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P17600 (SYN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Synapsin-1
Alternative name(s):
Brain protein 4.1
Synapsin I
Gene names
Name:SYN1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length705 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release. The complex formed with NOS1 and CAPON proteins is necessary for specific nitric-oxid functions at a presynaptic level.

Subunit structure

Homodimer. Interacts with CAPON. Forms a ternary complex with NOS1. Isoform Ibinteracts with PRNP By similarity.

Subcellular location

Cell junctionsynapse. Golgi apparatus By similarity.

Domain

The A region binds phospholipids with a preference for negatively charged species By similarity.

Post-translational modification

Substrate of at least four different protein kinases. It is probable that phosphorylation plays a role in the regulation of synapsin-1 in the nerve terminal.

Phosphorylation at Ser-9 dissociates synapsins from synaptic vesicles By similarity.

Involvement in disease

Epilepsy X-linked, with variable learning disabilities and behavior disorders (XELBD) [MIM:300491]: A neurologic disorder characterized by variable combinations of epilepsy, learning difficulties, macrocephaly, and aggressive behavior.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5

Sequence similarities

Belongs to the synapsin family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SNCAP378402EBI-717274,EBI-985879

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform IA (identifier: P17600-1)

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 IB (identifier: P17600-2)

The sequence of this isoform differs from the canonical sequence as follows:
     661-669: NKSQSLTNA → KASPAQAQP
     670-705: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 705705Synapsin-1
PRO_0000183018

Regions

Region1 – 2828A
Region29 – 11284B; linker
Region113 – 420308C; actin-binding and synaptic-vesicle binding
Region421 – 655235D; Pro-rich linker
Region656 – 70550E

Amino acid modifications

Modified residue91Phosphoserine; by CaMK1 and PKA; alternate
Modified residue91Phosphoserine; by PKA and CaMK1; alternate By similarity
Modified residue3121Phosphotyrosine By similarity
Modified residue4271Phosphoserine By similarity
Modified residue5511Phosphoserine; by PDPK1 Ref.6 Ref.7
Modified residue5531Phosphoserine Ref.6 Ref.7
Modified residue5681Phosphoserine; by CaMK2
Modified residue6051Phosphoserine; by CaMK2
Glycosylation551O-linked (GlcNAc) By similarity
Glycosylation871O-linked (GlcNAc) By similarity
Glycosylation961O-linked (GlcNAc) By similarity
Glycosylation1031O-linked (GlcNAc) By similarity
Glycosylation2611O-linked (GlcNAc) By similarity
Glycosylation4321O-linked (GlcNAc) By similarity
Glycosylation5261O-linked (GlcNAc) By similarity
Glycosylation5641O-linked (GlcNAc) By similarity
Glycosylation5781O-linked (GlcNAc) By similarity

Natural variations

Alternative sequence661 – 6699NKSQSLTNA → KASPAQAQP in isoform IB.
VSP_006316
Alternative sequence670 – 70536Missing in isoform IB.
VSP_006317

Experimental info

Sequence conflict1381E → G in AAC41930. Ref.1
Sequence conflict1381E → G in AAC41931. Ref.1
Sequence conflict6311R → A in AAC41930. Ref.1
Sequence conflict6311R → A in AAC41931. Ref.1

Sequences

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

Last modified August 30, 2005. Version 3.
Checksum: BE4CE46C942300B0

FASTA70574,111
        10         20         30         40         50         60 
MNYLRRRLSD SNFMANLPNG YMTDLQRPQP PPPPPGAHSP GATPGPGTAT AERSSGVAPA 

        70         80         90        100        110        120 
ASPAAPSPGS SGGGGFFSSL SNAVKQTTAA AAATFSEQVG GGSGGAGRGG AASRVLLVID 

       130        140        150        160        170        180 
EPHTDWAKYF KGKKIHGEID IKVEQAEFSD LNLVAHANGG FSVDMEVLRN GVKVVRSLKP 

       190        200        210        220        230        240 
DFVLIRQHAF SMARNGDYRS LVIGLQYAGI PSVNSLHSVY NFCDKPWVFA QMVRLHKKLG 

       250        260        270        280        290        300 
TEEFPLIDQT FYPNHKEMLS STTYPVVVKM GHAHSGMGKV KVDNQHDFQD IASVVALTKT 

       310        320        330        340        350        360 
YATAEPFIDA KYDVRVQKIG QNYKAYMRTS VSGNWKTNTG SAMLEQIAMS DRYKLWVDTC 

       370        380        390        400        410        420 
SEIFGGLDIC AVEALHGKDG RDHIIEVVGS SMPLIGDHQD EDKQLIVELV VNKMAQALPR 

       430        440        450        460        470        480 
QRQRDASPGR GSHGQTPSPG ALPLGRQTSQ QPAGPPAQQR PPPQGGPPQP GPGPQRQGPP 

       490        500        510        520        530        540 
LQQRPPPQGQ QHLSGLGPPA GSPLPQRLPS PTSAPQQPAS QAAPPTQGQG RQSRPVAGGP 

       550        560        570        580        590        600 
GAPPAARPPA SPSPQRQAGP PQATRQTSVS GPAPPKASGA PPGGQQRQGP PQKPPGPAGP 

       610        620        630        640        650        660 
TRQASQAGPV PRTGPPTTQQ PRPSGPGPAG RPKPQLAQKP SQDVPPPATA AAGGPPHPQL 

       670        680        690        700 
NKSQSLTNAF NLPEPAPPRP SLSQDEVKAE TIRSLRKSFA SLFSD 

« Hide

Isoform IB [UniParc].

Checksum: 5E400115415D3E32
Show »

FASTA66970,033

References

« Hide 'large scale' references
[1]"The structure of the human synapsin I gene and protein."
Suedhof T.C.
J. Biol. Chem. 265:7849-7852(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
Tissue: Brain.
[2]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The 5'-flanking region of the synapsin I gene. A G+C-rich, TATA- and CAAT-less, phylogenetically conserved sequence with cell type-specific promoter function."
Sauerwald A., Hoesche C., Oschwald R., Kilimann M.W.
J. Biol. Chem. 265:14932-14937(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125.
[5]"Identification of a mutation in synapsin I, a synaptic vesicle protein, in a family with epilepsy."
Garcia C.C., Blair H.J., Seager M., Coulthard A., Tennant S., Buddles M., Curtis A., Goodship J.A.
J. Med. Genet. 41:183-187(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN XELBD.
[6]"Phosphoproteomic analysis of synaptosomes from human cerebral cortex."
DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P., Pant H.C., Dosemeci A.
J. Proteome Res. 4:306-315(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-551 AND SER-553, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain cortex.
[7]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-551 AND SER-553, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M58378 expand/collapse EMBL AC list , M58321, M58341, M58351, M58353, M58359, M58371, M58372, M58373, M58374, M58375, M58376, M58377 Genomic DNA. Translation: AAC41930.1.
M58378 expand/collapse EMBL AC list , M58321, M58341, M58351, M58353, M58359, M58371, M58372, M58373, M58374, M58375, M58376, M58377 Genomic DNA. Translation: AAC41931.1. Sequence problems.
AL009172, Z84466 Genomic DNA. Translation: CAI42445.1.
AL009172, Z84466 Genomic DNA. Translation: CAI42446.1.
Z84466, AL009172 Genomic DNA. Translation: CAI42461.1.
Z84466, AL009172 Genomic DNA. Translation: CAI42462.1.
CH471164 Genomic DNA. Translation: EAW59313.1.
M55301 Genomic DNA. Translation: AAA60608.1.
PIRA35363.
RefSeqNP_008881.2. NM_006950.3.
NP_598006.1. NM_133499.2.
UniGeneHs.225936.

3D structure databases

ProteinModelPortalP17600.
SMRP17600. Positions 112-417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112719. 21 interactions.
IntActP17600. 4 interactions.
MINTMINT-1370745.
STRING9606.ENSP00000295987.

PTM databases

PhosphoSiteP17600.

Polymorphism databases

DMDM73920800.

Proteomic databases

PaxDbP17600.
PRIDEP17600.

Protocols and materials databases

DNASU6853.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295987; ENSP00000295987; ENSG00000008056. [P17600-1]
ENST00000340666; ENSP00000343206; ENSG00000008056. [P17600-2]
GeneID6853.
KEGGhsa:6853.
UCSCuc004did.3. human. [P17600-2]
uc004die.3. human. [P17600-1]

Organism-specific databases

CTD6853.
GeneCardsGC0XM047431.
HGNCHGNC:11494. SYN1.
HPACAB021929.
HPA000397.
MIM300491. phenotype.
313440. gene.
neXtProtNX_P17600.
Orphanet85294. X-linked epilepsy - learning disabilities - behavior disorders.
PharmGKBPA36276.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG284201.
HOGENOMHOG000231323.
HOVERGENHBG016354.
InParanoidP17600.
OMAPIRQASQ.
OrthoDBEOG793B7G.
PhylomeDBP17600.
TreeFamTF319919.

Enzyme and pathway databases

ReactomeREACT_13685. Neuronal System.

Gene expression databases

BgeeP17600.
CleanExHS_SYN1.
GenevestigatorP17600.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 2 hits.
3.40.50.20. 1 hit.
InterProIPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR016185. PreATP-grasp_dom.
IPR028713. SYN1.
IPR001359. Synapsin.
IPR020898. Synapsin_ATP-bd_dom.
IPR019735. Synapsin_CS.
IPR019736. Synapsin_P_site.
IPR020897. Synapsin_pre-ATP-grasp_dom.
[Graphical view]
PANTHERPTHR10841:SF8. PTHR10841:SF8. 1 hit.
PfamPF02078. Synapsin. 1 hit.
PF02750. Synapsin_C. 1 hit.
PF10581. Synapsin_N. 1 hit.
[Graphical view]
PRINTSPR01368. SYNAPSIN.
SUPFAMSSF52440. SSF52440. 1 hit.
PROSITEPS00415. SYNAPSIN_1. 1 hit.
PS00416. SYNAPSIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSYN1. human.
GeneWikiSynapsin_I.
GenomeRNAi6853.
NextBio26745.
PROP17600.
SOURCESearch...

Entry information

Entry nameSYN1_HUMAN
AccessionPrimary (citable) accession number: P17600
Secondary accession number(s): B1AJQ1, O75825, Q5H9A9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 30, 2005
Last modified: April 16, 2014
This is version 144 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human chromosome X

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