Tag | Content |
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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 |
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17 | AQSRLDSKWLKTDIQ | ubiquitination | [1] | 62 | NRELPLRKDDGVDAQ | ubiquitination | [1] | 548 | VISAFSGKQAGKHVV | ubiquitination | [1] | 654 | KTPKLIEKLQDLDVI | ubiquitination | [1] | 662 | LQDLDVIKVRCGSQF | ubiquitination | [1] | 750 | FDTLRVTKPEPTALP | ubiquitination | [1] | 991 | RSRTPLDKDLINTGI | ubiquitination | [1] | 1494 | QAKCSLIKTHQEQGR | ubiquitination | [1] | 1606 | SMKSPKDKWQPLLNT | ubiquitination | [1] | 1619 | NTVTGVHKYKWLKQN | ubiquitination | [1] | 1678 | EGIDTILKLAAKSFL | ubiquitination | [1] | 2182 | VTQSYAGKTSERAQL | ubiquitination | [1] | 2323 | LLRSQQLKLYILKAG | ubiquitination | [1] | 2339 | ALLSHQDKLRQILSQ | ubiquitination | [1] | 2474 | MEMGFPRKNIEFALK | ubiquitination | [1] | 2961 | STATIRTKVFVWGLN | ubiquitination | [1] | 3471 | SPNLWQEKREIVSSE | ubiquitination | [1] | 3633 | TSTSGTVKIPGAEGL | ubiquitination | [1] | 3690 | RIPGDELKWKFISDG | ubiquitination | [1] | 4398 | GILISQGKEAAFRKV | ubiquitination | [1] |
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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 | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |