VPS50_HUMAN
ID VPS50_HUMAN Reviewed; 964 AA.
AC Q96JG6; B3KX22; D1MQ00; F5H5U7; Q75N07; Q8WVK3; Q9H5C6;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Syndetin {ECO:0000303|PubMed:25799061};
DE AltName: Full=Coiled-coil domain-containing protein 132 {ECO:0000305};
DE AltName: Full=EARP/GARPII complex subunit VPS50 {ECO:0000312|HGNC:HGNC:25956};
GN Name=VPS50 {ECO:0000312|HGNC:HGNC:25956};
GN Synonyms=CCDC132, KIAA1861 {ECO:0000303|PubMed:11347906};
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 1).
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [2]
RP SEQUENCE REVISION.
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=21472204; DOI=10.3892/mmr_00000222;
RA Matsumoto Y., Imai Y., Sugita Y., Tanaka T., Tsujimoto G., Saito H.,
RA Oshida T.;
RT "CCDC132 is highly expressed in atopic dermatitis T cells.";
RL Mol. Med. Report. 3:83-87(2010).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 446-964 (ISOFORM 1).
RC TISSUE=Lung, and Uterus;
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=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
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 2).
RC TISSUE=Skin, and Testis;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494; SER-498; SER-559 AND
RP SER-561, AND IDENTIFICATION BY 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559 AND SER-561, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-559, AND
RP IDENTIFICATION BY 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559 AND SER-561, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-494; SER-498; SER-559
RP AND SER-561, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494; SER-559 AND SER-561, AND
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 [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-963, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-963, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [21]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP 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 [22]
RP IDENTIFICATION IN THE EARP COMPLEX, AND INTERACTION WITH EIPR1.
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 [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-963, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [24]
RP INTERACTION WITH VPS51 AND VPS53.
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 EARP complex that is involved in
CC endocytic recycling. The EARP complex associates with Rab4-positive
CC endosomes and promotes recycling of internalized transferrin receptor
CC (TFRC) to the plasma membrane. Within the EARP complex, required to
CC tether the complex to recycling endosomes. Not involved in retrograde
CC transport from early and late endosomes to the trans-Golgi network
CC (TGN). {ECO:0000269|PubMed:25799061}.
CC -!- SUBUNIT: Component of the endosome-associated retrograde protein (EARP)
CC complex, composed of VPS51, VPS52, VPS53 and VPS50/Syndetin
CC (PubMed:25799061, PubMed:27440922). The EARP complex interacts with
CC EIPR1 (PubMed:27440922). Interacts with VPS51 and VPS53 in an EIPR1-
CC independent manner (PubMed:31721635). {ECO:0000269|PubMed:25799061,
CC ECO:0000269|PubMed:27440922, ECO:0000269|PubMed:31721635}.
CC -!- INTERACTION:
CC Q96JG6; Q9UID3-1: VPS51; NbExp=6; IntAct=EBI-11044388, EBI-16067837;
CC Q96JG6; Q8N1B4: VPS52; NbExp=8; IntAct=EBI-11044388, EBI-2799833;
CC Q96JG6; Q5VIR6: VPS53; NbExp=8; IntAct=EBI-11044388, EBI-2850511;
CC -!- SUBCELLULAR LOCATION: Recycling endosome {ECO:0000269|PubMed:25799061}.
CC Membrane {ECO:0000250|UniProtKB:F1LSG8}. Note=Associates with membranes
CC in an EIPR1-dependent manner. {ECO:0000250|UniProtKB:F1LSG8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96JG6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96JG6-2; Sequence=VSP_028658, VSP_028659;
CC Name=3;
CC IsoId=Q96JG6-3; Sequence=VSP_045572;
CC -!- TISSUE SPECIFICITY: Ubiquitous, with higher expression in brain and
CC skeletal muscle. {ECO:0000269|PubMed:21472204}.
CC -!- MISCELLANEOUS: Was named 'syndetin' after the Greek 'syndeo', which
CC means 'connect' or 'tether'. {ECO:0000303|PubMed:25799061}.
CC -!- SIMILARITY: Belongs to the syndetin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15701.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB47490.2; Type=Frameshift; 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; AB058764; BAB47490.2; ALT_FRAME; mRNA.
DR EMBL; AB100163; BAI52922.1; -; mRNA.
DR EMBL; AK027234; BAB15701.1; ALT_INIT; mRNA.
DR EMBL; AK126478; BAG54334.1; -; mRNA.
DR EMBL; AC002379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC002453; AAS02023.1; -; Genomic_DNA.
DR EMBL; CH236949; EAL24143.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76816.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76818.1; -; Genomic_DNA.
DR EMBL; BC108708; AAI08709.1; -; mRNA.
DR EMBL; BC017888; AAH17888.1; -; mRNA.
DR EMBL; BC132740; AAI32741.1; -; mRNA.
DR EMBL; BC132742; AAI32743.1; -; mRNA.
DR CCDS; CCDS43617.1; -. [Q96JG6-1]
DR CCDS; CCDS5630.1; -. [Q96JG6-2]
DR CCDS; CCDS59065.1; -. [Q96JG6-3]
DR RefSeq; NP_001244927.1; NM_001257998.1. [Q96JG6-3]
DR RefSeq; NP_060137.2; NM_017667.3. [Q96JG6-1]
DR RefSeq; NP_078829.1; NM_024553.2. [Q96JG6-2]
DR AlphaFoldDB; Q96JG6; -.
DR SMR; Q96JG6; -.
DR BioGRID; 120750; 104.
DR ComplexPortal; CPX-6207; EARP tethering complex.
DR CORUM; Q96JG6; -.
DR DIP; DIP-61628N; -.
DR IntAct; Q96JG6; 36.
DR STRING; 9606.ENSP00000307666; -.
DR iPTMnet; Q96JG6; -.
DR PhosphoSitePlus; Q96JG6; -.
DR BioMuta; VPS50; -.
DR DMDM; 160019079; -.
DR EPD; Q96JG6; -.
DR jPOST; Q96JG6; -.
DR MassIVE; Q96JG6; -.
DR MaxQB; Q96JG6; -.
DR PaxDb; Q96JG6; -.
DR PeptideAtlas; Q96JG6; -.
DR PRIDE; Q96JG6; -.
DR ProteomicsDB; 26988; -.
DR ProteomicsDB; 76956; -. [Q96JG6-1]
DR ProteomicsDB; 76957; -. [Q96JG6-2]
DR Antibodypedia; 15650; 186 antibodies from 22 providers.
DR DNASU; 55610; -.
DR Ensembl; ENST00000251739.9; ENSP00000251739.5; ENSG00000004766.17. [Q96JG6-2]
DR Ensembl; ENST00000305866.10; ENSP00000307666.5; ENSG00000004766.17. [Q96JG6-1]
DR Ensembl; ENST00000544910.5; ENSP00000443104.1; ENSG00000004766.17. [Q96JG6-3]
DR GeneID; 55610; -.
DR KEGG; hsa:55610; -.
DR MANE-Select; ENST00000305866.10; ENSP00000307666.5; NM_017667.4; NP_060137.2.
DR UCSC; uc003umn.4; human. [Q96JG6-1]
DR CTD; 55610; -.
DR DisGeNET; 55610; -.
DR GeneCards; VPS50; -.
DR HGNC; HGNC:25956; VPS50.
DR HPA; ENSG00000004766; Low tissue specificity.
DR MIM; 616465; gene.
DR neXtProt; NX_Q96JG6; -.
DR OpenTargets; ENSG00000004766; -.
DR PharmGKB; PA162381332; -.
DR VEuPathDB; HostDB:ENSG00000004766; -.
DR eggNOG; KOG2939; Eukaryota.
DR GeneTree; ENSGT00390000003442; -.
DR HOGENOM; CLU_059643_0_0_1; -.
DR InParanoid; Q96JG6; -.
DR OMA; MAKVKWD; -.
DR OrthoDB; 293145at2759; -.
DR PhylomeDB; Q96JG6; -.
DR TreeFam; TF106152; -.
DR PathwayCommons; Q96JG6; -.
DR SignaLink; Q96JG6; -.
DR BioGRID-ORCS; 55610; 72 hits in 1067 CRISPR screens.
DR ChiTaRS; VPS50; human.
DR GeneWiki; FLJ20097_/_CCDC132; -.
DR GenomeRNAi; 55610; -.
DR Pharos; Q96JG6; Tbio.
DR PRO; PR:Q96JG6; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q96JG6; protein.
DR Bgee; ENSG00000004766; Expressed in calcaneal tendon and 185 other tissues.
DR ExpressionAtlas; Q96JG6; baseline and differential.
DR Genevisible; Q96JG6; HS.
DR GO; GO:1990745; C:EARP complex; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0000149; F:SNARE binding; IDA:MGI.
DR GO; GO:0032456; P:endocytic recycling; IDA:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR019514; Syndetin_C.
DR InterPro; IPR040047; VPS50.
DR InterPro; IPR019515; VPS54_N.
DR PANTHER; PTHR13258; PTHR13258; 1.
DR Pfam; PF10474; DUF2451; 1.
DR Pfam; PF10475; Vps54_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Endosome; Isopeptide bond;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport;
KW Ubl conjugation.
FT CHAIN 1..964
FT /note="Syndetin"
FT /id="PRO_0000307265"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 82..105
FT /evidence="ECO:0000255"
FT COILED 216..244
FT /evidence="ECO:0000255"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT CROSSLNK 963
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 963
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..34
FT /note="MQKIKSLMTRQGLKSPQESLSDLGAIESLRVPGK -> MLTL (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045572"
FT VAR_SEQ 315..327
FT /note="HVTPDSYIPCLAD -> VCSDLITIHISLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028658"
FT VAR_SEQ 328..964
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028659"
FT CONFLICT 96
FT /note="Q -> H (in Ref. 4; BAG54334)"
FT /evidence="ECO:0000305"
FT CONFLICT 670
FT /note="Missing (in Ref. 4; BAB15701)"
FT /evidence="ECO:0000305"
FT CONFLICT 812
FT /note="H -> Y (in Ref. 4; BAB15701)"
FT /evidence="ECO:0000305"
FT CONFLICT 926
FT /note="E -> K (in Ref. 4; BAB15701)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 964 AA; 111174 MW; 2C748490DDBCBAD5 CRC64;
MQKIKSLMTR QGLKSPQESL SDLGAIESLR VPGKEEFREL REQPSDPQAE QELINSIEQV
YFSVDSFDIV KYELEKLPPV LNLQELEAYR DKLKQQQAAV SKKVADLILE KQPAYVKELE
RVTSLQTGLQ LAAVICTNGR RHLNIAKEGF TQASLGLLAN QRKRQLLIGL LKSLRTIKTL
QRTDVRLSEM LEEEDYPGAI QLCLECQKAA STFKHYSCIS ELNSKLQDTL EQIEEQLDVA
LSKICKNFDI NHYTKVQQAY RLLGKTQTAM DQLHMHFTQA IHNTVFQVVL GYVELCAGNT
DTKFQKLQYK DLCTHVTPDS YIPCLADLCK ALWEVMLSYY RTMEWHEKHD NEDTASASEG
SNMIGTEETN FDRGYIKKKL EHGLTRIWQD VQLKVKTYLL GTDLSIFKYD DFIFVLDIIS
RLMQVGEEFC GSKSEVLQES IRKQSVNYFK NYHRTRLDEL RMFLENETWE LCPVKSNFSI
LQLHEFKFME QSRSPSVSPS KQPVSTSSKT VTLFEQYCSG GNPFEIQANH KDEETEDVLA
SNGYESDEQE KSAYQEYDSD SDVPEELKRD YVDEQTGDGP VKSVSRETLK SRKKSDYSLN
KVNAPILTNT TLNVIRLVGK YMQMMNILKP IAFDVIHFMS QLFDYYLYAI YTFFGRNDSL
ESTGLGLSSS RLRTTLNRIQ ESLIDLEVSA DPTATLTAAE ERKEKVPSPH LSHLVVLTSG
DTLYGLAERV VATESLVFLA EQFEFLQPHL DAVMPAVKKP FLQQFYSQTV STASELRKPI
YWIVAGKALD YEQMLLLMAN VKWDVKEIMS QHNIYVDALL KEFEQFNRRL NEVSKRVRIP
LPVSNILWEH CIRLANRTIV EGYANVKKCS NEGRALMQLD FQQFLMKLEK LTDIRPIPDK
EFVETYIKAY YLTENDMERW IKEHREYSTK QLTNLVNVCL GSHINKKARQ KLLAAIDDID
RPKR
