CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-042423
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 E3 ubiquitin-protein ligase HUWE1 
Protein Synonyms/Alias
  
Gene Name
 HUWE1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
71SDSKGKSKITPAMAAubiquitination[1]
84AARIKQIKPLLSASSubiquitination[2, 3]
141STASALTKLLTKGLSubiquitination[1, 2, 3, 4, 5, 6, 7]
145ALTKLLTKGLSWQPPubiquitination[1, 2, 3, 4, 5, 7]
181PMLFDERKYPYHLMLubiquitination[2]
259SPHSLPAKLPGGVQNubiquitination[2, 3, 4]
281RFLVVTQKAAFTCIKubiquitination[4]
288KAAFTCIKNLWNRKPubiquitination[1]
329RERLSKEKEGSRGEEubiquitination[4]
437PEEVACRKEEEERKAubiquitination[1]
454KQEEEEAKCLEKFQDubiquitination[3]
504DLIMTAIKRNGADYRubiquitination[1, 3, 5, 6, 7]
642KRRAQMTKYLQSNSNubiquitination[1, 2, 4, 5, 6, 7]
677STIDSAWKSGETSVRubiquitination[1, 6]
727PRLNKNSKNSNGQELubiquitination[4]
736SNGQELEKTLEESKEubiquitination[2, 3, 4]
742EKTLEESKEMDIKRKubiquitination[1, 3, 4]
747ESKEMDIKRKENKGNubiquitination[1, 3]
752DIKRKENKGNDTPLAubiquitination[4, 7]
767LESTNTEKETSLEETubiquitination[1, 3, 4, 7]
833AMMFAELKSTRMILNubiquitination[4]
874TLRHTMEKVVRSAATubiquitination[1, 3, 4]
951EFENLRIKGPNAVQLubiquitination[1, 2, 3, 4, 6, 7]
960PNAVQLVKTTPLKPSubiquitination[2, 4, 7]
965LVKTTPLKPSPLPVIubiquitination[1, 2, 3, 4, 7]
1206AMAESTEKHARLQAVubiquitination[1, 3]
1252NIIRLFLKKGLVNDLubiquitination[4]
1253IIRLFLKKGLVNDLAubiquitination[1, 3, 4, 6, 7]
1282NTVNAALKPLETLSRacetylation[3, 8]
1282NTVNAALKPLETLSRubiquitination[1, 2, 3, 4, 5, 7]
1301PSSLFGSKSASSKNKubiquitination[1, 2, 3, 4, 5, 6, 7]
1690TRWTEECKVLDAESMubiquitination[1, 3, 5]
1705HDCVSVVKVSIVNHLubiquitination[1, 3, 5]
1729ERREKRRKQLAEEETubiquitination[3, 4]
1737QLAEEETKITDKGKEubiquitination[1, 3, 4]
2278ELCIETPKLTTSEEKubiquitination[1, 3, 4, 6, 9]
2291EKGKKSSKSCGSSSHubiquitination[1, 3]
2308RPLDLLHKMESKSSNubiquitination[1, 3, 6]
2348GGRKHTEKHASGGSTubiquitination[1, 3]
2379DTLIQLAKVFPSHFTubiquitination[2, 3, 4, 5, 6, 7]
2391HFTQQRTKETNCESDubiquitination[6]
2404SDRERGNKACSPCSSubiquitination[1, 5, 6]
2443RKGKNSVKSVPVSAGubiquitination[7]
2486RSSLLTEKLLRLLSLubiquitination[1, 2, 3, 4, 5, 6, 7]
2592KGSKSPAKVSDGGSSubiquitination[1, 3, 4, 6, 7]
2655GTRDTVLKLLLNGARubiquitination[1, 2, 3, 4, 5, 10]
2670HLGYTLCKQIGTLLAubiquitination[1, 4]
2709EEQPQTTKLKGKMQSubiquitination[1, 3, 5, 6, 9]
2711QPQTTKLKGKMQSRFubiquitination[1, 3]
2731VVIVASQKRPLGGREubiquitination[1, 2, 3, 4, 5, 6, 7, 9, 10]
2750SMSMLTSKTSTQKFFubiquitination[1]
2755TSKTSTQKFFLRVLQubiquitination[1]
2869DGTPQGEKEKEERPPubiquitination[4, 7]
2946ESQLAHIKDEPPPLSubiquitination[1, 2, 3, 4, 7, 10]
2988SLPPDTQKFLRFAETubiquitination[2, 10]
3031RVLDFDVKRKYFRQEubiquitination[1, 3, 6]
3033LDFDVKRKYFRQELEubiquitination[1]
3048RLDEGLRKEDMAVHVubiquitination[1, 3]
3150FVGRIVAKAVYDNRLubiquitination[1, 4, 5]
3224VCEVRDLKPNGANILubiquitination[1, 3, 4]
3255RMTGAIRKQLAAFLEubiquitination[1]
3329FDQADRAKFLQFVTGubiquitination[1, 2, 3, 4, 10]
3339QFVTGTSKVPLQGFAubiquitination[2, 10]
3356EGMNGIQKFQIHRDDubiquitination[1, 2, 10]
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] 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]
 [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] 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] 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]
 [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]
 [8] 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]
 [9] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [10] 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
  
Sequence Annotation
  
Keyword
 Complete proteome; Ligase; Reference proteome; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3408 AA 
Protein Sequence
XSLPSGCEFG QADMQKLVPK DEKADGEQDG AAGSMDASTQ GLLEGIGLDG DTLAPMETDE 60
PTASDSKGKS KITPAMAARI KQIKPLLSAS SRLGRALAEL FGLLVKLCVG SPVRQRRSHH 120
AASTTTAPTP AARSTASALT KLLTKGLSWQ PPPYTPTPRF RLTFFICSVG FTSPMLFDER 180
KYPYHLMLQK FLCSGGHNAL FETFNWALSM GGKVPVSEGL EHSDLPDGTG EFLDAWLMLV 240
EKMVNPTTVL ESPHSLPAKL PGGVQNFPQF SALRFLVVTQ KAAFTCIKNL WNRKPLKVYG 300
GRMAESMLAI LCHILRGEPV IRERLSKEKE GSRGEEDTGQ EEGGSRREPQ VNQQQLQQLM 360
DMGFTREHAM EALLNTSTME QATEYLLTHP PPIMGGVVRD LSMSEEDQMM RAIAMSLGQD 420
IPMDQRAESP EEVACRKEEE ERKAREKQEE EEAKCLEKFQ DADPLEQDEL HTFTDTMLPG 480
CFHLLDELPD TVYRVCDLIM TAIKRNGADY RDMILKQVVN QVWEAADVLI KAALPLTTSD 540
TKTVSEWISQ MATLPQASNL ATRILLLTLL FEELKLPCAW VVESSGILNV LIKLLEVVQP 600
CLQAAKEQKE VQTPKWITPV LLLIDFYEKT AISSKRRAQM TKYLQSNSNN WRWFDDRSGR 660
WCSYSASNNS TIDSAWKSGE TSVRFTAGRR RYTVQFTTMV QVNEETGNRR PVMLTLLRVP 720
RLNKNSKNSN GQELEKTLEE SKEMDIKRKE NKGNDTPLAL ESTNTEKETS LEETKIGEIL 780
IQGLTEDMVT VLIRACVSML GVPVDPDTLH ATLRLCLRLT RDHKYAMMFA ELKSTRMILN 840
LTQSSGFNGF TPLVTLLLRH IIEDPCTLRH TMEKVVRSAA TSGAGSTTSG VVSGSLGSRE 900
INYILRVLGP AACRNPDIFT EVANCCIRIA LPAPRGSGTA SDDEFENLRI KGPNAVQLVK 960
TTPLKPSPLP VIPDTIKEVI YDMLNALAAY HAPEEADKSD PKPGVMTQEV GQLLQDMGDD 1020
VYQQYRSLTR QSSDFDTQSG FSINSQVFAA DGASTETSAS GTSQGEASTP EESRDGKKDK 1080
EGDRASEEGK QKGKGSKPLM PTSTILRLLA ELVRSYVGIA TLIANYSYTV GQSELIKEDC 1140
SVLAFVLDHL LPHTQNAEDK DTPALARLFL ASLAAAGSGT DAQVALVNEV KAALGRALAM 1200
AESTEKHARL QAVMCIISTI MESCPSTSSF YSSATAKTQH NGMNNIIRLF LKKGLVNDLA 1260
RVPHSLDLSS PNMANTVNAA LKPLETLSRI VNQPSSLFGS KSASSKNKSE QDAQGASQDS 1320
SSNQQDPGEP GEAEVQEEDH DVTQTEVADG DIMDGEAETD SVVIAGQPEV LSSQEMQVEN 1380
ELEDLIDELL ERDGGSGNST IIVSRSGEDE SQEDVLMDEA PSNLSQASTL QANREDSMNI 1440
LDPEDEEEHT QEEDSSGSNE DEDDSQDEEE EEEEDEEDDQ EDDEGEEGDE DDDDDGSEME 1500
LDEDYPDMNA SPLVRFERFD REDDLIIEFD NMFSSATDIP PSPGNIPTTH PLMVRHADHS 1560
SLTLGSGSST TRLTQGIGRS QRTLRQLTAN TGHTIHVHYP GNRQPNPPLI LQRLLGPSAA 1620
ADILQLSSSL PLQSRGRARL LVGNDDVHII ARSDDELLDD FFHDQSTATS QAGTLSSIPT 1680
ALTRWTEECK VLDAESMHDC VSVVKVSIVN HLEFLRDEEL EERREKRRKQ LAEEETKITD 1740
KGKEDKENRD QSAQCTASKS NDSTEQNLSD GTPMPDSYPT TPSSTDAATS ESKETLGTLQ 1800
SSQQQPTLPT PPALGEVPQE LQSPAGEGGS STQLLMPVEP EELGPTRPSG EAETTQMELS 1860
PAPTITSLSP ERAEDSDALT AVSSQLEGSP MDTSSLASCT LEEAVGDTSA AGSSEQPRAG 1920
SSTPGDAPPA VAEVQGRSDG SGESAQPPED SSPPASSESS STRDSAVAIS GADSRGILEE 1980
PLPSTSSEEE DPLAGISLPE GVDPSFLAAL PDDIRREVLQ NQLGIRPPTR TAPSTNSSAP 2040
AVVGNPGVTE VSPEFLAALP PAIQEEVLAQ QRAEQQRREL AQNASSDTPM DPVTFIQTLP 2100
SDLRRSVLED MEDSVLAVMP PDIAAEAQAL RREQEARQRQ LMHERLFGHS STSALSAILR 2160
SPAFTSRLSG NRGVQYTRLA VQRGGTFQMG GSSSHNRPSG SNVDTLLRLR GRLLLDHEAL 2220
SCLLVLLFVD EPKLNTSRLH RVLRNLCYHA QTRHWVIRSL LSILQRSSES ELCIETPKLT 2280
TSEEKGKKSS KSCGSSSHEN RPLDLLHKME SKSSNQLSWL SVSMDAALGC RTNIFQIQRS 2340
GGRKHTEKHA SGGSTVHIHP QAAPVVCRHV LDTLIQLAKV FPSHFTQQRT KETNCESDRE 2400
RGNKACSPCS SQSSSSGICT DFWDLLVKLD NMNVSRKGKN SVKSVPVSAG GEGETSPYSL 2460
EASPLGQLMN MLSHPVIRRS SLLTEKLLRL LSLISIALPE NKVSEAQANS GSGASSTTTA 2520
TSTTSTTTTT AASTTPTPPT APTPVTSAPA LVAATAISTI VVAASTTVTT PTTATTTVSI 2580
SPTTKGSKSP AKVSDGGSSS TDFKMVSSGL TENQLQLSVE VLTSHSCSEE GLEDAANVLL 2640
QLSRGDSGTR DTVLKLLLNG ARHLGYTLCK QIGTLLAELR EYNLEQQRRA QCETLSPDGL 2700
PEEQPQTTKL KGKMQSRFDM AENVVIVASQ KRPLGGRELQ LPSMSMLTSK TSTQKFFLRV 2760
LQVIIQLRDD TRRANKKAKQ TGRLGSSGLG SASSIQAAVR QLEAEADAII QMVREGQRAR 2820
RQQQAATSES SQSEASVRRE ESPMDVDQPS PSAQDTQSIA SDGTPQGEKE KEERPPELPL 2880
LSEQLSLDEL WDMLGECLKE LEESHDQHAV LVLQPAVEAF FLVHATERES KPPVRDTRES 2940
QLAHIKDEPP PLSPAPLTPA TPSSLDPFFS REPSSMHISS SLPPDTQKFL RFAETHRTVL 3000
NQILRQSTTH LADGPFAVLV DYIRVLDFDV KRKYFRQELE RLDEGLRKED MAVHVRRDHV 3060
FEDSYRELHR KSPEEMKNRL YIVFEGEEGQ DAGGLLREWY MIISREMFNP MYALFRTSPG 3120
DRVTYTINPS SHCNPNHLSY FKFVGRIVAK AVYDNRLLEC YFTRSFYKHI LGKSVRYTDM 3180
ESEDYHFYQG LVYLLENDVS TLGYDLTFST EVQEFGVCEV RDLKPNGANI LVTEENKKEY 3240
VHLVCQMRMT GAIRKQLAAF LEGFYEIIPK RLISIFTEQE LELLISGLPT IDIDDLKSNT 3300
EYHKYQSNSI QIQWFWRALR SFDQADRAKF LQFVTGTSKV PLQGFAALEG MNGIQKFQIH 3360
RDDRSTDRLP SAHTCFNQLD LPAYESFEKL RHMLLLAIQE CSEGFGLA 3408 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0004842; F:ubiquitin-protein ligase activity; IEA:InterPro.
 GO:0016567; P:protein ubiquitination; IEA:GOC. 
Interpro
 IPR025527; DUF4414.
 IPR000569; HECT.
 IPR009060; UBA-like.
 IPR000449; UBA/transl_elong_EF1B_N.
 IPR015940; UBA/transl_elong_EF1B_N_euk.
 IPR004170; WWE-dom. 
Pfam
 PF14377; DUF4414
 PF00632; HECT
 PF00627; UBA
 PF02825; WWE 
SMART
 SM00119; HECTc
 SM00165; UBA 
PROSITE
 PS50237; HECT
 PS50030; UBA
 PS50918; WWE 
PRINTS