CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012448
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pre-mRNA-splicing regulator WTAP 
Protein Synonyms/Alias
 Female-lethal(2)D homolog; hFL(2)D; WT1-associated protein; Wilms tumor 1-associating protein 
Gene Name
 WTAP 
Gene Synonyms/Alias
 KIAA0105 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
9TNEEPLPKKVRLSETubiquitination[1, 2]
10NEEPLPKKVRLSETDubiquitination[2]
19RLSETDFKVMARDELubiquitination[2, 3, 4, 5]
31DELILRWKQYEAYVQubiquitination[2, 6]
43YVQALEGKYTDLNSNubiquitination[2, 6]
61GLRESEEKLKQQQQEubiquitination[2]
63RESEEKLKQQQQESAubiquitination[6]
83LVMRLATKEQEMQECubiquitination[2, 5]
98TTQIQYLKQVQQPSVubiquitination[2, 5, 7]
123AINLFFLKMKGELEQubiquitination[2, 3, 4]
125NLFFLKMKGELEQTKubiquitination[2, 5, 6]
134ELEQTKDKLEQAQNEubiquitination[6]
146QNELSAWKFTPDSQTubiquitination[6]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [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]
 [6] 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]
 [7] 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
Functional Description
 Regulates G2/M cell-cycle transition by binding to the 3' UTR of CCNA2, which enhances its stability. Impairs WT1 DNA- binding ability and inhibits expression of WT1 target genes. May be involved in mRNA splicing regulation. 
Sequence Annotation
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 305 305 Phosphoserine.
 MOD_RES 306 306 Phosphoserine.
 MOD_RES 388 388 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Cell cycle; Complete proteome; Direct protein sequencing; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 396 AA 
Protein Sequence
MTNEEPLPKK VRLSETDFKV MARDELILRW KQYEAYVQAL EGKYTDLNSN DVTGLRESEE 60
KLKQQQQESA RRENILVMRL ATKEQEMQEC TTQIQYLKQV QQPSVAQLRS TMVDPAINLF 120
FLKMKGELEQ TKDKLEQAQN ELSAWKFTPD SQTGKKLMAK CRMLIQENQE LGRQLSQGRI 180
AQLEAELALQ KKYSEELKSS QDELNDFIIQ LDEEVEGMQS TILVLQQQLK ETRQQLAQYQ 240
QQQSQASAPS TSRTTASEPV EQSEATSKDC SRLTNGPSNG SSSRQRTSGS GFHREGNTTE 300
DDFPSSPGNG NKSSNSSEER TGRGGSGYVN QLSAGYESVD SPTGSENSLT HQSNDTDSSH 360
DPQEEKAVSG KGNRTVGSRH VQNGLDSSVN VQGSVL 396 
Gene Ontology
 GO:0031965; C:nuclear membrane; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; IEA:Compara.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. 
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