UniProt: Q498D8

Database: UniProt
Entry: Q498D8_RAT

LinkDB:  Q498D8_RAT 
Original site:  Q498D8_RAT

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Ontology (42)   
   GO (42)   
Gene (3)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   RGD (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (5)   
   InterPro (3)   
   Pfam (1)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (53)   

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ID   Q498D8_RAT              Unreviewed;       108 AA.
AC   Q498D8;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 156.
DE   SubName: Full=Ring-box 1 {ECO:0000313|EMBL:AAI00259.1};
GN   Name=Rbx1 {ECO:0000313|EMBL:AAI00259.1, ECO:0000313|RGD:1308453};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|EMBL:AAI00259.1};
RN   [1] {ECO:0000313|EMBL:AAI00259.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta {ECO:0000313|EMBL:AAI00259.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the RING-box family.
CC       {ECO:0000256|ARBA:ARBA00009273}.
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DR   EMBL; BC100258; AAI00259.1; -; mRNA.
DR   RefSeq; NP_001029307.1; NM_001034135.1.
DR   AlphaFoldDB; Q498D8; -.
DR   SMR; Q498D8; -.
DR   STRING; 10116.ENSRNOP00000069049; -.
DR   PhosphoSitePlus; Q498D8; -.
DR   PaxDb; 10116-ENSRNOP00000025979; -.
DR   GeneID; 300084; -.
DR   KEGG; rno:300084; -.
DR   UCSC; RGD:1308453; rat.
DR   AGR; RGD:1308453; -.
DR   CTD; 9978; -.
DR   RGD; 1308453; Rbx1.
DR   VEuPathDB; HostDB:ENSRNOG00000058914; -.
DR   eggNOG; KOG2930; Eukaryota.
DR   HOGENOM; CLU_115512_2_1_1; -.
DR   InParanoid; Q498D8; -.
DR   OrthoDB; 3546417at2759; -.
DR   TreeFam; TF105503; -.
DR   Reactome; R-RNO-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR   Reactome; R-RNO-1170546; Prolactin receptor signaling.
DR   Reactome; R-RNO-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR   Reactome; R-RNO-195253; Degradation of beta-catenin by the destruction complex.
DR   Reactome; R-RNO-4641258; Degradation of DVL.
DR   Reactome; R-RNO-5610780; Degradation of GLI1 by the proteasome.
DR   Reactome; R-RNO-5610785; GLI3 is processed to GLI3R by the proteasome.
DR   Reactome; R-RNO-5632684; Hedgehog 'on' state.
DR   Reactome; R-RNO-5658442; Regulation of RAS by GAPs.
DR   Reactome; R-RNO-5696394; DNA Damage Recognition in GG-NER.
DR   Reactome; R-RNO-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-RNO-5696400; Dual Incision in GG-NER.
DR   Reactome; R-RNO-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-RNO-6782135; Dual incision in TC-NER.
DR   Reactome; R-RNO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-RNO-68949; Orc1 removal from chromatin.
DR   Reactome; R-RNO-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-RNO-8951664; Neddylation.
DR   Reactome; R-RNO-9020702; Interleukin-1 signaling.
DR   Reactome; R-RNO-9755511; KEAP1-NFE2L2 pathway.
DR   Reactome; R-RNO-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR   Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   Bgee; ENSRNOG00000058914; Expressed in thymus and 20 other cell types or tissues.
DR   GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISO:RGD.
DR   GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISO:RGD.
DR   GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; ISO:RGD.
DR   GO; GO:0031465; C:Cul4B-RING E3 ubiquitin ligase complex; ISO:RGD.
DR   GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; ISO:RGD.
DR   GO; GO:0031467; C:Cul7-RING ubiquitin ligase complex; ISO:RGD.
DR   GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; ISO:RGD.
DR   GO; GO:0030891; C:VCB complex; IDA:RGD.
DR   GO; GO:0097602; F:cullin family protein binding; ISO:RGD.
DR   GO; GO:0060090; F:molecular adaptor activity; ISO:RGD.
DR   GO; GO:0061663; F:NEDD8 ligase activity; ISO:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:RGD.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR   GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; ISO:RGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0071230; P:cellular response to amino acid stimulus; ISO:RGD.
DR   GO; GO:0034644; P:cellular response to UV; ISO:RGD.
DR   GO; GO:0006974; P:DNA damage response; ISO:RGD.
DR   GO; GO:0032480; P:negative regulation of type I interferon production; ISO:RGD.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISO:RGD.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
DR   GO; GO:1902499; P:positive regulation of protein autoubiquitination; ISO:RGD.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:RGD.
DR   GO; GO:1904263; P:positive regulation of TORC1 signaling; ISO:RGD.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:RGD.
DR   GO; GO:0030163; P:protein catabolic process; ISO:RGD.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; ISO:RGD.
DR   GO; GO:0006513; P:protein monoubiquitination; ISO:RGD.
DR   GO; GO:0045116; P:protein neddylation; ISO:RGD.
DR   GO; GO:0000209; P:protein polyubiquitination; ISO:RGD.
DR   GO; GO:0016567; P:protein ubiquitination; ISO:RGD.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
DR   GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR   GO; GO:0042110; P:T cell activation; ISO:RGD.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:RGD.
DR   GO; GO:0140627; P:ubiquitin-dependent protein catabolic process via the C-end degron rule pathway; ISO:RGD.
DR   CDD; cd16485; mRING-H2-C3H2C2D_RBX1; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR024766; Znf_RING_H2.
DR   PANTHER; PTHR11210:SF2; E3 UBIQUITIN-PROTEIN LIGASE RBX1; 1.
DR   PANTHER; PTHR11210; RING BOX; 1.
DR   Pfam; PF12678; zf-rbx1; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
SQ   SEQUENCE   108 AA;  12274 MW;  30FC5ADF66096C0E CRC64;
     MAAAMDVDTP SGTNSGAGKK RFEVKKWNAV ALWAWDIVVD NCAICRNHIM DLCIECQANQ
     ASATSEECTV AWGVCNHAFH FHCISRWLKT RQVCPLDNRE WEFQKYGH
//

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