CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015343
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase TRAF7 
Protein Synonyms/Alias
 RING finger and WD repeat-containing protein 1; RING finger protein 119; TNF receptor-associated factor 7 
Gene Name
 TRAF7 
Gene Synonyms/Alias
 RFWD1; RNF119 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
199CRVAGSGKPPIFEVDubiquitination[1, 2, 3, 4, 5, 6]
252MNLEAHLKECEHIKCubiquitination[3, 6]
288TCRFEGLKEFLQQTDubiquitination[2, 7]
321FLRSMLGKLSEKIDQubiquitination[3, 6]
331EKIDQLEKSLELKFDubiquitination[1, 2, 5]
346VLDENQSKLSEDLMEubiquitination[2, 4]
387YDPQQIFKCKGTFVGubiquitination[3, 6]
430WDTCTTYKCQKTLEGubiquitination[3]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [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] 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]
 [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
 E3 ubiquitin ligase capable of auto-ubiquitination, following phosphorylation by MAP3K3. Potentiates MEKK3-mediated activation of the NF-kappa-B, JUN/AP1 and DDIT3 transcriptional regulators. Induces apoptosis when overexpressed. 
Sequence Annotation
 REPEAT 394 433 WD 1.
 REPEAT 437 474 WD 2.
 REPEAT 477 513 WD 3.
 REPEAT 515 554 WD 4.
 REPEAT 557 594 WD 5.
 REPEAT 597 638 WD 6.
 REPEAT 641 669 WD 7.
 ZN_FING 131 165 RING-type.
 ZN_FING 222 276 TRAF-type.
 MOD_RES 88 88 Phosphoserine.
 MOD_RES 91 91 Phosphoserine.  
Keyword
 Alternative splicing; Apoptosis; Complete proteome; Cytoplasmic vesicle; Ligase; Metal-binding; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation; Ubl conjugation; Ubl conjugation pathway; WD repeat; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 670 AA 
Protein Sequence
MSSGKSARYN RFSGGPSNLP TPDVTTGTRM ETTFGPAFSA VTTITKADGT STYKQHCRTP 60
SSSSTLAYSP RDEEDSMPPI STPRRSDSAI SVRSLHSESS MSLRSTFSLP EEEEEPEPLV 120
FAEQPSVKLC CQLCCSVFKD PVITTCGHTF CRRCALKSEK CPVDNVKLTV VVNNIAVAEQ 180
IGELFIHCRH GCRVAGSGKP PIFEVDPRGC PFTIKLSARK DHEGSCDYRP VRCPNNPSCP 240
PLLRMNLEAH LKECEHIKCP HSKYGCTFIG NQDTYETHLE TCRFEGLKEF LQQTDDRFHE 300
MHVALAQKDQ EIAFLRSMLG KLSEKIDQLE KSLELKFDVL DENQSKLSED LMEFRRDASM 360
LNDELSHINA RLNMGILGSY DPQQIFKCKG TFVGHQGPVW CLCVYSMGDL LFSGSSDKTI 420
KVWDTCTTYK CQKTLEGHDG IVLALCIQGC KLYSGSADCT IIVWDIQNLQ KVNTIRAHDN 480
PVCTLVSSHN VLFSGSLKAI KVWDIVGTEL KLKKELTGLN HWVRALVAAQ SYLYSGSYQT 540
IKIWDIRTLD CIHVLQTSGG SVYSIAVTNH HIVCGTYENL IHVWDIESKE QVRTLTGHVG 600
TVYALAVIST PDQTKVFSAS YDRSLRVWSM DNMICTQTLL RHQGSVTALA VSRGRLFSGA 660
VDSTVKVWTC 670 
Gene Ontology
 GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
 GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; NAS:UniProtKB.
 GO:0000185; P:activation of MAPKKK activity; IDA:UniProtKB.
 GO:0097194; P:execution phase of apoptosis; IMP:UniProtKB.
 GO:0043410; P:positive regulation of MAPK cascade; IDA:MGI.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR020472; G-protein_beta_WD-40_rep.
 IPR013323; SIAH-type.
 IPR008974; TRAF-like.
 IPR015943; WD40/YVTN_repeat-like_dom.
 IPR001680; WD40_repeat.
 IPR019775; WD40_repeat_CS.
 IPR017986; WD40_repeat_dom.
 IPR018957; Znf_C3HC4_RING-type.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS.
 IPR001293; Znf_TRAF. 
Pfam
 PF00400; WD40
 PF00097; zf-C3HC4 
SMART
 SM00184; RING
 SM00320; WD40 
PROSITE
 PS00678; WD_REPEATS_1
 PS50082; WD_REPEATS_2
 PS50294; WD_REPEATS_REGION
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2
 PS50145; ZF_TRAF 
PRINTS
 PR00320; GPROTEINBRPT.