CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020214
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 TNF receptor-associated factor 4 
Protein Synonyms/Alias
 Cysteine-rich domain associated with RING and Traf domains protein 1; Metastatic lymph node gene 62 protein; MLN 62; RING finger protein 83 
Gene Name
 TRAF4 
Gene Synonyms/Alias
 CART1; MLN62; RNF83 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
11FDYKFLEKPKRRLLCubiquitination[1]
170ESVYCENKCGARMMRubiquitination[1, 2, 3]
200QPCTYCTKEFVFDTIubiquitination[1]
415FHPDPNWKNFQKPGTubiquitination[4, 5]
419PNWKNFQKPGTWRGSubiquitination[1]
438SLGFGYPKFISHQDIubiquitination[1]
Reference
 [1] 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]
 [2] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [3] 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]
 [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
 Adapter protein and signal transducer that links members of the tumor necrosis factor receptor (TNFR) family to different signaling pathways. Plays a role in the activation of NF-kappa-B and JNK, and in the regulation of cell survival and apoptosis. Regulates activation of NF-kappa-B in response to signaling through Toll-like receptors. Required for normal skeleton development, and for normal development of the respiratory tract (By similarity). Required for activation of RPS6KB1 in response to TNF signaling. Modulates TRAF6 functions. 
Sequence Annotation
 DOMAIN 307 462 MATH.
 ZN_FING 18 58 RING-type.
 ZN_FING 102 154 TRAF-type 1.
 ZN_FING 155 208 TRAF-type 2.
 ZN_FING 209 266 TRAF-type 3.
 MOD_RES 426 426 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Apoptosis; Cell junction; Cell membrane; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein; Membrane; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Tight junction; Ubl conjugation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 470 AA 
Protein Sequence
MPGFDYKFLE KPKRRLLCPL CGKPMREPVQ VSTCGHRFCD TCLQEFLSEG VFKCPEDQLP 60
LDYAKIYPDP ELEVQVLGLP IRCIHSEEGC RWSGPLRHLQ GHLNTCSFNV IPCPNRCPMK 120
LSRRDLPAHL QHDCPKRRLK CEFCGCDFSG EAYESHEGMC PQESVYCENK CGARMMRRLL 180
AQHATSECPK RTQPCTYCTK EFVFDTIQSH QYQCPRLPVA CPNQCGVGTV AREDLPGHLK 240
DSCNTALVLC PFKDSGCKHR CPKLAMARHV EESVKPHLAM MCALVSRQRQ ELQELRRELE 300
ELSVGSDGVL IWKIGSYGRR LQEAKAKPNL ECFSPAFYTH KYGYKLQVSA FLNGNGSGEG 360
THLSLYIRVL PGAFDNLLEW PFARRVTFSL LDQSDPGLAK PQHVTETFHP DPNWKNFQKP 420
GTWRGSLDES SLGFGYPKFI SHQDIRKRNY VRDDAVFIRA AVELPRKILS 470 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; TAS:ProtInc.
 GO:0004842; F:ubiquitin-protein ligase activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IEA:InterPro.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0046330; P:positive regulation of JNK cascade; IDA:UniProtKB.
 GO:0090073; P:positive regulation of protein homodimerization activity; IDA:UniProtKB.
 GO:0045860; P:positive regulation of protein kinase activity; IDA:UniProtKB.
 GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
 GO:0007585; P:respiratory gaseous exchange; IEA:Compara.
 GO:0030323; P:respiratory tube development; IEA:Compara.
 GO:0007165; P:signal transduction; TAS:ProtInc. 
Interpro
 IPR002083; MATH.
 IPR013323; SIAH-type.
 IPR012227; TNF_rcpt--assoc_TRAF.
 IPR008974; TRAF-like.
 IPR027138; TRAF4.
 IPR018957; Znf_C3HC4_RING-type.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS.
 IPR001293; Znf_TRAF. 
Pfam
 PF00917; MATH
 PF00097; zf-C3HC4 
SMART
 SM00061; MATH
 SM00184; RING 
PROSITE
 PS50144; MATH
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2
 PS50145; ZF_TRAF 
PRINTS