TFG_HUMAN
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 03-AUG-2022, entry version 192.
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; 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; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-357061, EBI-11976299;
CC Q92734; Q53EZ4: CEP55; NbExp=6; IntAct=EBI-357061, EBI-747776;
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; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-357061, EBI-12000762;
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; 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; Q8IWL8: STH; NbExp=3; IntAct=EBI-357061, EBI-12843506;
CC Q92734; O60806: TBX19; NbExp=3; IntAct=EBI-357061, EBI-12096770;
CC Q92734; Q96LM6: TEX37; NbExp=3; IntAct=EBI-357061, EBI-743976;
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="http://atlasgeneticsoncology.org/Genes/TFGID281.html";
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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; 276.
DR IntAct; Q92734; 163.
DR MINT; Q92734; -.
DR STRING; 9606.ENSP00000240851; -.
DR MoonDB; Q92734; Predicted.
DR GlyGen; Q92734; 6 sites, 1 O-linked glycan (6 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; Q92734; -.
DR PeptideAtlas; Q92734; -.
DR PRIDE; Q92734; -.
DR ProteomicsDB; 34050; -.
DR ProteomicsDB; 75430; -. [Q92734-1]
DR Antibodypedia; 15864; 338 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 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; FNHRPAH; -.
DR OrthoDB; 1379054at2759; -.
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; 40 hits in 1077 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 194 other tissues.
DR ExpressionAtlas; Q92734; baseline and differential.
DR Genevisible; Q92734; HS.
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 I-kappaB kinase/NF-kappaB signaling; 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; PTHR15335; 1.
DR Pfam; PF00564; PB1; 1.
DR SMART; SM00666; PB1; 1.
DR PROSITE; PS51745; PB1; 1.
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; unknown pathological
FT 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
