ID TFG_HUMAN Reviewed; 400 AA. AC Q92734; D3DN49; G5E9V1; K0J5S8; K0J6K2; Q15656; Q969I2; DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 2. DT 27-MAR-2024, entry version 201. DE RecName: Full=Protein TFG; DE AltName: Full=TRK-fused gene protein; GN Name=TFG; 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 [MRNA] (ISOFORM 1). RC TISSUE=Pancreas; RX PubMed=9169129; DOI=10.1006/geno.1997.4625; RA Mencinger M., Panagopoluos I., Andreasson P., Lassen C., Mitelman F., RA Aman P.; RT "Characterization and chromosomal mapping of the human TFG gene involved in RT thyroid carcinoma."; RL Genomics 41:327-331(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), VARIANT HMSNO LEU-285, AND RP ALTERNATIVE SPLICING. RX PubMed=22883144; DOI=10.1016/j.ajhg.2012.07.014; RA Ishiura H., Sako W., Yoshida M., Kawarai T., Tanabe O., Goto J., RA Takahashi Y., Date H., Mitsui J., Ahsan B., Ichikawa Y., Iwata A., RA Yoshino H., Izumi Y., Fujita K., Maeda K., Goto S., Koizumi H., RA Morigaki R., Ikemura M., Yamauchi N., Murayama S., Nicholson G.A., Ito H., RA Sobue G., Nakagawa M., Kaji R., Tsuji S.; RT "The TRK-fused gene is mutated in hereditary motor and sensory neuropathy RT with proximal dominant involvement."; RL Am. J. Hum. Genet. 91:320-329(2012). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; 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 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [7] 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, Placenta, and Uterus; 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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-193, AND CHROMOSOMAL TRANSLOCATION WITH RP NTRK1. RX PubMed=7565764; DOI=10.1128/mcb.15.11.6118; RA Greco A., Mariani C., Miranda C., Lupas A., Pagliardini S., Pomati M., RA Pierotti M.A.; RT "The DNA rearrangement that generates the TRK-T3 oncogene involves a novel RT gene on chromosome 3 whose product has a potential coiled-coil domain."; RL Mol. Cell. Biol. 15:6118-6127(1995). RN [10] RP PROTEIN SEQUENCE OF 1-10; 15-22; 24-42 AND 48-57, ACETYLATION AT MET-1, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RA Bienvenut W.V., Calvo F., Kolch W.; RL Submitted (FEB-2008) to UniProtKB. RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, 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 [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND IDENTIFICATION BY RP 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 [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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SEC16B. RX PubMed=21478858; DOI=10.1038/ncb2225; RA Witte K., Schuh A.L., Hegermann J., Sarkeshik A., Mayers J.R., Schwarze K., RA Yates J.R. III, Eimer S., Audhya A.; RT "TFG-1 function in protein secretion and oncogenesis."; RL Nat. Cell Biol. 13:550-558(2011). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-197, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 FUNCTION, SUBUNIT, VARIANT SPG57 CYS-106, AND CHARACTERIZATION OF VARIANT RP SPG57 CYS-106. RX PubMed=23479643; DOI=10.1073/pnas.1217197110; RA Beetz C., Johnson A., Schuh A.L., Thakur S., Varga R.E., Fothergill T., RA Hertel N., Bomba-Warczak E., Thiele H., Nurnberg G., Altmuller J., RA Saxena R., Chapman E.R., Dent E.W., Nurnberg P., Audhya A.; RT "Inhibition of TFG function causes hereditary axon degeneration by RT impairing endoplasmic reticulum structure."; RL Proc. Natl. Acad. Sci. U.S.A. 110:5091-5096(2013). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND IDENTIFICATION BY RP 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 [20] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-385 AND ARG-400, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [21] RP VARIANT [LARGE SCALE ANALYSIS] SER-149. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [22] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PDCD6, CHARACTERIZATION OF RP VARIANT SPG57 CYS-106, AND CHARACTERIZATION OF VARIANT HMSNO LEU-285. RX PubMed=27813252; DOI=10.1111/febs.13949; RA Kanadome T., Shibata H., Kuwata K., Takahara T., Maki M.; RT "The calcium-binding protein ALG-2 promotes endoplasmic reticulum exit site RT localization and polymerization of Trk-fused gene (TFG) protein."; RL FEBS J. 284:56-76(2017). RN [23] RP VARIANTS SPG57 CYS-106 AND HIS-106, AND CHARACTERIZATION OF VARIANTS SPG57 RP CYS-106 AND HIS-106. RX PubMed=27492651; DOI=10.1002/humu.23060; RA Harlalka G.V., McEntagart M.E., Gupta N., Skrzypiec A.E., Mucha M.W., RA Chioza B.A., Simpson M.A., Sreekantan-Nair A., Pereira A., Guenther S., RA Jahic A., Modarres H., Moore-Barton H., Trembath R.C., Kabra M., RA Baple E.L., Thakur S., Patton M.A., Beetz C., Pawlak R., Crosby A.H.; RT "Novel genetic, clinical, and pathomechanistic insights into TFG-associated RT hereditary spastic paraplegia."; RL Hum. Mutat. 37:1157-1161(2016). RN [24] RP VARIANT SPG57 PRO-107. RX PubMed=30237576; DOI=10.1038/s41436-018-0138-x; RA Maddirevula S., Alzahrani F., Al-Owain M., Al Muhaizea M.A., Kayyali H.R., RA AlHashem A., Rahbeeni Z., Al-Otaibi M., Alzaidan H.I., Balobaid A., RA El Khashab H.Y., Bubshait D.K., Faden M., Yamani S.A., Dabbagh O., RA Al-Mureikhi M., Jasser A.A., Alsaif H.S., Alluhaydan I., Seidahmed M.Z., RA Alabbasi B.H., Almogarri I., Kurdi W., Akleh H., Qari A., Al Tala S.M., RA Alhomaidi S., Kentab A.Y., Salih M.A., Chedrawi A., Alameer S., Tabarki B., RA Shamseldin H.E., Patel N., Ibrahim N., Abdulwahab F., Samira M., Goljan E., RA Abouelhoda M., Meyer B.F., Hashem M., Shaheen R., AlShahwan S., RA Alfadhel M., Ben-Omran T., Al-Qattan M.M., Monies D., Alkuraya F.S.; RT "Autozygome and high throughput confirmation of disease genes candidacy."; RL Genet. Med. 21:736-742(2019). CC -!- FUNCTION: Plays a role in the normal dynamic function of the CC endoplasmic reticulum (ER) and its associated microtubules CC (PubMed:23479643, PubMed:27813252). Required for secretory cargo CC traffic from the endoplasmic reticulum to the Golgi apparatus CC (PubMed:21478858). {ECO:0000269|PubMed:21478858, CC ECO:0000269|PubMed:23479643, ECO:0000269|PubMed:27813252}. CC -!- SUBUNIT: Self-associates to form an oligomeric complex CC (PubMed:23479643). Interacts with PDCD6; promoting localization and CC polymerization of TFG at endoplasmic reticulum exit site CC (PubMed:27813252). Interacts with SEC16B (PubMed:21478858). CC {ECO:0000269|PubMed:21478858, ECO:0000269|PubMed:23479643, CC ECO:0000269|PubMed:27813252}. CC -!- INTERACTION: CC Q92734; Q5BKX5-3: ACTMAP; NbExp=3; IntAct=EBI-357061, EBI-11976299; CC Q92734; P50995: ANXA11; NbExp=4; IntAct=EBI-357061, EBI-715243; CC Q92734; Q5T0G8: ANXA11; NbExp=3; IntAct=EBI-357061, EBI-10245225; CC Q92734; Q5VV41: ARHGEF16; NbExp=3; IntAct=EBI-357061, EBI-1057448; CC Q92734; Q8N9W6: BOLL; NbExp=4; IntAct=EBI-357061, EBI-998198; CC Q92734; Q8N9W6-4: BOLL; NbExp=3; IntAct=EBI-357061, EBI-11983447; CC Q92734; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-357061, EBI-953896; CC Q92734; Q53EZ4: CEP55; NbExp=6; IntAct=EBI-357061, EBI-747776; CC Q92734; P13569: CFTR; NbExp=7; IntAct=EBI-357061, EBI-349854; CC Q92734; O43186: CRX; NbExp=3; IntAct=EBI-357061, EBI-748171; CC Q92734; P33240: CSTF2; NbExp=6; IntAct=EBI-357061, EBI-711360; CC Q92734; Q15038: DAZAP2; NbExp=5; IntAct=EBI-357061, EBI-724310; CC Q92734; Q92997: DVL3; NbExp=3; IntAct=EBI-357061, EBI-739789; CC Q92734; Q01844: EWSR1; NbExp=3; IntAct=EBI-357061, EBI-739737; CC Q92734; O00167-2: EYA2; NbExp=3; IntAct=EBI-357061, EBI-12807776; CC Q92734; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-357061, EBI-11978259; CC Q92734; O75593: FOXH1; NbExp=3; IntAct=EBI-357061, EBI-1759806; CC Q92734; A0A0S2Z4Q4: HGS; NbExp=3; IntAct=EBI-357061, EBI-16429135; CC Q92734; O14964: HGS; NbExp=3; IntAct=EBI-357061, EBI-740220; CC Q92734; P52597: HNRNPF; NbExp=3; IntAct=EBI-357061, EBI-352986; CC Q92734; P42858: HTT; NbExp=3; IntAct=EBI-357061, EBI-466029; CC Q92734; Q0VD86: INCA1; NbExp=3; IntAct=EBI-357061, EBI-6509505; CC Q92734; Q5TA45: INTS11; NbExp=3; IntAct=EBI-357061, EBI-748258; CC Q92734; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-357061, EBI-3957672; CC Q92734; Q14847-2: LASP1; NbExp=3; IntAct=EBI-357061, EBI-9088686; CC Q92734; Q96PV6: LENG8; NbExp=3; IntAct=EBI-357061, EBI-739546; CC Q92734; Q9Y5V3: MAGED1; NbExp=8; IntAct=EBI-357061, EBI-716006; CC Q92734; Q8NDC0: MAPK1IP1L; NbExp=6; IntAct=EBI-357061, EBI-741424; CC Q92734; Q71SY5: MED25; NbExp=3; IntAct=EBI-357061, EBI-394558; CC Q92734; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-357061, EBI-8487781; CC Q92734; Q4VC12: MSS51; NbExp=3; IntAct=EBI-357061, EBI-11599933; CC Q92734; Q6IA69: NADSYN1; NbExp=3; IntAct=EBI-357061, EBI-748610; CC Q92734; Q8IV28: NID2; NbExp=3; IntAct=EBI-357061, EBI-10261509; CC Q92734; Q8TDS5: OXER1; NbExp=3; IntAct=EBI-357061, EBI-12813389; CC Q92734; Q9UBV8: PEF1; NbExp=6; IntAct=EBI-357061, EBI-724639; CC Q92734; Q99471: PFDN5; NbExp=3; IntAct=EBI-357061, EBI-357275; CC Q92734; O15496: PLA2G10; NbExp=3; IntAct=EBI-357061, EBI-726466; CC Q92734; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-357061, EBI-949255; CC Q92734; O15162: PLSCR1; NbExp=2; IntAct=EBI-357061, EBI-740019; CC Q92734; Q16633: POU2AF1; NbExp=3; IntAct=EBI-357061, EBI-943588; CC Q92734; P86480: PRR20D; NbExp=3; IntAct=EBI-357061, EBI-12754095; CC Q92734; Q93062: RBPMS; NbExp=3; IntAct=EBI-357061, EBI-740322; CC Q92734; P78317: RNF4; NbExp=5; IntAct=EBI-357061, EBI-2340927; CC Q92734; Q7Z5V6-2: SAXO4; NbExp=3; IntAct=EBI-357061, EBI-12000762; CC Q92734; O95486: SEC24A; NbExp=3; IntAct=EBI-357061, EBI-749911; CC Q92734; Q15428: SF3A2; NbExp=3; IntAct=EBI-357061, EBI-2462271; CC Q92734; Q15427: SF3B4; NbExp=3; IntAct=EBI-357061, EBI-348469; CC Q92734; Q53HV7-2: SMUG1; NbExp=3; IntAct=EBI-357061, EBI-12275818; CC Q92734; Q9NZD8: SPG21; NbExp=6; IntAct=EBI-357061, EBI-742688; CC Q92734; Q96LM6: SPMIP9; NbExp=3; IntAct=EBI-357061, EBI-743976; CC Q92734; Q8IWL8: STH; NbExp=3; IntAct=EBI-357061, EBI-12843506; CC Q92734; O60806: TBX19; NbExp=3; IntAct=EBI-357061, EBI-12096770; CC Q92734; Q92734: TFG; NbExp=7; IntAct=EBI-357061, EBI-357061; CC Q92734; Q5T6F2: UBAP2; NbExp=3; IntAct=EBI-357061, EBI-2514383; CC Q92734; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-357061, EBI-10180829; CC Q92734; A5D8V6: VPS37C; NbExp=6; IntAct=EBI-357061, EBI-2559305; CC Q92734; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-357061, EBI-12040603; CC Q92734; Q9UJ78-2: ZMYM5; NbExp=3; IntAct=EBI-357061, EBI-17634549; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum CC {ECO:0000269|PubMed:27813252}. Note=Localizes to endoplasmic reticulum CC exit site (ERES), also known as transitional endoplasmic reticulum CC (tER) (PubMed:27813252, PubMed:21478858). {ECO:0000269|PubMed:21478858, CC ECO:0000269|PubMed:27813252}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q92734-1; Sequence=Displayed; CC Name=2; CC IsoId=Q92734-2; Sequence=VSP_047131; CC Name=3; CC IsoId=Q92734-3; Sequence=VSP_057414, VSP_057415; CC Name=4; CC IsoId=Q92734-4; Sequence=VSP_047131, VSP_057414, VSP_057415; CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- DISEASE: Note=A chromosomal aberration involving TFG is found in CC papillary thyroid carcinomas (PTCs). Translocation t(1;3)(q21;q11) with CC NTRK1. The TFG sequence is fused to the 3'-end of NTRK1 generating the CC TRKT3 (TRK-T3) fusion transcript. {ECO:0000269|PubMed:7565764}. CC -!- DISEASE: Neuropathy, hereditary motor and sensory, Okinawa type (HMSNO) CC [MIM:604484]: A neurodegenerative disorder characterized by young adult CC onset of proximal muscle weakness and atrophy, muscle cramps, and CC fasciculations, with later onset of distal sensory impairment. The CC disorder is slowly progressive and clinically resembles amyotrophic CC lateral sclerosis. {ECO:0000269|PubMed:22883144, CC ECO:0000269|PubMed:27813252}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Spastic paraplegia 57, autosomal recessive (SPG57) CC [MIM:615658]: A complicated form of spastic paraplegia, a CC neurodegenerative disorder characterized by a slow, gradual, CC progressive weakness and spasticity of the lower limbs. Rate of CC progression and the severity of symptoms are quite variable. Initial CC symptoms may include difficulty with balance, weakness and stiffness in CC the legs, muscle spasms, and dragging the toes when walking. CC Complicated forms are recognized by additional variable features CC including spastic quadriparesis, seizures, dementia, amyotrophy, CC extrapyramidal disturbance, cerebral or cerebellar atrophy, optic CC atrophy, and peripheral neuropathy, as well as by extra neurological CC manifestations. {ECO:0000269|PubMed:23479643, CC ECO:0000269|PubMed:27492651, ECO:0000269|PubMed:27813252, CC ECO:0000269|PubMed:30237576}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/281/TFG"; 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; Y07968; CAA69264.1; -; mRNA. DR EMBL; AB731569; BAM48926.1; -; mRNA. DR EMBL; AB731570; BAM48927.1; -; mRNA. DR EMBL; AK093456; BAG52721.1; -; mRNA. DR EMBL; BT007428; AAP36096.1; -; mRNA. DR EMBL; CR456781; CAG33062.1; -; mRNA. DR EMBL; AC068763; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF457659; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF457666; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471052; EAW79813.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79814.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79815.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79816.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79817.1; -; Genomic_DNA. DR EMBL; BC001483; AAH01483.1; -; mRNA. DR EMBL; BC009241; AAH09241.1; -; mRNA. DR EMBL; BC023599; AAH23599.1; -; mRNA. DR EMBL; X85960; CAA59936.1; ALT_TERM; mRNA. DR CCDS; CCDS2939.1; -. [Q92734-1] DR CCDS; CCDS56266.1; -. [Q92734-2] DR RefSeq; NP_001007566.1; NM_001007565.2. [Q92734-1] DR RefSeq; NP_001182407.1; NM_001195478.1. [Q92734-1] DR RefSeq; NP_001182408.1; NM_001195479.1. [Q92734-2] DR RefSeq; NP_006061.2; NM_006070.5. [Q92734-1] DR RefSeq; XP_005247123.1; XM_005247066.1. [Q92734-2] DR RefSeq; XP_006713535.1; XM_006713472.1. [Q92734-1] DR RefSeq; XP_006713536.1; XM_006713473.1. DR RefSeq; XP_011510636.1; XM_011512334.1. [Q92734-1] DR RefSeq; XP_016861016.1; XM_017005527.1. [Q92734-2] DR RefSeq; XP_016861017.1; XM_017005528.1. DR RefSeq; XP_016861018.1; XM_017005529.1. DR RefSeq; XP_016861019.1; XM_017005530.1. DR AlphaFoldDB; Q92734; -. DR SMR; Q92734; -. DR BioGRID; 115624; 324. DR IntAct; Q92734; 176. DR MINT; Q92734; -. DR STRING; 9606.ENSP00000240851; -. DR MoonDB; Q92734; Predicted. DR GlyCosmos; Q92734; 6 sites, 1 glycan. DR GlyGen; Q92734; 9 sites, 1 O-linked glycan (9 sites). DR iPTMnet; Q92734; -. DR MetOSite; Q92734; -. DR PhosphoSitePlus; Q92734; -. DR SwissPalm; Q92734; -. DR BioMuta; TFG; -. DR DMDM; 223634676; -. DR EPD; Q92734; -. DR jPOST; Q92734; -. DR MassIVE; Q92734; -. DR MaxQB; Q92734; -. DR PaxDb; 9606-ENSP00000240851; -. DR PeptideAtlas; Q92734; -. DR ProteomicsDB; 34050; -. DR ProteomicsDB; 75430; -. [Q92734-1] DR Pumba; Q92734; -. DR Antibodypedia; 15864; 392 antibodies from 35 providers. DR DNASU; 10342; -. DR Ensembl; ENST00000240851.9; ENSP00000240851.4; ENSG00000114354.15. [Q92734-1] DR Ensembl; ENST00000463568.6; ENSP00000419504.2; ENSG00000114354.15. [Q92734-2] DR Ensembl; ENST00000476228.5; ENSP00000417952.1; ENSG00000114354.15. [Q92734-2] DR Ensembl; ENST00000487505.6; ENSP00000420797.2; ENSG00000114354.15. [Q92734-1] DR Ensembl; ENST00000490574.6; ENSP00000419960.1; ENSG00000114354.15. [Q92734-1] DR Ensembl; ENST00000615993.2; ENSP00000479269.2; ENSG00000114354.15. [Q92734-4] DR Ensembl; ENST00000620299.5; ENSP00000479981.1; ENSG00000114354.15. [Q92734-3] DR Ensembl; ENST00000674615.1; ENSP00000502734.1; ENSG00000114354.15. [Q92734-1] DR Ensembl; ENST00000674645.1; ENSP00000501892.1; ENSG00000114354.15. [Q92734-2] DR Ensembl; ENST00000674758.1; ENSP00000502502.1; ENSG00000114354.15. [Q92734-2] DR Ensembl; ENST00000675047.1; ENSP00000502497.1; ENSG00000114354.15. [Q92734-2] DR Ensembl; ENST00000675243.1; ENSP00000502592.1; ENSG00000114354.15. [Q92734-1] DR Ensembl; ENST00000675420.1; ENSP00000502516.1; ENSG00000114354.15. [Q92734-2] DR Ensembl; ENST00000675499.1; ENSP00000502450.1; ENSG00000114354.15. [Q92734-1] DR Ensembl; ENST00000675543.1; ENSP00000502229.1; ENSG00000114354.15. [Q92734-3] DR Ensembl; ENST00000675553.1; ENSP00000501815.1; ENSG00000114354.15. [Q92734-1] DR Ensembl; ENST00000675586.1; ENSP00000502329.1; ENSG00000114354.15. [Q92734-4] DR Ensembl; ENST00000676111.1; ENSP00000502139.1; ENSG00000114354.15. [Q92734-4] DR Ensembl; ENST00000676308.1; ENSP00000502697.1; ENSG00000114354.15. [Q92734-4] DR Ensembl; ENST00000676395.1; ENSP00000502071.1; ENSG00000114354.15. [Q92734-1] DR Ensembl; ENST00000676431.1; ENSP00000502698.1; ENSG00000114354.15. [Q92734-2] DR GeneID; 10342; -. DR KEGG; hsa:10342; -. DR MANE-Select; ENST00000240851.9; ENSP00000240851.4; NM_006070.6; NP_006061.2. DR UCSC; uc003due.4; human. [Q92734-1] DR UCSC; uc031sau.2; human. DR AGR; HGNC:11758; -. DR CTD; 10342; -. DR DisGeNET; 10342; -. DR GeneCards; TFG; -. DR HGNC; HGNC:11758; TFG. DR HPA; ENSG00000114354; Low tissue specificity. DR MalaCards; TFG; -. DR MIM; 602498; gene. DR MIM; 604484; phenotype. DR MIM; 615658; phenotype. DR neXtProt; NX_Q92734; -. DR OpenTargets; ENSG00000114354; -. DR Orphanet; 435819; Autosomal dominant Charcot-Marie-Tooth disease type 2 due to TFG mutation. DR Orphanet; 431329; Autosomal recessive spastic paraplegia type 57. DR Orphanet; 146; Differentiated thyroid carcinoma. DR Orphanet; 209916; Extraskeletal myxoid chondrosarcoma. DR Orphanet; 90117; Hereditary motor and sensory neuropathy, Okinawa type. DR PharmGKB; PA36473; -. DR VEuPathDB; HostDB:ENSG00000114354; -. DR eggNOG; ENOG502QR6R; Eukaryota. DR GeneTree; ENSGT00510000047809; -. DR HOGENOM; CLU_058059_2_0_1; -. DR InParanoid; Q92734; -. DR OMA; SEYRFGM; -. DR OrthoDB; 5359405at2759; -. DR PhylomeDB; Q92734; -. DR TreeFam; TF318743; -. DR PathwayCommons; Q92734; -. DR Reactome; R-HSA-204005; COPII-mediated vesicle transport. DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants. DR SignaLink; Q92734; -. DR SIGNOR; Q92734; -. DR BioGRID-ORCS; 10342; 47 hits in 1155 CRISPR screens. DR ChiTaRS; TFG; human. DR GeneWiki; TFG_(gene); -. DR GenomeRNAi; 10342; -. DR Pharos; Q92734; Tbio. DR PRO; PR:Q92734; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q92734; Protein. DR Bgee; ENSG00000114354; Expressed in secondary oocyte and 196 other cell types or tissues. DR ExpressionAtlas; Q92734; baseline and differential. DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0048208; P:COPII vesicle coating; IEA:InterPro. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; HMP:UniProtKB. DR CDD; cd06401; PB1_TFG; 1. DR InterPro; IPR000270; PB1_dom. DR InterPro; IPR034857; PB1_TFG. DR InterPro; IPR033512; TFG. DR PANTHER; PTHR15335; PROTEIN TFG; 1. DR PANTHER; PTHR15335:SF7; PROTEIN TFG; 1. DR Pfam; PF00564; PB1; 1. DR SMART; SM00666; PB1; 1. DR SUPFAM; SSF54277; CAD & PB1 domains; 1. DR PROSITE; PS51745; PB1; 1. DR Genevisible; Q92734; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Chromosomal rearrangement; Coiled coil; KW Direct protein sequencing; Disease variant; Endoplasmic reticulum; KW ER-Golgi transport; Hereditary spastic paraplegia; Methylation; KW Neurodegeneration; Neuropathy; Phosphoprotein; Proto-oncogene; KW Reference proteome; Transport. FT CHAIN 1..400 FT /note="Protein TFG" FT /id="PRO_0000072500" FT DOMAIN 10..91 FT /note="PB1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081" FT REGION 120..160 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 187..400 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 97..124 FT /evidence="ECO:0000255" FT COMPBIAS 206..220 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 227..347 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 193..194 FT /note="Breakpoint for translocation to form TRK-T3" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" FT MOD_RES 50 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 197 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 385 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 400 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT VAR_SEQ 237..240 FT /note="Missing (in isoform 2 and isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_047131" FT VAR_SEQ 274..284 FT /note="ASYSQQTGPQQ -> GFQSMERFHCK (in isoform 3 and isoform FT 4)" FT /evidence="ECO:0000303|PubMed:22883144" FT /id="VSP_057414" FT VAR_SEQ 285..400 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:22883144" FT /id="VSP_057415" FT VARIANT 106 FT /note="R -> C (in SPG57; defective self-assembly into an FT oligomeric complex; impaired interaction with PDCD6; causes FT mitochondrial fragmentation; dbSNP:rs587777175)" FT /evidence="ECO:0000269|PubMed:23479643, FT ECO:0000269|PubMed:27492651, ECO:0000269|PubMed:27813252" FT /id="VAR_070986" FT VARIANT 106 FT /note="R -> H (in SPG57; causes mitochondrial FT fragmentation; dbSNP:rs376971794)" FT /evidence="ECO:0000269|PubMed:27492651" FT /id="VAR_078075" FT VARIANT 107 FT /note="R -> P (in SPG57; uncertain significance)" FT /evidence="ECO:0000269|PubMed:30237576" FT /id="VAR_082155" FT VARIANT 149 FT /note="A -> S (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035668" FT VARIANT 211 FT /note="A -> V (in dbSNP:rs430945)" FT /id="VAR_054322" FT VARIANT 285 FT /note="P -> L (in HMSNO; does not affect interaction with FT PDCD6; dbSNP:rs207482230)" FT /evidence="ECO:0000269|PubMed:22883144, FT ECO:0000269|PubMed:27813252" FT /id="VAR_068917" FT VARIANT 364 FT /note="T -> P (in dbSNP:rs6772054)" FT /id="VAR_054323" FT CONFLICT 13 FT /note="I -> V (in Ref. 1; CAA69264 and 9; CAA59936)" FT /evidence="ECO:0000305" SQ SEQUENCE 400 AA; 43448 MW; D8A559D0F7314D1F CRC64; MNGQLDLSGK LIIKAQLGED IRRIPIHNED ITYDELVLMM QRVFRGKLLS NDEVTIKYKD EDGDLITIFD SSDLSFAIQC SRILKLTLFV NGQPRPLESS QVKYLRRELI ELRNKVNRLL DSLEPPGEPG PSTNIPENDT VDGREEKSAS DSSGKQSTQV MAASMSAFDP LKNQDEINKN VMSAFGLTDD QVSGPPSAPA EDRSGTPDSI ASSSSAAHPP GVQPQQPPYT GAQTQAGQIE GQMYQQYQQQ AGYGAQQPQA PPQQPQQYGI QYSASYSQQT GPQQPQQFQG YGQQPTSQAP APAFSGQPQQ LPAQPPQQYQ ASNYPAQTYT AQTSQPTNYT VAPASQPGMA PSQPGAYQPR PGFTSLPGST MTPPPSGPNP YARNRPPFGQ GYTQPGPGYR //