STX12_HUMAN
ID STX12_HUMAN Reviewed; 276 AA.
AC Q86Y82; B1AJQ7; O95564;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Syntaxin-12;
GN Name=STX12;
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].
RA Yang J., Yu L., Zhao S.Y.;
RT "Cloning a new human cDNA homologous to R.norvegicus syntaxin 12 mRNA.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Rhodes S.;
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION BY
RP 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 [8]
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 [9]
RP ASSOCIATION WITH THE BLOC-1 COMPLEX, AND INTERACTION WITH BLOC1S6.
RX PubMed=19546860; DOI=10.1038/mp.2009.58;
RA Ghiani C.A., Starcevic M., Rodriguez-Fernandez I.A., Nazarian R.,
RA Cheli V.T., Chan L.N., Malvar J.S., de Vellis J., Sabatti C.,
RA Dell'Angelica E.C.;
RT "The dysbindin-containing complex (BLOC-1) in brain: developmental
RT regulation, interaction with SNARE proteins and role in neurite
RT outgrowth.";
RL Mol. Psychiatry 15:204-215(2010).
RN [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP STRUCTURE BY NMR OF 18-134.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-063, an N-terminal domain of syntaxin 12
RT from human cDNA.";
RL Submitted (OCT-2006) to the PDB data bank.
RN [16]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-88.
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).
CC -!- FUNCTION: SNARE that acts to regulate protein transport between late
CC endosomes and the trans-Golgi network. The SNARE complex containing
CC STX6, STX12, VAMP4 and VTI1A mediates vesicle fusion (in vitro) (By
CC similarity). Through complex formation with GRIP1, GRIA2 and NSG1
CC controls the intracellular fate of AMPAR and the endosomal sorting of
CC the GRIA2 subunit toward recycling and membrane targeting (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:G3V7P1}.
CC -!- SUBUNIT: Interacts with NAPA and SNAP23. Identified in a complex
CC containing STX6, STX12, VAMP4 and VTI1A (By similarity). Associates
CC with the BLOC-1 complex (PubMed:19546860). Interacts with BLOC1S6
CC (PubMed:19546860). Interacts with GRIPAP1 (By similarity). Forms a
CC complex with GRIP1, GRIA2 and NSG1; controls the intracellular fate of
CC AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling
CC and membrane targeting. Interacts with NSG1 (By similarity). Interacts
CC with TPC1 (By similarity). {ECO:0000250|UniProtKB:G3V7P1,
CC ECO:0000250|UniProtKB:Q9ER00, ECO:0000269|PubMed:19546860}.
CC -!- INTERACTION:
CC Q86Y82; O95477: ABCA1; NbExp=9; IntAct=EBI-2691717, EBI-784112;
CC Q86Y82; Q13520: AQP6; NbExp=3; IntAct=EBI-2691717, EBI-13059134;
CC Q86Y82; O94778: AQP8; NbExp=3; IntAct=EBI-2691717, EBI-19124986;
CC Q86Y82; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-2691717, EBI-747430;
CC Q86Y82; P11912: CD79A; NbExp=3; IntAct=EBI-2691717, EBI-7797864;
CC Q86Y82; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-2691717, EBI-1045797;
CC Q86Y82; Q86UW9: DTX2; NbExp=7; IntAct=EBI-2691717, EBI-740376;
CC Q86Y82; Q15125: EBP; NbExp=3; IntAct=EBI-2691717, EBI-3915253;
CC Q86Y82; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-2691717, EBI-781551;
CC Q86Y82; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-2691717, EBI-3917143;
CC Q86Y82; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-2691717, EBI-749265;
CC Q86Y82; O95214: LEPROTL1; NbExp=3; IntAct=EBI-2691717, EBI-750776;
CC Q86Y82; Q6ZSS7: MFSD6; NbExp=3; IntAct=EBI-2691717, EBI-2858252;
CC Q86Y82; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-2691717, EBI-6163737;
CC Q86Y82; O14524-2: NEMP1; NbExp=3; IntAct=EBI-2691717, EBI-10969203;
CC Q86Y82; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-2691717, EBI-716063;
CC Q86Y82; Q96GM1: PLPPR2; NbExp=3; IntAct=EBI-2691717, EBI-12955265;
CC Q86Y82; Q7Z5B4-5: RIC3; NbExp=3; IntAct=EBI-2691717, EBI-12375429;
CC Q86Y82; Q9BY50: SEC11C; NbExp=3; IntAct=EBI-2691717, EBI-2855401;
CC Q86Y82; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-2691717, EBI-18159983;
CC Q86Y82; Q8N2U9: SLC66A2; NbExp=3; IntAct=EBI-2691717, EBI-3907610;
CC Q86Y82; O95721: SNAP29; NbExp=5; IntAct=EBI-2691717, EBI-490676;
CC Q86Y82; Q5SQN1: SNAP47; NbExp=2; IntAct=EBI-2691717, EBI-10244848;
CC Q86Y82; Q16623: STX1A; NbExp=3; IntAct=EBI-2691717, EBI-712466;
CC Q86Y82; P32856-2: STX2; NbExp=3; IntAct=EBI-2691717, EBI-11956649;
CC Q86Y82; Q12846: STX4; NbExp=8; IntAct=EBI-2691717, EBI-744942;
CC Q86Y82; Q9Y2K9: STXBP5L; NbExp=3; IntAct=EBI-2691717, EBI-11294039;
CC Q86Y82; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-2691717, EBI-6268651;
CC Q86Y82; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-2691717, EBI-12947623;
CC Q86Y82; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-2691717, EBI-8638294;
CC Q86Y82; Q9NRX6: TMEM167B; NbExp=3; IntAct=EBI-2691717, EBI-17684533;
CC Q86Y82; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-2691717, EBI-2548832;
CC Q86Y82; Q9Y320: TMX2; NbExp=3; IntAct=EBI-2691717, EBI-6447886;
CC -!- SUBCELLULAR LOCATION: Endosome membrane; Single-pass type IV membrane
CC protein {ECO:0000250|UniProtKB:G3V7P1}. Golgi apparatus membrane;
CC Single-pass type IV membrane protein {ECO:0000250|UniProtKB:G3V7P1}.
CC Endomembrane system {ECO:0000305}; Single-pass type IV membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome membrane
CC {ECO:0000250|UniProtKB:G3V7P1}; Single-pass type IV membrane protein
CC {ECO:0000305}. Recycling endosome membrane
CC {ECO:0000250|UniProtKB:G3V7P1}; Single-pass type IV membrane protein
CC {ECO:0000250|UniProtKB:G3V7P1}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA22911.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF123769; AAP97248.1; -; mRNA.
DR EMBL; AL035306; CAA22911.1; ALT_INIT; mRNA.
DR EMBL; AK297585; BAG59973.1; -; mRNA.
DR EMBL; AL020997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07738.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07739.1; -; Genomic_DNA.
DR EMBL; BC046999; AAH46999.1; -; mRNA.
DR CCDS; CCDS310.1; -.
DR RefSeq; NP_803173.1; NM_177424.2.
DR PDB; 2DNX; NMR; -; A=18-134.
DR PDBsum; 2DNX; -.
DR AlphaFoldDB; Q86Y82; -.
DR SMR; Q86Y82; -.
DR BioGRID; 117191; 202.
DR CORUM; Q86Y82; -.
DR DIP; DIP-44225N; -.
DR IntAct; Q86Y82; 118.
DR MINT; Q86Y82; -.
DR STRING; 9606.ENSP00000363054; -.
DR GlyGen; Q86Y82; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86Y82; -.
DR PhosphoSitePlus; Q86Y82; -.
DR SwissPalm; Q86Y82; -.
DR BioMuta; STX12; -.
DR DMDM; 47117211; -.
DR EPD; Q86Y82; -.
DR jPOST; Q86Y82; -.
DR MassIVE; Q86Y82; -.
DR MaxQB; Q86Y82; -.
DR PaxDb; Q86Y82; -.
DR PeptideAtlas; Q86Y82; -.
DR PRIDE; Q86Y82; -.
DR ProteomicsDB; 70382; -.
DR Antibodypedia; 30837; 193 antibodies from 28 providers.
DR DNASU; 23673; -.
DR Ensembl; ENST00000373943.9; ENSP00000363054.4; ENSG00000117758.14.
DR GeneID; 23673; -.
DR KEGG; hsa:23673; -.
DR MANE-Select; ENST00000373943.9; ENSP00000363054.4; NM_177424.3; NP_803173.1.
DR UCSC; uc001bou.4; human.
DR CTD; 23673; -.
DR DisGeNET; 23673; -.
DR GeneCards; STX12; -.
DR HGNC; HGNC:11430; STX12.
DR HPA; ENSG00000117758; Low tissue specificity.
DR MIM; 606892; gene.
DR neXtProt; NX_Q86Y82; -.
DR OpenTargets; ENSG00000117758; -.
DR PharmGKB; PA36230; -.
DR VEuPathDB; HostDB:ENSG00000117758; -.
DR eggNOG; KOG0811; Eukaryota.
DR GeneTree; ENSGT01000000214440; -.
DR HOGENOM; CLU_059257_1_1_1; -.
DR InParanoid; Q86Y82; -.
DR OMA; EHRQKLH; -.
DR OrthoDB; 1204812at2759; -.
DR PhylomeDB; Q86Y82; -.
DR TreeFam; TF315607; -.
DR PathwayCommons; Q86Y82; -.
DR SignaLink; Q86Y82; -.
DR BioGRID-ORCS; 23673; 16 hits in 1080 CRISPR screens.
DR ChiTaRS; STX12; human.
DR EvolutionaryTrace; Q86Y82; -.
DR GeneWiki; STX12; -.
DR GenomeRNAi; 23673; -.
DR Pharos; Q86Y82; Tbio.
DR PRO; PR:Q86Y82; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q86Y82; protein.
DR Bgee; ENSG00000117758; Expressed in middle temporal gyrus and 200 other tissues.
DR ExpressionAtlas; Q86Y82; baseline and differential.
DR Genevisible; Q86Y82; HS.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:BHF-UCL.
DR GO; GO:0000407; C:phagophore assembly site; IMP:ParkinsonsUK-UCL.
DR GO; GO:0098837; C:postsynaptic recycling endosome; IBA:GO_Central.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0031982; C:vesicle; IMP:ParkinsonsUK-UCL.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IMP:ParkinsonsUK-UCL.
DR GO; GO:0033344; P:cholesterol efflux; IDA:BHF-UCL.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR CDD; cd00179; SynN; 1.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR006011; Syntaxin_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR Pfam; PF05739; SNARE; 1.
DR Pfam; PF14523; Syntaxin_2; 1.
DR SMART; SM00503; SynN; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Endosome; Golgi apparatus;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..276
FT /note="Syntaxin-12"
FT /id="PRO_0000210223"
FT TOPO_DOM 2..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..276
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 178..240
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT COILED 33..131
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ER00"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ER00"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ER00"
FT VARIANT 88
FT /note="P -> R (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035643"
FT HELIX 22..50
FT /evidence="ECO:0007829|PDB:2DNX"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:2DNX"
FT HELIX 57..86
FT /evidence="ECO:0007829|PDB:2DNX"
FT HELIX 93..132
FT /evidence="ECO:0007829|PDB:2DNX"
SQ SEQUENCE 276 AA; 31642 MW; 2338061572ED7DA1 CRC64;
MSYGPLDMYR NPGPSGPQLR DFSSIIQTCS GNIQRISQAT AQIKNLMSQL GTKQDSSKLQ
ENLQQLQHST NQLAKETNEL LKELGSLPLP LSTSEQRQQR LQKERLMNDF SAALNNFQAV
QRRVSEKEKE SIARARAGSR LSAEERQREE QLVSFDSHEE WNQMQSQEDE VAITEQDLEL
IKERETAIRQ LEADILDVNQ IFKDLAMMIH DQGDLIDSIE ANVESSEVHV ERATEQLQRA
AYYQKKSRKK MCILVLVLSV IILILGLIIW LVYKTK
