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Protein

Syntaxin-12

Gene

Stx12

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

SNARE that acts to regulate protein transport between late endosomes and the trans-Golgi network. The SNARE complex containing STX6, STX12, VAMP4 and VTI1A mediates vesicle fusion (in vitro) (By similarity).By similarity

GO - Molecular functioni

  1. SNAP receptor activity Source: GO_Central
  2. SNARE binding Source: GO_Central

GO - Biological processi

  1. cholesterol efflux Source: MGI
  2. intracellular protein transport Source: GO_Central
  3. protein stabilization Source: MGI
  4. vesicle docking Source: GO_Central
  5. vesicle fusion Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Syntaxin-12
Gene namesi
Name:Stx12
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1931027. Stx12.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 250249CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei251 – 27121Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
BLAST
Topological domaini272 – 2743VesicularSequence Analysis

GO - Cellular componenti

  1. BLOC-1 complex Source: Ensembl
  2. endomembrane system Source: GO_Central
  3. endosome membrane Source: UniProtKB-SubCell
  4. extracellular vesicular exosome Source: MGI
  5. Golgi membrane Source: UniProtKB-SubCell
  6. integral component of membrane Source: GO_Central
  7. membrane raft Source: MGI
  8. phagocytic vesicle Source: MGI
  9. SNARE complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 274273Syntaxin-12PRO_0000210224Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei139 – 1391Phosphoserine1 Publication
Modified residuei142 – 1421Phosphoserine1 Publication
Modified residuei218 – 2181Phosphoserine1 Publication
Modified residuei225 – 2251Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9ER00.
PaxDbiQ9ER00.
PRIDEiQ9ER00.

PTM databases

PhosphoSiteiQ9ER00.

Expressioni

Gene expression databases

BgeeiQ9ER00.
CleanExiMM_STX12.
GenevestigatoriQ9ER00.

Interactioni

Subunit structurei

Associates with the BLOC-1 complex. Interacts with BLOC1S6. Interacts with NAPA and SNAP23. Identified in a complex containing STX6, STX12, VAMP4 and VTI1A (By similarity).By similarity

Protein-protein interaction databases

BioGridi221409. 1 interaction.
IntActiQ9ER00. 8 interactions.
MINTiMINT-1865936.

Structurei

3D structure databases

ProteinModelPortaliQ9ER00.
SMRiQ9ER00. Positions 15-139, 184-248.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini178 – 24063t-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili33 – 13098Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the syntaxin family.Curated
Contains 1 t-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5325.
GeneTreeiENSGT00450000040239.
HOGENOMiHOG000188453.
HOVERGENiHBG053083.
InParanoidiQ9ER00.
KOiK13813.
OMAiQMQSQEE.
OrthoDBiEOG7B31PS.
PhylomeDBiQ9ER00.
TreeFamiTF315607.

Family and domain databases

InterProiIPR006012. Syntaxin/epimorphin_CS.
IPR006011. Syntaxin_N.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF05739. SNARE. 1 hit.
[Graphical view]
SMARTiSM00503. SynN. 1 hit.
SM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMiSSF47661. SSF47661. 1 hit.
PROSITEiPS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9ER00-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSYGPLDMYR NPGPSGPQPR DFNSIIQTCS GNIQRISQAT AQIKNLMSQL
60 70 80 90 100
GTKQDSSKLQ ENLQQLQHST NQLAKETNEL LKELGSLPLP LSASEQRQQK
110 120 130 140 150
LQKERLMNDF SSALNNFQVV QRKVSEKEKE SIARARAGSR LSAEDRQREE
160 170 180 190 200
QLVSFDSHEE WNQMQSQEEE AAITEQDLEL IKERETAIRQ LEADILDVNQ
210 220 230 240 250
IFKDLAMMIH DQGDLIDSIE ANVESSEVHV ERATDQLQRA AYYQKKSRKK
260 270
MCILVLVLSV IVTVLVVVIW VASK
Length:274
Mass (Da):31,195
Last modified:March 1, 2001 - v1
Checksum:i443A294A1A1E2905
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti171 – 1711A → V in AAH10669. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB019211 mRNA. Translation: BAB20282.1.
AK077678 mRNA. Translation: BAC36951.1.
AK078948 mRNA. Translation: BAC37473.1.
AK146544 mRNA. Translation: BAE27249.1.
AK146735 mRNA. Translation: BAE27397.1.
AK167087 mRNA. Translation: BAE39244.1.
BC010669 mRNA. Translation: AAH10669.1.
CCDSiCCDS18737.1.
RefSeqiNP_598648.1. NM_133887.4.
UniGeneiMm.28237.
Mm.491148.

Genome annotation databases

EnsembliENSMUST00000030698; ENSMUSP00000030698; ENSMUSG00000028879.
GeneIDi100226.
KEGGimmu:100226.
UCSCiuc008vbx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB019211 mRNA. Translation: BAB20282.1.
AK077678 mRNA. Translation: BAC36951.1.
AK078948 mRNA. Translation: BAC37473.1.
AK146544 mRNA. Translation: BAE27249.1.
AK146735 mRNA. Translation: BAE27397.1.
AK167087 mRNA. Translation: BAE39244.1.
BC010669 mRNA. Translation: AAH10669.1.
CCDSiCCDS18737.1.
RefSeqiNP_598648.1. NM_133887.4.
UniGeneiMm.28237.
Mm.491148.

3D structure databases

ProteinModelPortaliQ9ER00.
SMRiQ9ER00. Positions 15-139, 184-248.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi221409. 1 interaction.
IntActiQ9ER00. 8 interactions.
MINTiMINT-1865936.

PTM databases

PhosphoSiteiQ9ER00.

Proteomic databases

MaxQBiQ9ER00.
PaxDbiQ9ER00.
PRIDEiQ9ER00.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030698; ENSMUSP00000030698; ENSMUSG00000028879.
GeneIDi100226.
KEGGimmu:100226.
UCSCiuc008vbx.1. mouse.

Organism-specific databases

CTDi23673.
MGIiMGI:1931027. Stx12.

Phylogenomic databases

eggNOGiCOG5325.
GeneTreeiENSGT00450000040239.
HOGENOMiHOG000188453.
HOVERGENiHBG053083.
InParanoidiQ9ER00.
KOiK13813.
OMAiQMQSQEE.
OrthoDBiEOG7B31PS.
PhylomeDBiQ9ER00.
TreeFamiTF315607.

Miscellaneous databases

NextBioi354343.
PROiQ9ER00.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ER00.
CleanExiMM_STX12.
GenevestigatoriQ9ER00.

Family and domain databases

InterProiIPR006012. Syntaxin/epimorphin_CS.
IPR006011. Syntaxin_N.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF05739. SNARE. 1 hit.
[Graphical view]
SMARTiSM00503. SynN. 1 hit.
SM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMiSSF47661. SSF47661. 1 hit.
PROSITEiPS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse syntaxin12."
    Nakamura N., Wada Y., Futai M.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Amnion, Cecum and Kidney.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139; SER-142; SER-218 AND SER-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSTX12_MOUSE
AccessioniPrimary (citable) accession number: Q9ER00
Secondary accession number(s): Q3UIV9, Q921T9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: March 1, 2001
Last modified: February 4, 2015
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.