CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016219
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 NEDD4-binding protein 2 
Protein Synonyms/Alias
 N4BP2; BCL-3-binding protein 
Gene Name
 N4BP2 
Gene Synonyms/Alias
 B3BP; KIAA1413 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
20FRKTANPKEVVVSSVubiquitination[1, 2, 3, 4]
327PSEGFNFKPHKHPELubiquitination[5]
330GFNFKPHKHPELPTKubiquitination[5, 6]
337KHPELPTKGKDVSYCacetylation[7]
409ISHTSPTKVWRNKDGubiquitination[5]
414PTKVWRNKDGTSAYQubiquitination[2, 5, 8]
453RGLPGSGKSFLARTLubiquitination[5]
507AKEAFEKKISPIIIDubiquitination[5]
524NLQAWEMKPYVALSQubiquitination[5]
532PYVALSQKHKYKVLFubiquitination[5]
534VALSQKHKYKVLFREubiquitination[5]
551TWWKFKPKELARRNIubiquitination[5]
590MSSSVPEKIERIELCubiquitination[5]
642EKNLDVTKETMLPENubiquitination[2]
660LSNADLNKRRKEISDubiquitination[5]
876DAYKNIDKNSFNIMGubiquitination[5]
1030ALLWKIEKNKISISDubiquitination[5]
1032LWKIEKNKISISDSIubiquitination[5]
1040ISISDSIKVLTGRLDubiquitination[5]
1050TGRLDGFKPKVFNINubiquitination[5]
1052RLDGFKPKVFNINTKubiquitination[5]
1059KVFNINTKSDVQEAIubiquitination[5]
1074PYRVMYDKSTFVEESubiquitination[5]
1229PSAAVGLKNNNDILPubiquitination[5]
1247EELLYSSKQSFPGILubiquitination[2, 5]
1260ILKATTPKDMSETEKubiquitination[5]
1339NEDEKEMKEILMAGSubiquitination[2]
1422LAKVIHEKWKESVMEubiquitination[5]
1424KVIHEKWKESVMERQubiquitination[5]
1440QEEVSCGKFMQDPSLubiquitination[2, 5]
1459GLDNPEQKSSQRTGKubiquitination[2, 5]
1470RTGKKLLKTLTASEMubiquitination[5]
1490HWNTQTKKVSLREIMubiquitination[5]
1506EEIALQEKHNLKRETubiquitination[5]
1510LQEKHNLKRETLMFEubiquitination[5]
1518RETLMFEKDCATKLKubiquitination[5]
1527CATKLKEKQLFKIFPubiquitination[5]
1649EAYRIGKKNVATFYAubiquitination[5]
1665QGTLHEQKMKEANHLubiquitination[5]
1667TLHEQKMKEANHLAAubiquitination[5]
1717EKKTEEFKQNGGKPYubiquitination[5]
1722EFKQNGGKPYLSVITubiquitination[5]
1761SFRFSEIKPGCLKVMubiquitination[5]
1766EIKPGCLKVMLK***ubiquitination[5]
Reference
 [1] 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]
 [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] 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]
 [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] 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]
 [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]
 [7] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [8] 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
 Has 5'-polynucleotide kinase and nicking endonuclease activity. May play a role in DNA repair or recombination. 
Sequence Annotation
 DOMAIN 46 89 CUE.
 DOMAIN 1691 1770 Smr.
 NP_BIND 447 454 ATP (Potential).  
Keyword
 3D-structure; Alternative splicing; ATP-binding; Coiled coil; Complete proteome; Cytoplasm; Hydrolase; Nucleotide-binding; Polymorphism; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1770 AA 
Protein Sequence
MPRRRKNLGG NPFRKTANPK EVVVSSVASR EEPTTTLPSM GETKVDQEEL FTSISEIFSD 60
LDPDVVYLML SECDFKVENA MDCLLELSAT DTKIEESSSQ SFVASENQVG AAESKIMEKR 120
PEEESEDSKM DSFLDMQLTE DLDSLIQNAF EKLNSSPDDQ VYSFLPSQDV NSFNDSSEFI 180
NPDSSNMTPI FSTQNMNLNG ENLENSGSTL SLNPLPSHSV LNESKCFIKD NTLALESNYP 240
EDSLLSSSLN VASDSIAGCS SLNQKQKELL ESECVEAQFS EAPVDLDASE PQACLNLPGL 300
DLPGTGGDQK STRVSDVFLP SEGFNFKPHK HPELPTKGKD VSYCPVLAPL PLLLPPPPPP 360
PMWNPMIPAF DLFQGNHGFV APVVTTAAHW RSVNYTFPPS VISHTSPTKV WRNKDGTSAY 420
QVQETPVSQV VRKKTSYVGL VLVLLRGLPG SGKSFLARTL QEDNPSGVIL STDDYFYING 480
QYQFDVKYLG EAHEWNQNRA KEAFEKKISP IIIDNTNLQA WEMKPYVALS QKHKYKVLFR 540
EPDTWWKFKP KELARRNIHG VSKEKITRML EHYQRFVSVP IIMSSSVPEK IERIELCAYS 600
CEDRSTSPRD DEDIISEKEE NILSLSLKHL EFTEEKNLDV TKETMLPENV AYLSNADLNK 660
RRKEISDMNP SIQSALILET PHMYFSDSES KLQATDKSEN EQIEMVAVKG YSKTDTDSSM 720
ERVSPSTCCS ENNQEDCDLA NSGPLQNEKS SPGEIVEERA TVTKKAFGKQ KSKSTLEKFP 780
RHELSNFVGD WPVDKTIGQR TKRNRKTEKT SSVQSDKKYN YPQSHKLVNS VSVNTDCVQQ 840
RGSPHESVED GRKSQCDDAS EPLNSYKYDA YKNIDKNSFN IMGDWPSSDS LAQREHRSRM 900
PKTGLSEPNL EIGTNDKMNE ISLSTAHEAC WGTSSQKLKT LGSSNLGSSE MLLSEMTCES 960
QTCLSKKSHG QHTSLPLTFT NSAPTVSGVV EPQTLAECQE QMPKRDPGKE VGMCTQTEPQ 1020
DFALLWKIEK NKISISDSIK VLTGRLDGFK PKVFNINTKS DVQEAIPYRV MYDKSTFVEE 1080
SELTSADESE NLNILCKLFG SFSLEALKDL YERCNKDIIW ATSLLLDSET KLCEDTEFEN 1140
FQKSCDGSQI GPFSLGLNLK EIISQRGTLE NSNSPVPEFS HGIGISNADS QSTCDAERGN 1200
SEQAEMRAVT PENHESMTSI FPSAAVGLKN NNDILPNSQE ELLYSSKQSF PGILKATTPK 1260
DMSETEKNLV VTETGDNIHS PSHFSDIFNF VSSTSNLELN EEIYFTDSLE IKRNENFPKD 1320
YVKFSDEEEF MNEDEKEMKE ILMAGSSLSA GVSGEDKTEI LNPTPAMAKS LTIDCLELAL 1380
PPELAFQLNE LFGPVGIDSG SLTVEDCVVH IDLNLAKVIH EKWKESVMER QRQEEVSCGK 1440
FMQDPSLVGH TGLDNPEQKS SQRTGKKLLK TLTASEMLPL LDHWNTQTKK VSLREIMSEE 1500
IALQEKHNLK RETLMFEKDC ATKLKEKQLF KIFPAINQNF LVDIFKDHNY SLEHTVQFLN 1560
CVLEGDPVKT VVAQEFVHQN ENVTSHTGQK SKEKKPKKLK ETEETPSELS FQDFEYPDYD 1620
DYRAEAFLHQ QKRMECYSKA KEAYRIGKKN VATFYAQQGT LHEQKMKEAN HLAAIEIFEK 1680
VNASLLPQNV LDLHGLHVDE ALEHLMRVLE KKTEEFKQNG GKPYLSVITG RGNHSQGGVA 1740
RIKPAVIKYL ISHSFRFSEI KPGCLKVMLK 1770 
Gene Ontology
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005524; F:ATP binding; IDA:MGI.
 GO:0046404; F:ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity; IDA:MGI.
 GO:0004519; F:endonuclease activity; IDA:MGI. 
Interpro
 IPR003892; CUE.
 IPR013899; DUF1771.
 IPR027417; P-loop_NTPase.
 IPR002625; Smr/MutS2_C.
 IPR009060; UBA-like. 
Pfam
 PF08590; DUF1771
 PF01713; Smr 
SMART
  
PROSITE
 PS51140; CUE
 PS50828; SMR 
PRINTS