ID H0VPT0_CAVPO Unreviewed; 493 AA.
AC H0VPT0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=RING-type E3 ubiquitin transferase RAD18 {ECO:0000256|ARBA:ARBA00031783};
GN Name=RAD18 {ECO:0000313|Ensembl:ENSCPOP00000012519.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000012519.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000012519.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000012519.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RAD18 family.
CC {ECO:0000256|ARBA:ARBA00009506}.
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DR EMBL; AAKN02049226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02049227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02049228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_013001786.1; XM_013146332.1.
DR RefSeq; XP_013001787.1; XM_013146333.1.
DR AlphaFoldDB; H0VPT0; -.
DR STRING; 10141.ENSCPOP00000012519; -.
DR Ensembl; ENSCPOT00000014031.3; ENSCPOP00000012519.3; ENSCPOG00000013890.4.
DR GeneID; 100720939; -.
DR KEGG; cpoc:100720939; -.
DR CTD; 56852; -.
DR VEuPathDB; HostDB:ENSCPOG00000013890; -.
DR eggNOG; KOG0287; Eukaryota.
DR GeneTree; ENSGT00390000011230; -.
DR HOGENOM; CLU_028491_0_0_1; -.
DR InParanoid; H0VPT0; -.
DR OMA; IPNTGPR; -.
DR OrthoDB; 6177at2759; -.
DR TreeFam; TF101214; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000013890; Expressed in liver and 13 other cell types or tissues.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0042405; C:nuclear inclusion body; IEA:Ensembl.
DR GO; GO:0005657; C:replication fork; IEA:Ensembl.
DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0000403; F:Y-form DNA binding; IEA:Ensembl.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; IEA:Ensembl.
DR GO; GO:0006301; P:postreplication repair; IEA:InterPro.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR GO; GO:0006513; P:protein monoubiquitination; IEA:InterPro.
DR CDD; cd16529; RING-HC_RAD18; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 1.10.720.30; SAP domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039577; Rad18.
DR InterPro; IPR006642; Rad18_UBZ4.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR14134; E3 UBIQUITIN-PROTEIN LIGASE RAD18; 1.
DR PANTHER; PTHR14134:SF2; E3 UBIQUITIN-PROTEIN LIGASE RAD18; 1.
DR Pfam; PF02037; SAP; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00513; SAP; 1.
DR SMART; SM00734; ZnF_Rad18; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF68906; SAP domain; 1.
DR PROSITE; PS50800; SAP; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51908; ZF_UBZ4; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PROSITE-
KW ProRule:PRU01256};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|PROSITE-
KW ProRule:PRU01256}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 25..63
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 200..227
FT /note="UBZ4-type"
FT /evidence="ECO:0000259|PROSITE:PS51908"
FT DOMAIN 247..281
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT REGION 414..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 296..347
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 424..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 493 AA; 55955 MW; 6C8110FFCE60D533 CRC64;
MEPLDEPRWP PGLAVMRTVD DLLRCGICFE YFNIAMIIPQ CSHNYCSLCI RKFLSYKTQC
PTCCVTVTEP DLKNNRLLDE LVKSLKLARN HLLQFALESL PISPASSSKK LAVKVQSPGA
FKHSLKQGNT LMDKFLIRET GGSTSELLIK ENDSKFSHGR EASPSIETKD TCFVENMTPG
YSDTNRPEIP STSFLKQVVK VDCPVCSVSI PENHINKHLD SCLSREEKKD SLRSSAQKRK
QLPKTVYNLL SDRDLKKKLK EHGLSTHGNK QQLIKRHQEF VHMYNAQCDA LHPKSAAEIV
EEIENMEKTR MRLEASKLNE SAMAFTKDQT EEEIDEIHRK YRKKHRNEFQ LLVDQAKKGY
KKTGGVLKDK LMKKDESAEK MLSVCLDDTV KFSGVAPTAD HFHPSQLGSA LKLEPERADD
SSSCTDIQEV SSESDSCNSS SSDIIRDLLE EEEAWEAAHR NDLQDVETSP RLNRRTRAAE
SAETEPRNKR NRN
//
