CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014929
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongator complex protein 2 
Protein Synonyms/Alias
 ELP2; SHINC-2; STAT3-interacting protein 1; StIP1 
Gene Name
 ELP2 
Gene Synonyms/Alias
 STATIP1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
241RIWKLYIKSTSLETQubiquitination[1, 2, 3, 4]
256DDDNIRLKENTFTIEacetylation[5]
256DDDNIRLKENTFTIEubiquitination[1, 3, 4, 6]
314LLSASMDKTMILWAPubiquitination[1]
419TRLFAPWKRKDQSQVubiquitination[6, 7]
421LFAPWKRKDQSQVTWubiquitination[4, 6]
442QIHGYDLKCLAMINRubiquitination[4, 6]
459FVSGADEKVLRVFSAubiquitination[1, 3, 4, 6, 7, 8, 9, 10]
507PALGLSNKAVFQGDIubiquitination[6]
579CVTCNSSKTLLASACubiquitination[6]
587TLLASACKAAKKEHAubiquitination[2]
590ASACKAAKKEHAAIIubiquitination[6]
682CDWSPDSKYFFTGSRubiquitination[2, 6]
788AIRKLCWKNCSGKTEubiquitination[6]
797CSGKTEQKEAEGAEWubiquitination[6]
823VKIHRVNKCAL****ubiquitination[6]
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] 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]
 [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] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [6] 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]
 [7] 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]
 [8] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [9] 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]
 [10] 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
 Regulates the ligand-dependent activation of STAT3 (By similarity). 
Sequence Annotation
 REPEAT 13 53 WD 1.
 REPEAT 56 100 WD 2.
 REPEAT 105 152 WD 3.
 REPEAT 158 200 WD 4.
 REPEAT 205 246 WD 5.
 REPEAT 281 329 WD 6.
 REPEAT 339 378 WD 7.
 REPEAT 386 425 WD 8.
 REPEAT 436 474 WD 9.
 REPEAT 565 609 WD 10.
 REPEAT 612 651 WD 11.
 REPEAT 667 706 WD 12.
 REPEAT 712 753 WD 13.
 REPEAT 777 826 WD 14.  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Nucleus; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; WD repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 826 AA 
Protein Sequence
MVAPVLETSH VFCCPNRVRG VLNWSSGPRG LLAFGTSCSV VLYDPLKRVV VTNLNGHTAR 60
VNCIQWICKQ DGSPSTELVS GGSDNQVIHW EIEDNQLLKA VHLQGHEGPV YAVHAVYQRR 120
TSDPALCTLI VSAAADSAVR LWSKKGPEVM CLQTLNFGNG FALALCLSFL PNTDVPILAC 180
GNDDCRIHIF AQQNDQFQKV LSLCGHEDWI RGVEWAAFGR DLFLASCSQD CLIRIWKLYI 240
KSTSLETQDD DNIRLKENTF TIENESVKIA FAVTLETVLA GHENWVNAVH WQPVFYKDGV 300
LQQPVRLLSA SMDKTMILWA PDEESGVWLE QVRVGEVGGN TLGFYDCQFN EDGSMIIAHA 360
FHGALHLWKQ NTVNPREWTP EIVISGHFDG VQDLVWDPEG EFIITVGTDQ TTRLFAPWKR 420
KDQSQVTWHE IARPQIHGYD LKCLAMINRF QFVSGADEKV LRVFSAPRNF VENFCAITGQ 480
SLNHVLCNQD SDLPEGATVP ALGLSNKAVF QGDIASQPSD EEELLTSTGF EYQQVAFQPS 540
ILTEPPTEDH LLQNTLWPEV QKLYGHGYEI FCVTCNSSKT LLASACKAAK KEHAAIILWN 600
TTSWKQVQNL VFHSLTVTQM AFSPNEKFLL AVSRDRTWSL WKKQDTISPE FEPVFSLFAF 660
TNKITSVHSR IIWSCDWSPD SKYFFTGSRD KKVVVWGECD STDDCIEHNI GPCSSVLDVG 720
GAVTAVSVCP VLHPSQRYVV AVGLECGKIC LYTWKKTDQV PEINDWTHCV ETSQSQSHTL 780
AIRKLCWKNC SGKTEQKEAE GAEWLHFASC GEDHTVKIHR VNKCAL 826 
Gene Ontology
 GO:0005737; C:cytoplasm; NAS:HGNC.
 GO:0016591; C:DNA-directed RNA polymerase II, holoenzyme; IC:HGNC.
 GO:0033588; C:Elongator holoenzyme complex; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IC:HGNC.
 GO:0008023; C:transcription elongation factor complex; IDA:HGNC.
 GO:0046425; P:regulation of JAK-STAT cascade; IEA:Compara.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:HGNC.
 GO:0006368; P:transcription elongation from RNA polymerase II promoter; IC:HGNC. 
Interpro
 IPR015943; WD40/YVTN_repeat-like_dom.
 IPR001680; WD40_repeat.
 IPR017986; WD40_repeat_dom. 
Pfam
 PF00400; WD40 
SMART
 SM00320; WD40 
PROSITE
 PS00678; WD_REPEATS_1
 PS50082; WD_REPEATS_2
 PS50294; WD_REPEATS_REGION 
PRINTS