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Protein

Synapsin-1

Gene

SYN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • ATP binding Source: ParkinsonsUK-UCL
  • catalytic activity Source: InterPro
  • protein kinase binding Source: ParkinsonsUK-UCL
  • transporter activity Source: ProtInc

GO - Biological processi

  • neurotransmitter secretion Source: InterPro
  • regulation of neurotransmitter secretion Source: ParkinsonsUK-UCL
  • regulation of synaptic vesicle exocytosis Source: ParkinsonsUK-UCL
  • synaptic transmission Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_15293. Dopamine Neurotransmitter Release Cycle.
REACT_15425. Serotonin Neurotransmitter Release Cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Synapsin-1
Alternative name(s):
Brain protein 4.1
Synapsin I
Gene namesi
Name:SYN1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:11494. SYN1.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytosol Source: Ensembl
  • dendrite Source: Ensembl
  • Golgi apparatus Source: UniProtKB-SubCell
  • myelin sheath Source: Ensembl
  • presynaptic active zone Source: Ensembl
  • synaptic vesicle Source: ParkinsonsUK-UCL
  • terminal bouton Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Golgi apparatus, Synapse

Pathology & Biotechi

Involvement in diseasei

Epilepsy X-linked, with variable learning disabilities and behavior disorders (XELBD)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA neurologic disorder characterized by variable combinations of epilepsy, learning difficulties, macrocephaly, and aggressive behavior.

See also OMIM:300491

Keywords - Diseasei

Epilepsy

Organism-specific databases

MIMi300491. phenotype.
Orphaneti85294. X-linked epilepsy - learning disabilities - behavior disorders.
PharmGKBiPA36276.

Polymorphism and mutation databases

BioMutaiSYN1.
DMDMi73920800.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 705705Synapsin-1PRO_0000183018Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91Phosphoserine; by CaMK1 and PKABy similarity
Glycosylationi55 – 551O-linked (GlcNAc)By similarity
Glycosylationi87 – 871O-linked (GlcNAc)By similarity
Glycosylationi96 – 961O-linked (GlcNAc)By similarity
Glycosylationi103 – 1031O-linked (GlcNAc)By similarity
Glycosylationi261 – 2611O-linked (GlcNAc)By similarity
Modified residuei312 – 3121PhosphotyrosineBy similarity
Modified residuei427 – 4271PhosphoserineBy similarity
Glycosylationi432 – 4321O-linked (GlcNAc)By similarity
Glycosylationi526 – 5261O-linked (GlcNAc)By similarity
Modified residuei551 – 5511Phosphoserine; by PDPK12 Publications
Modified residuei553 – 5531Phosphoserine2 Publications
Glycosylationi564 – 5641O-linked (GlcNAc)By similarity
Modified residuei568 – 5681Phosphoserine; by CaMK2By similarity
Glycosylationi578 – 5781O-linked (GlcNAc)By similarity
Modified residuei605 – 6051Phosphoserine; by CaMK2By similarity

Post-translational modificationi

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

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP17600.
PaxDbiP17600.
PRIDEiP17600.

PTM databases

PhosphoSiteiP17600.

Expressioni

Gene expression databases

BgeeiP17600.
CleanExiHS_SYN1.
GenevisibleiP17600. HS.

Organism-specific databases

HPAiCAB021929.
HPA000397.

Interactioni

Subunit structurei

Homodimer. Interacts with CAPON. Forms a ternary complex with NOS1. Isoform Ib interacts with PRNP (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
SNCAP378402EBI-717274,EBI-985879

Protein-protein interaction databases

BioGridi112719. 27 interactions.
IntActiP17600. 5 interactions.
MINTiMINT-1370745.
STRINGi9606.ENSP00000295987.

Structurei

3D structure databases

ProteinModelPortaliP17600.
SMRiP17600. Positions 112-417.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 2828AAdd
BLAST
Regioni29 – 11284B; linkerAdd
BLAST
Regioni113 – 420308C; actin-binding and synaptic-vesicle bindingAdd
BLAST
Regioni421 – 655235D; Pro-rich linkerAdd
BLAST
Regioni656 – 70550EAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the synapsin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG284201.
GeneTreeiENSGT00530000063319.
HOGENOMiHOG000231323.
HOVERGENiHBG016354.
InParanoidiP17600.
OMAiPIRQASQ.
OrthoDBiEOG793B7G.
PhylomeDBiP17600.
TreeFamiTF319919.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 2 hits.
3.40.50.20. 1 hit.
InterProiIPR013815. 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]
PANTHERiPTHR10841. PTHR10841. 1 hit.
PTHR10841:SF8. PTHR10841:SF8. 1 hit.
PfamiPF02078. Synapsin. 1 hit.
PF02750. Synapsin_C. 1 hit.
PF10581. Synapsin_N. 1 hit.
[Graphical view]
PRINTSiPR01368. SYNAPSIN.
SUPFAMiSSF52440. SSF52440. 1 hit.
PROSITEiPS00415. SYNAPSIN_1. 1 hit.
PS00416. SYNAPSIN_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform IA (identifier: P17600-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MNYLRRRLSD SNFMANLPNG YMTDLQRPQP PPPPPGAHSP GATPGPGTAT
60 70 80 90 100
AERSSGVAPA ASPAAPSPGS SGGGGFFSSL SNAVKQTTAA AAATFSEQVG
110 120 130 140 150
GGSGGAGRGG AASRVLLVID EPHTDWAKYF KGKKIHGEID IKVEQAEFSD
160 170 180 190 200
LNLVAHANGG FSVDMEVLRN GVKVVRSLKP DFVLIRQHAF SMARNGDYRS
210 220 230 240 250
LVIGLQYAGI PSVNSLHSVY NFCDKPWVFA QMVRLHKKLG TEEFPLIDQT
260 270 280 290 300
FYPNHKEMLS STTYPVVVKM GHAHSGMGKV KVDNQHDFQD IASVVALTKT
310 320 330 340 350
YATAEPFIDA KYDVRVQKIG QNYKAYMRTS VSGNWKTNTG SAMLEQIAMS
360 370 380 390 400
DRYKLWVDTC SEIFGGLDIC AVEALHGKDG RDHIIEVVGS SMPLIGDHQD
410 420 430 440 450
EDKQLIVELV VNKMAQALPR QRQRDASPGR GSHGQTPSPG ALPLGRQTSQ
460 470 480 490 500
QPAGPPAQQR PPPQGGPPQP GPGPQRQGPP LQQRPPPQGQ QHLSGLGPPA
510 520 530 540 550
GSPLPQRLPS PTSAPQQPAS QAAPPTQGQG RQSRPVAGGP GAPPAARPPA
560 570 580 590 600
SPSPQRQAGP PQATRQTSVS GPAPPKASGA PPGGQQRQGP PQKPPGPAGP
610 620 630 640 650
TRQASQAGPV PRTGPPTTQQ PRPSGPGPAG RPKPQLAQKP SQDVPPPATA
660 670 680 690 700
AAGGPPHPQL NKSQSLTNAF NLPEPAPPRP SLSQDEVKAE TIRSLRKSFA

SLFSD
Length:705
Mass (Da):74,111
Last modified:August 30, 2005 - v3
Checksum:iBE4CE46C942300B0
GO
Isoform IB (identifier: P17600-2) [UniParc]FASTAAdd to basket

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

Show »
Length:669
Mass (Da):70,033
Checksum:i5E400115415D3E32
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1381E → G in AAC41930 (PubMed:2110562).Curated
Sequence conflicti138 – 1381E → G in AAC41931 (PubMed:2110562).Curated
Sequence conflicti631 – 6311R → A in AAC41930 (PubMed:2110562).Curated
Sequence conflicti631 – 6311R → A in AAC41931 (PubMed:2110562).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei661 – 6699NKSQSLTNA → KASPAQAQP in isoform IB. CuratedVSP_006316
Alternative sequencei670 – 70536Missing in isoform IB. CuratedVSP_006317Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58378
, M58321, M58341, M58351, M58353, M58359, M58371, M58372, M58373, M58374, M58375, M58376, M58377 Genomic DNA. Translation: AAC41930.1.
M58378
, 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.
CCDSiCCDS14280.1. [P17600-1]
CCDS35233.1. [P17600-2]
PIRiA35363.
RefSeqiNP_008881.2. NM_006950.3. [P17600-1]
NP_598006.1. NM_133499.2. [P17600-2]
UniGeneiHs.225936.

Genome annotation databases

EnsembliENST00000295987; ENSP00000295987; ENSG00000008056.
ENST00000340666; ENSP00000343206; ENSG00000008056. [P17600-2]
GeneIDi6853.
KEGGihsa:6853.
UCSCiuc004did.3. human. [P17600-2]
uc004die.3. human. [P17600-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58378
, M58321, M58341, M58351, M58353, M58359, M58371, M58372, M58373, M58374, M58375, M58376, M58377 Genomic DNA. Translation: AAC41930.1.
M58378
, 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.
CCDSiCCDS14280.1. [P17600-1]
CCDS35233.1. [P17600-2]
PIRiA35363.
RefSeqiNP_008881.2. NM_006950.3. [P17600-1]
NP_598006.1. NM_133499.2. [P17600-2]
UniGeneiHs.225936.

3D structure databases

ProteinModelPortaliP17600.
SMRiP17600. Positions 112-417.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112719. 27 interactions.
IntActiP17600. 5 interactions.
MINTiMINT-1370745.
STRINGi9606.ENSP00000295987.

PTM databases

PhosphoSiteiP17600.

Polymorphism and mutation databases

BioMutaiSYN1.
DMDMi73920800.

Proteomic databases

MaxQBiP17600.
PaxDbiP17600.
PRIDEiP17600.

Protocols and materials databases

DNASUi6853.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295987; ENSP00000295987; ENSG00000008056.
ENST00000340666; ENSP00000343206; ENSG00000008056. [P17600-2]
GeneIDi6853.
KEGGihsa:6853.
UCSCiuc004did.3. human. [P17600-2]
uc004die.3. human. [P17600-1]

Organism-specific databases

CTDi6853.
GeneCardsiGC0XM047431.
HGNCiHGNC:11494. SYN1.
HPAiCAB021929.
HPA000397.
MIMi300491. phenotype.
313440. gene.
neXtProtiNX_P17600.
Orphaneti85294. X-linked epilepsy - learning disabilities - behavior disorders.
PharmGKBiPA36276.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG284201.
GeneTreeiENSGT00530000063319.
HOGENOMiHOG000231323.
HOVERGENiHBG016354.
InParanoidiP17600.
OMAiPIRQASQ.
OrthoDBiEOG793B7G.
PhylomeDBiP17600.
TreeFamiTF319919.

Enzyme and pathway databases

ReactomeiREACT_15293. Dopamine Neurotransmitter Release Cycle.
REACT_15425. Serotonin Neurotransmitter Release Cycle.

Miscellaneous databases

ChiTaRSiSYN1. human.
GeneWikiiSynapsin_I.
GenomeRNAii6853.
NextBioi26745.
PROiP17600.
SOURCEiSearch...

Gene expression databases

BgeeiP17600.
CleanExiHS_SYN1.
GenevisibleiP17600. HS.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 2 hits.
3.40.50.20. 1 hit.
InterProiIPR013815. 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]
PANTHERiPTHR10841. PTHR10841. 1 hit.
PTHR10841:SF8. PTHR10841:SF8. 1 hit.
PfamiPF02078. Synapsin. 1 hit.
PF02750. Synapsin_C. 1 hit.
PF10581. Synapsin_N. 1 hit.
[Graphical view]
PRINTSiPR01368. SYNAPSIN.
SUPFAMiSSF52440. SSF52440. 1 hit.
PROSITEiPS00415. SYNAPSIN_1. 1 hit.
PS00416. SYNAPSIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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].

Entry informationi

Entry nameiSYN1_HUMAN
AccessioniPrimary (citable) accession number: P17600
Secondary accession number(s): B1AJQ1, O75825, Q5H9A9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 30, 2005
Last modified: July 22, 2015
This is version 155 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.