ID TGON2_HUMAN Reviewed; 479 AA. AC O43493; B2R686; B8ZZ88; D6W5K3; F8W8W7; F8WBK2; J3KQ45; O15282; AC O43492; O43499; O43500; O43501; Q53G68; Q53GV2; Q6MZV1; Q6ZTM7; AC Q8N6T8; Q92760; Q96QL2; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 28-MAR-2018, sequence version 3. DT 13-FEB-2019, entry version 162. DE RecName: Full=Trans-Golgi network integral membrane protein 2; DE AltName: Full=TGN38 homolog; DE AltName: Full=TGN46; DE AltName: Full=TGN48; DE AltName: Full=Trans-Golgi network protein TGN51; DE Flags: Precursor; GN Name=TGOLN2; Synonyms=TGN46, TGN51; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS TGN51; TGN46 AND RP TGN48), MUTAGENESIS OF TYR-430, AND VARIANTS VAL-10; GLY-86; LEU-91; RP GLN-103; 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 RT 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; 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 RP VARIANT 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., 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., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA 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., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA 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., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND IDENTIFICATION RP 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 [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 RT enrichment and fractionation of phosphopeptides with strong anion RT exchange 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation 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., RA Buerckstuemmer T., 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 RP 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., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver 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 RT 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., RA Ayoub D., 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 CC from trans-Golgi network. CC -!- INTERACTION: CC P60411:KRTAP10-9; NbExp=3; IntAct=EBI-1752146, EBI-10172052; CC P16333:NCK1; NbExp=3; IntAct=EBI-1752146, EBI-389883; CC P27986:PIK3R1; NbExp=2; IntAct=EBI-1752146, EBI-79464; CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Golgi apparatus, trans-Golgi network membrane; Single- CC pass type I membrane protein. Note=Primarily in trans-Golgi CC network. Cycles between the trans-Golgi network and the cell CC surface returning via endosomes. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=TGN51; CC IsoId=O43493-1; Sequence=Displayed; CC Name=TGN46; CC IsoId=O43493-2; Sequence=VSP_004454; CC Name=TGN48; CC IsoId=O43493-3; Sequence=VSP_004455; CC Note=Ref.1 (AAC39541) sequence is in conflict in position: CC 439:F->S. Ref.1 (AAC39541) sequence is in conflict in position: CC 441:L->P. {ECO:0000305}; CC Name=4; CC IsoId=O43493-4; Sequence=VSP_027470, VSP_004454; CC Note=No experimental confirmation available.; CC Name=5; CC IsoId=O43493-5; Sequence=VSP_027471; CC Note=No experimental confirmation available.; CC Name=6; CC IsoId=O43493-6; Sequence=VSP_027469, VSP_027470, VSP_004454; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Isoform TGN46 is widely expressed. Isoform CC TGN51 is more abundant in fetal lung and kidney. Isoform TGN48 is CC barely 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; 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 UniGene; Hs.593382; -. DR BioGrid; 115864; 52. DR IntAct; O43493; 424. DR MINT; O43493; -. DR STRING; 9606.ENSP00000386443; -. DR iPTMnet; O43493; -. DR PhosphoSitePlus; O43493; -. DR BioMuta; TGOLN2; -. DR EPD; O43493; -. DR jPOST; O43493; -. DR PaxDb; O43493; -. DR PeptideAtlas; O43493; -. DR PRIDE; O43493; -. DR ProteomicsDB; 48976; -. 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 DNASU; 10618; -. DR Ensembl; ENST00000282120; ENSP00000282120; ENSG00000152291. [O43493-1] DR Ensembl; ENST00000377386; ENSP00000366603; ENSG00000152291. [O43493-2] DR Ensembl; ENST00000398263; ENSP00000381312; ENSG00000152291. [O43493-4] DR Ensembl; ENST00000409232; ENSP00000386443; ENSG00000152291. [O43493-3] DR Ensembl; ENST00000444342; ENSP00000391190; ENSG00000152291. [O43493-5] DR GeneID; 10618; -. DR KEGG; hsa:10618; -. DR UCSC; uc002soz.4; human. [O43493-1] DR CTD; 10618; -. DR DisGeNET; 10618; -. DR EuPathDB; HostDB:ENSG00000152291.13; -. DR GeneCards; TGOLN2; -. DR H-InvDB; HIX0022878; -. DR HGNC; HGNC:15450; TGOLN2. DR HPA; CAB011489; -. DR HPA; HPA012609; -. DR HPA; HPA012723; -. DR MIM; 603062; gene. DR neXtProt; NX_O43493; -. DR OpenTargets; ENSG00000152291; -. DR PharmGKB; PA37959; -. DR eggNOG; ENOG410IXPE; Eukaryota. DR eggNOG; ENOG410XUUR; LUCA. DR GeneTree; ENSGT00530000064712; -. DR HOGENOM; HOG000089969; -. DR HOVERGEN; HBG108564; -. DR InParanoid; O43493; -. DR OMA; EEQGPID; -. DR OrthoDB; 1481309at2759; -. DR PhylomeDB; O43493; -. DR TreeFam; TF332514; -. 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 ChiTaRS; TGOLN2; human. DR GeneWiki; TGOLN2; -. DR GenomeRNAi; 10618; -. DR PRO; PR:O43493; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; ENSG00000152291; Expressed in 245 organ(s), highest expression level in adult mammalian kidney. DR Genevisible; O43493; HS. DR GO; GO:0030665; C:clathrin-coated 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. DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome. DR GO; GO:0061024; P:membrane organization; TAS:Reactome. DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome. DR InterPro; IPR026084; TGN38. DR PANTHER; PTHR23211; PTHR23211; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Complete proteome; Glycoprotein; KW Golgi apparatus; Membrane; Phosphoprotein; Polymorphism; KW Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 479 Trans-Golgi network integral membrane FT protein 2. FT /FTId=PRO_0000022486. FT TOPO_DOM 22 381 Extracellular. {ECO:0000255}. FT TRANSMEM 382 402 Helical. {ECO:0000255}. FT TOPO_DOM 403 479 Cytoplasmic. {ECO:0000255}. FT REPEAT 54 67 1. FT REPEAT 68 81 2. FT REPEAT 82 95 3. FT REPEAT 96 109 4. FT REPEAT 110 123 5. FT REPEAT 124 137 6. FT REPEAT 138 151 7. FT REPEAT 152 165 8. FT REPEAT 166 179 9. FT REPEAT 180 193 10. FT REPEAT 194 207 11. FT REPEAT 208 221 12. FT REPEAT 222 234 13. FT REPEAT 235 249 14. FT REGION 54 249 14 X 14 AA tandem repeats. FT MOTIF 430 433 Endocytosis signal; in isoform TGN46 and FT isoform TGN48. FT MOTIF 437 440 Endocytosis signal; in isoform TGN51. FT MOTIF 460 463 Endocytosis signal; in isoform TGN51. FT MOD_RES 71 71 Phosphoserine; by FAM20C. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:23186163, FT ECO:0000244|PubMed:24275569, FT ECO:0000269|PubMed:26091039}. FT MOD_RES 221 221 Phosphoserine; by FAM20C. FT {ECO:0000269|PubMed:26091039}. FT MOD_RES 298 298 Phosphoserine; by FAM20C. FT {ECO:0000244|PubMed:23186163, FT ECO:0000269|PubMed:26091039}. FT MOD_RES 302 302 Phosphothreonine; by FAM20C. FT {ECO:0000269|PubMed:26091039}. FT MOD_RES 351 351 Phosphoserine; by FAM20C. FT {ECO:0000244|PubMed:24275569, FT ECO:0000269|PubMed:26091039}. FT CARBOHYD 39 39 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 82 82 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 96 96 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 152 152 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 180 180 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 208 208 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 222 222 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 373 373 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 377 377 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT VAR_SEQ 64 161 Missing (in isoform 6). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_027469. FT VAR_SEQ 252 309 Missing (in isoform 4 and isoform 6). FT {ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:17974005}. FT /FTId=VSP_027470. FT VAR_SEQ 437 479 YVLILNVFPAPPKRSFFPVLTEWYIPLEKDERHQWIVLLSF FT QL -> VRKEEPGPWEG (in isoform 5). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_027471. FT VAR_SEQ 437 479 YVLILNVFPAPPKRSFFPVLTEWYIPLEKDERHQWIVLLSF FT QL -> S (in isoform TGN46, isoform 4 and FT isoform 6). {ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:17974005, FT ECO:0000303|PubMed:8907712, FT ECO:0000303|PubMed:9422759, FT ECO:0000303|Ref.4}. FT /FTId=VSP_004454. FT VAR_SEQ 437 479 YVLILNVFPAPPKRSFFPVLTEWYIPLEKDERHQWIVLLSF FT QL -> IFFPLSPNRMVYSSGKR (in isoform FT TGN48). {ECO:0000303|PubMed:9422759}. FT /FTId=VSP_004455. FT VARIANT 10 10 L -> V (in dbSNP:rs1128140). FT {ECO:0000269|PubMed:9422759}. FT /FTId=VAR_034724. FT VARIANT 86 86 A -> G (in dbSNP:rs1044962). FT {ECO:0000269|PubMed:9422759}. FT /FTId=VAR_034725. FT VARIANT 91 91 Q -> L (in dbSNP:rs1044963). FT {ECO:0000269|PubMed:9422759}. FT /FTId=VAR_034726. FT VARIANT 103 103 K -> Q (in dbSNP:rs1044964). FT {ECO:0000269|PubMed:9422759}. FT /FTId=VAR_034727. FT VARIANT 105 105 Q -> P. {ECO:0000269|PubMed:9422759}. FT /FTId=VAR_034728. FT VARIANT 259 259 R -> W (in dbSNP:rs4247303). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:8907712, FT ECO:0000269|Ref.4, ECO:0000269|Ref.7}. FT /FTId=VAR_034729. FT VARIANT 322 322 E -> G (in dbSNP:rs1044969). FT {ECO:0000269|PubMed:9422759}. FT /FTId=VAR_034730. FT MUTAGEN 430 430 Y->A: Loss of relocalization to the FT trans-Golgi. FT {ECO:0000269|PubMed:9422759}. FT CONFLICT 30 30 E -> D (in Ref. 8; AAH08461). FT {ECO:0000305}. FT CONFLICT 71 71 S -> G (in Ref. 4; BAD96549). FT {ECO:0000305}. FT CONFLICT 74 74 A -> P (in Ref. 4; BAD96783). FT {ECO:0000305}. FT CONFLICT 158 158 A -> P (in Ref. 1; AAB96906/AAB96907/ FT AAB96908/AAC39539/AAC39541/AAC39542). FT {ECO:0000305}. FT CONFLICT 386 386 F -> S (in Ref. 5; CAE45926). FT {ECO:0000305}. FT CONFLICT 453 454 FP -> LPQ (in Ref. 1; AAB96908). FT CONFLICT 454 454 P -> PQ (in Ref. 7; EAW99536/EAW99539). FT {ECO:0000305}. SQ SEQUENCE 479 AA; 51019 MW; 65253DBCF3D7927B 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 QRLDQKYVLI LNVFPAPPKR SFFPVLTEWY IPLEKDERHQ WIVLLSFQL //