CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013319
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein unc-13 homolog A 
Protein Synonyms/Alias
 Munc13-1 
Gene Name
 Unc13a 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
1130MNLHFKVKWLYNEYVubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 Plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool (RRP). Essential for synaptic vesicle maturation in most excitatory/glutamatergic but not inhibitory/GABA-mediated synapses. Also involved in secretory granule priming in insulin secretion. 
Sequence Annotation
 DOMAIN 1 79 C2 1.
 DOMAIN 672 778 C2 2.
 DOMAIN 1102 1245 MHD1.
 DOMAIN 1354 1521 MHD2.
 DOMAIN 1541 1646 C2 3.
 ZN_FING 562 612 Phorbol-ester/DAG-type.
 METAL 576 576 Zinc 1 (By similarity).
 METAL 579 579 Zinc 1 (By similarity).
 METAL 593 593 Zinc 2 (By similarity).
 METAL 596 596 Zinc 2 (By similarity).
 METAL 604 604 Zinc 1 (By similarity).
 METAL 612 612 Zinc 2 (By similarity).
 MOD_RES 244 244 Phosphoserine.  
Keyword
 Cell junction; Cell membrane; Coiled coil; Complete proteome; Cytoplasm; Exocytosis; Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat; Synapse; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1712 AA 
Protein Sequence
MSLLCVGVKK AKFDGAQEKF NTYVTLKVQN VKSTTIAVRG SQPSWEQDFM FEINRLDLGL 60
TVEVWNKGLI WDTMVGTVWI PLRTIRQSNE EGPGEWLTLD SQAIMADSEI CGTKDPTFHR 120
ILLDAHFELP LDIPEEEARY WAKKLEQLNA MRDQDEYSFQ DQQDKPLPVP SSQCCNWNYF 180
GWGEQNDDPD SAVDDRDSDY RSETSNSIPP PYYTTSQPNA SVHQYSVRPP PLGSRESYSD 240
SMHSYEEFSE PRALSPTGSS RYASSGELSQ GSSQLSEDFD PDEHSLQGSE LDDERDRDSY 300
HSCHSSVSYH KDSPRWDQDD EDLEDLEDLE DEELPEEEEE LEEEGEEELE EEDLEEEEEV 360
PDDLASYTQQ EDTTVAEPKE FKRISFPTAA PQKDDKVSAV PTEAPEVAKG IPKAATPEEK 420
AAAERAQEAE PPKSEESFRS REEEEGQEGQ DAMSRAKANW LRAFNKVRMQ LQEARGEGDM 480
SKSLWFKGGP GGGLIIIDSM PDIRKRKPIP LVSDLAMSLV QSRKAGITSA LASSTLNNEE 540
LKNHVYKKTL QALIYPISCT TPHNFEVWTA TTPTYCYECE GLLWGIARQG MRCTECGVKC 600
HEKCQDLLNA DCLQRAAEKS SKHGAEDRTQ NIIMVLKDRM KIRERNKPEI FELIQEIFAV 660
TKSAHTQQMK AVKQSVLDGT SKWSAKISIT VVCAQGLQAK DKTGSSDPYV TVQVGKTKKR 720
TKTIYGNLNP VWEENFHFEC HNSSDRIKVR VWDEDDDIKS RVKQRFKRES DDFLGQTIIE 780
VRTLSGEMDV WYNLDKRTDK SAVSGAIRLH ISVEIKGEEK VAPYHVQYTC LHENLFHFVT 840
DVQNNGVVKI PDAKGDDAWK VYYDETAQEI VDEFAMRYGV ESIYQAMTHF ACLSSKYMCP 900
GVPAVMSTLL ANINAYYAHT TASTNVSASD RFAASNFGKE RFVKLLDQLH NSLRIDLSMY 960
RNNFPASSPE RLQDLKSTVD LLTSITFFRM KVQELQSPPR ASQVVKDCVK ACLNSTYEYI 1020
FNNCHELYGR EYQTDPAKKG EVPPEEQGPS IKNLDFWSKL ITLIVSIIEE DKNSYTPCLN 1080
QFPQELNVGK ISAEVMWSLF AQDMKYAMEE HDKHRLCKSA DYMNLHFKVK WLYNEYVAEL 1140
PTFKDRVPEY PAWFEPFVIQ WLDENEEVSR DFLHGALERD KKDGFQQTSE HALFSCSVVD 1200
VFSQLNQSFE IIKKLECPDP QIVGHYMRRF AKTISNVLLQ YADIVSKDFA SYCSKEKEKV 1260
PCILMNNTQQ LRVQLEKMFE AMGGKELDAE ASGTLKELQV KLNNVLDELS HVFATSFQPH 1320
IEECVRQMGD ILSQVKGTGN VPASACSSVA QDADNVLQPI MDLLDSNLTL FAKICEKTVL 1380
KRVLKELWKL VMNTMEKTIV LPPLTDQTMI GTLLRKHGKG LEKGRVKLPS HSDGTQMIFN 1440
AAKELGQLSK LKDHMVREEA KSLTPKQCAV VELALDTIKQ YFHAGGVGLK KTFLEKSPDL 1500
QSLRYALSLY TQATDLLIKT FVQTQSAQGS GVEDPVGEVS VHVELFTHPG TGEQKVTVKV 1560
VAANDLKWQT SGIFRPFIEV NIVGPQLSDK KRKFATKSKN NSWAPKYNES FQFSLSADAG 1620
PECYELQVCV KDYCFAREDR TVGLAVLQLR ELAQRGSAAC WLPLGRRIHM DDTGLTVLRI 1680
LSQRSNDEVA KEFVKLKSDT RSAEEGGAAP AP 1712 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0031594; C:neuromuscular junction; IDA:MGI.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
 GO:0019992; F:diacylglycerol binding; IDA:MGI.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0050435; P:beta-amyloid metabolic process; IMP:MGI.
 GO:0060384; P:innervation; IGI:MGI.
 GO:0035556; P:intracellular signal transduction; IEA:InterPro.
 GO:0007528; P:neuromuscular junction development; IGI:MGI.
 GO:0001956; P:positive regulation of neurotransmitter secretion; IMP:MGI.
 GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IMP:MGI.
 GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
 GO:0016081; P:synaptic vesicle docking involved in exocytosis; IGI:MGI.
 GO:0016188; P:synaptic vesicle maturation; IMP:MGI.
 GO:0016082; P:synaptic vesicle priming; IEA:InterPro. 
Interpro
 IPR000008; C2_Ca-dep.
 IPR008973; C2_Ca/lipid-bd_dom_CaLB.
 IPR020477; C2_dom.
 IPR018029; C2_membr_targeting.
 IPR010439; Ca-dep_secretion_activator.
 IPR014770; Munc13_1.
 IPR014772; Munc13_dom-2.
 IPR019558; Munc13_subgr_dom-2.
 IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
 IPR027080; Unc-13.
 IPR027082; Unc13A. 
Pfam
 PF00130; C1_1
 PF00168; C2
 PF06292; DUF1041
 PF10540; Membr_traf_MHD 
SMART
 SM00109; C1
 SM00239; C2 
PROSITE
 PS50004; C2
 PS51258; MHD1
 PS51259; MHD2
 PS00479; ZF_DAG_PE_1
 PS50081; ZF_DAG_PE_2 
PRINTS
 PR00360; C2DOMAIN.