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O14662 (STX16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 18, 2012. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
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-16
Short name=Syn16
Gene names
Name:STX16
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length325 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network. Ref.8

Subunit structure

Interacts with GCC2. Ref.8

Subcellular location

Golgi apparatus membrane; Single-pass type IV membrane protein.

Isoform C: Cytoplasm.

Tissue specificity

Ubiquitous.

Involvement in 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. Ref.6 Ref.7

Sequence similarities

Belongs to the syntaxin family.

Contains 1 t-SNARE coiled-coil homology domain.

Sequence caution

The sequence AAB69282.1 differs from that shown. Reason: Frameshift at positions 142, 163 and 165.

The sequence AAB69283.1 differs from that shown. Reason: Frameshift at positions 142, 163 and 165.

The sequence AAC05647.1 differs from that shown. Reason: Frameshift at positions 142, 163 and 165.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform B (identifier: O14662-1)

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 A (identifier: O14662-2)

The sequence of this isoform differs from the canonical sequence as follows:
     28-48: Missing.
Isoform C (identifier: O14662-3)

The sequence of this isoform differs from the canonical sequence as follows:
     28-44: Missing.
     132-132: L → A
     133-325: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform D (identifier: O14662-4)

The sequence of this isoform differs from the canonical sequence as follows:
     28-44: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 325325Syntaxin-16
PRO_0000210226

Regions

Topological domain1 – 301301Cytoplasmic Potential
Transmembrane302 – 32221Helical; Anchor for type IV membrane protein; Potential
Topological domain323 – 3253Vesicular Potential
Domain230 – 29263t-SNARE coiled-coil homology

Amino acid modifications

Modified residue351Phosphoserine By similarity

Natural variations

Alternative sequence28 – 4821Missing in isoform A.
VSP_006348
Alternative sequence28 – 4417Missing in isoform C and isoform D.
VSP_006349
Alternative sequence1321L → A in isoform C.
VSP_006350
Alternative sequence133 – 325193Missing in isoform C.
VSP_006351

Experimental info

Sequence conflict991L → S in AAB69282. Ref.1
Sequence conflict991L → S in AAB69283. Ref.1
Sequence conflict1471A → E in AAC05647. Ref.1
Sequence conflict2431I → M in AAB69282. Ref.1
Sequence conflict2431I → M in AAB69283. Ref.1

Sequences

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

Last modified January 24, 2006. Version 3.
Checksum: 65F566541A042C3C

FASTA32537,031
        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

« Hide

Isoform A [UniParc].

Checksum: 9EEF54F753B7AB83
Show »

FASTA30434,813
Isoform C [UniParc].

Checksum: 51BBBACE2158720E
Show »

FASTA11513,018
Isoform D [UniParc].

Checksum: 1915107ACB686EAA
Show »

FASTA30835,299

References

« Hide 'large scale' references
[1]"Syntaxin-16, a putative Golgi t-SNARE."
Simonsen A., Bremnes B., Ronning E., Aasland R., Stenmark H.
Eur. J. Cell Biol. 75:223-231(1998) [PubMed: 9587053] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C AND D).
Tissue: Brain.
[2]"Molecular cloning and localization of human syntaxin 16, a member of the syntaxin family of SNARE proteins."
Tang B.L., Low D.Y.H., Lee S.S., Tan A.E.H., Ho W.
Biochem. Biophys. Res. Commun. 242:673-679(1998) [PubMed: 9464276] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D).
[3]"The DNA sequence and comparative analysis of human chromosome 20."
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. expand/collapse author list , 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.
Nature 414:865-871(2001) [PubMed: 11780052] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Tissue: Kidney.
[6]"Autosomal dominant pseudohypoparathyroidism type Ib is associated with a heterozygous microdeletion that likely disrupts a putative imprinting control element of GNAS."
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.
J. Clin. Invest. 112:1255-1263(2003) [PubMed: 14561710] [Abstract]
Cited for: INVOLVEMENT IN PHP1B.
[7]"A novel STX16 deletion in autosomal dominant pseudohypoparathyroidism type Ib redefines the boundaries of a cis-acting imprinting control element of GNAS."
Linglart A., Gensure R.C., Olney R.C., Jueppner H., Bastepe M.
Am. J. Hum. Genet. 76:804-814(2005) [PubMed: 15800843] [Abstract]
Cited for: INVOLVEMENT IN PHP1B.
[8]"A syntaxin 10-SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells."
Ganley I.G., Espinosa E., Pfeffer S.R.
J. Cell Biol. 180:159-172(2008) [PubMed: 18195106] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GCC2.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF008936 mRNA. Translation: AAB69283.1. Frameshift.
AF008935 mRNA. Translation: AAB69282.1. Frameshift.
AF008937 mRNA. Translation: AAB69284.1.
AF038897 mRNA. Translation: AAC05647.1. Frameshift.
AL139349, AL050327 Genomic DNA. Translation: CAX14989.1.
AL139349, AL050327 Genomic DNA. Translation: CAX14990.1.
AL139349, AL050327 Genomic DNA. Translation: CAX14991.1.
AL050327, AL139349 Genomic DNA. Translation: CAI23277.1.
AL050327, AL139349 Genomic DNA. Translation: CAI23278.1.
AL050327, AL139349 Genomic DNA. Translation: CAI23279.1.
CH471077 Genomic DNA. Translation: EAW75485.1.
CH471077 Genomic DNA. Translation: EAW75486.1.
BC019042 mRNA. Translation: AAH19042.1.
IPIIPI00023149.
IPI00220261.
IPI00220263.
IPI00414290.
PIRJC5927.
RefSeqNP_001001433.1. NM_001001433.2.
NP_001128245.1. NM_001134773.2.
NP_001191797.1. NM_001204868.1.
NP_003754.2. NM_003763.5.
UniGeneHs.307913.

3D structure databases

ProteinModelPortalO14662.
SMRO14662. Positions 235-300.
ModBaseSearch...

Protein-protein interaction databases

IntActO14662. 1 interaction.
MINTMINT-1196639.
STRINGO14662.

PTM databases

PhosphoSiteO14662.

Proteomic databases

PRIDEO14662.

Protocols and materials databases

DNASU8675.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355957; ENSP00000348229; ENSG00000124222.
ENST00000371141; ENSP00000360183; ENSG00000124222.
GeneID8675.
KEGGhsa:8675.
UCSCuc002xzi.3. human.
uc002xzj.3. human.
uc002xzk.3. human.

Organism-specific databases

CTD8675.
GeneCardsGC20P057226.
HGNCHGNC:11431. STX16.
HPAHPA041019.
HPA042033.
MIM603233. phenotype.
603666. gene.
neXtProtNX_O14662.
PharmGKBPA36231.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5325.
GeneTreeENSGT00550000075126.
HOVERGENHBG057612.
KOK08489.
OrthoDBEOG4K3KWP.
PhylomeDBO14662.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_13685. Neuronal System.

Gene expression databases

ArrayExpressO14662.
BgeeO14662.
GenevestigatorO14662.
GermOnlineENSG00000124222. Homo sapiens.

Family and domain databases

InterProIPR006012. Syntaxin/epimorphin_CS.
IPR006011. Syntaxin_N.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamPF05739. SNARE. 1 hit.
PF00804. Syntaxin. 1 hit.
[Graphical view]
SMARTSM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMSSF47661. t-snare. 1 hit.
PROSITEPS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio32541.
SOURCESearch...

Entry information

Entry nameSTX16_HUMAN
AccessionPrimary (citable) accession number: O14662
Secondary accession number(s): A6NN69 expand/collapse secondary AC list , B7ZBN1, B7ZBN2, B7ZBN3, E1P607, O14661, O14663, O60517, Q5W084, Q5W086, Q5W087, Q5XKI6, Q9H0Z0, Q9H1T7, Q9H1T8, Q9UIX5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 24, 2006
Last modified: April 18, 2012
This is version 117 of the entry and version 3 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

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

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