CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013349
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
 Jdf2; Kiaa0393; Rjs 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
17AQSRLDSKWLKTDIQubiquitination[1]
62NRELPLRKDDGVDAQubiquitination[1]
548VISAFSGKQAGKHVVubiquitination[1]
654KTPKLIEKLQDLDVIubiquitination[1]
662LQDLDVIKVRCGSQFubiquitination[1]
750FDTLRVTKPEPTALPubiquitination[1]
991RSRTPLDKDLINTGIubiquitination[1]
1494QAKCSLIKTHQEQGRubiquitination[1]
1606SMKSPKDKWQPLLNTubiquitination[1]
1619NTVTGVHKYKWLKQNubiquitination[1]
1678EGIDTILKLAAKSFLubiquitination[1]
2182VTQSYAGKTSERAQLubiquitination[1]
2323LLRSQQLKLYILKAGubiquitination[1]
2339ALLSHQDKLRQILSQubiquitination[1]
2474MEMGFPRKNIEFALKubiquitination[1]
2961STATIRTKVFVWGLNubiquitination[1]
3471SPNLWQEKREIVSSEubiquitination[1]
3633TSTSGTVKIPGAEGLubiquitination[1]
3690RIPGDELKWKFISDGubiquitination[1]
4398GILISQGKEAAFRKVubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
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 (By similarity). 
Sequence Annotation
 REPEAT 3 46 WD 1.
 REPEAT 287 328 WD 2.
 REPEAT 491 530 WD 3.
 REPEAT 514 569 RCC1 1.
 REPEAT 570 621 RCC1 2.
 REPEAT 624 675 RCC1 3.
 REPEAT 676 727 RCC1 4.
 REPEAT 705 744 WD 4.
 REPEAT 729 779 RCC1 5.
 DOMAIN 1208 1284 Cytochrome b5 heme-binding.
 DOMAIN 1860 1933 MIB/HERC2.
 DOMAIN 2760 2937 DOC.
 REPEAT 2959 3010 RCC1 6.
 REPEAT 3011 3065 RCC1 7.
 REPEAT 3066 3117 RCC1 8.
 REPEAT 3097 3134 WD 5.
 REPEAT 3118 3169 RCC1 9.
 REPEAT 3172 3223 RCC1 10.
 REPEAT 3225 3275 RCC1 11.
 REPEAT 3276 3327 RCC1 12.
 REPEAT 3928 3969 WD 6.
 REPEAT 3953 4004 RCC1 13.
 REPEAT 4006 4058 RCC1 14.
 REPEAT 4060 4110 RCC1 15.
 REPEAT 4112 4164 RCC1 16.
 REPEAT 4166 4216 RCC1 17.
 REPEAT 4218 4268 RCC1 18.
 REPEAT 4243 4285 WD 7.
 REPEAT 4270 4320 RCC1 19.
 DOMAIN 4459 4796 HECT.
 ZN_FING 2703 2750 ZZ-type.
 ACT_SITE 4764 4764 Glycyl thioester intermediate (By
 MOD_RES 648 648 Phosphothreonine (By similarity).
 MOD_RES 1945 1945 Phosphothreonine (By similarity).
 MOD_RES 2455 2455 Phosphoserine (By similarity).
 MOD_RES 2929 2929 Phosphoserine.
 MOD_RES 4812 4812 Phosphoserine (By similarity).
 MOD_RES 4813 4813 Phosphoserine (By similarity).
 MOD_RES 4816 4816 Phosphoserine (By similarity).
 MOD_RES 4829 4829 Phosphothreonine (By similarity).  
Keyword
 Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; 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
 4836 AA 
Protein Sequence
MPSESFCLAA QSRLDSKWLK TDIQLAFTRD GLCGLWNEMV KDGEIVYTGT ELAQNRELPL 60
RKDDGVDAQS GTKKEDLNDK EKKEEEETPA PVYRAKSILE SWVWGRQPDV NELKECLSVL 120
VKEQQALAVQ SATTTLSALR LKQRLVILER YFIALNRTVF QENVKVKWKS SSISVPPTEK 180
KSARPTGRGV EGLARVGSRA ALSFAFAFLR RAWRSGEDAD LCSELLQESL DALRALPEAS 240
LFDESTVSSV WLEVVERATR FLRSVVTGDV HGTPGTKGPG GVPLQDQHLA LAILLELAVQ 300
RGTLSQMLSA ILLLLQLWDS GAQETDNERS AQGTSAPLLP LLQRFQSIIC SKDVPHTESD 360
MHLLSGPLSP NESFLRYLTL PQDNELAIDL RQTAVVVMAH LDRLATPCMP PLCSSPTSHK 420
GSLQEVIGWG LIGWKYYANV IGPIQCEGLA SLGVMQVACA EKRFLILSRN GRVYTQAYNS 480
DMLAPQLVQG LASRNIVKIA AHSDGHHYLA LAATGEVYSW GCGDGGRLGH GDTVPLEEPK 540
VISAFSGKQA GKHVVHIACG STYSAAITAE GELYTWGRGN YGRLGHGSSE DEAIPMLVAG 600
LKGLKVIDVA CGSGDAQTLA VTENGQVWSW GDGDYGKLGR GGSDGCKTPK LIEKLQDLDV 660
IKVRCGSQFS IALTKDGQVY SWGKGDNQRL GHGTEEHVRY PKLLEGLQGK KVIDVAAGST 720
HCLALTEDSE VHSWGSNDQC QHFDTLRVTK PEPTALPGLD SKHIVGIACG PAQSFAWSSC 780
SEWSIGLRVP FVVDICSMTF EQLDLLLRQV SEGMDGTADW PPPQEKECMA VATLNLLRLQ 840
LHAAISHQVD PEFLGLGLGS VLLNSLKQTV VTLASSAGVL STVQSAAQAV LQSGWSVLLP 900
TAEERARALS ALLPCTVSGN EVNISPGRRF MIDLLVGSLM ADGGLESALN AAITAEIQDI 960
EAKKEAQKEK EIDEQEASAS TFHRSRTPLD KDLINTGIYE SSGKQCLPLV QLIQQLLRNI 1020
ASQTVARLKD VARRISSCLD FEQQSCERSA SLDLLLRFQR LLISKLYPGE KIGPISDTSS 1080
PELMGVGSLL KKYTALVCTH IGDILPVAAS IASSSWQHFA EVACVMEGDF TGVLLPELVV 1140
SIVLLLSKNA SLMQEAGAIP LLGGLLEHLD RFNHLAPGKE RDDHEELAWP GIMESFFTGQ 1200
NCRNNEEVTL IRKADLENHN KDGGFWTVID GKVYGIKDFQ TQSLTGNSIL AQFAGEDPVV 1260
ALEAALQFED TQESMHAFCV GQYLEPDQEV VTIPDLGSLS SPLIDTERNL GLLLGLHASY 1320
LAMSTPLSPV EVECAKWLQS SIFSGGLQTS QIHYSYNEEK DEDHCSSPGG TPISKSRLCS 1380
HRWALGDHSQ AFLQAIADNN IQDYNVKDFL CQIERYCRQC HLTTPITFPP EHPVEEVGRL 1440
LLCCLLKHED LGHVALSLVH VGTLGIEQVK HRTLPKSVVD VCRVVYQAKC SLIKTHQEQG 1500
RSYKEVCAPV IERLRFLFNE LRPAVCSDLS IMSKFKLLGS LPRWRRIAQK IIRERRKKRV 1560
PKKPESIDSE EKIGNEESDL EEACVLPHSP INVDKRPISM KSPKDKWQPL LNTVTGVHKY 1620
KWLKQNVQGL YPQSALLNTI VEFALKEEPV DVEKMRKCLL KQLERAEVRL EGIDTILKLA 1680
AKSFLLPSVQ YAMFCGWQRL IPEGIDIGEP LTDCLRDVDL IPPFNRMLLE VTFGKLYAWA 1740
VQNIRSVLMD ASARFKELGI QPVPLQTITN ENPAGPSLGT IPQARFLLVM LSMLTLQHGA 1800
NNLDLLLNSG TLALTQTALR LIGPTCDSVE DDMNASARGA SATVLEETRK ETAPVQLPVS 1860
GPELAAMMKI GTRVMRGVDW KWGDQDGPPP GLGRVIGELG EDGWIRVQWD TGSTNSYRMG 1920
KEGKYDLKLV ELPVSSQPSA EDSDTEDDSE AEQGERNIHP TAMMLTSVIN LLQTLCLSVG 1980
VHADIMQSEA TKTLCGLLRM LVESGTTDKP APPDRLVARE QHRSWCTLGF VRSIALTPQA 2040
CGALSSPRWI TLLMKVVEGH APFTAASLQR QILAVHLLQA VLPSWDKTER ARDMKCLVEK 2100
LFGFLGSLLT TCSSDVPLLR ESTLRKRRAR PQASLTATHS STLAEEVVGL LRTLHSLTQW 2160
NGLINKYINS QLCSVTQSYA GKTSERAQLE DYFPDSENLE VGGLMAVLAV IGGIDGRLRL 2220
GGQVMHDEFG EGTVTRITPK GRITVQFCDM RMCRVCPLNQ LKPLPAVAFS VNNLPFTEPM 2280
LSVWAELVNL AGSKLEKHKT KKSAKPAFAG QVDLDLLRSQ QLKLYILKAG RALLSHQDKL 2340
RQILSQPAVQ GTGTLQTDDG AAASPDLGDM SPEGPQPPMI LLQQLLSSAT QPSPVKAIFD 2400
KQELEAAALA LCQCLAVEST HPSSPGCEDC SSSEATTPVS VQHIHLARAK KRRQSPAPAL 2460
PIVVQLMEMG FPRKNIEFAL KSLTGTSGNA SGLPGVEALV GWLLDHSDVQ VTEFSDAETL 2520
SDEYSDEEVV EDVDDTPYPV AAGAVVTESQ TYKKRADFLS NDDYAVYVRE NVQVGMMVRC 2580
CRTYEEVCEG DVGKVIKLDR DGLHDLNVQC DWQQKGGTYW VRYIHVELIG YPPPSSSSHI 2640
KIGDKVRVKA SVTTPKYKWG SVTHQSVGLV KAFSANGKDI IVDFPQQSHW TGLLSEMELV 2700
PSIHPGVTCD GCQTFPINGS RFKCRNCDDF DFCETCFKTK KHNTRHTFGR INEPGQSAVF 2760
CGRSGKQLKR CHSSQPGMLL DSWSRMVKSL NVSSSVNQAS RLIDGSEPCW QSSGSQGKHW 2820
IRLEIFPDVL VHRLKMIVDP ADSSYMPSLV VVSGGNSLNN LIELKTININ QTDTTVPLLS 2880
DCAEYHRYIE IAIKQCRSSG IDCKIHGLIL LGRIRAEEED LAAVPFLASD NEEEEDDKGS 2940
TGSLIRKKTP GLESTATIRT KVFVWGLNDK DQLGGLKGSK IKVPSFSETL SALNVVQVAG 3000
GSKSLFAVTV EGKVYSCGEA TNGRLGLGMS SGTVPIPRQI TALSSYVVKK VAVHSGGRHA 3060
TALTVDGKVF SWGEGDDGKL GHFSRMNCDK PRLIEALKTK RIRDIACGSS HSAALTSSGE 3120
LYTWGLGEYG RLGHGDNTTQ LKPKMVKVLL GHRVIQVACG SRDAQTLALT DEGLVFSWGD 3180
GDFGKLGRGG SEGCNIPQNI ERLNGQGVCQ IECGAQFSLA LTKSGVVWTW GKGDYFRLGH 3240
GSDVHVRKPQ VVEGLRGKKI VHVAVGALHC LAVTDSGQVY AWGDNDHGQQ GNGTTTVNRK 3300
PTLVQGLEGQ KITRVACGSS HSVAWTTVDV ATPSVHEPVL FQTARDPLGA SYLGVPSDAD 3360
SSSSSNKISG ANNCKPNRPS LAKILLSLEG NLAKQQALSH ILTALQIMYA RDAVVGALMP 3420
AGMLAPVECP SFSSSAPASD VSAMASPMHM EDSTLAADLE DRLSPNLWQE KREIVSSEDA 3480
VTPSAVTPSA PSASSRPFIP VTDDPGAASI IAETMTKTKE DVESQNKTSG PEPQSLDEFT 3540
SLLIPDDTRV VVELLKLSVC SRAGDKGREV LSAVLSGMGT AYPQVADMLL ELCVTELEDV 3600
ATDSQSGRLS SQPVVVESSH PYTDDTSTSG TVKIPGAEGL RVEFDRQCST ERRHDPLTVM 3660
DGVNRIVSVR SGREWSDWSS ELRIPGDELK WKFISDGSVN GWGWRFTVYP IMPAAGPKDL 3720
LSDRCVLSCP SMDLVTCLLD FRLNLTSNRS IVPRLAASLA ACAQLSALAA SHRMWALQRL 3780
RRLLTTEFGQ SININRLLGE NDGESRALSF TGSALAALVK GLPEALQRQF EYEDPIVRGG 3840
KQLLHSPFFK VLVALACDLE LDTLPCCAET HKWAWFRRYC MASRVAVALD KRTPLPRLFL 3900
DEVAKKIREL MADSESMDVL HESHSIFKRE QDEQLVQWMN RRPDDWTLSA GGSGTIYGWG 3960
HNHRGQLGGI EGAKVKVPTP CEALATLRPV QLIGGEQTLF AVTADGKLYA TGYGAGGRLG 4020
IGGTESVSTP TLLESIQHVF IKKVAVNSGG KHCLALSSEG EVYSWGEAED GKLGHGNRSP 4080
CDRPRVIESL RGIEVVDVAA GGAHSACVTA AGDLYTWGKG RYGRLGHSDS EDQLKPKLVE 4140
ALQGHRVIDI ACGSGDAQTL CLTDDDTVWS WGDGDYGKLG RGGSDGCKVP MKIDSLTGLG 4200
VVKVECGSQF SVALTKSGAV YTWGKGDYHR LGHGSDDHVR RPRQVQGLQG KKVIAIATGS 4260
LHCVCCTEDG EVYTWGDNDE GQLGDGTTNA IQRPRLVAAL QGKKVNRVAC GSAHTLAWST 4320
SKPASAGKLP AQVPMEYNHL QEIPIIALRN RLLLLHHISE LFCPCIPMFD LEGSLDETGL 4380
GPSVGFDTLR GILISQGKEA AFRKVVQATM VRDRQHGPVV ELNRIQVKRS RSKGGLAGPD 4440
GTKSVFGQMC AKMSSFSPDS LLLPHRVWKV KFVGESVDDC GGGYSESIAE ICEELQNGLT 4500
PLLIVTPNGR DESGANRDCY LLNPATRAPV HCSMFRFLGV LLGIAIRTGS PLSLNLAEPV 4560
WKQLAGMSLT IADLSEVDKD FIPGLMYIRD NEATSEEFEA MSLPFTVPSA SGQDIQLSSK 4620
HTHITLDNRA EYVRLAINYR LHEFDEQVAA VREGMARVVP VPLLSLFTGY ELETMVCGSP 4680
DIPLHLLKSV ATYKGIEPSA SLVQWFWEVM ESFSNTERSL FLRFVWGRTR LPRTIADFRG 4740
RDFVIQVLDK YNPPDHFLPE SYTCFFLLKL PRYSCKQVLE EKLKYAIHFC KSIDTDDYAR 4800
IALTGEPAAD DSSEDSDNED ADSFASDSTQ DYLTGH 4836 
Gene Ontology
 GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0020037; F:heme binding; IEA:InterPro.
 GO:0032183; F:SUMO binding; ISS:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006281; P:DNA repair; ISS:UniProtKB.
 GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IBA:RefGenome.
 GO:0007283; P:spermatogenesis; IMP:MGI. 
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.