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Reviewed, UniProtKB/Swiss-Prot Q62277 (SYPH_MOUSE)

Last modified March 2, 2010. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
Synaptophysin
Alternative name(s):
Major synaptic vesicle protein p38
BM89 antigen
Gene names
Name:Syp
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Possibly involved in structural functions as organizing other membrane components or in targeting the vesicles to the plasma membrane By similarity. Involved in the regulation of short-term and long-term synaptic plasticity. Ref.5

Subunit structure

Homohexamer or homotetramer By similarity.

Subcellular location

Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane; Multi-pass membrane protein By similarity. Cell junctionsynapsesynaptosome By similarity.

Domain

The calcium-binding activity is thought to be localized in the cytoplasmic tail of the protein.

Post-translational modification

Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its subsequent proteasomal degradation By similarity.

Disruption phenotype

Mice lackin both SYNGR1 and SYP show normal brain structure and composition, but impaired short-term and long-term synaptic plasticity. Ref.5

Sequence similarities

Belongs to the synaptophysin/synaptobrevin family.

Contains 1 MARVEL domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 314314Synaptophysin
PRO_0000179162

Regions

Topological domain1 – 2525Cytoplasmic Potential
Transmembrane26 – 4924 Potential
Topological domain50 – 10758Vesicular Potential
Transmembrane108 – 13124 Potential
Topological domain132 – 1387Cytoplasmic Potential
Transmembrane139 – 16224 Potential
Topological domain163 – 20038Vesicular Potential
Transmembrane201 – 22424 Potential
Topological domain225 – 31490Cytoplasmic Potential
Domain21 – 228208MARVEL
Region255 – 30551Repeats, Gly-rich

Amino acid modifications

Modified residue811Phosphotyrosine Ref.6
Modified residue2271Phosphothreonine Potential
Modified residue2791Phosphotyrosine Potential
Modified residue2961Phosphotyrosine Potential
Glycosylation591N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1051A → G in CAA65084. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q62277-1 [UniParc].

Last modified October 10, 2003. Version 2.
Checksum: F6AC6E30AECE10CE

FASTA31434,025
        10         20         30         40         50         60 
MLLLADMDVV NQLVAGGQFR VVKEPLGFVK VLQWVFAIFA FATCGSYTGE LRLSVECANK 

        70         80         90        100        110        120 
TESALNIEVE FEYPFRLHQV YFDAPSCVKG GTTKIFLVGD YSSSAEFFVT VAVFAFLYSM 

       130        140        150        160        170        180 
GALATYIFLQ NKYRENNKGP MMDFLATAVF AFMWLVSSSA WAKGLSDVKM ATDPENIIKE 

       190        200        210        220        230        240 
MPMCRQTGNT CKELRDPVTS GLNTSVVFGF LNLVLWVGNL WFVFKETGWA APFMRAPPGA 

       250        260        270        280        290        300 
PEKQPAPGDA YGDAGYGQGP GGYGPQDSYG PQGGYQPDYG QPASGGGGGY GPQGDYGQQG 

       310 
YGQQGAPTSF SNQM 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Brain cortex.
[2]"Purification and cDNA cloning of mouse BM89 antigen shows that it is identical with the synaptic vesicle protein synaptophysin."
Gaitanou M., Mamalaki A., Merkouri E., Matsas R.
J. Neurosci. Res. 48:507-514(1997) [PubMed: 9210520] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-314.
Strain: C57BL/6.
Tissue: Brain.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-314.
Tissue: Eye.
[4]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 77-89; 170-179 AND 226-235, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[5]"Essential roles in synaptic plasticity for synaptogyrin I and synaptophysin I."
Janz R., Suedhof T.C., Hammer R.E., Unni V., Siegelbaum S.A., Bolshakov V.Y.
Neuron 24:687-700(1999) [PubMed: 10595519] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[6]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-81, MASS SPECTROMETRY.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK043756 mRNA. Translation: BAC31642.1.
X95818 mRNA. Translation: CAA65084.1.
BC014823 mRNA. Translation: AAH14823.1.
IPIIPI00123505.
RefSeqNP_033331.2.
UniGeneMm.223674

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ62277. 3 interactions.
STRINGQ62277.

PTM databases

PhosphoSiteQ62277.

Proteomic databases

PRIDEQ62277.

Genome annotation databases

EnsemblENSMUST00000069520; ENSMUSP00000069429; ENSMUSG00000031144; Mus musculus. [Genome view]
ENSMUST00000116638; ENSMUSP00000112337; ENSMUSG00000031144; Mus musculus. [Genome view]
GeneID20977.
KEGGmmu:20977.
UCSCuc009sls.1. mouse.

Organism-specific databases

CTD20977.
MGIMGI:98467. Syp.

Phylogenomic databases

HOGENOMHBG714484.
HOVERGENHBG006681.
InParanoidQ62277.
OMATGNTCKE.
OrthoDBEOG976NJX.
PhylomeDBQ62277.

Gene expression databases

ArrayExpressQ62277.
BgeeQ62277.
CleanExMM_SYP.
GenevestigatorQ62277.
GermOnlineENSMUSG00000031144. Mus musculus.

Family and domain databases

InterProIPR008253. Marvel.
IPR021128. MARVEL-like_dom.
IPR001285. Synaptophysin/porin.
IPR015457. Synaptophysin_.
[Graphical view]
PANTHERPTHR10306. Synaptophysin. 1 hit.
PTHR10306:SF2. Synaptophysin_. 1 hit.
PfamPF01284. MARVEL. 1 hit.
[Graphical view]
PRINTSPR00220. SYNAPTOPHYSN.
PROSITEPS51225. MARVEL. 1 hit.
PS00604. SYNAPTOP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio299960.
SOURCESearch...

Entry information

Entry nameSYPH_MOUSE
AccessionPrimary (citable) accession number: Q62277
Secondary accession number(s): Q8BRQ0, Q91WI8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 10, 2003
Last modified: March 2, 2010
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents