CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006234
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Syntaxin-1A 
Protein Synonyms/Alias
 Neuron-specific antigen HPC-1; Synaptotagmin-associated 35 kDa protein; P35A 
Gene Name
 Stx1a 
Gene Synonyms/Alias
 Sap 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
46EIRGFIDKIAENVEEacetylation[1]
83EELMSDIKKTANKVRacetylation[1]
88DIKKTANKVRSKLKSacetylation[1]
92TANKVRSKLKSIEQSacetylation[1]
94NKVRSKLKSIEQSIEubiquitination[2]
256SDTKKAVKYQSKARRubiquitination[2]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113] 
Functional Description
 Potentially involved in docking of synaptic vesicles at presynaptic active zones. May play a critical role in neurotransmitter exocytosis. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm. 
Sequence Annotation
 DOMAIN 192 254 t-SNARE coiled-coil homology.
 MOD_RES 14 14 Phosphoserine (By similarity).
 MOD_RES 188 188 Phosphoserine; by DAPK1.  
Keyword
 3D-structure; Cell junction; Coiled coil; Complete proteome; Cytoplasmic vesicle; Direct protein sequencing; Exocytosis; Membrane; Neurotransmitter transport; Phosphoprotein; Reference proteome; Synapse; Synaptosome; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 288 AA 
Protein Sequence
MKDRTQELRT AKDSDDDDDV TVTVDRDRFM DEFFEQVEEI RGFIDKIAEN VEEVKRKHSA 60
ILASPNPDEK TKEELEELMS DIKKTANKVR SKLKSIEQSI EQEEGLNRSS ADLRIRKTQH 120
STLSRKFVEV MSEYNATQSD YRERCKGRIQ RQLEITGRTT TSEELEDMLE SGNPAIFASG 180
IIMDSSISKQ ALSEIETRHS EIIKLENSIR ELHDMFMDMA MLVESQGEMI DRIEYNVEHA 240
VDYVERAVSD TKKAVKYQSK ARRKKIMIII CCVILGIIIA STIGGIFG 288 
Gene Ontology
 GO:0042641; C:actomyosin; IDA:RGD.
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0016021; C:integral to membrane; NAS:UniProtKB.
 GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IDA:RGD.
 GO:0030141; C:secretory granule; IDA:UniProtKB.
 GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
 GO:0070044; C:synaptobrevin 2-SNAP-25-syntaxin-1a complex; IDA:MGI.
 GO:0070032; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex; IDA:MGI.
 GO:0070033; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex; IDA:RGD.
 GO:0019855; F:calcium channel inhibitor activity; IEA:Compara.
 GO:0001948; F:glycoprotein binding; IDA:MGI.
 GO:0046982; F:protein heterodimerization activity; IDA:RGD.
 GO:0047485; F:protein N-terminus binding; IDA:RGD.
 GO:0000149; F:SNARE binding; IDA:MGI.
 GO:0017156; P:calcium ion-dependent exocytosis; IEA:Compara.
 GO:0006886; P:intracellular protein transport; IEA:InterPro.
 GO:0045921; P:positive regulation of exocytosis; IDA:RGD.
 GO:0001956; P:positive regulation of neurotransmitter secretion; IMP:RGD.
 GO:0009629; P:response to gravity; IDA:RGD.
 GO:0016081; P:synaptic vesicle docking involved in exocytosis; IEP:UniProtKB. 
Interpro
 IPR015709; Syntaxin-1.
 IPR006012; Syntaxin/epimorphin_CS.
 IPR006011; Syntaxin_N.
 IPR010989; t-SNARE.
 IPR000727; T_SNARE_dom. 
Pfam
 PF05739; SNARE
 PF00804; Syntaxin 
SMART
 SM00503; SynN
 SM00397; t_SNARE 
PROSITE
 PS00914; SYNTAXIN
 PS50192; T_SNARE 
PRINTS