CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-039985
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 E3 ubiquitin-protein ligase 
Protein Synonyms/Alias
  
Gene Name
 NEDD4L 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
8MERPYTFKDFLLRPRubiquitination[1]
321SAPLEGAKDSPVRRAubiquitination[2, 3]
330SPVRRAVKDTLSNPQubiquitination[1, 2, 3]
348PSPYNSPKPQHKVTQubiquitination[3]
352NSPKPQHKVTQSFLPubiquitination[3]
380FFIDHNTKTTTWEDPubiquitination[1, 3, 4]
390TWEDPRLKFPVHMRSubiquitination[1, 3]
398FPVHMRSKTSLNPNDubiquitination[2, 3]
431FYIDHNSKITQWEDPubiquitination[3]
516WIEFESEKGLDYGGVubiquitination[2, 3, 4]
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] 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] 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
  
Sequence Annotation
  
Keyword
 Complete proteome; Ligase; Reference proteome; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 835 AA 
Protein Sequence
MERPYTFKDF LLRPRSHKSR VKGFLRLKMA YMPKNGGQDE ENSDQRDDME HGWEVVDSND 60
SASQHQEELP PPPLPPGWEE KVDNLGRTYY VNHNNRTTQW HRPSLMDVSS ESDNNIRQIN 120
QEAAHRRFRS RRHISEDLEP EPSEGGDVPE PWETISEEVN IAGDSLGLAL PPPPASPGSR 180
TSPQELSEEL SRRLQITPDS NGEQFSSLIQ REPSSRLRSC SVTDAVAEQG HLPPPSVAYV 240
HTTPGLPSGW EERKDAKGRT YYVNHNNRTT TWTRPIMQLA EDGASGSATN SNNHLIEPQI 300
RRPRSLSSPT VTLSAPLEGA KDSPVRRAVK DTLSNPQSPQ PSPYNSPKPQ HKVTQSFLPP 360
GWEMRIAPNG RPFFIDHNTK TTTWEDPRLK FPVHMRSKTS LNPNDLGPLP PGWEERIHLD 420
GRTFYIDHNS KITQWEDPRL QNPAITGPKA VPYSREFKQK YDYFRKKLKK PADIPNRFEM 480
KLHRNNIFEE SYRRIMSVKR PDVLKARLWI EFESEKGLDY GGVAREWFFL LSKEMFNPYY 540
GLFEYSATDN YTLQINPNSG LCNEDHLSYF TFIGRVAGLA VFHGKLLDGF FIRPFYKMML 600
GKQITLNDME SVDSEYYNSL KWILENDPTE LDLMFCIDEE NFGQTYQVDL KPNGSEIMVT 660
NENKREYIDL VIQWRFVNRV QKQMNAFLEG FTELLPIDLI KIFDENELEL LMCGLGDVDV 720
NDWRQHSIYK NGYCPNHPVI QWFWKAVLLM DAEKRIRLLQ FVTGTSRVPM NGFAELYGSN 780
GPQLFTIEQW GSPEKLPRAH TCFNRLDLPP YETFEDLREK LLMAVENAQG FEGVD 835 
Gene Ontology
 GO:0005622; C:intracellular; IEA:InterPro.
 GO:0004842; F:ubiquitin-protein ligase activity; IEA:InterPro. 
Interpro
 IPR024928; E3_ub_ligase_SMURF1.
 IPR000569; HECT.
 IPR001202; WW_dom. 
Pfam
 PF00632; HECT
 PF00397; WW 
SMART
 SM00119; HECTc
 SM00456; WW 
PROSITE
 PS50237; HECT
 PS01159; WW_DOMAIN_1
 PS50020; WW_DOMAIN_2 
PRINTS