TXLNA_HUMAN
ID TXLNA_HUMAN Reviewed; 546 AA.
AC P40222; D3DPP6; Q5TFJ6; Q66K62; Q86T54; Q86T85; Q86T86; Q86Y86; Q86YW3;
AC Q8N2Y3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Alpha-taxilin;
GN Name=TXLNA; Synonyms=TXLN;
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], INTERACTION WITH SYNTAXIN, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12558796; DOI=10.1046/j.1365-2443.2003.00612.x;
RA Nogami S., Satoh S., Nakano M., Shimizu H., Fukushima H., Maruyama A.,
RA Terano A., Shirataki H.;
RT "Taxilin; a novel syntaxin-binding protein that is involved in Ca2+-
RT dependent exocytosis in neuroendocrine cells.";
RL Genes Cells 8:17-28(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle, and Spinal cord;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, 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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 234-546.
RX PubMed=8327514; DOI=10.1073/pnas.90.13.6330;
RA Ambrus J.L. Jr., Pippin J., Joseph A., Xu C., Blumenthal D., Tamayo A.,
RA Claypool K., McCourt D., Srikiatchatochorn A., Ford R.J.;
RT "Identification of a cDNA for a human high-molecular-weight B-cell growth
RT factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:6330-6334(1993).
RN [7]
RP ERRATUM OF PUBMED:8327514.
RX PubMed=8755619; DOI=10.1073/pnas.93.15.8154-b;
RA Ambrus J.L. Jr., Pippin J., Joseph A., Xu C., Blumenthal D., Tamayo A.,
RA Claypool K., McCourt D., Srikiatchatochorn A., Ford R.J.;
RL Proc. Natl. Acad. Sci. U.S.A. 93:8154-8154(1996).
RN [8]
RP INTERACTION WITH STX1A; STX3A AND STX4A.
RX PubMed=14623251; DOI=10.1016/j.bbrc.2003.10.069;
RA Nogami S., Satoh S., Nakano M., Terano A., Shirataki H.;
RT "Interaction of taxilin with syntaxin which does not form the SNARE
RT complex.";
RL Biochem. Biophys. Res. Commun. 311:797-802(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, 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 [13]
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, AND IDENTIFICATION BY
RP 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 [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-515, 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, 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).
CC -!- FUNCTION: May be involved in intracellular vesicle traffic and
CC potentially in calcium-dependent exocytosis in neuroendocrine cells.
CC -!- SUBUNIT: Binds to the C-terminal coiled coil region of syntaxin family
CC members STX1A, STX3A and STX4A, but not when these proteins are
CC complexed with SNAP25, VAMP2 or STXBP1, suggesting that it interacts
CC with syntaxins that do not form the SNARE complex.
CC {ECO:0000269|PubMed:12558796, ECO:0000269|PubMed:14623251}.
CC -!- INTERACTION:
CC P40222; Q9Y2T1: AXIN2; NbExp=3; IntAct=EBI-359793, EBI-4400025;
CC P40222; Q9NQY0: BIN3; NbExp=3; IntAct=EBI-359793, EBI-2653038;
CC P40222; Q5PSV4: BRMS1L; NbExp=3; IntAct=EBI-359793, EBI-5666615;
CC P40222; P20290: BTF3; NbExp=3; IntAct=EBI-359793, EBI-1054687;
CC P40222; Q96K17: BTF3L4; NbExp=6; IntAct=EBI-359793, EBI-6137496;
CC P40222; Q8NA61: CBY2; NbExp=3; IntAct=EBI-359793, EBI-741724;
CC P40222; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-359793, EBI-11524851;
CC P40222; Q8NEF3-2: CCDC112; NbExp=3; IntAct=EBI-359793, EBI-12095166;
CC P40222; Q96JN2-2: CCDC136; NbExp=5; IntAct=EBI-359793, EBI-10171416;
CC P40222; Q8IYE0: CCDC146; NbExp=3; IntAct=EBI-359793, EBI-10749669;
CC P40222; A0A1B0GWI1: CCDC196; NbExp=5; IntAct=EBI-359793, EBI-10181422;
CC P40222; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-359793, EBI-10961624;
CC P40222; Q8TD31-3: CCHCR1; NbExp=6; IntAct=EBI-359793, EBI-10175300;
CC P40222; Q99459: CDC5L; NbExp=3; IntAct=EBI-359793, EBI-374880;
CC P40222; Q01850: CDR2; NbExp=7; IntAct=EBI-359793, EBI-1181367;
CC P40222; Q9C0F1: CEP44; NbExp=6; IntAct=EBI-359793, EBI-744115;
CC P40222; Q86XR8-3: CEP57; NbExp=3; IntAct=EBI-359793, EBI-11752486;
CC P40222; Q8IYX8: CEP57L1; NbExp=3; IntAct=EBI-359793, EBI-1104570;
CC P40222; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-359793, EBI-10181988;
CC P40222; Q96MT8: CEP63; NbExp=4; IntAct=EBI-359793, EBI-741977;
CC P40222; Q96M91: CFAP53; NbExp=3; IntAct=EBI-359793, EBI-742422;
CC P40222; Q05D60: DEUP1; NbExp=11; IntAct=EBI-359793, EBI-748597;
CC P40222; Q9NPF5: DMAP1; NbExp=3; IntAct=EBI-359793, EBI-399105;
CC P40222; O60941: DTNB; NbExp=5; IntAct=EBI-359793, EBI-740402;
CC P40222; O60941-5: DTNB; NbExp=3; IntAct=EBI-359793, EBI-11984733;
CC P40222; Q9NRA8: EIF4ENIF1; NbExp=3; IntAct=EBI-359793, EBI-301024;
CC P40222; O95208-2: EPN2; NbExp=3; IntAct=EBI-359793, EBI-12135243;
CC P40222; Q8TBF8: FAM81A; NbExp=3; IntAct=EBI-359793, EBI-11993062;
CC P40222; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-359793, EBI-8468186;
CC P40222; O95995: GAS8; NbExp=3; IntAct=EBI-359793, EBI-1052570;
CC P40222; Q08379: GOLGA2; NbExp=3; IntAct=EBI-359793, EBI-618309;
CC P40222; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-359793, EBI-11163335;
CC P40222; Q9H8Y8: GORASP2; NbExp=7; IntAct=EBI-359793, EBI-739467;
CC P40222; Q68CZ6: HAUS3; NbExp=9; IntAct=EBI-359793, EBI-2558217;
CC P40222; Q9NX55: HYPK; NbExp=6; IntAct=EBI-359793, EBI-1048743;
CC P40222; Q63ZY3: KANK2; NbExp=6; IntAct=EBI-359793, EBI-2556193;
CC P40222; Q86T90: KIAA1328; NbExp=3; IntAct=EBI-359793, EBI-3437878;
CC P40222; A1A4E9: KRT13; NbExp=3; IntAct=EBI-359793, EBI-10171552;
CC P40222; P19012: KRT15; NbExp=6; IntAct=EBI-359793, EBI-739566;
CC P40222; P35900: KRT20; NbExp=6; IntAct=EBI-359793, EBI-742094;
CC P40222; Q2M2I5: KRT24; NbExp=3; IntAct=EBI-359793, EBI-2952736;
CC P40222; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-359793, EBI-3044087;
CC P40222; Q15323: KRT31; NbExp=6; IntAct=EBI-359793, EBI-948001;
CC P40222; O76011: KRT34; NbExp=3; IntAct=EBI-359793, EBI-1047093;
CC P40222; Q92764: KRT35; NbExp=3; IntAct=EBI-359793, EBI-1058674;
CC P40222; O76013-2: KRT36; NbExp=3; IntAct=EBI-359793, EBI-11958506;
CC P40222; O76015: KRT38; NbExp=6; IntAct=EBI-359793, EBI-1047263;
CC P40222; Q6A162: KRT40; NbExp=6; IntAct=EBI-359793, EBI-10171697;
CC P40222; O95678: KRT75; NbExp=3; IntAct=EBI-359793, EBI-2949715;
CC P40222; Q86VQ0: LCA5; NbExp=3; IntAct=EBI-359793, EBI-6658186;
CC P40222; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-359793, EBI-1216080;
CC P40222; Q9NS73-5: MBIP; NbExp=3; IntAct=EBI-359793, EBI-10182361;
CC P40222; P23508: MCC; NbExp=3; IntAct=EBI-359793, EBI-307531;
CC P40222; Q9NPJ6: MED4; NbExp=8; IntAct=EBI-359793, EBI-394607;
CC P40222; P50221: MEOX1; NbExp=3; IntAct=EBI-359793, EBI-2864512;
CC P40222; P50222: MEOX2; NbExp=3; IntAct=EBI-359793, EBI-748397;
CC P40222; Q9NYP9: MIS18A; NbExp=4; IntAct=EBI-359793, EBI-1104552;
CC P40222; Q13765: NACA; NbExp=2; IntAct=EBI-359793, EBI-712216;
CC P40222; O14777: NDC80; NbExp=7; IntAct=EBI-359793, EBI-715849;
CC P40222; Q6ZUT1: NKAPD1; NbExp=3; IntAct=EBI-359793, EBI-3920396;
CC P40222; Q13287: NMI; NbExp=9; IntAct=EBI-359793, EBI-372942;
CC P40222; Q96MF7: NSMCE2; NbExp=6; IntAct=EBI-359793, EBI-2557388;
CC P40222; P37198: NUP62; NbExp=8; IntAct=EBI-359793, EBI-347978;
CC P40222; Q13516: OLIG2; NbExp=3; IntAct=EBI-359793, EBI-3914525;
CC P40222; O75928-2: PIAS2; NbExp=3; IntAct=EBI-359793, EBI-348567;
CC P40222; Q13136: PPFIA1; NbExp=5; IntAct=EBI-359793, EBI-745426;
CC P40222; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-359793, EBI-1105153;
CC P40222; O43395: PRPF3; NbExp=3; IntAct=EBI-359793, EBI-744322;
CC P40222; Q8NHQ8-2: RASSF8; NbExp=3; IntAct=EBI-359793, EBI-10976415;
CC P40222; Q9P2K3: RCOR3; NbExp=3; IntAct=EBI-359793, EBI-743428;
CC P40222; Q6NUQ1: RINT1; NbExp=6; IntAct=EBI-359793, EBI-726876;
CC P40222; Q9BRV8: SIKE1; NbExp=3; IntAct=EBI-359793, EBI-1773646;
CC P40222; Q969G3: SMARCE1; NbExp=3; IntAct=EBI-359793, EBI-455078;
CC P40222; Q96H20: SNF8; NbExp=3; IntAct=EBI-359793, EBI-747719;
CC P40222; O60504: SORBS3; NbExp=3; IntAct=EBI-359793, EBI-741237;
CC P40222; Q8WXA9: SREK1; NbExp=3; IntAct=EBI-359793, EBI-1044237;
CC P40222; Q93045: STMN2; NbExp=4; IntAct=EBI-359793, EBI-714194;
CC P40222; Q16623: STX1A; NbExp=4; IntAct=EBI-359793, EBI-712466;
CC P40222; P61266: STX1B; NbExp=3; IntAct=EBI-359793, EBI-9071709;
CC P40222; Q86TI0: TBC1D1; NbExp=3; IntAct=EBI-359793, EBI-1644036;
CC P40222; Q9UHD2: TBK1; NbExp=6; IntAct=EBI-359793, EBI-356402;
CC P40222; P56279: TCL1A; NbExp=6; IntAct=EBI-359793, EBI-749995;
CC P40222; Q9UBB9: TFIP11; NbExp=8; IntAct=EBI-359793, EBI-1105213;
CC P40222; Q15025: TNIP1; NbExp=6; IntAct=EBI-359793, EBI-357849;
CC P40222; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-359793, EBI-11952721;
CC P40222; Q13625-3: TP53BP2; NbExp=3; IntAct=EBI-359793, EBI-10175039;
CC P40222; Q6PID6: TTC33; NbExp=6; IntAct=EBI-359793, EBI-2555404;
CC P40222; Q8N3L3: TXLNB; NbExp=11; IntAct=EBI-359793, EBI-6116822;
CC P40222; Q8N6Y0: USHBP1; NbExp=6; IntAct=EBI-359793, EBI-739895;
CC P40222; Q5TAP6: UTP14C; NbExp=3; IntAct=EBI-359793, EBI-11737646;
CC P40222; Q8N1B4: VPS52; NbExp=6; IntAct=EBI-359793, EBI-2799833;
CC P40222; Q9Y3C0: WASHC3; NbExp=8; IntAct=EBI-359793, EBI-712969;
CC P40222; Q9QYP6: Azi2; Xeno; NbExp=2; IntAct=EBI-359793, EBI-6115874;
CC -!- TISSUE SPECIFICITY: Ubiquitous, with much higher expression in heart,
CC kidney, liver and pancreas. {ECO:0000269|PubMed:12558796}.
CC -!- SIMILARITY: Belongs to the taxilin family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a high molecular weight
CC interleukin (IL-14 or IL14). {ECO:0000305|PubMed:8327514}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH46565.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF516206; AAO42465.1; -; mRNA.
DR EMBL; AL832636; CAD89951.1; -; mRNA.
DR EMBL; AL832637; CAD89952.1; -; mRNA.
DR EMBL; AL832338; CAD91138.1; -; mRNA.
DR EMBL; AL049795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07565.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07566.1; -; Genomic_DNA.
DR EMBL; BC029686; AAH29686.1; -; mRNA.
DR EMBL; BC046565; AAH46565.1; ALT_INIT; mRNA.
DR EMBL; BC080578; AAH80578.1; -; mRNA.
DR EMBL; BC103823; AAI03824.1; -; mRNA.
DR EMBL; BC103824; AAI03825.1; -; mRNA.
DR EMBL; L15344; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS353.1; -.
DR PIR; A48203; A48203.
DR RefSeq; NP_787048.1; NM_175852.3.
DR RefSeq; XP_016856051.1; XM_017000562.1.
DR AlphaFoldDB; P40222; -.
DR SMR; P40222; -.
DR BioGRID; 128297; 204.
DR CORUM; P40222; -.
DR DIP; DIP-27612N; -.
DR IntAct; P40222; 138.
DR MINT; P40222; -.
DR STRING; 9606.ENSP00000362711; -.
DR GlyGen; P40222; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P40222; -.
DR MetOSite; P40222; -.
DR PhosphoSitePlus; P40222; -.
DR SwissPalm; P40222; -.
DR BioMuta; TXLNA; -.
DR DMDM; 55584162; -.
DR EPD; P40222; -.
DR jPOST; P40222; -.
DR MassIVE; P40222; -.
DR MaxQB; P40222; -.
DR PaxDb; P40222; -.
DR PeptideAtlas; P40222; -.
DR PRIDE; P40222; -.
DR ProteomicsDB; 55349; -.
DR Antibodypedia; 31239; 154 antibodies from 29 providers.
DR DNASU; 200081; -.
DR Ensembl; ENST00000373609.1; ENSP00000362711.1; ENSG00000084652.16.
DR Ensembl; ENST00000373610.8; ENSP00000362712.3; ENSG00000084652.16.
DR GeneID; 200081; -.
DR KEGG; hsa:200081; -.
DR MANE-Select; ENST00000373610.8; ENSP00000362712.3; NM_175852.4; NP_787048.1.
DR UCSC; uc001bui.4; human.
DR CTD; 200081; -.
DR DisGeNET; 200081; -.
DR GeneCards; TXLNA; -.
DR HGNC; HGNC:30685; TXLNA.
DR HPA; ENSG00000084652; Low tissue specificity.
DR MIM; 608676; gene.
DR neXtProt; NX_P40222; -.
DR OpenTargets; ENSG00000084652; -.
DR PharmGKB; PA142670668; -.
DR VEuPathDB; HostDB:ENSG00000084652; -.
DR eggNOG; KOG1850; Eukaryota.
DR GeneTree; ENSGT00940000158303; -.
DR HOGENOM; CLU_025501_3_0_1; -.
DR InParanoid; P40222; -.
DR OMA; VTEAPCC; -.
DR OrthoDB; 904532at2759; -.
DR PhylomeDB; P40222; -.
DR TreeFam; TF318595; -.
DR PathwayCommons; P40222; -.
DR Reactome; R-HSA-449836; Other interleukin signaling.
DR SignaLink; P40222; -.
DR BioGRID-ORCS; 200081; 19 hits in 1082 CRISPR screens.
DR ChiTaRS; TXLNA; human.
DR GeneWiki; TXLNA; -.
DR GenomeRNAi; 200081; -.
DR Pharos; P40222; Tbio.
DR PRO; PR:P40222; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P40222; protein.
DR Bgee; ENSG00000084652; Expressed in stromal cell of endometrium and 180 other tissues.
DR Genevisible; P40222; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0019905; F:syntaxin binding; IEA:InterPro.
DR GO; GO:0042113; P:B cell activation; IEA:Ensembl.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR InterPro; IPR026183; Taxilin_fam.
DR PANTHER; PTHR16127; PTHR16127; 1.
DR Pfam; PF09728; Taxilin; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Exocytosis; Phosphoprotein; Reference proteome.
FT CHAIN 1..546
FT /note="Alpha-taxilin"
FT /id="PRO_0000189421"
FT REGION 1..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 186..491
FT /evidence="ECO:0000255"
FT COMPBIAS 136..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CONFLICT 12
FT /note="K -> Q (in Ref. 2; CAD89951)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="K -> R (in Ref. 2; CAD89952)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="R -> C (in Ref. 5; AAH80578)"
FT /evidence="ECO:0000305"
FT CONFLICT 249..250
FT /note="QR -> HG (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="Q -> L (in Ref. 2; CAD89952)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="E -> A (in Ref. 2; CAD89952)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="K -> E (in Ref. 2; CAD89951)"
FT /evidence="ECO:0000305"
FT CONFLICT 530
FT /note="T -> A (in Ref. 2; CAD91138)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 546 AA; 61891 MW; 698CD74F78897DF6 CRC64;
MKNQDKKNGA AKQSNPKSSP GQPEAGPEGA QERPSQAAPA VEAEGPGSSQ APRKPEGAQA
RTAQSGALRD VSEELSRQLE DILSTYCVDN NQGGPGEDGA QGEPAEPEDA EKSRTYVARN
GEPEPTPVVN GEKEPSKGDP NTEEIRQSDE VGDRDHRRPQ EKKKAKGLGK EITLLMQTLN
TLSTPEEKLA ALCKKYAELL EEHRNSQKQM KLLQKKQSQL VQEKDHLRGE HSKAVLARSK
LESLCRELQR HNRSLKEEGV QRAREEEEKR KEVTSHFQVT LNDIQLQMEQ HNERNSKLRQ
ENMELAERLK KLIEQYELRE EHIDKVFKHK DLQQQLVDAK LQQAQEMLKE AEERHQREKD
FLLKEAVESQ RMCELMKQQE THLKQQLALY TEKFEEFQNT LSKSSEVFTT FKQEMEKMTK
KIKKLEKETT MYRSRWESSN KALLEMAEEK TVRDKELEGL QVKIQRLEKL CRALQTERND
LNKRVQDLSA GGQGSLTDSG PERRPEGPGA QAPSSPRVTE APCYPGAPST EASGQTGPQE
PTSARA
