TXLNG_HUMAN
ID TXLNG_HUMAN Reviewed; 528 AA.
AC Q9NUQ3; Q2KQ75; Q5JNZ7; Q9P0X1;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Gamma-taxilin;
DE AltName: Full=Environmental lipopolysaccharide-responding gene protein;
DE AltName: Full=Factor inhibiting ATF4-mediated transcription;
DE Short=FIAT;
DE AltName: Full=Lipopolysaccharide-specific response protein 5;
GN Name=TXLNG; Synonyms=CXorf15, ELRG, LSR5;
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 2).
RA Dohnal A.M., Panzer-Gruemayer R.E.;
RT "Anti-leukemia-specific humoral immune response in children with T-lineage
RT acute lymphoblastic leukemia.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 343-528.
RA Chai Y.B., Zhao Z.L., Zhu F., Yan W., Chen N.C., Wang Q., Yue L.,
RA Chen S.M.;
RT "New Homo sapiens gene from dental pulp cells.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP TISSUE SPECIFICITY, AND INTERACTION WITH STX1A; STX3A AND STX4A.
RX PubMed=15184072; DOI=10.1016/j.bbrc.2004.05.073;
RA Nogami S., Satoh S., Tanaka-Nakadate S., Yoshida K., Nakano M., Terano A.,
RA Shirataki H.;
RT "Identification and characterization of taxilin isoforms.";
RL Biochem. Biophys. Res. Commun. 319:936-943(2004).
RN [8]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=15911876; DOI=10.1083/jcb.200412139;
RA Yu V.W., Ambartsoumian G., Verlinden L., Moir J.M., Prud'homme J.,
RA Gauthier C., Roughley P.J., St-Arnaud R.;
RT "FIAT represses ATF4-mediated transcription to regulate bone mass in
RT transgenic mice.";
RL J. Cell Biol. 169:591-601(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-105, AND
RP IDENTIFICATION 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 [11]
RP FUNCTION, AND INDUCTION.
RX PubMed=18068885; DOI=10.1016/j.tox.2007.10.025;
RA Du K., Chai Y., Hou L., Chang W., Chen S., Luo W., Cai T., Zhang X.,
RA Chen N., Chen Y., Chen J.;
RT "Over-expression and siRNA of a novel environmental lipopolysaccharide-
RT responding gene on the cell cycle of the human hepatoma-derived cell line
RT HepG2.";
RL Toxicology 243:303-310(2008).
RN [12]
RP IDENTIFICATION BY MASS 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-86, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND TYR-283, AND
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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; SER-97 AND SER-105, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, 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 [19]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-12 AND ARG-24, AND IDENTIFICATION
RP 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).
CC -!- FUNCTION: May be involved in intracellular vesicle traffic. Inhibits
CC ATF4-mediated transcription, possibly by dimerizing with ATF4 to form
CC inactive dimers that cannot bind DNA. May be involved in regulating
CC bone mass density through an ATF4-dependent pathway. May be involved in
CC cell cycle progression. {ECO:0000269|PubMed:15911876,
CC ECO:0000269|PubMed:18068885}.
CC -!- SUBUNIT: Binds to the C-terminal coiled coil region of syntaxin family
CC members STX1A, STX3A and STX4A. Forms a heterodimer with ATF4 in
CC osteoblasts. {ECO:0000269|PubMed:15911876}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:15911876}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8BHN1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NUQ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NUQ3-2; Sequence=VSP_039391;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at high level in
CC heart and skeletal muscle. Expressed in brain, placenta, lung, liver,
CC kidney and pancreas. {ECO:0000269|PubMed:15184072}.
CC -!- INDUCTION: By bacterial lipopolysaccharides (LPS) in Hep-G2 cells.
CC {ECO:0000269|PubMed:18068885}.
CC -!- MISCELLANEOUS: Depletion of TXLNG by siRNA decreases the percentage of
CC Hep-G2 cells arrested in G1 phase.
CC -!- SIMILARITY: Belongs to the taxilin family. {ECO:0000305}.
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DR EMBL; AY739713; AAW65982.1; -; mRNA.
DR EMBL; AK002071; BAA92068.1; -; mRNA.
DR EMBL; AL929302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX004861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471074; EAW98918.1; -; Genomic_DNA.
DR EMBL; BC101572; AAI01573.1; -; mRNA.
DR EMBL; BC101576; AAI01577.1; -; mRNA.
DR EMBL; AF143740; AAF70546.2; -; mRNA.
DR CCDS; CCDS14178.1; -. [Q9NUQ3-1]
DR CCDS; CCDS55373.1; -. [Q9NUQ3-2]
DR RefSeq; NP_001162154.1; NM_001168683.1. [Q9NUQ3-2]
DR RefSeq; NP_060830.2; NM_018360.2. [Q9NUQ3-1]
DR AlphaFoldDB; Q9NUQ3; -.
DR SMR; Q9NUQ3; -.
DR BioGRID; 120901; 88.
DR IntAct; Q9NUQ3; 29.
DR MINT; Q9NUQ3; -.
DR STRING; 9606.ENSP00000369465; -.
DR GlyGen; Q9NUQ3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NUQ3; -.
DR MetOSite; Q9NUQ3; -.
DR PhosphoSitePlus; Q9NUQ3; -.
DR BioMuta; TXLNG; -.
DR DMDM; 212276476; -.
DR EPD; Q9NUQ3; -.
DR jPOST; Q9NUQ3; -.
DR MassIVE; Q9NUQ3; -.
DR MaxQB; Q9NUQ3; -.
DR PaxDb; Q9NUQ3; -.
DR PeptideAtlas; Q9NUQ3; -.
DR PRIDE; Q9NUQ3; -.
DR ProteomicsDB; 82707; -. [Q9NUQ3-1]
DR ProteomicsDB; 82708; -. [Q9NUQ3-2]
DR Antibodypedia; 410; 93 antibodies from 15 providers.
DR DNASU; 55787; -.
DR Ensembl; ENST00000380122.10; ENSP00000369465.5; ENSG00000086712.13. [Q9NUQ3-1]
DR Ensembl; ENST00000398155.4; ENSP00000381222.4; ENSG00000086712.13. [Q9NUQ3-2]
DR GeneID; 55787; -.
DR KEGG; hsa:55787; -.
DR MANE-Select; ENST00000380122.10; ENSP00000369465.5; NM_018360.3; NP_060830.2.
DR UCSC; uc004cxq.3; human. [Q9NUQ3-1]
DR CTD; 55787; -.
DR DisGeNET; 55787; -.
DR GeneCards; TXLNG; -.
DR HGNC; HGNC:18578; TXLNG.
DR HPA; ENSG00000086712; Low tissue specificity.
DR MIM; 300677; gene.
DR neXtProt; NX_Q9NUQ3; -.
DR OpenTargets; ENSG00000086712; -.
DR PharmGKB; PA38588; -.
DR VEuPathDB; HostDB:ENSG00000086712; -.
DR eggNOG; KOG1850; Eukaryota.
DR GeneTree; ENSGT00940000155463; -.
DR HOGENOM; CLU_025501_4_1_1; -.
DR InParanoid; Q9NUQ3; -.
DR OMA; WRKKSHH; -.
DR OrthoDB; 904532at2759; -.
DR PhylomeDB; Q9NUQ3; -.
DR TreeFam; TF318595; -.
DR PathwayCommons; Q9NUQ3; -.
DR SignaLink; Q9NUQ3; -.
DR BioGRID-ORCS; 55787; 10 hits in 705 CRISPR screens.
DR ChiTaRS; TXLNG; human.
DR GenomeRNAi; 55787; -.
DR Pharos; Q9NUQ3; Tbio.
DR PRO; PR:Q9NUQ3; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9NUQ3; protein.
DR Bgee; ENSG00000086712; Expressed in secondary oocyte and 172 other tissues.
DR Genevisible; Q9NUQ3; HS.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0019905; F:syntaxin binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030500; P:regulation of bone mineralization; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0010564; P:regulation of cell cycle process; IMP:UniProtKB.
DR InterPro; IPR026183; Taxilin_fam.
DR PANTHER; PTHR16127; PTHR16127; 1.
DR Pfam; PF09728; Taxilin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Coiled coil; Cytoplasm; Membrane;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..528
FT /note="Gamma-taxilin"
FT /id="PRO_0000189426"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 153..464
FT /evidence="ECO:0000255"
FT COMPBIAS 21..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 24
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BHN1"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 283
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 35..166
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_039391"
FT VARIANT 246
FT /note="I -> V (in dbSNP:rs5969783)"
FT /id="VAR_019809"
FT CONFLICT 249
FT /note="N -> D (in Ref. 2; BAA92068)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="H -> R (in Ref. 2; BAA92068)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="K -> I (in Ref. 6; AAF70546)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 60586 MW; 4EAC314330CE4490 CRC64;
MATRVEEAAR GRGGGAEEAT EAGRGGRRRS PRQKFEIGTM EEAGICGLGV KADMLCNSQS
NDILQHQGSN CGGTSNKHSL EEDEGSDFIT ENRNLVSPAY CTQESREEIP GGEARTDPPD
GQQDSECNRN KEKTLGKEVL LLMQALNTLS TPEEKLAALC KKYADLLEES RSVQKQMKIL
QKKQAQIVKE KVHLQSEHSK AILARSKLES LCRELQRHNK TLKEENMQQA REEEERRKEA
TAHFQITLNE IQAQLEQHDI HNAKLRQENI ELGEKLKKLI EQYALREEHI DKVFKHKELQ
QQLVDAKLQQ TTQLIKEADE KHQREREFLL KEATESRHKY EQMKQQEVQL KQQLSLYMDK
FEEFQTTMAK SNELFTTFRQ EMEKMTKKIK KLEKETIIWR TKWENNNKAL LQMAEEKTVR
DKEYKALQIK LERLEKLCRA LQTERNELNE KVEVLKEQVS IKAAIKAANR DLATPVMQPC
TALDSHKELN TSSKRALGAH LEAEPKSQRS AVQKPPSTGS APAIESVD
