TGON2_HUMAN
ID TGON2_HUMAN Reviewed; 437 AA.
AC O43493; B2R686; B8ZZ88; D6W5K3; F8W8W7; F8WBK2; J3KQ45; O15282; O43492;
AC O43499; O43500; O43501; Q53G68; Q53GV2; Q6MZV1; Q6ZTM7; Q8N6T8; Q92760;
AC Q96QL2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 4.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Trans-Golgi network integral membrane protein 2 {ECO:0000305};
DE AltName: Full=Trans-Golgi network glycoprotein 46 {ECO:0000303|PubMed:9422759};
DE Short=TGN38 homolog {ECO:0000305|PubMed:9422759};
DE Short=hTGN46 {ECO:0000303|PubMed:9422759};
DE AltName: Full=Trans-Golgi network glycoprotein 48 {ECO:0000303|PubMed:9422759};
DE Short=hTGN48 {ECO:0000303|PubMed:9422759};
DE AltName: Full=Trans-Golgi network glycoprotein 51 {ECO:0000303|PubMed:9422759};
DE Short=hTGN51 {ECO:0000303|PubMed:9422759};
DE AltName: Full=Trans-Golgi network protein 2 {ECO:0000312|HGNC:HGNC:15450};
DE Flags: Precursor;
GN Name=TGOLN2 {ECO:0000312|HGNC:HGNC:15450}; Synonyms=TGN46, TGN51;
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 [GENOMIC DNA / MRNA] (ISOFORMS TGN46 AND TGN48),
RP MUTAGENESIS OF TYR-430, AND VARIANTS VAL-10; GLY-86; LEU-91; GLN-103;
RP PRO-105 AND GLY-322.
RC TISSUE=Liver, and Placenta;
RX PubMed=9422759; DOI=10.1074/jbc.273.2.981;
RA Kain R., Angata K., Kerjaschki D., Fukuda M.;
RT "Molecular cloning and expression of a novel human trans-Golgi network
RT glycoprotein, TGN51, that contains multiple tyrosine-containing motifs.";
RL J. Biol. Chem. 273:981-988(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TGN46), AND VARIANT TRP-259.
RC TISSUE=Fetal liver, and Fetal thymus;
RX PubMed=8907712; DOI=10.1242/jcs.109.3.675;
RA Ponnambalam S., Girotti M., Yaspo M.-L., Owen C.E., Perry A.C.,
RA Suganuma T., Nilsson T., Fried M., Banting G., Warren G.;
RT "Primate homologues of rat TGN38: primary structure, expression and
RT functional implications.";
RL J. Cell Sci. 109:675-685(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS TGN46 AND 6), AND VARIANT
RP TRP-259.
RC TISSUE=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM TGN46), AND VARIANT
RP TRP-259.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Cervix;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT TRP-259.
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS TGN46 AND 5).
RC TISSUE=Prostate;
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [11]
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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND IDENTIFICATION BY
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 AND SER-298, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 AND SER-351, 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 [16]
RP PHOSPHORYLATION AT SER-71; SER-221; SER-298; THR-302 AND SER-351.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: May be involved in regulating membrane traffic to and from
CC trans-Golgi network.
CC -!- INTERACTION:
CC O43493; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-1752146, EBI-10172052;
CC O43493; P16333: NCK1; NbExp=3; IntAct=EBI-1752146, EBI-389883;
CC O43493-5; P01019: AGT; NbExp=3; IntAct=EBI-25830716, EBI-751728;
CC O43493-5; P78371: CCT2; NbExp=3; IntAct=EBI-25830716, EBI-357407;
CC O43493-5; P03952: KLKB1; NbExp=3; IntAct=EBI-25830716, EBI-10087153;
CC O43493-5; P06858: LPL; NbExp=3; IntAct=EBI-25830716, EBI-715909;
CC O43493-5; P40337-2: VHL; NbExp=3; IntAct=EBI-25830716, EBI-12157263;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Golgi apparatus, trans-Golgi network membrane; Single-pass
CC type I membrane protein. Note=Primarily in trans-Golgi network. Cycles
CC between the trans-Golgi network and the cell surface returning via
CC endosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=TGN46;
CC IsoId=O43493-2; Sequence=Displayed;
CC Name=TGN48;
CC IsoId=O43493-3; Sequence=VSP_060323;
CC Name=4;
CC IsoId=O43493-4; Sequence=VSP_060319;
CC Name=5;
CC IsoId=O43493-5; Sequence=VSP_060321;
CC Name=6;
CC IsoId=O43493-6; Sequence=VSP_060318, VSP_060320;
CC Name=7;
CC IsoId=O43493-7; Sequence=VSP_060322;
CC -!- TISSUE SPECIFICITY: Isoform TGN46 is widely expressed. Isoform TGN51 is
CC more abundant in fetal lung and kidney. Isoform TGN48 is barely
CC expressed in embryonic kidney and promyelocytic cells.
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DR EMBL; AF029316; AAB96906.1; -; Genomic_DNA.
DR EMBL; AF029313; AAB96906.1; JOINED; Genomic_DNA.
DR EMBL; AF029314; AAB96906.1; JOINED; Genomic_DNA.
DR EMBL; AF029315; AAB96906.1; JOINED; Genomic_DNA.
DR EMBL; AF029316; AAB96907.1; -; Genomic_DNA.
DR EMBL; AF029313; AAB96907.1; JOINED; Genomic_DNA.
DR EMBL; AF029314; AAB96907.1; JOINED; Genomic_DNA.
DR EMBL; AF029315; AAB96907.1; JOINED; Genomic_DNA.
DR EMBL; AF029316; AAB96908.1; -; Genomic_DNA.
DR EMBL; AF029313; AAB96908.1; JOINED; Genomic_DNA.
DR EMBL; AF029314; AAB96908.1; JOINED; Genomic_DNA.
DR EMBL; AF029315; AAB96908.1; JOINED; Genomic_DNA.
DR EMBL; U62390; AAC39539.1; -; mRNA.
DR EMBL; AF027515; AAC39541.1; -; mRNA.
DR EMBL; AF027516; AAC39542.1; -; mRNA.
DR EMBL; X94333; CAA64002.1; -; mRNA.
DR EMBL; AK126465; BAC86559.1; -; mRNA.
DR EMBL; AK222829; BAD96549.1; -; mRNA.
DR EMBL; AK223063; BAD96783.1; -; mRNA.
DR EMBL; AK312479; BAG35383.1; -; mRNA.
DR EMBL; BX640868; CAE45926.1; -; mRNA.
DR EMBL; AC093162; AAY24095.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99535.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99536.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99539.1; -; Genomic_DNA.
DR EMBL; BC008461; AAH08461.1; -; mRNA.
DR EMBL; BC028219; AAH28219.1; -; mRNA.
DR CCDS; CCDS46351.1; -. [O43493-2]
DR CCDS; CCDS56126.1; -. [O43493-3]
DR CCDS; CCDS56127.1; -. [O43493-4]
DR RefSeq; NP_001193769.1; NM_001206840.1.
DR RefSeq; NP_001193770.1; NM_001206841.1.
DR RefSeq; NP_001193773.1; NM_001206844.1. [O43493-4]
DR RefSeq; NP_006455.2; NM_006464.3. [O43493-2]
DR PDB; 6YAF; EM; 9.10 A; P=420-434.
DR PDBsum; 6YAF; -.
DR AlphaFoldDB; O43493; -.
DR SMR; O43493; -.
DR BioGRID; 115864; 472.
DR IntAct; O43493; 456.
DR MINT; O43493; -.
DR STRING; 9606.ENSP00000386443; -.
DR GlyConnect; 2945; 3 N-Linked glycans (1 site).
DR GlyGen; O43493; 13 sites, 5 N-linked glycans (1 site), 1 O-linked glycan (4 sites).
DR iPTMnet; O43493; -.
DR PhosphoSitePlus; O43493; -.
DR BioMuta; TGOLN2; -.
DR EPD; O43493; -.
DR jPOST; O43493; -.
DR MassIVE; O43493; -.
DR MaxQB; O43493; -.
DR PaxDb; O43493; -.
DR PeptideAtlas; O43493; -.
DR PRIDE; O43493; -.
DR ProteomicsDB; 30219; -.
DR ProteomicsDB; 30837; -.
DR ProteomicsDB; 48977; -. [O43493-2]
DR ProteomicsDB; 48978; -. [O43493-3]
DR ProteomicsDB; 48979; -. [O43493-4]
DR ProteomicsDB; 48980; -. [O43493-5]
DR ProteomicsDB; 48981; -. [O43493-6]
DR Antibodypedia; 2516; 335 antibodies from 33 providers.
DR DNASU; 10618; -.
DR Ensembl; ENST00000377386.8; ENSP00000366603.3; ENSG00000152291.15. [O43493-2]
DR Ensembl; ENST00000398263.6; ENSP00000381312.2; ENSG00000152291.15. [O43493-4]
DR Ensembl; ENST00000409015.5; ENSP00000387035.1; ENSG00000152291.15. [O43493-7]
DR Ensembl; ENST00000444342.2; ENSP00000391190.2; ENSG00000152291.15. [O43493-5]
DR GeneID; 10618; -.
DR KEGG; hsa:10618; -.
DR MANE-Select; ENST00000377386.8; ENSP00000366603.3; NM_006464.4; NP_006455.2.
DR UCSC; uc002soz.4; human. [O43493-2]
DR UCSC; uc021vjw.2; human.
DR CTD; 10618; -.
DR DisGeNET; 10618; -.
DR GeneCards; TGOLN2; -.
DR HGNC; HGNC:15450; TGOLN2.
DR HPA; ENSG00000152291; Low tissue specificity.
DR MIM; 603062; gene.
DR neXtProt; NX_O43493; -.
DR OpenTargets; ENSG00000152291; -.
DR PharmGKB; PA37959; -.
DR VEuPathDB; HostDB:ENSG00000152291; -.
DR eggNOG; ENOG502S6YU; Eukaryota.
DR GeneTree; ENSGT00530000064712; -.
DR HOGENOM; CLU_047350_0_0_1; -.
DR InParanoid; O43493; -.
DR OMA; DPQKQST; -.
DR OrthoDB; 1481309at2759; -.
DR PhylomeDB; O43493; -.
DR TreeFam; TF332514; -.
DR PathwayCommons; O43493; -.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; O43493; -.
DR BioGRID-ORCS; 10618; 6 hits in 1081 CRISPR screens.
DR ChiTaRS; TGOLN2; human.
DR GeneWiki; TGOLN2; -.
DR GenomeRNAi; 10618; -.
DR Pharos; O43493; Tbio.
DR PRO; PR:O43493; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O43493; protein.
DR Bgee; ENSG00000152291; Expressed in renal medulla and 211 other tissues.
DR ExpressionAtlas; O43493; baseline and differential.
DR Genevisible; O43493; HS.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IBA:GO_Central.
DR GO; GO:0030133; C:transport vesicle; TAS:ProtInc.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Glycoprotein;
KW Golgi apparatus; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..437
FT /note="Trans-Golgi network integral membrane protein 2"
FT /id="PRO_0000022486"
FT TOPO_DOM 22..381
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 54..67
FT /note="1"
FT REPEAT 68..81
FT /note="2"
FT REPEAT 82..95
FT /note="3"
FT REPEAT 96..109
FT /note="4"
FT REPEAT 110..123
FT /note="5"
FT REPEAT 124..137
FT /note="6"
FT REPEAT 138..151
FT /note="7"
FT REPEAT 152..165
FT /note="8"
FT REPEAT 166..179
FT /note="9"
FT REPEAT 180..193
FT /note="10"
FT REPEAT 194..207
FT /note="11"
FT REPEAT 208..221
FT /note="12"
FT REPEAT 222..234
FT /note="13"
FT REPEAT 235..249
FT /note="14"
FT REGION 27..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..249
FT /note="14 X 14 AA tandem repeats"
FT MOTIF 395..398
FT /note="Endocytosis signal; in isoform TGN51"
FT MOTIF 418..421
FT /note="Endocytosis signal; in isoform TGN51"
FT MOTIF 430..433
FT /note="Endocytosis signal; in isoform TGN46 and isoform
FT TGN48"
FT COMPBIAS 38..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..335
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 71
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 221
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 298
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 302
FT /note="Phosphothreonine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 351
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039,
FT ECO:0007744|PubMed:24275569"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 71..168
FT /note="Missing (in isoform 6)"
FT /id="VSP_060318"
FT VAR_SEQ 251..309
FT /note="KVVPEQPSRKDHSKPISNPSDNKELPKADTNQLADKGKLSPHAFKTESGEET
FT DLISPPQ -> K (in isoform 4)"
FT /id="VSP_060319"
FT VAR_SEQ 252..309
FT /note="Missing (in isoform 6)"
FT /id="VSP_060320"
FT VAR_SEQ 437
FT /note="S -> VRKEEPGPWEG (in isoform 5)"
FT /id="VSP_060321"
FT VAR_SEQ 437
FT /note="S -> YVLILNVFPAPPKRSFFP (in isoform 7)"
FT /id="VSP_060322"
FT VAR_SEQ 437
FT /note="S -> IFSPPSPNRMVYSSGKR (in isoform TGN48)"
FT /evidence="ECO:0000303|PubMed:9422759"
FT /id="VSP_060323"
FT VARIANT 10
FT /note="L -> V (in dbSNP:rs1128140)"
FT /evidence="ECO:0000269|PubMed:9422759"
FT /id="VAR_034724"
FT VARIANT 86
FT /note="A -> G (in dbSNP:rs1044962)"
FT /evidence="ECO:0000269|PubMed:9422759"
FT /id="VAR_034725"
FT VARIANT 91
FT /note="Q -> L (in dbSNP:rs1044963)"
FT /evidence="ECO:0000269|PubMed:9422759"
FT /id="VAR_034726"
FT VARIANT 103
FT /note="K -> Q (in dbSNP:rs1044964)"
FT /evidence="ECO:0000269|PubMed:9422759"
FT /id="VAR_034727"
FT VARIANT 105
FT /note="Q -> P (in dbSNP:rs1573051515)"
FT /evidence="ECO:0000269|PubMed:9422759"
FT /id="VAR_034728"
FT VARIANT 259
FT /note="R -> W (in dbSNP:rs4247303)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:8907712, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.7"
FT /id="VAR_034729"
FT VARIANT 322
FT /note="E -> G (in dbSNP:rs1044969)"
FT /evidence="ECO:0000269|PubMed:9422759"
FT /id="VAR_034730"
FT MUTAGEN 430
FT /note="Y->A: Loss of relocalization to the trans-Golgi."
FT /evidence="ECO:0000269|PubMed:9422759"
FT CONFLICT 30
FT /note="E -> D (in Ref. 8; AAH08461)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="S -> G (in Ref. 4; BAD96549)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="A -> P (in Ref. 4; BAD96783)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="A -> P (in Ref. 1; AAB96906/AAB96907/AAB96908/
FT AAC39539/AAC39541/AAC39542)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="F -> S (in Ref. 5; CAE45926)"
FT /evidence="ECO:0000305"
FT VARIANT O43493-3:441
FT /note="P -> L (in dbSNP:rs4240199)"
FT /evidence="ECO:0000305"
FT /id="VAR_082887"
FT CONFLICT O43493-3:439
FT /note="S -> F (in Ref. 1; AAC39541/AAB96907)"
FT CONFLICT O43493-7:453
FT /note="F -> L (in Ref. 1; AAB96908/AAC39542)"
SQ SEQUENCE 437 AA; 45880 MW; 6F72467FED83A1A3 CRC64;
MRFVVALVLL NVAAAGAVPL LATESVKQEE AGVRPSAGNV STHPSLSQRP GGSTKSHPEP
QTPKDSPSKS SAEAQTPEDT PNKSGAEAKT QKDSSNKSGA EAKTQKGSTS KSGSEAQTTK
DSTSKSHPEL QTPKDSTGKS GAEAQTPEDS PNRSGAEAKT QKDSPSKSGS EAQTTKDVPN
KSGADGQTPK DGSSKSGAED QTPKDVPNKS GAEKQTPKDG SNKSGAEEQG PIDGPSKSGA
EEQTSKDSPN KVVPEQPSRK DHSKPISNPS DNKELPKADT NQLADKGKLS PHAFKTESGE
ETDLISPPQE EVKSSEPTED VEPKEAEDDD TGPEEGSPPK EEKEKMSGSA SSENREGTLS
DSTGSEKDDL YPNGSGNGSA ESSHFFAYLV TAAILVAVLY IAHHNKRKII AFVLEGKRSK
VTRRPKASDY QRLDQKS
