IntAct=EBI-2799833, EBI-746309;
CC Q8N1B4; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-2799833, EBI-2514791;
CC Q8N1B4; P56524-2: HDAC4; NbExp=3; IntAct=EBI-2799833, EBI-11953488;
CC Q8N1B4; Q96ES5: HEATR1; NbExp=3; IntAct=EBI-2799833, EBI-10285245;
CC Q8N1B4; V9HW29: HEL-S-61; NbExp=3; IntAct=EBI-2799833, EBI-10330057;
CC Q8N1B4; A0A0S2Z4Q4: HGS; NbExp=3; IntAct=EBI-2799833, EBI-16429135;
CC Q8N1B4; O14964: HGS; NbExp=3; IntAct=EBI-2799833, EBI-740220;
CC Q8N1B4; P09067: HOXB5; NbExp=3; IntAct=EBI-2799833, EBI-3893317;
CC Q8N1B4; Q96AA8: JAKMIP2; NbExp=3; IntAct=EBI-2799833, EBI-752007;
CC Q8N1B4; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-2799833, EBI-2556193;
CC Q8N1B4; Q5T5P2-6: KIAA1217; NbExp=3; IntAct=EBI-2799833, EBI-10188326;
CC Q8N1B4; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-2799833, EBI-8472129;
CC Q8N1B4; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-2799833, EBI-14069005;
CC Q8N1B4; Q6P597: KLC3; NbExp=3; IntAct=EBI-2799833, EBI-1643885;
CC Q8N1B4; Q9P2K6: KLHL42; NbExp=3; IntAct=EBI-2799833, EBI-739890;
CC Q8N1B4; P61968: LMO4; NbExp=3; IntAct=EBI-2799833, EBI-2798728;
CC Q8N1B4; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-2799833, EBI-739832;
CC Q8N1B4; Q8N6R0: METTL13; NbExp=3; IntAct=EBI-2799833, EBI-1053295;
CC Q8N1B4; P55081: MFAP1; NbExp=6; IntAct=EBI-2799833, EBI-1048159;
CC Q8N1B4; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-2799833, EBI-14086479;
CC Q8N1B4; Q9BYD6: MRPL1; NbExp=3; IntAct=EBI-2799833, EBI-5325394;
CC Q8N1B4; Q9Y3B7: MRPL11; NbExp=3; IntAct=EBI-2799833, EBI-5453723;
CC Q8N1B4; O14777: NDC80; NbExp=3; IntAct=EBI-2799833, EBI-715849;
CC Q8N1B4; Q15653: NFKBIB; NbExp=3; IntAct=EBI-2799833, EBI-352889;
CC Q8N1B4; P46087: NOP2; NbExp=3; IntAct=EBI-2799833, EBI-356811;
CC Q8N1B4; Q86WQ0: NR2C2AP; NbExp=3; IntAct=EBI-2799833, EBI-10260040;
CC Q8N1B4; Q7L8S5: OTUD6A; NbExp=3; IntAct=EBI-2799833, EBI-11960139;
CC Q8N1B4; Q9BSJ6: PIMREG; NbExp=3; IntAct=EBI-2799833, EBI-2568609;
CC Q8N1B4; Q6P5Z2: PKN3; NbExp=3; IntAct=EBI-2799833, EBI-1384335;
CC Q8N1B4; Q6NYC8: PPP1R18; NbExp=6; IntAct=EBI-2799833, EBI-2557469;
CC Q8N1B4; Q13131: PRKAA1; NbExp=3; IntAct=EBI-2799833, EBI-1181405;
CC Q8N1B4; P54646: PRKAA2; NbExp=3; IntAct=EBI-2799833, EBI-1383852;
CC Q8N1B4; P20338: RAB4A; NbExp=4; IntAct=EBI-2799833, EBI-722284;
CC Q8N1B4; P61018: RAB4B; NbExp=3; IntAct=EBI-2799833, EBI-10218066;
CC Q8N1B4; Q9H4P4: RNF41; NbExp=6; IntAct=EBI-2799833, EBI-2130266;
CC Q8N1B4; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-2799833, EBI-11984663;
CC Q8N1B4; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-2799833, EBI-748391;
CC Q8N1B4; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-2799833, EBI-747035;
CC Q8N1B4; Q969G3: SMARCE1; NbExp=3; IntAct=EBI-2799833, EBI-455078;
CC Q8N1B4; O75558: STX11; NbExp=3; IntAct=EBI-2799833, EBI-714135;
CC Q8N1B4; Q9NYJ8: TAB2; NbExp=3; IntAct=EBI-2799833, EBI-358708;
CC Q8N1B4; Q86TI0: TBC1D1; NbExp=3; IntAct=EBI-2799833, EBI-1644036;
CC Q8N1B4; Q9NU19: TBC1D22B; NbExp=7; IntAct=EBI-2799833, EBI-8787464;
CC Q8N1B4; Q8N8B7: TCEANC; NbExp=3; IntAct=EBI-2799833, EBI-954696;
CC Q8N1B4; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-2799833, EBI-11955057;
CC Q8N1B4; Q9NUJ3: TCP11L1; NbExp=3; IntAct=EBI-2799833, EBI-2555179;
CC Q8N1B4; D3DUQ6: TEAD4; NbExp=3; IntAct=EBI-2799833, EBI-10176734;
CC Q8N1B4; Q15561: TEAD4; NbExp=3; IntAct=EBI-2799833, EBI-747736;
CC Q8N1B4; Q96EK4: THAP11; NbExp=3; IntAct=EBI-2799833, EBI-1790529;
CC Q8N1B4; P06753: TPM3; NbExp=3; IntAct=EBI-2799833, EBI-355607;
CC Q8N1B4; Q5VU62: TPM3; NbExp=3; IntAct=EBI-2799833, EBI-10184033;
CC Q8N1B4; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-2799833, EBI-3650647;
CC Q8N1B4; Q9Y4K3: TRAF6; NbExp=6; IntAct=EBI-2799833, EBI-359276;
CC Q8N1B4; Q96PN8: TSSK3; NbExp=6; IntAct=EBI-2799833, EBI-3918381;
CC Q8N1B4; Q5T7W7: TSTD2; NbExp=6; IntAct=EBI-2799833, EBI-8994397;
CC Q8N1B4; P40222: TXLNA; NbExp=6; IntAct=EBI-2799833, EBI-359793;
CC Q8N1B4; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-2799833, EBI-6116822;
CC Q8N1B4; Q99757: TXN2; NbExp=6; IntAct=EBI-2799833, EBI-2932492;
CC Q8N1B4; O75604: USP2; NbExp=6; IntAct=EBI-2799833, EBI-743272;
CC Q8N1B4; Q14119: VEZF1; NbExp=3; IntAct=EBI-2799833, EBI-11980193;
CC Q8N1B4; Q548N1: VPS28; NbExp=3; IntAct=EBI-2799833, EBI-10243107;
CC Q8N1B4; Q9UK41: VPS28; NbExp=4; IntAct=EBI-2799833, EBI-727424;
CC Q8N1B4; Q96JG6: VPS50; NbExp=8; IntAct=EBI-2799833, EBI-11044388;
CC Q8N1B4; Q9UID3-1: VPS51; NbExp=4; IntAct=EBI-2799833, EBI-16067837;
CC Q8N1B4; Q9Y3C0: WASHC3; NbExp=3; IntAct=EBI-2799833, EBI-712969;
CC Q8N1B4; Q15007: WTAP; NbExp=6; IntAct=EBI-2799833, EBI-751647;
CC Q8N1B4; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-2799833, EBI-14104088;
CC Q8N1B4; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-2799833, EBI-2682299;
CC Q8N1B4; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-2799833, EBI-740727;
CC Q8N1B4; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-2799833, EBI-6427977;
CC Q8N1B4; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-2799833, EBI-25492395;
CC Q8N1B4; PRO_0000037551 [Q9WMX2]; Xeno; NbExp=2; IntAct=EBI-2799833, EBI-6863748;
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=2;
CC Name=1;
CC IsoId=Q8N1B4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N1B4-2; Sequence=VSP_056476;
CC -!- SIMILARITY: Belongs to the VPS52 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI95619.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK297935; BAG60251.1; -; mRNA.
DR EMBL; AK222867; BAD96587.1; -; mRNA.
DR EMBL; AL645940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031228; CAI95619.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BX248408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR762434; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03688.1; -; Genomic_DNA.
DR EMBL; BC032108; AAH32108.1; -; mRNA.
DR EMBL; BC040114; AAH40114.2; -; mRNA.
DR EMBL; AL390171; CAB99099.1; -; mRNA.
DR CCDS; CCDS4770.2; -. [Q8N1B4-1]
DR PIR; T51882; T51882.
DR RefSeq; NP_001276104.1; NM_001289175.1. [Q8N1B4-2]
DR RefSeq; NP_001276105.1; NM_001289176.1.
DR RefSeq; NP_072047.4; NM_022553.5. [Q8N1B4-1]
DR RefSeq; XP_016866667.1; XM_017011178.1. [Q8N1B4-2]
DR AlphaFoldDB; Q8N1B4; -.
DR BioGRID; 112200; 184.
DR ComplexPortal; CPX-6207; EARP tethering complex.
DR ComplexPortal; CPX-6208; GARP tethering complex.
DR CORUM; Q8N1B4; -.
DR DIP; DIP-57843N; -.
DR IntAct; Q8N1B4; 143.
DR MINT; Q8N1B4; -.
DR STRING; 9606.ENSP00000409952; -.
DR iPTMnet; Q8N1B4; -.
DR MetOSite; Q8N1B4; -.
DR PhosphoSitePlus; Q8N1B4; -.
DR BioMuta; VPS52; -.
DR DMDM; 74750887; -.
DR EPD; Q8N1B4; -.
DR jPOST; Q8N1B4; -.
DR MassIVE; Q8N1B4; -.
DR MaxQB; Q8N1B4; -.
DR PaxDb; Q8N1B4; -.
DR PeptideAtlas; Q8N1B4; -.
DR PRIDE; Q8N1B4; -.
DR ProteomicsDB; 4699; -.
DR ProteomicsDB; 71582; -. [Q8N1B4-1]
DR Antibodypedia; 28991; 134 antibodies from 22 providers.
DR DNASU; 6293; -.
DR Ensembl; ENST00000383210.4; ENSP00000372697.4; ENSG00000206286.11. [Q8N1B4-1]
DR Ensembl; ENST00000428608.2; ENSP00000406988.2; ENSG00000236014.10. [Q8N1B4-1]
DR Ensembl; ENST00000441058.2; ENSP00000390831.2; ENSG00000228425.9. [Q8N1B4-1]
DR Ensembl; ENST00000443860.2; ENSP00000404016.2; ENSG00000224455.9. [Q8N1B4-1]
DR Ensembl; ENST00000445902.3; ENSP00000409952.2; ENSG00000223501.9. [Q8N1B4-1]
DR Ensembl; ENST00000448042.2; ENSP00000391197.2; ENSG00000225590.9. [Q8N1B4-1]
DR GeneID; 6293; -.
DR KEGG; hsa:6293; -.
DR MANE-Select; ENST00000445902.3; ENSP00000409952.2; NM_022553.6; NP_072047.4.
DR UCSC; uc003odm.3; human. [Q8N1B4-1]
DR CTD; 6293; -.
DR DisGeNET; 6293; -.
DR GeneCards; VPS52; -.
DR HGNC; HGNC:10518; VPS52.
DR HPA; ENSG00000223501; Low tissue specificity.
DR MIM; 603443; gene.
DR neXtProt; NX_Q8N1B4; -.
DR OpenTargets; ENSG00000223501; -.
DR PharmGKB; PA34926; -.
DR VEuPathDB; HostDB:ENSG00000223501; -.
DR eggNOG; KOG1961; Eukaryota.
DR GeneTree; ENSGT00390000008815; -.
DR HOGENOM; CLU_010797_0_0_1; -.
DR InParanoid; Q8N1B4; -.
DR OMA; IHVVMVE; -.
DR PhylomeDB; Q8N1B4; -.
DR TreeFam; TF314937; -.
DR PathwayCommons; Q8N1B4; -.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR SignaLink; Q8N1B4; -.
DR BioGRID-ORCS; 6293; 189 hits in 1091 CRISPR screens.
DR ChiTaRS; VPS52; human.
DR GeneWiki; VPS52; -.
DR GenomeRNAi; 6293; -.
DR Pharos; Q8N1B4; Tbio.
DR PRO; PR:Q8N1B4; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8N1B4; protein.
DR Bgee; ENSG00000223501; Expressed in right lobe of thyroid gland and 93 other tissues.
DR ExpressionAtlas; Q8N1B4; baseline and differential.
DR Genevisible; Q8N1B4; HS.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
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: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:0019905; F:syntaxin binding; IPI:UniProtKB.
DR GO; GO:0010668; P:ectodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0048611; P:embryonic ectodermal digestive tract development; IEA:Ensembl.
DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central.
DR GO; GO:0007041; P:lysosomal transport; IDA:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR InterPro; IPR007258; Vps52.
DR PANTHER; PTHR14190; PTHR14190; 1.
DR Pfam; PF04129; Vps52; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Endosome; Golgi apparatus;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..723
FT /note="Vacuolar protein sorting-associated protein 52
FT homolog"
FT /id="PRO_0000213315"
FT COILED 107..127
FT /evidence="ECO:0000255"
FT COILED 194..215
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 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..125
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056476"
FT CONFLICT 710
FT /note="H -> P (in Ref. 2; BAD96587)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 723 AA; 82221 MW; C0961E2BE50B24DF CRC64;
MAAAATMAAA ARELVLRAGT SDMEEEEGPL AGGPGLQEPL QLGELDITSD EFILDEVDVH
IQANLEDELV KEALKTGVDL RHYSKQVELE LQQIEQKSIR DYIQESENIA SLHNQITACD
AVLERMEQML GAFQSDLSSI SSEIRTLQEQ SGAMNIRLRN RQAVRGKLGE LVDGLVVPSA
LVTAILEAPV TEPRFLEQLQ ELDAKAAAVR EQEARGTAAC ADVRGVLDRL RVKAVTKIRE
FILQKIYSFR KPMTNYQIPQ TALLKYRFFY QFLLGNERAT AKEIRDEYVE TLSKIYLSYY
RSYLGRLMKV QYEEVAEKDD LMGVEDTAKK GFFSKPSLRS RNTIFTLGTR GSVISPTELE
APILVPHTAQ RGEQRYPFEA LFRSQHYALL DNSCREYLFI CEFFVVSGPA AHDLFHAVMG
RTLSMTLKHL DSYLADCYDA IAVFLCIHIV LRFRNIAAKR DVPALDRYWE QVLALLWPRF
ELILEMNVQS VRSTDPQRLG GLDTRPHYIT RRYAEFSSAL VSINQTIPNE RTMQLLGQLQ
VEVENFVLRV AAEFSSRKEQ LVFLINNYDM MLGVLMERAA DDSKEVESFQ QLLNARTQEF
IEELLSPPFG GLVAFVKEAE ALIERGQAER LRGEEARVTQ LIRGFGSSWK SSVESLSQDV
MRSFTNFRNG TSIIQGALTQ LIQLYHRFHR VLSQPQLRAL PARAELINIH HLMVELKKHK
PNF
