CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018342
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Negative elongation factor B 
Protein Synonyms/Alias
 NELF-B; Cofactor of BRCA1 
Gene Name
 NELFB 
Gene Synonyms/Alias
 COBRA1; KIAA1182 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
85SAIASEGKAEERYKKubiquitination[1, 2, 3]
99KLEDLLEKSFSLVKMubiquitination[4, 5]
135LKLVMADKELYRACAubiquitination[2, 4, 5]
146RACAVEVKRQIWQDNubiquitination[2]
166DEVSPLLKQYILEKEubiquitination[1]
291QGFLDGVKKGQEQVLubiquitination[1]
361MIDSQVFKEPKMEVEubiquitination[1]
398QKLPAEEKAPVSYPNubiquitination[1, 6]
413TLPESFTKFLQEQRMubiquitination[1, 6, 7]
519HPRVAPSKLEALQKAacetylation[3, 8, 9, 10]
519HPRVAPSKLEALQKAubiquitination[1, 2, 3]
525SKLEALQKALEPTGQubiquitination[1]
538GQSGEAVKELYSQLGubiquitination[1]
555LEQLDHRKPSPAQAAubiquitination[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] 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] 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]
 [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]
 [6] 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]
 [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]
 [8] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [9] 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]
 [10] 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
Functional Description
 Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex. May be able to induce chromatin unfolding. 
Sequence Annotation
 MOD_RES 519 519 N6-acetyllysine.
 MOD_RES 557 557 Phosphoserine.  
Keyword
 Acetylation; Complete proteome; Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 580 AA 
Protein Sequence
MFAGLQDLGV ANGEDLKETL TNCTEPLKAI EQFQTENGVL LPSLQSALPF LDLHGTPRLE 60
FHQSVFDELR DKLLERVSAI ASEGKAEERY KKLEDLLEKS FSLVKMPSLQ PVVMCVMKHL 120
PKVPEKKLKL VMADKELYRA CAVEVKRQIW QDNQALFGDE VSPLLKQYIL EKESALFSTE 180
LSVLHNFFSP SPKTRRQGEV VQRLTRMVGK NVKLYDMVLQ FLRTLFLRTR NVHYCTLRAE 240
LLMSLHDLDV GEICTVDPCH KFTWCLDACI RERFVDSKRA RELQGFLDGV KKGQEQVLGD 300
LSMILCDPFA INTLALSTVR HLQELVGQET LPRDSPDLLL LLRLLALGQG AWDMIDSQVF 360
KEPKMEVELI TRFLPMLMSF LVDDYTFNVD QKLPAEEKAP VSYPNTLPES FTKFLQEQRM 420
ACEVGLYYVL HITKQRNKNA LLRLLPGLVE TFGDLAFGDI FLHLLTGNLA LLADEFALED 480
FCSSLFDGFF LTASPRKENV HRHALRLLIH LHPRVAPSKL EALQKALEPT GQSGEAVKEL 540
YSQLGEKLEQ LDHRKPSPAQ AAETPALELP LPSVPAPAPL 580 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:LIFEdb.
 GO:0032021; C:NELF complex; IDA:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IEA:InterPro.
 GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
 GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
 GO:0022415; P:viral reproductive process; TAS:Reactome. 
Interpro
 IPR010405; COBRA1. 
Pfam
 PF06209; COBRA1 
SMART
  
PROSITE
  
PRINTS