CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015619
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein unc-13 homolog D 
Protein Synonyms/Alias
 Munc13-4 
Gene Name
 UNC13D 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
108QRVRELEKPIFCLKAubiquitination[1]
126QAKGILGKDVSGFSDubiquitination[1]
216TVESVRQKLGELTDLubiquitination[1]
235RIFKEARKDKGQDDFubiquitination[1]
237FKEARKDKGQDDFLGubiquitination[1]
285LQFQLIHKRRATSASubiquitination[1]
440RVLVQMCKMKAFGELubiquitination[1]
511QCQRTWDKIFHNTLKacetylation[2]
511QCQRTWDKIFHNTLKubiquitination[3]
599AIPSWLQKTYNEALAubiquitination[1, 4]
625VPLGELTKHSTSAVDubiquitination[1]
678LVYCSLIKARARELSubiquitination[1]
689RELSSGQKDQGQAANubiquitination[1]
714QLRLVIGKLPAQLAWubiquitination[1, 4, 5, 6]
773QLEVGIAKHIQKLVGubiquitination[1, 5, 6]
777GIAKHIQKLVGVRESubiquitination[1, 6]
894SSRELIRKYFCSRIQubiquitination[1]
917ELGAVTVKASYRASEubiquitination[1, 5]
1079RLRRHRAKQASQHALubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse. Regulates assembly of recycling and late endosomal structures, leading to the formation of an endosomal exocytic compartment that fuses with perforin-containing granules at the immunologic synapse and licences them for exocytosis. Regulates Ca(2+)-dependent secretory lysosome exocytosis in mast cells. 
Sequence Annotation
 DOMAIN 98 221 C2 1.
 DOMAIN 557 677 MHD1.
 DOMAIN 788 895 MHD2.
 DOMAIN 912 1019 C2 2.
 REGION 240 543 Interaction with RAB27A.
 MOD_RES 150 150 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Endosome; Exocytosis; Familial hemophagocytic lymphohistiocytosis; Lysosome; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1090 AA 
Protein Sequence
MATLLSHPQQ RPPFLRQAIK IRRRRVRDLQ DPPPQMAPEI QPPSHHFSPE QRALLYEDAL 60
YTVLHRLGHP EPNHVTEASE LLRYLQEAFH VEPEEHQQTL QRVRELEKPI FCLKATVKQA 120
KGILGKDVSG FSDPYCLLGI EQGVGVPGGS PGSRHRQKAV VRHTIPEEET HRTQVITQTL 180
NPVWDETFIL EFEDITNASF HLDMWDLDTV ESVRQKLGEL TDLHGLRRIF KEARKDKGQD 240
DFLGNVVLRL QDLRCREDQW YPLEPRTETY PDRGQCHLQF QLIHKRRATS ASRSQPSYTV 300
HLHLLQQLVS HEVTQHEAGS TSWDGSLSPQ AATVLFLHAT QKDLSDFHQS MAQWLAYSRL 360
YQSLEFPSSC LLHPITSIEY QWIQGRLKAE QQEELAASFS SLLTYGLSLI RRFRSVFPLS 420
VSDSPARLQS LLRVLVQMCK MKAFGELCPN TAPLPQLVTE ALQTGTTEWF HLKQQHHQPM 480
VQGIPEAGKA LLGLVQDVIG DLHQCQRTWD KIFHNTLKIH LFSMAFRELQ WLVAKRVQDH 540
TTVVGDVVSP EMGESLFQLY ISLKELCQLR MSSSERDGVL ALDNFHRWFQ PAIPSWLQKT 600
YNEALARVQR AVQMDELVPL GELTKHSTSA VDLSTCFAQI SHTARQLDWP DPEEAFMITV 660
KFVEDTCRLA LVYCSLIKAR ARELSSGQKD QGQAANMLCV VVNDMEQLRL VIGKLPAQLA 720
WEALEQRVGA VLEQGQLQNT LHAQLQSALA GLGHEIRTGV RTLAEQLEVG IAKHIQKLVG 780
VRESVLPEDA ILPLMKFLEV ELCYMNTNLV QENFSSLLTL LWTHTLTVLV EAAASQRSSS 840
LASNRLKIAL QNLEICFHAE GCGLPPKALH TATFQALQRD LELQAASSRE LIRKYFCSRI 900
QQQAETTSEE LGAVTVKASY RASEQKLRVE LLSASSLLPL DSNGSSDPFV QLTLEPRHEF 960
PELAARETQK HKKDLHPLFD ETFEFLVPAE PCRKAGACLL LTVLDYDTLG ADDLEGEAFL 1020
PLREVPGLSG SEEPGEVPQT RLPLTYPAPN GDPILQLLEG RKGDREAQVF VRLRRHRAKQ 1080
ASQHALRPAP 1090 
Gene Ontology
 GO:0070382; C:exocytic vesicle; IDA:UniProtKB.
 GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
 GO:0005764; C:lysosome; IDA:UniProtKB.
 GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
 GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
 GO:0051607; P:defense response to virus; IEA:Compara.
 GO:0002467; P:germinal center formation; IEA:Compara.
 GO:0002432; P:granuloma formation; IEA:Compara.
 GO:0043320; P:natural killer cell degranulation; IEA:Compara.
 GO:0006909; P:phagocytosis; IEA:Compara.
 GO:0045921; P:positive regulation of exocytosis; IMP:UniProtKB.
 GO:0043304; P:regulation of mast cell degranulation; IMP:UniProtKB. 
Interpro
 IPR000008; C2_Ca-dep.
 IPR008973; C2_Ca/lipid-bd_dom_CaLB.
 IPR018029; C2_membr_targeting.
 IPR014770; Munc13_1.
 IPR014772; Munc13_dom-2.
 IPR019558; Munc13_subgr_dom-2. 
Pfam
 PF00168; C2
 PF10540; Membr_traf_MHD 
SMART
 SM00239; C2 
PROSITE
 PS50004; C2
 PS51258; MHD1
 PS51259; MHD2 
PRINTS