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O43752 (STX6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Syntaxin-6
Gene names
Name:STX6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length255 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in intracellular vesicle trafficking.

Subunit structure

Binds EEA1. Interacts with VPS45A. Interacts with MARCH2 and MARCH3 By similarity. Interacts with GOPC. Identified in a complex containing STX6, STX12, VAMP4 and VTI1A. Ref.7 Ref.10

Subcellular location

Golgi apparatus membrane; Single-pass type IV membrane protein Potential Ref.7.

Sequence similarities

Belongs to the syntaxin family.

Contains 1 t-SNARE coiled-coil homology domain.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentGolgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Transmembrane
Transmembrane helix
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi vesicle transport

Inferred from electronic annotation. Source: InterPro

endosome organization

Inferred from electronic annotation. Source: Ensembl

intracellular protein transport

Inferred from Biological aspect of Ancestor. Source: RefGenome

retrograde transport, endosome to Golgi

Inferred from mutant phenotype PubMed 19224922. Source: UniProtKB

vesicle fusion

Inferred from physical interaction PubMed 10506127. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 19224922. Source: UniProtKB

Golgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

SNARE complex

Inferred from direct assay PubMed 19620288. Source: MGI

clathrin-coated vesicle

Traceable author statement PubMed 9697774. Source: UniProtKB

early endosome

Inferred from direct assay PubMed 10506127. Source: UniProtKB

integral component of membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

perinuclear region of cytoplasm

Inferred from direct assay PubMed 10506127. Source: UniProtKB

plasma membrane

Traceable author statement PubMed 9697774. Source: UniProtKB

trans-Golgi network membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionSNAP receptor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction Ref.7PubMed 11707463PubMed 20685960. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43752-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O43752-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-101: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 255254Syntaxin-6
PRO_0000210208

Regions

Topological domain2 – 234233Cytoplasmic Potential
Transmembrane235 – 25521Helical; Anchor for type IV membrane protein; Potential
Domain163 – 22563t-SNARE coiled-coil homology
Coiled coil41 – 7434 Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.9
Modified residue21Phosphoserine Ref.9
Modified residue1521Phosphoserine Ref.8

Natural variations

Alternative sequence1 – 101101Missing in isoform 2.
VSP_054763

Experimental info

Sequence conflict771K → R in CAG46654. Ref.2

Secondary structure

............. 255
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: CC05C025DE1FE89E

FASTA25529,176
        10         20         30         40         50         60 
MSMEDPFFVV KGEVQKAVNT AQGLFQRWTE LLQDPSTATR EEIDWTTNEL RNNLRSIEWD 

        70         80         90        100        110        120 
LEDLDETISI VEANPRKFNL DATELSIRKA FITSTRQVVR DMKDQMSTSS VQALAERKNR 

       130        140        150        160        170        180 
QALLGDSGSQ NWSTGTTDKY GRLDRELQRA NSHFIEEQQA QQQLIVEQQD EQLELVSGSI 

       190        200        210        220        230        240 
GVLKNMSQRI GGELEEQAVM LEDFSHELES TQSRLDNVMK KLAKVSHMTS DRRQWCAIAI 

       250 
LFAVLLVVLI LFLVL 

« Hide

Isoform 2 [UniParc].

Checksum: 63C26276F286C7E9
Show »

FASTA15417,434

References

« Hide 'large scale' references
[1]"Co-expression of several human syntaxin genes in neutrophils and differentiating HL-60 cells: variant isoforms and detection of syntaxin 1."
Martin-Martin B., Nabokina S.M., Lazo P.A., Mollinedo F.
J. Leukoc. Biol. 65:397-406(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM 1).
Tissue: Muscle.
[7]"Association of a novel PDZ domain-containing peripheral Golgi protein with the Q-SNARE (Q-soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein receptor) protein syntaxin 6."
Charest A., Lane K., McMahon K., Housman D.E.
J. Biol. Chem. 276:29456-29465(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH GOPC.
[8]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies."
Zwilling D., Cypionka A., Pohl W.H., Fasshauer D., Walla P.J., Wahl M.C., Jahn R.
EMBO J. 26:9-18(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 47-117 IN COMPLEX WITH STX12; VTI1A AND VAMP4, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ002078 mRNA. Translation: CAA05177.1.
CR541856 mRNA. Translation: CAG46654.1.
CR541873 mRNA. Translation: CAG46671.1.
AK299063 mRNA. Translation: BAG61129.1.
AK312440 mRNA. Translation: BAG35349.1.
AL356267, AL162431 Genomic DNA. Translation: CAH72301.1.
AL162431, AL356267 Genomic DNA. Translation: CAH74088.1.
CH471067 Genomic DNA. Translation: EAW91091.1.
BC009944 mRNA. Translation: AAH09944.1.
CCDSCCDS1341.1.
RefSeqNP_001273139.1. NM_001286210.1. [O43752-2]
NP_005810.1. NM_005819.5. [O43752-1]
XP_005244881.1. XM_005244824.1. [O43752-2]
UniGeneHs.518417.
Hs.737037.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2NPSX-ray2.50D169-234[»]
4J2CX-ray1.80A/C3-110[»]
ProteinModelPortalO43752.
SMRO43752. Positions 2-108, 170-232.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115522. 13 interactions.
DIPDIP-44224N.
IntActO43752. 9 interactions.
MINTMINT-5002256.
STRING9606.ENSP00000258301.

PTM databases

PhosphoSiteO43752.

Proteomic databases

MaxQBO43752.
PaxDbO43752.
PeptideAtlasO43752.
PRIDEO43752.

Protocols and materials databases

DNASU10228.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000258301; ENSP00000258301; ENSG00000135823.
ENST00000542060; ENSP00000440188; ENSG00000135823.
GeneID10228.
KEGGhsa:10228.
UCSCuc010pnr.2. human. [O43752-1]

Organism-specific databases

CTD10228.
GeneCardsGC01M180941.
HGNCHGNC:11441. STX6.
HPAHPA038557.
HPA038558.
MIM603944. gene.
neXtProtNX_O43752.
PharmGKBPA36238.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46901.
HOGENOMHOG000237350.
HOVERGENHBG007194.
InParanoidO43752.
KOK08498.
OMAQVVREMK.
OrthoDBEOG7JHM7F.
PhylomeDBO43752.
TreeFamTF313254.

Gene expression databases

ArrayExpressO43752.
BgeeO43752.
CleanExHS_STX6.
GenevestigatorO43752.

Family and domain databases

InterProIPR015260. Syntaxin-6_N.
IPR006012. Syntaxin/epimorphin_CS.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamPF05739. SNARE. 1 hit.
PF09177. Syntaxin-6_N. 1 hit.
[Graphical view]
SMARTSM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMSSF47661. SSF47661. 1 hit.
PROSITEPS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSTX6. human.
EvolutionaryTraceO43752.
GeneWikiSTX6.
GenomeRNAi10228.
NextBio35474275.
PROO43752.
SOURCESearch...

Entry information

Entry nameSTX6_HUMAN
AccessionPrimary (citable) accession number: O43752
Secondary accession number(s): B2R652 expand/collapse secondary AC list , B4DR17, Q5VY08, Q6FH83
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM