CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001535
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongator complex protein 1 
Protein Synonyms/Alias
 ELP1; IkappaB kinase complex-associated protein; IKK complex-associated protein; p150 
Gene Name
 IKBKAP 
Gene Synonyms/Alias
 ELP1; IKAP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
157QDDFGESKFITVGWGubiquitination[1]
247LGPALAWKPSGSLIAubiquitination[1]
464PSADPTVKLGAVGGSubiquitination[2, 3]
474AVGGSGFKVCLRTPHubiquitination[3]
591ESPSLAIKPWKNSGGubiquitination[3]
671CLRDASFKTLQAGLSubiquitination[1]
706TVVPQDTKLVLQMPRubiquitination[1, 3]
735QIRKWLDKLMFKEAFubiquitination[3, 4, 5]
815SRDPDGNKIDLVCDAubiquitination[3]
834MESINPHKYCLSILTubiquitination[3]
846ILTSHVKKTTPELEIubiquitination[3]
925LPFLNTLKKMETNYQubiquitination[3]
938YQRFTIDKYLKRYEKubiquitination[3]
952KAIGHLSKCGPEYFPubiquitination[3]
968CLNLIKDKNLYNEALubiquitination[3]
1055LGRTLAGKLVEQRKHubiquitination[3]
1098EALRLVYKYNRLDIIubiquitination[3]
1319AELFIPPKINRRTQWubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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] 
Functional Description
 May act as a scaffold protein that may assemble active IKK-MAP3K14 complexes (IKKA, IKKB and MAP3K14/NIK). 
Sequence Annotation
 MOD_RES 867 867 Phosphoserine.
 MOD_RES 1171 1171 Phosphoserine.
 MOD_RES 1174 1174 Phosphoserine.  
Keyword
 Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; Neuropathy; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1332 AA 
Protein Sequence
MRNLKLFRTL EFRDIQGPGN PQCFSLRTEQ GTVLIGSEHG LIEVDPVSRE VKNEVSLVAE 60
GFLPEDGSGR IVGVQDLLDQ ESVCVATASG DVILCSLSTQ QLECVGSVAS GISVMSWSPD 120
QELVLLATGQ QTLIMMTKDF EPILEQQIHQ DDFGESKFIT VGWGRKETQF HGSEGRQAAF 180
QMQMHESALP WDDHRPQVTW RGDGQFFAVS VVCPETGARK VRVWNREFAL QSTSEPVAGL 240
GPALAWKPSG SLIASTQDKP NQQDIVFFEK NGLLHGHFTL PFLKDEVKVN DLLWNADSSV 300
LAVWLEDLQR EESSIPKTCV QLWTVGNYHW YLKQSLSFST CGKSKIVSLM WDPVTPYRLH 360
VLCQGWHYLA YDWHWTTDRS VGDNSSDLSN VAVIDGNRVL VTVFRQTVVP PPMCTYQLLF 420
PHPVNQVTFL AHPQKSNDLA VLDASNQISV YKCGDCPSAD PTVKLGAVGG SGFKVCLRTP 480
HLEKRYKIQF ENNEDQDVNP LKLGLLTWIE EDVFLAVSHS EFSPRSVIHH LTAASSEMDE 540
EHGQLNVSSS AAVDGVIISL CCNSKTKSVV LQLADGQIFK YLWESPSLAI KPWKNSGGFP 600
VRFPYPCTQT ELAMIGEEEC VLGLTDRCRF FINDIEVASN ITSFAVYDEF LLLTTHSHTC 660
QCFCLRDASF KTLQAGLSSN HVSHGEVLRK VERGSRIVTV VPQDTKLVLQ MPRGNLEVVH 720
HRALVLAQIR KWLDKLMFKE AFECMRKLRI NLNLIYDHNP KVFLGNVETF IKQIDSVNHI 780
NLFFTELKEE DVTKTMYPAP VTSSVYLSRD PDGNKIDLVC DAMRAVMESI NPHKYCLSIL 840
TSHVKKTTPE LEIVLQKVHE LQGNAPSDPD AVSAEEALKY LLHLVDVNEL YDHSLGTYDF 900
DLVLMVAEKS QKDPKEYLPF LNTLKKMETN YQRFTIDKYL KRYEKAIGHL SKCGPEYFPE 960
CLNLIKDKNL YNEALKLYSP SSQQYQDISI AYGEHLMQEH MYEPAGLMFA RCGAHEKALS 1020
AFLTCGNWKQ ALCVAAQLNF TKDQLVGLGR TLAGKLVEQR KHIDAAMVLE ECAQDYEEAV 1080
LLLLEGAAWE EALRLVYKYN RLDIIETNVK PSILEAQKNY MAFLDSQTAT FSRHKKRLLV 1140
VRELKEQAQQ AGLDDEVPHG QESDLFSETS SVVSGSEMSG KYSHSNSRIS ARSSKNRRKA 1200
ERKKHSLKEG SPLEDLALLE ALSEVVQNTE NLKDEVYHIL KVLFLFEFDE QGRELQKAFE 1260
DTLQLMERSL PEIWTLTYQQ NSATPVLGPN STANSIMASY QQQKTSVPVL DAELFIPPKI 1320
NRRTQWKLSL LD 1332 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0016591; C:DNA-directed RNA polymerase II, holoenzyme; IDA:HGNC.
 GO:0033588; C:Elongator holoenzyme complex; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:HGNC.
 GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB.
 GO:0008607; F:phosphorylase kinase regulator activity; IDA:UniProtKB.
 GO:0004871; F:signal transducer activity; TAS:ProtInc.
 GO:0006955; P:immune response; TAS:ProtInc.
 GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
 GO:0006461; P:protein complex assembly; TAS:ProtInc.
 GO:0006468; P:protein phosphorylation; TAS:ProtInc.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:HGNC. 
Interpro
 IPR011042; 6-blade_b-propeller_TolB-like.
 IPR006849; IKI3. 
Pfam
 PF04762; IKI3 
SMART
  
PROSITE
  
PRINTS