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Protein

Synaptosomal-associated protein 29

Gene

Snap29

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. SNAP29 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Autophagy, Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptosomal-associated protein 29Imported
Short name:
SNAP-29By similarity
Alternative name(s):
Golgi SNARE of 32 kDa
Short name:
Gs32
Soluble 29 kDa NSF attachment proteinBy similarity
Vesicle-membrane fusion protein SNAP-29
Gene namesi
Name:Snap29Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1914724. Snap29.

Subcellular locationi

  • Cytoplasm By similarity
  • Golgi apparatus membrane By similarity; Peripheral membrane protein Curated
  • Cytoplasmic vesicleautophagosome membrane By similarity; Peripheral membrane protein Curated

  • Note: Appears to be mostly membrane-bound, probably via interaction with syntaxins, but a significant portion is cytoplasmic (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 260260Synaptosomal-associated protein 29PRO_0000213602Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei114 – 1141PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9ERB0.
PaxDbiQ9ERB0.
PRIDEiQ9ERB0.

PTM databases

PhosphoSiteiQ9ERB0.

Expressioni

Gene expression databases

BgeeiQ9ERB0.
CleanExiMM_SNAP29.
GenevisibleiQ9ERB0. MM.

Interactioni

Subunit structurei

Forms a SNARE complex, composed of VAMP8, SNAP29 and STX17, involved in fusion of autophagosome with lysosome (By similarity). Interacts with multiple syntaxins including STX6 (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-60853N.
IntActiQ9ERB0. 1 interaction.
MINTiMINT-4998219.
STRINGi10090.ENSMUSP00000023449.

Structurei

3D structure databases

ProteinModelPortaliQ9ERB0.
SMRiQ9ERB0. Positions 42-103, 204-260.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini198 – 26063t-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili76 – 10732Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the SNAP-25 family.Curated
Contains 1 t-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG244202.
GeneTreeiENSGT00510000048053.
HOGENOMiHOG000046806.
HOVERGENiHBG057045.
InParanoidiQ9ERB0.
KOiK08509.
OMAiQEAQYQA.
OrthoDBiEOG7FNC8G.
PhylomeDBiQ9ERB0.
TreeFamiTF320226.

Family and domain databases

InterProiIPR000928. SNAP-25.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF00835. SNAP-25. 1 hit.
PF05739. SNARE. 1 hit.
[Graphical view]
SMARTiSM00397. t_SNARE. 2 hits.
[Graphical view]
PROSITEiPS50192. T_SNARE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ERB0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGYPKSYNP FDDDVEEEDT RPAPWKDVRD LPDGPDAPID RQQYLRQEVL
60 70 80 90 100
RRAEATAAST SRSLSLMYES EKIGVASSEE LVRQRGVLEH TEKMVDKMDQ
110 120 130 140 150
DLKMSQKHIN SIKSVFGGFI NYFKSKPVEP PPEQNGSIVS QPNSRLKEAI
160 170 180 190 200
NTSKDQENKY QASHPNLRRL QDAELDSVPK EPSSTVNTEV YPKNSTLRTY
210 220 230 240 250
HQKIDSNLDE LSVGLGHLKD IALGMQTEIE EQDDILDRLT TKVDKLDVNI
260
KSTEKKVRQL
Length:260
Mass (Da):29,572
Last modified:March 1, 2001 - v1
Checksum:iDD813A78C605576F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti183 – 1842SS → FF in BAB23769 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY008722 mRNA. Translation: AAG32076.1.
AK005042 mRNA. Translation: BAB23769.1.
AK007065 mRNA. Translation: BAB24850.1.
AK039203 mRNA. Translation: BAC30277.1.
AK147845 mRNA. Translation: BAE28177.1.
BC030066 mRNA. Translation: AAH30066.1.
CCDSiCCDS28001.1.
RefSeqiNP_075837.3. NM_023348.4.
UniGeneiMm.271992.

Genome annotation databases

EnsembliENSMUST00000023449; ENSMUSP00000023449; ENSMUSG00000022765.
GeneIDi67474.
KEGGimmu:67474.
UCSCiuc007yku.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY008722 mRNA. Translation: AAG32076.1.
AK005042 mRNA. Translation: BAB23769.1.
AK007065 mRNA. Translation: BAB24850.1.
AK039203 mRNA. Translation: BAC30277.1.
AK147845 mRNA. Translation: BAE28177.1.
BC030066 mRNA. Translation: AAH30066.1.
CCDSiCCDS28001.1.
RefSeqiNP_075837.3. NM_023348.4.
UniGeneiMm.271992.

3D structure databases

ProteinModelPortaliQ9ERB0.
SMRiQ9ERB0. Positions 42-103, 204-260.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60853N.
IntActiQ9ERB0. 1 interaction.
MINTiMINT-4998219.
STRINGi10090.ENSMUSP00000023449.

PTM databases

PhosphoSiteiQ9ERB0.

Proteomic databases

MaxQBiQ9ERB0.
PaxDbiQ9ERB0.
PRIDEiQ9ERB0.

Protocols and materials databases

DNASUi67474.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023449; ENSMUSP00000023449; ENSMUSG00000022765.
GeneIDi67474.
KEGGimmu:67474.
UCSCiuc007yku.1. mouse.

Organism-specific databases

CTDi9342.
MGIiMGI:1914724. Snap29.

Phylogenomic databases

eggNOGiNOG244202.
GeneTreeiENSGT00510000048053.
HOGENOMiHOG000046806.
HOVERGENiHBG057045.
InParanoidiQ9ERB0.
KOiK08509.
OMAiQEAQYQA.
OrthoDBiEOG7FNC8G.
PhylomeDBiQ9ERB0.
TreeFamiTF320226.

Miscellaneous databases

ChiTaRSiSnap29. mouse.
NextBioi324690.
PROiQ9ERB0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ERB0.
CleanExiMM_SNAP29.
GenevisibleiQ9ERB0. MM.

Family and domain databases

InterProiIPR000928. SNAP-25.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF00835. SNAP-25. 1 hit.
PF05739. SNARE. 1 hit.
[Graphical view]
SMARTiSM00397. t_SNARE. 2 hits.
[Graphical view]
PROSITEiPS50192. T_SNARE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Bui T.D., Hong W.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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: Hypothalamus, Liver and Testis.
  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].
    Tissue: Lung.

Entry informationi

Entry nameiSNP29_MOUSE
AccessioniPrimary (citable) accession number: Q9ERB0
Secondary accession number(s): Q3UGN0, Q9DBC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: March 1, 2001
Last modified: June 24, 2015
This is version 105 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.