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 28-JAN-2026, entry version 193. 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 promoting fusion of transport vesicles with target CC membranes. Together with SNARE STX6, promotes movement of vesicles from CC endosomes to the cell membrane, and may therefore function in the CC endocytic recycling pathway. Through complex formation with GRIP1, CC GRIA2 and NSG1 controls the intracellular fate of AMPAR and the CC endosomal sorting of the GRIA2 subunit toward recycling and membrane CC targeting. {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). Interacts (via N-terminus) with VPS13B (By CC 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=10; IntAct=EBI-2691717, EBI-490676; CC Q86Y82; Q5SQN1: SNAP47; NbExp=6; 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=9; 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 {ECO:0000250|UniProtKB:G3V7P1}; CC Single-pass type IV membrane protein {ECO:0000250|UniProtKB:G3V7P1}. CC Golgi apparatus membrane {ECO:0000250|UniProtKB:G3V7P1}; Single-pass CC type IV membrane protein {ECO:0000250|UniProtKB:G3V7P1}. Endomembrane CC system {ECO:0000250|UniProtKB:G3V7P1}; Single-pass type IV membrane CC protein {ECO:0000250|UniProtKB:G3V7P1}; Cytoplasmic side CC {ECO:0000250|UniProtKB:G3V7P1}. Early endosome membrane CC {ECO:0000250|UniProtKB:G3V7P1}; Single-pass type IV membrane protein CC {ECO:0000250|UniProtKB:G3V7P1}. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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_177424.3. DR PDB; 2DNX; NMR; -; A=18-134. DR PDBsum; 2DNX; -. DR AlphaFoldDB; Q86Y82; -. DR SMR; Q86Y82; -. DR BioGRID; 117191; 280. DR CORUM; Q86Y82; -. DR DIP; DIP-44225N; -. DR FunCoup; Q86Y82; 3365. DR IntAct; Q86Y82; 222. 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 jPOST; Q86Y82; -. DR MassIVE; Q86Y82; -. DR PaxDb; 9606-ENSP00000363054; -. DR PeptideAtlas; Q86Y82; -. DR ProteomicsDB; 70382; -. DR Pumba; Q86Y82; -. DR Antibodypedia; 30837; 189 antibodies from 28 providers. DR DNASU; 23673; -. DR Ensembl; ENST00000373943.9; ENSP00000363054.4; ENSG00000117758.15. 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 AGR; HGNC:11430; -. DR ClinPGx; PA36230; -. 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 OpenTargets; ENSG00000117758; -. DR VEuPathDB; HostDB:ENSG00000117758; -. DR eggNOG; KOG0811; Eukaryota. DR GeneTree; ENSGT01000000214440; -. DR HOGENOM; CLU_059257_1_1_1; -. DR InParanoid; Q86Y82; -. DR OMA; QPFLMEQ; -. DR OrthoDB; 364348at2759; -. DR PAN-GO; Q86Y82; 10 GO annotations based on evolutionary models. DR PhylomeDB; Q86Y82; -. DR PathwayCommons; Q86Y82; -. DR SignaLink; Q86Y82; -. DR Agora; ENSG00000117758; -. DR BioGRID-ORCS; 23673; 18 hits in 1159 CRISPR screens. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. 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 202 other cell types or tissues. DR ExpressionAtlas; Q86Y82; baseline and differential. 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: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:0055037; C:recycling endosome; ISS:UniProtKB. 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:0030672; C:synaptic vesicle membrane; 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:0032456; P:endocytic recycling; ISS:UniProtKB. 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; cd15876; SNARE_syntaxin12; 1. DR CDD; cd00179; SynN; 1. DR FunFam; 1.20.5.110:FF:000016; Syntaxin 12; 1. DR FunFam; 1.20.58.70:FF:000009; Syntaxin 12; 1. DR Gene3D; 1.20.5.110; -; 1. DR Gene3D; 1.20.58.70; -; 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; SYNTAXIN; 1. DR PANTHER; PTHR19957:SF88; SYNTAXIN-12; 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; t-snare proteins; 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; Proteomics identification; KW Reference proteome; 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 //