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UniProtKB/Swiss-Prot entry O14662


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name STX16_HUMAN
Primary accession number O14662
Secondary accession numbers O14661 O14663 O60517 Q5W084 Q5W086 Q5W087 Q5XKI6 Q9H0Z0 Q9H1T7 Q9H1T8 Q9UIX5
Integrated into Swiss-Prot on February 21, 2001
Sequence was last modified on January 24, 2006 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 92)
Name and origin of the protein
Protein name Syntaxin-16
Synonym Syn16
Gene name
Name: STX16
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
TISSUE=Brain;
PubMed=9587053 [NCBI, ExPASy, EBI, Israel, Japan]
Simonsen A., Bremnes B., Ronning E., Aasland R., Stenmark H.;
"Syntaxin-16, a putative Golgi t-SNARE.";
Eur. J. Cell Biol. 75:223-231(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D).
DOI=10.1006/bbrc.1997.8029; PubMed=9464276 [NCBI, ExPASy, EBI, Israel, Japan]
Tang B.L., Low D.Y.H., Lee S.S., Tan A.E.H., Ho W.;
"Molecular cloning and localization of human syntaxin 16, a member of the syntaxin family of SNARE proteins.";
Biochem. Biophys. Res. Commun. 242:673-679(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/414865a; PubMed=11780052 [NCBI, ExPASy, EBI, Israel, Japan]
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
TISSUE=Kidney;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INVOLVEMENT IN PHP1B.
DOI=10.1172/JCI200319159; PubMed=14561710 [NCBI, ExPASy, EBI, Israel, Japan]
Bastepe M., Froehlich L.F., Hendy G.N., Indridason O.S., Josse R.G., Koshiyama H., Koerkkoe J., Nakamoto J.M., Rosenbloom A.L., Slyper A.H., Sugimoto T., Tsatsoulis A., Crawford J.D., Jueppner H.;
"Autosomal dominant pseudohypoparathyroidism type Ib is associated with a heterozygous microdeletion that likely disrupts a putative imprinting control element of GNAS.";
J. Clin. Invest. 112:1255-1263(2003).
[6]
INVOLVEMENT IN PHP1B.
DOI=10.1086/429932; PubMed=15800843 [NCBI, ExPASy, EBI, Israel, Japan]
Linglart A., Gensure R.C., Olney R.C., Jueppner H., Bastepe M.;
"A novel STX16 deletion in autosomal dominant pseudohypoparathyroidism type Ib redefines the boundaries of a cis-acting imprinting control element of GNAS.";
Am. J. Hum. Genet. 76:804-814(2005).
[7]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
  • FUNCTION: SNARE involved in a vesicular transport step within the Golgi stack.
  • SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type IV membrane protein.
  • SUBCELLULAR LOCATION: Isoform C: Cytoplasm.
  • ALTERNATIVE PRODUCTS: 4 named isoforms [FASTA] produced by alternative splicing.
    NameB
    Isoform IDO14662-1
    This is the isoform sequence displayed in this entry.
    NameA
    Isoform IDO14662-2
    Features which should be applied to build the isoform sequence: VSP_006348.
    NameC
    Isoform IDO14662-3
    Features which should be applied to build the isoform sequence: VSP_006349, VSP_006350, VSP_006351.
    NameD
    Isoform IDO14662-4
    Features which should be applied to build the isoform sequence: VSP_006349.
  • TISSUE SPECIFICITY: Ubiquitous.
  • DISEASE: Genetic variations in STX16 may be a cause of pseudohypoparathyroidism type 1B (PHP1B) [MIM:603233]. Pseudohypoparathyroidism refers to a heterogeneous group of disorders characterized by resistance to parathyroid hormone (PTH). PHP1B is characterized by PTH-resistant hypocalcemia and hyperphosphatemia. Patients affected with PHP1B lack developmental defects characteristic of Albright hereditary osteodystrophy, and typically show no other endocrine abnormalities besides resistance to PTH. In some cases microdeletions involving STX16 appear to cause loss of methylation at exon A/B of the GNAS gene, resulting in PHP1B.
  • SIMILARITY: Belongs to the syntaxin family.
  • SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF008936; AAB69283.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF008935; AAB69282.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF008937; AAB69284.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF038897; AAC05647.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL050327; CAI23277.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL139349; CAI23277.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL050327; CAI23278.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL139349; CAI23278.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL050327; CAI23279.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL139349; CAI23279.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC019042; AAH19042.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00023149; -.
IPI00220261; -.
IPI00220263; -.
IPI00414290; -.
PIR JC5927; JC5927.
RefSeq NP_001001433.1; -.
NP_001128245.1; -.
NP_003754.2; -.
UniGene Hs.307913
3D structure databases
HSSP P32851; 1JTH. [HSSP ENTRY / PDB]
ModBase O14662.
PTM databases
PhosphoSite O14662; -.
Enzyme and pathway databases
Reactome REACT_11184; Botulinum neurotoxicity.
Organism-specific databases
GeneCards GC20P056659; -.
H-InvDB HIX0015953; -.
HGNC HGNC:11431; STX16.
GenAtlas STX16.
MIM 603233; phenotype. [NCBI / EBI]
603666; gene. [NCBI / EBI]
PharmGKB PA36231; -.
Gene expression databases
ArrayExpress O14662; -.
Bgee O14662; -.
GermOnline ENSG00000124222; Homo sapiens.
Ontologies
GO
GO:0000139; Cellular component: Golgi membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005792; Cellular component: microsome (traceable author statement from ProtInc).
GO:0031201; Cellular component: SNARE complex (traceable author statement from HGNC).
GO:0005484; Molecular function: SNAP receptor activity (inferred from direct assay from HGNC).
GO:0006891; Biological process: intra-Golgi vesicle-mediated transport (traceable author statement from ProtInc).
GO:0006886; Biological process: intracellular protein transport (inferred from electronic annotation from InterPro).
GO:0042147; Biological process: retrograde transport, endosome to Golgi (inferred from direct assay from HGNC).
QuickGo view.
Family and domain databases
InterPro IPR006012; Syntaxin/epimorphin_CS.
IPR006011; Syntaxin_N.
IPR000727; T_SNARE.
Graphical view of domain structure.
Pfam PF05739; SNARE; 1.
PF00804; Syntaxin; 1.
Pfam graphical view of domain structure.
SMART SM00397; t_SNARE; 1.
SMART graphical view of domain structure.
PROSITE PS00914; SYNTAXIN; 1.
PS50192; T_SNARE; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE O14662; -.
Genome annotation databases
Ensembl ENSG00000124222; Homo sapiens. [Contig view]
GeneID 8675; -.
KEGG hsa:8675; -.
Phylogenomic databases
HOVERGEN O14662; -.
OMA O14662; ENDALMD.
Other
NextBio 32541; -.
SOURCE STX16; Homo sapiens.
ProtoNet O14662.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Coiled coil; Cytoplasm; Golgi apparatus; Membrane; Phosphoprotein; Protein transport; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   325  325     Syntaxin-16. PRO_0000210226
TOPO_DOM   1   301  301     Cytoplasmic (Potential). 
TRANSMEM   302   322  21     Anchor for type IV membrane protein (Potential). 
TOPO_DOM   323   325  3     Vesicular (Potential). 
DOMAIN   230   292  63     t-SNARE coiled-coil homology. 
MOD_RES   35    35        Phosphoserine (By similarity). 
VAR_SEQ   28    48        Missing (in isoform A). VSP_006348
VAR_SEQ   28    44        Missing (in isoform C and isoform D). VSP_006349
VAR_SEQ   132   132        L -> A (in isoform C). VSP_006350
VAR_SEQ   133   325        Missing (in isoform C). VSP_006351
CONFLICT   99    99        L -> S (in Ref. 1; AAB69283/AAB69282). 
CONFLICT   142   165        ALPSRARACSEQEGRLLGNVVASL -> PCRAGPGPAPSRRGGCLGTWCLV (in Ref. 1 and 2). 
CONFLICT   243   243        I -> M (in Ref. 1; AAC05647). 
Sequence information
Length: 325 AA [This is the length of the unprocessed precursor] Molecular weight: 37031 Da [This is the MW of the unprocessed precursor] CRC64: 65F566541A042C3C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MATRRLTDAF LLLRNNSIQN RQLLAEQVSS HITSSPLHSR SIAAELDELA DDRMALVSGI 

        70         80         90        100        110        120 
SLDPEAAIGV TKRPPPKWVD GVDEIQYDVG RIKQKMKELA SLHDKHLNRP TLDDSSEEEH 

       130        140        150        160        170        180 
AIEITTQEIT QLFHRCQRAV QALPSRARAC SEQEGRLLGN VVASLAQALQ ELSTSFRHAQ 

       190        200        210        220        230        240 
SGYLKRMKNR EERSQHFFDT SVPLMDDGDD NTLYHRGFTE DQLVLVEQNT LMVEEREREI 

       250        260        270        280        290        300 
RQIVQSISDL NEIFRDLGAM IVEQGTVLDR IDYNVEQSCI KTEDGLKQLH KAEQYQKKNR 

       310        320 
KMLVILILFV IIIVLIVVLV GVKSR 

O14662 in FASTA format

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