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Q62277 (SYPH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

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

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. Interacts with SRCIN1 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 – 4924Helical; Potential
Topological domain50 – 10758Vesicular Potential
Transmembrane108 – 13124Helical; Potential
Topological domain132 – 1387Cytoplasmic Potential
Transmembrane139 – 16224Helical; Potential
Topological domain163 – 20038Vesicular Potential
Transmembrane201 – 22424Helical; 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 [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. NM_009305.2.
UniGeneMm.223674.

3D structure databases

ProteinModelPortalQ62277.
ModBaseSearch...

Protein-protein interaction databases

IntActQ62277. 16 interactions.
STRINGQ62277.

PTM databases

PhosphoSiteQ62277.

Proteomic databases

PRIDEQ62277.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033484; ENSMUSP00000033484; ENSMUSG00000031144.
ENSMUST00000069520; ENSMUSP00000069429; ENSMUSG00000031144.
GeneID20977.
KEGGmmu:20977.

Organism-specific databases

CTD6855.
MGIMGI:98467. Syp.

Phylogenomic databases

GeneTreeENSGT00390000010039.
HOGENOMHBG714484.
HOVERGENHBG006681.
InParanoidQ62277.
OMAQTGNTCK.
OrthoDBEOG4JM7QJ.
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.
[Graphical view]
PANTHERPTHR10306. Synaptophysin. 1 hit.
PfamPF01284. MARVEL. 1 hit.
[Graphical view]
PRINTSPR00220. SYNAPTOPHYSN.
PROSITEPS51225. MARVEL. 1 hit.
PS00604. SYNAPTOP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

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: November 16, 2011
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families