CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013204
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Poly [ADP-ribose] polymerase 14 
Protein Synonyms/Alias
 PARP-14; ADP-ribosyltransferase diphtheria toxin-like 8; ARTD8; B aggressive lymphoma protein 2 
Gene Name
 PARP14 
Gene Synonyms/Alias
 BAL2; KIAA1268 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
26PPKNLNTKLQMYFQSubiquitination[1]
35QMYFQSPKRSGGGECubiquitination[1]
71RQKVLERKNHELVWQubiquitination[1]
210RFVDDCTKHHSIKQLubiquitination[1]
215CTKHHSIKQLQLSPRubiquitination[1]
245GADDYSLKLFFENPYubiquitination[1]
278LIEFFDRKVLDTIMAubiquitination[1]
287LDTIMATKLDFNKMPubiquitination[1]
311LGTALYGKEKPLIKLubiquitination[1]
313TALYGKEKPLIKLPAubiquitination[1]
317GKEKPLIKLPAPFEEubiquitination[1]
332SLDLPLWKFLQKKNHubiquitination[1]
337LWKFLQKKNHLIEEIubiquitination[1]
381NEGRPRIKTWQADTSubiquitination[1, 2, 3, 4]
399SSIRSKYKVNPIKVDubiquitination[1]
404KYKVNPIKVDPTMWDubiquitination[1]
414PTMWDTIKNDVKDDRubiquitination[1]
418DTIKNDVKDDRILIEubiquitination[1]
459LIESTTQKIKREEQSubiquitination[1]
461ESTTQKIKREEQSLKubiquitination[1]
470EEQSLKEKMIISPGRubiquitination[1]
511VTQHLCLKGPSADVYubiquitination[1]
519GPSADVYKAKCEIQEubiquitination[1]
527AKCEIQEKVYTMAQKubiquitination[1]
599MLSALNYKRIEVENKubiquitination[2, 4]
613KEVLHGKKWKGLTHNubiquitination[1]
615VLHGKKWKGLTHNLLubiquitination[1]
624LTHNLLKKQNSSPNTubiquitination[1]
670NFVEQNMKIERLVEVubiquitination[1]
678IERLVEVKPSLVIDYubiquitination[1]
687SLVIDYLKTEKKLFWubiquitination[1]
711VSFNPENKQKGILLTubiquitination[3]
713FNPENKQKGILLTGSubiquitination[1]
721GILLTGSKTEVLKAVubiquitination[1]
726GSKTEVLKAVDIVKQubiquitination[1]
732LKAVDIVKQVWDSVCubiquitination[1]
741VWDSVCVKSVHTDKPubiquitination[1]
747VKSVHTDKPGAKQFFubiquitination[1]
751HTDKPGAKQFFQDKAubiquitination[1]
757AKQFFQDKARFYQSEubiquitination[1]
782LQENEVMKEGGSPAGubiquitination[1]
791GGSPAGQKCFSRTVLubiquitination[1]
828NASNEDLKHYGGLAAubiquitination[1]
839GLAAALSKAAGPELQubiquitination[1]
854ADCDQIVKREGRLLPubiquitination[1, 3]
868PGNATISKAGKLPYHubiquitination[1]
871ATISKAGKLPYHHVIubiquitination[1]
910LSLCLAEKYKYRSIAubiquitination[1]
942ETIVSAIKENFQFKKubiquitination[1]
955KKDGHCLKEIYLVDVubiquitination[1]
975EAFAEAVKTVFKATLubiquitination[1]
979EAVKTVFKATLPDTAubiquitination[1]
1005PGKTSWEKGSLVSPGubiquitination[1, 3]
1020GLQMLLVKEGVQNAKubiquitination[1, 3]
1027KEGVQNAKTDVVVNSubiquitination[1]
1048LSRGPLSKSLLEKAGubiquitination[1, 3]
1198NGNLVSDKIPKAKDTubiquitination[1]
1203SDKIPKAKDTQGFYGubiquitination[1, 3]
1260NLKAGVSKAILECAGubiquitination[1, 3]
1282SQQAQQRKNDYIITGubiquitination[1]
1296GGGFLRCKNIIHVIGubiquitination[1]
1308VIGGNDVKSSVSSVLubiquitination[1]
1321VLQECEKKNYSSICLubiquitination[1]
1400SQQSVMSKLASFLGFubiquitination[1]
1409ASFLGFSKQSPQKKNubiquitination[1]
1465TSEDECIKDFDEKEYubiquitination[1]
1481ELNELQKKLNINISLubiquitination[1]
1496DHKRPLIKVLGISRDubiquitination[1]
1516DEIEAMIKRVRLAKEubiquitination[1, 3]
1555FNKMTNLKLEDARREubiquitination[1]
1570KKKTVDVKINHRHYTubiquitination[1]
1589TYTATDTKGHSLSVQubiquitination[1, 3]
1602VQRLTKSKVDIPAHWubiquitination[1]
1613PAHWSDMKQQNFCVVubiquitination[1]
1664WNSYQAKKKTMDAKNubiquitination[1]
1665NSYQAKKKTMDAKNGubiquitination[1]
1670KKKTMDAKNGQTMNEubiquitination[1]
1678NGQTMNEKQLFHGTDubiquitination[1]
1704FNRSYAGKNAVAYGKubiquitination[1, 3, 5]
1736RPDANGRKHVYYVRVubiquitination[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] 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]
 [3] 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]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] 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
 Enhances STAT6-dependent transcription (By similarity). Has ADP-ribosyltransferase activity. 
Sequence Annotation
 DOMAIN 791 978 Macro 1.
 DOMAIN 1003 1190 Macro 2.
 DOMAIN 1216 1387 Macro 3.
 DOMAIN 1523 1601 WWE.
 DOMAIN 1605 1801 PARP catalytic.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Glycosyltransferase; NAD; Nucleus; Reference proteome; Repeat; Transcription; Transcription regulation; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1801 AA 
Protein Sequence
MAVPGSFPLL VEGSWGPDPP KNLNTKLQMY FQSPKRSGGG ECEVRQDPRS PSRFLVFFYP 60
EDVRQKVLER KNHELVWQGK GTFKLTVQLP ATPDEIDHVF EEELLTKESK TKEDVKEPDV 120
SEELDTKLPL DGGLDKMEDI PEECENISSL VAFENLKANV TDIMLILLVE NISGLSNDDF 180
QVEIIRDFDV AVVTFQKHID TIRFVDDCTK HHSIKQLQLS PRLLEVTNTI RVENLPPGAD 240
DYSLKLFFEN PYNGGGRVAN VEYFPEESSA LIEFFDRKVL DTIMATKLDF NKMPLSVFPY 300
YASLGTALYG KEKPLIKLPA PFEESLDLPL WKFLQKKNHL IEEINDEMRR CHCELTWSQL 360
SGKVTIRPAA TLVNEGRPRI KTWQADTSTT LSSIRSKYKV NPIKVDPTMW DTIKNDVKDD 420
RILIEFDTLK EMVILAGKSE DVQSIEVQVR ELIESTTQKI KREEQSLKEK MIISPGRYFL 480
LCHSSLLDHL LTECPEIEIC YDRVTQHLCL KGPSADVYKA KCEIQEKVYT MAQKNIQVSP 540
EIFQFLQQVN WKEFSKCLFI AQKILALYEL EGTTVLLTSC SSEALLEAEK QMLSALNYKR 600
IEVENKEVLH GKKWKGLTHN LLKKQNSSPN TVIINELTSE TTAEVIITGC VKEVNETYKL 660
LFNFVEQNMK IERLVEVKPS LVIDYLKTEK KLFWPKIKKV NVQVSFNPEN KQKGILLTGS 720
KTEVLKAVDI VKQVWDSVCV KSVHTDKPGA KQFFQDKARF YQSEIKRLFG CYIELQENEV 780
MKEGGSPAGQ KCFSRTVLAP GVVLIVQQGD LARLPVDVVV NASNEDLKHY GGLAAALSKA 840
AGPELQADCD QIVKREGRLL PGNATISKAG KLPYHHVIHA VGPRWSGYEA PRCVYLLRRA 900
VQLSLCLAEK YKYRSIAIPA ISSGVFGFPL GRCVETIVSA IKENFQFKKD GHCLKEIYLV 960
DVSEKTVEAF AEAVKTVFKA TLPDTAAPPG LPPAAAGPGK TSWEKGSLVS PGGLQMLLVK 1020
EGVQNAKTDV VVNSVPLDLV LSRGPLSKSL LEKAGPELQE ELDTVGQGVA VSMGTVLKTS 1080
SWNLDCRYVL HVVAPEWRNG STSSLKIMED IIRECMEITE SLSLKSIAFP AIGTGNLGFP 1140
KNIFAELIIS EVFKFSSKNQ LKTLQEVHFL LHPSDHENIQ AFSDEFARRA NGNLVSDKIP 1200
KAKDTQGFYG TVSSPDSGVY EMKIGSIIFQ VASGDITKEE ADVIVNSTSN SFNLKAGVSK 1260
AILECAGQNV ERECSQQAQQ RKNDYIITGG GFLRCKNIIH VIGGNDVKSS VSSVLQECEK 1320
KNYSSICLPA IGTGNAKQHP DKVAEAIIDA IEDFVQKGSA QSVKKVKVVI FLPQVLDVFY 1380
ANMKKREGTQ LSSQQSVMSK LASFLGFSKQ SPQKKNHLVL EKKTESATFR VCGENVTCVE 1440
YAISWLQDLI EKEQCPYTSE DECIKDFDEK EYQELNELQK KLNINISLDH KRPLIKVLGI 1500
SRDVMQARDE IEAMIKRVRL AKEQESRADC ISEFIEWQYN DNNTSHCFNK MTNLKLEDAR 1560
REKKKTVDVK INHRHYTVNL NTYTATDTKG HSLSVQRLTK SKVDIPAHWS DMKQQNFCVV 1620
ELLPSDPEYN TVASKFNQTC SHFRIEKIER IQNPDLWNSY QAKKKTMDAK NGQTMNEKQL 1680
FHGTDAGSVP HVNRNGFNRS YAGKNAVAYG KGTYFAVNAN YSANDTYSRP DANGRKHVYY 1740
VRVLTGIYTH GNHSLIVPPS KNPQNPTDLY DTVTDNVHHP SLFVAFYDYQ AYPEYLITFR 1800
K 1801 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:EC.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR002589; A1pp.
 IPR012317; Poly(ADP-ribose)pol_cat_dom.
 IPR004170; WWE-dom. 
Pfam
 PF01661; Macro
 PF00644; PARP
 PF02825; WWE 
SMART
 SM00506; A1pp 
PROSITE
 PS51154; MACRO
 PS51059; PARP_CATALYTIC
 PS50918; WWE 
PRINTS