CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023098
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Poly [ADP-ribose] polymerase 4 
Protein Synonyms/Alias
 PARP-4; 193 kDa vault protein; ADP-ribosyltransferase diphtheria toxin-like 4; ARTD4; PARP-related/IalphaI-related H5/proline-rich; PH5P; Vault poly(ADP-ribose) polymerase; VPARP 
Gene Name
 PARP4 
Gene Synonyms/Alias
 ADPRTL1; KIAA0177; PARPL 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
31KKLQTDIKENGGKFSubiquitination[1]
90EKRLLDVKNYDPYKPubiquitination[2, 3]
96VKNYDPYKPLDITPPubiquitination[2]
223ENYIEELKKQGFLLRubiquitination[1, 2, 3]
224NYIEELKKQGFLLREubiquitination[1]
296ISLNDVSKAEGILLLubiquitination[1]
305EGILLLVKAALKNGEubiquitination[2]
309LLVKAALKNGETAEQubiquitination[1, 2, 3, 4]
336PHKGTMPKEVNLGLLubiquitination[5]
346NLGLLAKKADLCQLIubiquitination[1]
406VLQNHHSKSPVDVLQubiquitination[1]
429ETTEFLSKLGNVRPLubiquitination[2]
457CRGLLLPKVVEDRGVubiquitination[1]
509ICDVALGKCMDLHEKubiquitination[1]
594PEFSNFSKVEDYQLPubiquitination[2, 3, 6]
604DYQLPDAKTSSSTKAubiquitination[1, 2, 4]
610AKTSSSTKAGLQDASubiquitination[1]
629PLEDVHIKGRIIDTVubiquitination[1, 4]
664YIFPLDDKAAVCGFEubiquitination[2]
677FEAFINGKHIVGEIKubiquitination[1]
771NLQDTVEKICIKEIGubiquitination[1]
775TVEKICIKEIGTKQSubiquitination[1]
847LPRMWVEKHPEKESEubiquitination[1]
1030VFEYFNAKSKHSWRKubiquitination[1, 4, 7]
1032EYFNAKSKHSWRKQIubiquitination[1]
1037KSKHSWRKQIEDQMTubiquitination[1]
1126TTGTMIHKLAARALIubiquitination[1]
1151NETSHEMKKQTLKSLubiquitination[2]
1152ETSHEMKKQTLKSLIubiquitination[1]
1200KVSELIAKEDVDFLPubiquitination[1, 2, 3]
1294LSWTESCKPTATEPLubiquitination[1, 2, 6]
1303TATEPLFKKVSPWETubiquitination[1]
1304ATEPLFKKVSPWETSubiquitination[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] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [7] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724
Functional Description
  
Sequence Annotation
 DOMAIN 1 94 BRCT.
 DOMAIN 242 370 PARP alpha-helical.
 DOMAIN 369 573 PARP catalytic.
 DOMAIN 607 735 VIT.
 DOMAIN 876 1046 VWFA.
 REGION 1562 1724 Interaction with the major vault protein.
 MOTIF 19 25 Nuclear localization signal (Potential).
 MOTIF 1237 1249 Nuclear localization signal (Potential).
 MOD_RES 101 101 Phosphothreonine.
 MOD_RES 1236 1236 Phosphoserine.
 MOD_RES 1335 1335 Phosphoserine.
 MOD_RES 1504 1504 Phosphoserine.  
Keyword
 Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Glycosyltransferase; NAD; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ribonucleoprotein; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1724 AA 
Protein Sequence
MVMGIFANCI FCLKVKYLPQ QQKKKLQTDI KENGGKFSFS LNPQCTHIIL DNADVLSQYQ 60
LNSIQKNHVH IANPDFIWKS IREKRLLDVK NYDPYKPLDI TPPPDQKASS SEVKTEGLCP 120
DSATEEEDTV ELTEFGMQNV EIPHLPQDFE VAKYNTLEKV GMEGGQEAVV VELQCSRDSR 180
DCPFLISSHF LLDDGMETRR QFAIKKTSED ASEYFENYIE ELKKQGFLLR EHFTPEATQL 240
ASEQLQALLL EEVMNSSTLS QEVSDLVEMI WAEALGHLEH MLLKPVNRIS LNDVSKAEGI 300
LLLVKAALKN GETAEQLQKM MTEFYRLIPH KGTMPKEVNL GLLAKKADLC QLIRDMVNVC 360
ETNLSKPNPP SLAKYRALRC KIEHVEQNTE EFLRVRKEVL QNHHSKSPVD VLQIFRVGRV 420
NETTEFLSKL GNVRPLLHGS PVQNIVGILC RGLLLPKVVE DRGVQRTDVG NLGSGIYFSD 480
SLSTSIKYSH PGETDGTRLL LICDVALGKC MDLHEKDFSL TEAPPGYDSV HGVSQTASVT 540
TDFEDDEFVV YKTNQVKMKY IIKFSMPGDQ IKDFHPSDHT ELEEYRPEFS NFSKVEDYQL 600
PDAKTSSSTK AGLQDASGNL VPLEDVHIKG RIIDTVAQVI VFQTYTNKSH VPIEAKYIFP 660
LDDKAAVCGF EAFINGKHIV GEIKEKEEAQ QEYLEAVTQG HGAYLMSQDA PDVFTVSVGN 720
LPPKAKVLIK ITYITELSIL GTVGVFFMPA TVAPWQQDKA LNENLQDTVE KICIKEIGTK 780
QSFSLTMSIE MPYVIEFIFS DTHELKQKRT DCKAVISTME GSSLDSSGFS LHIGLSAAYL 840
PRMWVEKHPE KESEACMLVF QPDLDVDLPD LASESEVIIC LDCSSSMEGV TFLQAKQIAL 900
HALSLVGEKQ KVNIIQFGTG YKELFSYPKH ITSNTMAAEF IMSATPTMGN TDFWKTLRYL 960
SLLYPARGSR NILLVSDGHL QDESLTLQLV KRSRPHTRLF ACGIGSTANR HVLRILSQCG 1020
AGVFEYFNAK SKHSWRKQIE DQMTRLCSPS CHSVSVKWQQ LNPDVPEALQ APAQVPSLFL 1080
NDRLLVYGFI PHCTQATLCA LIQEKEFRTM VSTTELQKTT GTMIHKLAAR ALIRDYEDGI 1140
LHENETSHEM KKQTLKSLII KLSKENSLIT QFTSFVAVEK RDENESPFPD IPKVSELIAK 1200
EDVDFLPYMS WQGEPQEAVR NQSLLASSEW PELRLSKRKH RKIPFSKRKM ELSQPEVSED 1260
FEEDGLGVLP AFTSNLERGG VEKLLDLSWT ESCKPTATEP LFKKVSPWET STSSFFPILA 1320
PAVGSYLPPT ARAHSPASLS FASYRQVASF GSAAPPRQFD ASQFSQGPVP GTCADWIPQS 1380
ASCPTGPPQN PPSSPYCGIV FSGSSLSSAQ SAPLQHPGGF TTRPSAGTFP ELDSPQLHFS 1440
LPTDPDPIRG FGSYHPSASS PFHFQPSAAS LTANLRLPMA SALPEALCSQ SRTTPVDLCL 1500
LEESVGSLEG SRCPVFAFQS SDTESDELSE VLQDSCFLQI KCDTKDDSIL CFLEVKEEDE 1560
IVCIQHWQDA VPWTELLSLQ TEDGFWKLTP ELGLILNLNT NGLHSFLKQK GIQSLGVKGR 1620
ECLLDLIATM LVLQFIRTRL EKEGIVFKSL MKMDDASISR NIPWAFEAIK QASEWVRRTE 1680
GQYPSICPRL ELGNDWDSAT KQLLGLQPIS TVSPLHRVLH YSQG 1724 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005634; C:nucleus; NAS:UniProtKB.
 GO:0030529; C:ribonucleoprotein complex; NAS:UniProtKB.
 GO:0005876; C:spindle microtubule; IDA:UniProtKB.
 GO:0003677; F:DNA binding; TAS:ProtInc.
 GO:0019899; F:enzyme binding; IDA:MGI.
 GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:UniProtKB.
 GO:0008219; P:cell death; IMP:UniProtKB.
 GO:0006281; P:DNA repair; NAS:UniProtKB.
 GO:0006954; P:inflammatory response; IMP:UniProtKB.
 GO:0006471; P:protein ADP-ribosylation; NAS:UniProtKB.
 GO:0042493; P:response to drug; NAS:UniProtKB.
 GO:0006810; P:transport; NAS:UniProtKB. 
Interpro
 IPR001357; BRCT_dom.
 IPR012317; Poly(ADP-ribose)pol_cat_dom.
 IPR004102; Poly(ADP-ribose)pol_reg_dom.
 IPR013694; VIT.
 IPR002035; VWF_A. 
Pfam
 PF00533; BRCT
 PF00644; PARP
 PF08487; VIT
 PF00092; VWA 
SMART
 SM00292; BRCT
 SM00609; VIT
 SM00327; VWA 
PROSITE
 PS50172; BRCT
 PS51060; PARP_ALPHA_HD
 PS51059; PARP_CATALYTIC
 PS51468; VIT
 PS50234; VWFA 
PRINTS