CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012548
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin-protein ligase E3C 
Protein Synonyms/Alias
 HectH2 
Gene Name
 UBE3C 
Gene Synonyms/Alias
 KIAA0010; KIAA10 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
9FSFEGDFKTRPKVSLubiquitination[1, 2]
63IRGYRDRKQQYSIQRubiquitination[3]
130KHSSLFVKQLDGSERubiquitination[1, 2, 4, 5]
145LTCLFQIKRLMSLCCubiquitination[3, 5]
218LYLLINSKLPSSIEYubiquitination[4]
235LSRVPIAKILLENVLubiquitination[1, 2]
243ILLENVLKPLHFTYNubiquitination[1, 2, 3, 6]
398ITEECLKKLDTKQQTubiquitination[3]
402CLKKLDTKQQTNTLLubiquitination[3, 4, 5]
558DACLGIIKLAYPETKubiquitination[1, 2, 3, 5]
565KLAYPETKPEVREEYubiquitination[3, 4, 5]
610KVITNLVKMLKSRDTubiquitination[1, 2, 3, 4]
638QEDIKADKVTQLYVPubiquitination[1, 2, 4]
700VPFEERVKIFQRLIYubiquitination[3]
710QRLIYADKQEVQGDGubiquitination[4, 7]
739IYEDAYDKLSPENEPubiquitination[4, 7]
749PENEPDLKKRIRVHLubiquitination[4]
782EFLNELLKSGFNPNQubiquitination[4, 5, 7]
793NPNQGFFKTTNEGLLubiquitination[4, 5]
907VELKFGGKDIPVTSAubiquitination[4, 7]
1008EGFTDEEKRKLLKFVubiquitination[4, 6]
1013EEKRKLLKFVTSCSRubiquitination[3]
1056STCMNLLKLPEFYDEubiquitination[5]
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] 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]
 [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] 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]
 [5] 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]
 [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] 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
Functional Description
 E3 ubiquitin-protein ligase that accepts ubiquitin from the E2 ubiquitin-conjugating enzyme UBE2D1 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Can assemble unanchored poly-ubiquitin chains in either 'Lys-29'- or 'Lys-48'-linked polyubiquitin chains. Has preference for 'Lys-48' linkages. It can target itself for ubiquitination in vitro and may promote its own degradation in vivo. 
Sequence Annotation
 DOMAIN 45 74 IQ.
 DOMAIN 744 1083 HECT.
 REGION 1 60 Cis-determinant of acceptor ubiquitin-
 ACT_SITE 1051 1051 Glycyl thioester intermediate.  
Keyword
 Alternative splicing; Complete proteome; Direct protein sequencing; Ligase; Nucleus; Proteasome; Reference proteome; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1083 AA 
Protein Sequence
MFSFEGDFKT RPKVSLGGAS RKEEKASLLH RTQEERRKRE EERRRLKNAI IIQSFIRGYR 60
DRKQQYSIQR SAFDRCATLS QSGGAFPIAN GPNLTLLVRQ LLFFYKQNED SKRLIWLYQN 120
LIKHSSLFVK QLDGSERLTC LFQIKRLMSL CCRLLQNCND DSLNVALPMR MLEVFSSENT 180
YLPVLQDASY VVSVIEQILH YMIHNGYYRS LYLLINSKLP SSIEYSDLSR VPIAKILLEN 240
VLKPLHFTYN SCPEGARQQV FTAFTEEFLA APFTDQIFHF IIPALADAQT VFPYEPFLNA 300
LLLIESRCSR KSGGAPWLFY FVLTVGENYL GALSEEGLLV YLRVLQTFLS QLPVSPASAS 360
CHDSASDSEE ESEEADKPSS PEDGRLSVSY ITEECLKKLD TKQQTNTLLN LVWRDSASEE 420
VFTTMASVCH TLMVQHRMMV PKVRLLYSLA FNARFLRHLW FLISSMSTRM ITGSMVPLLQ 480
VISRGSPMSF EDSSRIIPLF YLFSSLFSHS LISIHDNEFF GDPIEVVGQR QSSMMPFTLE 540
ELIMLSRCLR DACLGIIKLA YPETKPEVRE EYITAFQSIG VTTSSEMQQC IQMEQKRWIQ 600
LFKVITNLVK MLKSRDTRRN FCPPNHWLSE QEDIKADKVT QLYVPASRHV WRFRRMGRIG 660
PLQSTLDVGL ESPPLSVSEE RQLAVLTELP FVVPFEERVK IFQRLIYADK QEVQGDGPFL 720
DGINVTIRRN YIYEDAYDKL SPENEPDLKK RIRVHLLNAH GLDEAGIDGG GIFREFLNEL 780
LKSGFNPNQG FFKTTNEGLL YPNPAAQMLV GDSFARHYYF LGRMLGKALY ENMLVELPFA 840
GFFLSKLLGT SADVDIHHLA SLDPEVYKNL LFLKSYEDDV EELGLNFTVV NNDLGEAQVV 900
ELKFGGKDIP VTSANRIAYI HLVADYRLNR QIRQHCLAFR QGLANVVSLE WLRMFDQQEI 960
QVLISGAQVP ISLEDLKSFT NYSGGYSADH PVIKVFWRVV EGFTDEEKRK LLKFVTSCSR 1020
PPLLGFKELY PAFCIHNGGS DLERLPTAST CMNLLKLPEF YDETLLRSKL LYAIECAAGF 1080
ELS 1083 
Gene Ontology
 GO:0005737; C:cytoplasm; IBA:RefGenome.
 GO:0005634; C:nucleus; IBA:RefGenome.
 GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
 GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IBA:RefGenome. 
Interpro
 IPR000569; HECT.
 IPR000048; IQ_motif_EF-hand-BS. 
Pfam
 PF00632; HECT 
SMART
 SM00119; HECTc
 SM00015; IQ 
PROSITE
 PS50237; HECT
 PS50096; IQ 
PRINTS