CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021659
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Synaptotagmin-like protein 2 
Protein Synonyms/Alias
 Breast cancer-associated antigen SGA-72M; Exophilin-4 
Gene Name
 SYTL2 
Gene Synonyms/Alias
 KIAA1597; SGA72M; SLP2; SLP2A 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
1028KKTLVVKKTLNPVYNubiquitination[1]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965
Functional Description
 Isoform 1 acts as a RAB27A effector protein and plays a role in cytotoxic granule exocytosis in lymphocytes. It is required for cytotoxic granule docking at the immunologic synapse. Isoform 4 binds phosphatidylserine (PS) and phosphatidylinositol- 4,5-bisphosphate (PIP2) and promotes the recruitment of glucagon- containing granules to the cell membrane in pancreatic alpha cells. Binding to PS is inhibited by Ca(2+) while binding to PIP2 is Ca(2+) insensitive. 
Sequence Annotation
 DOMAIN 1 57 RabBD.
 DOMAIN 629 733 C2 1.
 DOMAIN 778 880 C2 2.
 MOD_RES 262 262 Phosphoserine (By similarity).
 MOD_RES 278 278 Phosphoserine (By similarity).
 MOD_RES 488 488 Phosphoserine (By similarity).
 MOD_RES 562 562 Phosphoserine (By similarity).  
Keyword
 3D-structure; Alternative splicing; Cell membrane; Complete proteome; Cytoplasm; Exocytosis; Membrane; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 934 AA 
Protein Sequence
MDEPNAEQVY NPSQFENLRK FWDLEANSNS KDNDKNITTT SQKNSAPFNR QKHKEFSDIK 60
LSGKNTHEAE VLLSPKKVMA REEMEKLNSK GILQVLPDEI TFPLSPLRKY TYQLPGNESS 120
KENVEKNTEG IVTPVFKEEK DYSEQEIQES IIKTNVLSKD CKDTFNDSLQ KLLSETSTPA 180
IQPSGGKVHG KQVLEPSVSE NRTWPQKTDF ADTEEEVKGP EKIINEHVDK TVVHPKVKRN 240
SLTASLDKLL KEATGTSPSP LQAKLAPVIT GTNSKLEEGR FFGKGIEQSH NTSADKREIL 300
APFPVRDETF GNTALLKKAE SGECQLSTQN LIQMAAEDSH PLDPTSQLSR KGSFGDVASP 360
PQDMLFPQDA HLVPQARVHP SQTEISETVE KVILPPRPVL NDVSAALQKL CGEVWLSYPA 420
GREVGPGEVN PEFPEAVQPV CSPLNPPGVI SPWATMDTIV PDRKDFYSSN VVPDKTHEVG 480
SYLAAQMSPS DQTLSSFASI VAQYGKGLPQ EVEEIVRETI VQPKSEFLEF SAGLEKLLKE 540
ETETFPSKYE SDTGNLSPSK LIGSTEEPRR ATSECHPEEL KETVEKAEAP LITESAFDAG 600
FEKLLKEITE APPYQPQVSV REETHEKESS QSEQTRFLGT VPHFYRAASQ TSEMKDKSNG 660
LESQVNQCDK MLGGDALVTD LLVDFCGSRS GVEIPRTPQL YVAHEIGTIK TVTPPEDRDS 720
ESGVAGGQGT LQEPGFGEAS EAISVSRNRQ PIPLLMNKEN STKTSKVELT LASPYMKQEK 780
EEEKEGFSES DFSDGNTSSN AESWRNPSSS EEEPSPVLKT LERSAARKMP SKSLEDISSD 840
SSNQAKVDNQ PEELVRSAED DEKPDQKPVT NECVPRISTV PTQPDNPFSH PDKLKRMSKS 900
VPAFLQDESD DRETDTASES SYQLSRHKKS PSSLTNLSSS SGMTSLSSVS GSVMSVYSGD 960
FGNLEVKGNI QFAIEYVESL KELHVFVAQC KDLAAADVKK QRSDPYVKAY LLPDKGKMGK 1020
KKTLVVKKTL NPVYNEILRY KIEKQILKTQ KLNLSIWHRD TFKRNSFLGE VELDLETWDW 1080
DNKQNKQLRW YPLKRKTAPV ALEAENRGEM KLALQYVPEP VPGKKLPTTG EVHIWVKECL 1140
DLPLLRGSHL NSFVKCTILP DTSRKSRQKT RAVGKTTNPI FNHTMVYDGF RPEDLMEACV 1200
ELTVWDHYKL TNQFLGGLRI GFGTGKSYGT EVDWMDSTSE EVALWEKMVN SPNTWIEATL 1260
PLRMLLIAKI SK 1272 
Gene Ontology
 GO:0070382; C:exocytic vesicle; IDA:UniProtKB.
 GO:0019897; C:extrinsic to plasma membrane; ISS:UniProtKB.
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0042470; C:melanosome; ISS:UniProtKB.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0042043; F:neurexin family protein binding; ISS:UniProtKB.
 GO:0019902; F:phosphatase binding; IDA:UniProtKB.
 GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IMP:UniProtKB.
 GO:0001786; F:phosphatidylserine binding; IMP:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006886; P:intracellular protein transport; IEA:InterPro.
 GO:0010923; P:negative regulation of phosphatase activity; IDA:UniProtKB.
 GO:0006904; P:vesicle docking involved in exocytosis; IDA:UniProtKB. 
Interpro
 IPR000008; C2_Ca-dep.
 IPR008973; C2_Ca/lipid-bd_dom_CaLB.
 IPR018029; C2_membr_targeting.
 IPR010911; Rab-bd_domain.
 IPR027006; SYTL2.
 IPR011011; Znf_FYVE_PHD.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00168; C2 
SMART
 SM00239; C2 
PROSITE
 PS50004; C2
 PS50916; RABBD 
PRINTS