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UniProtKB/Swiss-Prot entry Q63537


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

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Entry information
Entry name SYN2_RAT
Primary accession number Q63537
Secondary accession number Q9Z1H0
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 72)
Name and origin of the protein
Protein name Synapsin-2
Synonym Synapsin II
Gene name
Name: Syn2
From
Rattus norvegicus (Rat) [TaxID: 10116] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Rattus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IIA AND IIB).
TISSUE=Brain;
DOI=10.1126/science.2506642; PubMed=2506642 [NCBI, ExPASy, EBI, Israel, Japan]
Suedhof T.C., Czernik A.J., Kao H.-T., Takei K., Johnston P.A., Horiuchi A., Kanazir S.D., Wagner M.A., Perin M.S., de Camilli P., Greengard P.;
"Synapsins: mosaics of shared and individual domains in a family of synaptic vesicle phosphoproteins.";
Science 245:1474-1480(1989).
[2]
PROTEIN SEQUENCE OF 136-143; 178-200; 245-257; 405-414 AND 544-560, AND MASS SPECTROMETRY.
STRAIN=Sprague-Dawley;
TISSUE=Hippocampus;
Lubec G., Chen W.-Q.;
Submitted (APR-2007) to UniProtKB.
[3]
INTERACTION WITH CAPON.
DOI=10.1073/pnas.261705799; PubMed=11867766 [NCBI, ExPASy, EBI, Israel, Japan]
Jaffrey S.R., Benfenati F., Snowman A.M., Czernik A.J., Snyder S.H.;
"Neuronal nitric-oxide synthase localization mediated by a ternary complex with synapsin and CAPON.";
Proc. Natl. Acad. Sci. U.S.A. 99:3199-3204(2002).
Comments
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
M27925; AAA42100.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M27926; AAA42101.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00210036; -.
IPI00231408; -.
PIR C30411; C30411.
RefSeq NP_001029192.1; -.
NP_062032.1; -.
UniGene Rn.506
3D structure databases
PDB
1I7L; X-ray; 2.35 A; A/B=113-421.[ExPASy / RCSB / EBI]
1I7N; X-ray; 1.90 A; A/B=113-421.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1I7L; -.
1I7N; -.
ModBase Q63537.
PTM databases
PhosphoSite Q63537; -.
Organism-specific databases
RGD 3798; Syn2.
Gene expression databases
ArrayExpress Q63537; -.
GermOnline ENSRNOG00000008157; Rattus norvegicus.
Ontologies
GO
GO:0030054; Cellular component: cell junction (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0003824; Molecular function: catalytic activity (inferred from electronic annotation from InterPro).
GO:0008092; Molecular function: cytoskeletal protein binding (traceable author statement from RGD).
GO:0007269; Biological process: neurotransmitter secretion (inferred from electronic annotation from InterPro).
GO:0046928; Biological process: regulation of neurotransmitter secretion (traceable author statement from RGD).
QuickGo view.
Family and domain databases
InterPro IPR013816; ATP_grasp_subdomain_2.
IPR001359; Synapsin.
IPR019735; Synapsin_CS.
IPR019569; Synapsin_N.
IPR019736; Synapsin_phosporylation.
Graphical view of domain structure.
Gene3D G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1.
Pfam PF02078; Synapsin; 1.
PF02750; Synapsin_C; 1.
PF10581; Synapsin_N; 1.
Pfam graphical view of domain structure.
PRINTS PR01368; SYNAPSIN.
PROSITE PS00415; SYNAPSIN_1; 1.
PS00416; SYNAPSIN_2; 1.
Proteomic databases
PRIDE Q63537; -.
Genome annotation databases
Ensembl ENSRNOG00000008157; Rattus norvegicus. [Contig view]
GeneID 29179; -.
KEGG rno:29179; -.
Phylogenomic databases
HOVERGEN Q63537; -.
Other
NextBio 608259; -.
PMAP-CutDB Q63537; -.
ProtoNet Q63537.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Cell junction; Direct protein sequencing; Phosphoprotein; Synapse.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   586  586     Synapsin-2. PRO_0000183023
REGION   1    29  29     A. 
REGION   33   113  81     B; linker. 
REGION   114   421  308     C; actin-binding and synaptic-vesicle binding. 
REGION   422   458  37     G; Pro-rich linker. 
REGION   459   537  79     H; Pro/Ser-rich linker. 
REGION   538   586  49     E. 
COMPBIAS   487   499  13     Poly-Ser. 
COMPBIAS   515   520  6     Poly-Ser. 
MOD_RES   422   422        Phosphothreonine (By similarity). 
MOD_RES   426   426        Phosphoserine (By similarity). 
VAR_SEQ   459   479        GPGQPQGMQPPGKVLPPRRLP -> CLQYILNCNGIAVGPKQVQAS (in isoform IIb). VSP_006322
VAR_SEQ   480   586        Missing (in isoform IIb). VSP_006323
STRAND   114   120  7      
HELIX   127   131  5      
TURN   137   139  3      
STRAND   140   147  8      
HELIX   149   151  3      
STRAND   152   157  6      
STRAND   162   169  8      
STRAND   171   173  3      
STRAND   175   179  5      
STRAND   182   186  5      
HELIX   200   208  9      
STRAND   213   215  3      
HELIX   217   222  6      
HELIX   226   240  15      
TURN   242   244  3      
STRAND   251   255  5      
HELIX   256   260  5      
STRAND   265   273  9      
TURN   276   279  4      
STRAND   280   283  4      
HELIX   288   299  12      
STRAND   303   307  5      
STRAND   311   320  10      
STRAND   323   333  11      
STRAND   340   348  9      
HELIX   352   361  10      
HELIX   362   366  5      
STRAND   369   378  10      
STRAND   383   389  7      
HELIX   400   418  19      
Sequence information
Length: 586 AA [This is the length of the unprocessed precursor] Molecular weight: 63457 Da [This is the MW of the unprocessed precursor] CRC64: 630B7071B2F38857 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MMNFLRRRLS DSSFIANLPN GYMTDLQRPE PQQPPPAPGP GTATASAATS AASPGPERRP 

        70         80         90        100        110        120 
PPAQAPAPQP APQPAPTPSV GSSFFSSLSQ AVKQTAASAG LVDAPAPSAA SRKAKVLLVV 

       130        140        150        160        170        180 
DEPHTDWAKC FRGKKILGDY DIKVEQAEFS ELNLVAHADG TYAVDMQVLR NGTKVVRSFR 

       190        200        210        220        230        240 
PDFVLIRQHA FGMAENEDFR HLVIGMQYAG LPSINSLESI YNFCDKPWVF AQMVAIFKTL 

       250        260        270        280        290        300 
GGEKFPLIEQ TYYPNHREML TLPTFPVVVK IGHAHSGMGK VKVENHYDFQ DIASVVALTQ 

       310        320        330        340        350        360 
TYATAEPFID AKYDIRVQKI GNNYKAYMRT SISGNWKTNT GSAMLEQIAM SDRYKLWVDA 

       370        380        390        400        410        420 
CSEMFGGLDI CAVKAVHGKD GKDYIFEVMD CSMPLIGEHQ VEDRQLITDL VISKMNQLLS 

       430        440        450        460        470        480 
RTPALSPQRP LTTQQPQSGT LKEPDSSKTP PQRPAPQGGP GQPQGMQPPG KVLPPRRLPS 

       490        500        510        520        530        540 
GPSLPPSSSS SSSSSSSSSA PQRPGGPTST QVNASSSSNS LAEPQAPQAA PPQKPQPHPQ 

       550        560        570        580 
LNKSQSLTNA FSFSESSFFR SSANEDEAKA ETIRSLRKSF ASLFSD 

Q63537 in FASTA format

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