CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001643
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase HERC2 
Protein Synonyms/Alias
 HECT domain and RCC1-like domain-containing protein 2 
Gene Name
 HERC2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
17AQARLDSKWLKTDIQubiquitination[1]
20RLDSKWLKTDIQLAFubiquitination[1]
72SVEPSGTKKEDLNDKubiquitination[2]
95PAPIYRAKSILDSWVubiquitination[1, 3, 4, 5]
105LDSWVWGKQPDVNELubiquitination[2, 3, 4]
351FQSIICRKDAPHSEGubiquitination[1]
547VISAFSGKQAGKHVVubiquitination[1, 5]
653KTPKLIEKLQDLDVVubiquitination[1, 5]
661LQDLDVVKVRCGSQFubiquitination[1]
683GQVYSWGKGDNQRLGubiquitination[1]
990RSRTPLDKDLINTGIubiquitination[3, 6]
1503QEQGRSYKEVCAPVIubiquitination[1, 5, 6]
1677EGIDTILKLASKNFLubiquitination[1]
2008VESGTTDKTSSPNRLubiquitination[1, 5]
2304HKIKKSTKQAFAGQVubiquitination[1]
2338ALLSHQDKLRQILSQubiquitination[1]
2657SVTTPKYKWGSVTHQubiquitination[3]
2817QSSGSQGKHWIRLEIubiquitination[1]
2893RYIEIAIKQCRSSGIubiquitination[1]
2976KDQLGGLKGSKIKVPubiquitination[1]
2979LGGLKGSKIKVPSFSubiquitination[1]
3141GDNTTQLKPKMVKVLubiquitination[1, 5]
3146QLKPKMVKVLLGHRVubiquitination[1, 6]
3247GSDVHVRKPQVVEGLubiquitination[1]
3382PNRPSLAKILLSLDGubiquitination[6]
3469SPNPWQEKREIVSSEubiquitination[1]
3554RVVVDLLKLSVCSRAubiquitination[1]
3690PGDELKWKFISDGSVubiquitination[3]
3716IMPAAGPKELLSDRCubiquitination[1]
3780WALQRLRKLLTTEFGubiquitination[1, 3, 6]
3839DPIVRGGKQLLHSPFubiquitination[3]
4396GILISQGKEAAFRKVubiquitination[1]
4402GKEAAFRKVVQATMVubiquitination[1]
4774KLPRYSCKQVLEEKLubiquitination[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] 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] 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]
 [4] 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]
 [5] 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]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965
Functional Description
 E3 ubiquitin-protein ligase that regulates ubiquitin- dependent retention of repair proteins on damaged chromosomes. Recruited to sites of DNA damage in response to ionizing radiation (IR) and facilitates the assembly of UBE2N and RNF8 promoting DNA damage-induced formation of 'Lys-63'-linked ubiquitin chains. Acts as a mediator of binding specificity between UBE2N and RNF8. Involved in the maintenance of RNF168 levels. E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of XPA which influences the circadian oscillation of DNA excision repair activity. 
Sequence Annotation
 REPEAT 2 46 WD 1.
 REPEAT 286 327 WD 2.
 REPEAT 490 529 WD 3.
 REPEAT 513 568 RCC1 1.
 REPEAT 569 620 RCC1 2.
 REPEAT 623 674 RCC1 3.
 REPEAT 675 726 RCC1 4.
 REPEAT 704 743 WD 4.
 REPEAT 728 778 RCC1 5.
 DOMAIN 1207 1283 Cytochrome b5 heme-binding.
 DOMAIN 1859 1932 MIB/HERC2.
 DOMAIN 2759 2936 DOC.
 REPEAT 2958 3009 RCC1 6.
 REPEAT 3010 3064 RCC1 7.
 REPEAT 3065 3116 RCC1 8.
 REPEAT 3118 3168 RCC1 9.
 REPEAT 3171 3222 RCC1 10.
 REPEAT 3224 3274 RCC1 11.
 REPEAT 3275 3326 RCC1 12.
 REPEAT 3926 3967 WD 5.
 REPEAT 3951 4002 RCC1 13.
 REPEAT 4004 4056 RCC1 14.
 REPEAT 4058 4108 RCC1 15.
 REPEAT 4110 4162 RCC1 16.
 REPEAT 4164 4214 RCC1 17.
 REPEAT 4216 4266 RCC1 18.
 REPEAT 4241 4283 WD 6.
 REPEAT 4268 4318 RCC1 19.
 DOMAIN 4457 4794 HECT.
 ZN_FING 2702 2749 ZZ-type.
 ACT_SITE 4762 4762 Glycyl thioester intermediate (By
 MOD_RES 647 647 Phosphothreonine.
 MOD_RES 1944 1944 Phosphothreonine.
 MOD_RES 2454 2454 Phosphoserine.
 MOD_RES 2928 2928 Phosphoserine.
 MOD_RES 4810 4810 Phosphoserine.
 MOD_RES 4811 4811 Phosphoserine.
 MOD_RES 4814 4814 Phosphoserine.
 MOD_RES 4827 4827 Phosphothreonine.  
Keyword
 3D-structure; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation; DNA damage; DNA repair; Ligase; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; Ubl conjugation pathway; WD repeat; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 4834 AA 
Protein Sequence
MPSESFCLAA QARLDSKWLK TDIQLAFTRD GLCGLWNEMV KDGEIVYTGT ESTQNGELPP 60
RKDDSVEPSG TKKEDLNDKE KKDEEETPAP IYRAKSILDS WVWGKQPDVN ELKECLSVLV 120
KEQQALAVQS ATTTLSALRL KQRLVILERY FIALNRTVFQ ENVKVKWKSS GISLPPVDKK 180
SSRPAGKGVE GLARVGSRAA LSFAFAFLRR AWRSGEDADL CSELLQESLD ALRALPEASL 240
FDESTVSSVW LEVVERATRF LRSVVTGDVH GTPATKGPGS IPLQDQHLAL AILLELAVQR 300
GTLSQMLSAI LLLLQLWDSG AQETDNERSA QGTSAPLLPL LQRFQSIICR KDAPHSEGDM 360
HLLSGPLSPN ESFLRYLTLP QDNELAIDLR QTAVVVMAHL DRLATPCMPP LCSSPTSHKG 420
SLQEVIGWGL IGWKYYANVI GPIQCEGLAN LGVTQIACAE KRFLILSRNG RVYTQAYNSD 480
TLAPQLVQGL ASRNIVKIAA HSDGHHYLAL AATGEVYSWG CGDGGRLGHG DTVPLEEPKV 540
ISAFSGKQAG KHVVHIACGS TYSAAITAEG ELYTWGRGNY GRLGHGSSED EAIPMLVAGL 600
KGLKVIDVAC GSGDAQTLAV TENGQVWSWG DGDYGKLGRG GSDGCKTPKL IEKLQDLDVV 660
KVRCGSQFSI ALTKDGQVYS WGKGDNQRLG HGTEEHVRYP KLLEGLQGKK VIDVAAGSTH 720
CLALTEDSEV HSWGSNDQCQ HFDTLRVTKP EPAALPGLDT KHIVGIACGP AQSFAWSSCS 780
EWSIGLRVPF VVDICSMTFE QLDLLLRQVS EGMDGSADWP PPQEKECVAV ATLNLLRLQL 840
HAAISHQVDP EFLGLGLGSI LLNSLKQTVV TLASSAGVLS TVQSAAQAVL QSGWSVLLPT 900
AEERARALSA LLPCAVSGNE VNISPGRRFM IDLLVGSLMA DGGLESALHA AITAEIQDIE 960
AKKEAQKEKE IDEQEANAST FHRSRTPLDK DLINTGICES SGKQCLPLVQ LIQQLLRNIA 1020
SQTVARLKDV ARRISSCLDF EQHSRERSAS LDLLLRFQRL LISKLYPGES IGQTSDISSP 1080
ELMGVGSLLK KYTALLCTHI GDILPVAASI ASTSWRHFAE VAYIVEGDFT GVLLPELVVS 1140
IVLLLSKNAG LMQEAGAVPL LGGLLEHLDR FNHLAPGKER DDHEELAWPG IMESFFTGQN 1200
CRNNEEVTLI RKADLENHNK DGGFWTVIDG KVYDIKDFQT QSLTGNSILA QFAGEDPVVA 1260
LEAALQFEDT RESMHAFCVG QYLEPDQEIV TIPDLGSLSS PLIDTERNLG LLLGLHASYL 1320
AMSTPLSPVE IECAKWLQSS IFSGGLQTSQ IHYSYNEEKD EDHCSSPGGT PASKSRLCSH 1380
RRALGDHSQA FLQAIADNNI QDHNVKDFLC QIERYCRQCH LTTPIMFPPE HPVEEVGRLL 1440
LCCLLKHEDL GHVALSLVHA GALGIEQVKH RTLPKSVVDV CRVVYQAKCS LIKTHQEQGR 1500
SYKEVCAPVI ERLRFLFNEL RPAVCNDLSI MSKFKLLSSL PRWRRIAQKI IRERRKKRVP 1560
KKPESTDDEE KIGNEESDLE EACILPHSPI NVDKRPIAIK SPKDKWQPLL STVTGVHKYK 1620
WLKQNVQGLY PQSPLLSTIA EFALKEEPVD VEKMRKCLLK QLERAEVRLE GIDTILKLAS 1680
KNFLLPSVQY AMFCGWQRLI PEGIDIGEPL TDCLKDVDLI PPFNRMLLEV TFGKLYAWAV 1740
QNIRNVLMDA SAKFKELGIQ PVPLQTITNE NPSGPSLGTI PQARFLLVML SMLTLQHGAN 1800
NLDLLLNSGM LALTQTALRL IGPSCDNVEE DMNASAQGAS ATVLEETRKE TAPVQLPVSG 1860
PELAAMMKIG TRVMRGVDWK WGDQDGPPPG LGRVIGELGE DGWIRVQWDT GSTNSYRMGK 1920
EGKYDLKLAE LPAAAQPSAE DSDTEDDSEA EQTERNIHPT AMMFTSTINL LQTLCLSAGV 1980
HAEIMQSEAT KTLCGLLRML VESGTTDKTS SPNRLVYREQ HRSWCTLGFV RSIALTPQVC 2040
GALSSPQWIT LLMKVVEGHA PFTATSLQRQ ILAVHLLQAV LPSWDKTERA RDMKCLVEKL 2100
FDFLGSLLTT CSSDVPLLRE STLRRRRVRP QASLTATHSS TLAEEVVALL RTLHSLTQWN 2160
GLINKYINSQ LRSITHSFVG RPSEGAQLED YFPDSENPEV GGLMAVLAVI GGIDGRLRLG 2220
GQVMHDEFGE GTVTRITPKG KITVQFSDMR TCRVCPLNQL KPLPAVAFNV NNLPFTEPML 2280
SVWAQLVNLA GSKLEKHKIK KSTKQAFAGQ VDLDLLRCQQ LKLYILKAGR ALLSHQDKLR 2340
QILSQPAVQE TGTVHTDDGA VVSPDLGDMS PEGPQPPMIL LQQLLASATQ PSPVKAIFDK 2400
QELEAAALAV CQCLAVESTH PSSPGFEDCS SSEATTPVAV QHIRPARVKR RKQSPVPALP 2460
IVVQLMEMGF SRRNIEFALK SLTGASGNAS SLPGVEALVG WLLDHSDIQV TELSDADTVS 2520
DEYSDEEVVE DVDDAAYSMS TGAVVTESQT YKKRADFLSN DDYAVYVREN IQVGMMVRCC 2580
RAYEEVCEGD VGKVIKLDRD GLHDLNVQCD WQQKGGTYWV RYIHVELIGY PPPSSSSHIK 2640
IGDKVRVKAS VTTPKYKWGS VTHQSVGVVK AFSANGKDII VDFPQQSHWT GLLSEMELVP 2700
SIHPGVTCDG CQMFPINGSR FKCRNCDDFD FCETCFKTKK HNTRHTFGRI NEPGQSAVFC 2760
GRSGKQLKRC HSSQPGMLLD SWSRMVKSLN VSSSVNQASR LIDGSEPCWQ SSGSQGKHWI 2820
RLEIFPDVLV HRLKMIVDPA DSSYMPSLVV VSGGNSLNNL IELKTININP SDTTVPLLND 2880
CTEYHRYIEI AIKQCRSSGI DCKIHGLILL GRIRAEEEDL AAVPFLASDN EEEEDEKGNS 2940
GSLIRKKAAG LESAATIRTK VFVWGLNDKD QLGGLKGSKI KVPSFSETLS ALNVVQVAGG 3000
SKSLFAVTVE GKVYACGEAT NGRLGLGISS GTVPIPRQIT ALSSYVVKKV AVHSGGRHAT 3060
ALTVDGKVFS WGEGDDGKLG HFSRMNCDKP RLIEALKTKR IRDIACGSSH SAALTSSGEL 3120
YTWGLGEYGR LGHGDNTTQL KPKMVKVLLG HRVIQVACGS RDAQTLALTD EGLVFSWGDG 3180
DFGKLGRGGS EGCNIPQNIE RLNGQGVCQI ECGAQFSLAL TKSGVVWTWG KGDYFRLGHG 3240
SDVHVRKPQV VEGLRGKKIV HVAVGALHCL AVTDSGQVYA WGDNDHGQQG NGTTTVNRKP 3300
TLVQGLEGQK ITRVACGSSH SVAWTTVDVA TPSVHEPVLF QTARDPLGAS YLGVPSDADS 3360
SAASNKISGA SNSKPNRPSL AKILLSLDGN LAKQQALSHI LTALQIMYAR DAVVGALMPA 3420
AMIAPVECPS FSSAAPSDAS AMASPMNGEE CMLAVDIEDR LSPNPWQEKR EIVSSEDAVT 3480
PSAVTPSAPS ASARPFIPVT DDLGAASIIA ETMTKTKEDV ESQNKAAGPE PQALDEFTSL 3540
LIADDTRVVV DLLKLSVCSR AGDRGRDVLS AVLSGMGTAY PQVADMLLEL CVTELEDVAT 3600
DSQSGRLSSQ PVVVESSHPY TDDTSTSGTV KIPGAEGLRV EFDRQCSTER RHDPLTVMDG 3660
VNRIVSVRSG REWSDWSSEL RIPGDELKWK FISDGSVNGW GWRFTVYPIM PAAGPKELLS 3720
DRCVLSCPSM DLVTCLLDFR LNLASNRSIV PRLAASLAAC AQLSALAASH RMWALQRLRK 3780
LLTTEFGQSI NINRLLGEND GETRALSFTG SALAALVKGL PEALQRQFEY EDPIVRGGKQ 3840
LLHSPFFKVL VALACDLELD TLPCCAETHK WAWFRRYCMA SRVAVALDKR TPLPRLFLDE 3900
VAKKIRELMA DSENMDVLHE SHDIFKREQD EQLVQWMNRR PDDWTLSAGG SGTIYGWGHN 3960
HRGQLGGIEG AKVKVPTPCE ALATLRPVQL IGGEQTLFAV TADGKLYATG YGAGGRLGIG 4020
GTESVSTPTL LESIQHVFIK KVAVNSGGKH CLALSSEGEV YSWGEAEDGK LGHGNRSPCD 4080
RPRVIESLRG IEVVDVAAGG AHSACVTAAG DLYTWGKGRY GRLGHSDSED QLKPKLVEAL 4140
QGHRVVDIAC GSGDAQTLCL TDDDTVWSWG DGDYGKLGRG GSDGCKVPMK IDSLTGLGVV 4200
KVECGSQFSV ALTKSGAVYT WGKGDYHRLG HGSDDHVRRP RQVQGLQGKK VIAIATGSLH 4260
CVCCTEDGEV YTWGDNDEGQ LGDGTTNAIQ RPRLVAALQG KKVNRVACGS AHTLAWSTSK 4320
PASAGKLPAQ VPMEYNHLQE IPIIALRNRL LLLHHLSELF CPCIPMFDLE GSLDETGLGP 4380
SVGFDTLRGI LISQGKEAAF RKVVQATMVR DRQHGPVVEL NRIQVKRSRS KGGLAGPDGT 4440
KSVFGQMCAK MSSFGPDSLL LPHRVWKVKF VGESVDDCGG GYSESIAEIC EELQNGLTPL 4500
LIVTPNGRDE SGANRDCYLL SPAARAPVHS SMFRFLGVLL GIAIRTGSPL SLNLAEPVWK 4560
QLAGMSLTIA DLSEVDKDFI PGLMYIRDNE ATSEEFEAMS LPFTVPSASG QDIQLSSKHT 4620
HITLDNRAEY VRLAINYRLH EFDEQVAAVR EGMARVVPVP LLSLFTGYEL ETMVCGSPDI 4680
PLHLLKSVAT YKGIEPSASL IQWFWEVMES FSNTERSLFL RFVWGRTRLP RTIADFRGRD 4740
FVIQVLDKYN PPDHFLPESY TCFFLLKLPR YSCKQVLEEK LKYAIHFCKS IDTDDYARIA 4800
LTGEPAADDS SDDSDNEDVD SFASDSTQDY LTGH 4834 
Gene Ontology
 GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005743; C:mitochondrial inner membrane; IEA:Compara.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005085; F:guanyl-nucleotide exchange factor activity; NAS:UniProtKB.
 GO:0020037; F:heme binding; IEA:InterPro.
 GO:0032183; F:SUMO binding; IDA:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006281; P:DNA repair; IDA:UniProtKB.
 GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
 GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IBA:RefGenome.
 GO:0007283; P:spermatogenesis; IEA:Compara. 
Interpro
 IPR004939; APC_su10/DOC_dom.
 IPR006624; Beta-propeller_rpt_TECPR.
 IPR021097; CPH_domain.
 IPR001199; Cyt_B5-like_heme/steroid-bd.
 IPR008979; Galactose-bd-like.
 IPR000569; HECT.
 IPR010606; Mib_Herc2.
 IPR009091; RCC1/BLIP-II.
 IPR000408; Reg_chr_condens.
 IPR014722; Rib_L2_dom2.
 IPR000433; Znf_ZZ. 
Pfam
 PF03256; APC10
 PF11515; Cul7
 PF00173; Cyt-b5
 PF00632; HECT
 PF06701; MIB_HERC2
 PF00415; RCC1
 PF00569; ZZ 
SMART
 SM00119; HECTc
 SM00706; TECPR
 SM00291; ZnF_ZZ 
PROSITE
 PS00191; CYTOCHROME_B5_1
 PS50255; CYTOCHROME_B5_2
 PS51284; DOC
 PS50237; HECT
 PS51416; MIB_HERC2
 PS00625; RCC1_1
 PS00626; RCC1_2
 PS50012; RCC1_3
 PS00678; WD_REPEATS_1
 PS50082; WD_REPEATS_2
 PS50294; WD_REPEATS_REGION
 PS01357; ZF_ZZ_1
 PS50135; ZF_ZZ_2 
PRINTS
 PR00633; RCCNDNSATION.