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 02-OCT-2024, entry version 193. 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. 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; 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; CCDS56127.1; -. [O43493-4] DR CCDS; CCDS92789.1; -. [O43493-7] 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; 1588. DR IntAct; O43493; 463. DR MINT; O43493; -. DR STRING; 9606.ENSP00000386443; -. DR GlyConnect; 2945; 3 N-Linked glycans (1 site). DR GlyCosmos; O43493; 13 sites, 7 glycans. DR GlyGen; O43493; 39 sites, 6 N-linked glycans (1 site), 3 O-linked glycans (30 sites). DR iPTMnet; O43493; -. DR PhosphoSitePlus; O43493; -. DR SwissPalm; O43493; -. DR BioMuta; TGOLN2; -. DR jPOST; O43493; -. DR MassIVE; O43493; -. DR PaxDb; 9606-ENSP00000386443; -. DR PeptideAtlas; 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 Pumba; O43493; -. DR Antibodypedia; 2516; 370 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 Ensembl; ENST00000710332.1; ENSP00000518212.1; ENSG00000292253.1. [O43493-4] 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 AGR; HGNC:15450; -. 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; NDGPGKL; -. DR OrthoDB; 5362179at2759; -. 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; 8 hits in 1159 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 213 other cell types or tissues. DR ExpressionAtlas; O43493; baseline and differential. 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: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. DR PANTHER; PTHR23211:SF0; TRANS-GOLGI NETWORK INTEGRAL MEMBRANE PROTEIN 2; 1. DR PANTHER; PTHR23211; TRANS-GOLGI NETWORK INTEGRAL MEMBRANE PROTEIN TGN38; 1. DR Pfam; PF17818; KCT2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Glycoprotein; KW Golgi apparatus; Membrane; Phosphoprotein; Proteomics identification; KW Reference proteome; Repeat; 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 //