RBX2_MOUSE
ID RBX2_MOUSE Reviewed; 113 AA.
AC Q9WTZ1; Q3UKF8;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=RING-box protein 2;
DE Short=Rbx2;
DE AltName: Full=RING finger protein 7;
DE AltName: Full=Sensitive to apoptosis gene protein;
GN Name=Rnf7; Synonyms=Rbx2, Sag;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X CBA; TISSUE=Lung;
RX PubMed=10082581; DOI=10.1128/mcb.19.4.3145;
RA Duan H., Wang Y., Aviram M., Swaroop M., Loo J.A., Bian J., Tian Y.,
RA Mueller T., Bisgaier C.L., Sun Y.;
RT "SAG, a novel zinc RING finger protein that protects cells from apoptosis
RT induced by redox agents.";
RL Mol. Cell. Biol. 19:3145-3155(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
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 -!- FUNCTION: Probable component of the SCF (SKP1-CUL1-F-box protein) E3
CC ubiquitin ligase complex which mediates the ubiquitination and
CC subsequent proteasomal degradation of target proteins involved in cell
CC cycle progression, signal transduction and transcription (By
CC similarity). CRLs complexes and ARIH1 collaborate in tandem to mediate
CC ubiquitination of target proteins, ARIH1 mediating addition of the
CC first ubiquitin on CRLs targets (By similarity). Through the RING-type
CC zinc finger, seems to recruit the E2 ubiquitination enzyme to the
CC complex and brings it into close proximity to the substrate. Promotes
CC the neddylation of CUL5 via its interaction with UBE2F. May play a role
CC in protecting cells from apoptosis induced by redox agents (By
CC similarity). {ECO:0000250|UniProtKB:P62877,
CC ECO:0000250|UniProtKB:Q9UBF6}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Probable part of SCF complexes, which consist of SKP1, CUL1,
CC RNF7/RBX2 and a F-box protein. Interacts (preferentially) with CUL5.
CC Also interacts (with lower preference) with CUL1, CUL2, CUL3, CUL4A and
CC CUL4B. Interacts with UBE2F (By similarity). May also interact with
CC DCUN1D1, DCUN1D2, DCUN1D3, DCUN1D4 and DCUN1D5 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q15370}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC ligase activity. It coordinates an additional third zinc ion.
CC -!- SIMILARITY: Belongs to the RING-box family. {ECO:0000305}.
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DR EMBL; AF092877; AAD25961.1; -; mRNA.
DR EMBL; AK003248; BAB22666.1; -; mRNA.
DR EMBL; AK146030; BAE26843.1; -; mRNA.
DR EMBL; BC011127; AAH11127.1; -; mRNA.
DR CCDS; CCDS40730.1; -.
DR RefSeq; NP_001298064.1; NM_001311135.1.
DR RefSeq; NP_035409.1; NM_011279.3.
DR PDB; 6V9I; EM; 5.20 A; R=1-113.
DR PDBsum; 6V9I; -.
DR AlphaFoldDB; Q9WTZ1; -.
DR BMRB; Q9WTZ1; -.
DR SMR; Q9WTZ1; -.
DR BioGRID; 202921; 21.
DR IntAct; Q9WTZ1; 7.
DR MINT; Q9WTZ1; -.
DR STRING; 10090.ENSMUSP00000052856; -.
DR iPTMnet; Q9WTZ1; -.
DR PhosphoSitePlus; Q9WTZ1; -.
DR EPD; Q9WTZ1; -.
DR MaxQB; Q9WTZ1; -.
DR PaxDb; Q9WTZ1; -.
DR PeptideAtlas; Q9WTZ1; -.
DR PRIDE; Q9WTZ1; -.
DR ProteomicsDB; 255163; -.
DR DNASU; 19823; -.
DR Ensembl; ENSMUST00000057500; ENSMUSP00000052856; ENSMUSG00000051234.
DR GeneID; 19823; -.
DR KEGG; mmu:19823; -.
DR UCSC; uc009rcm.1; mouse.
DR CTD; 9616; -.
DR MGI; MGI:1337096; Rnf7.
DR VEuPathDB; HostDB:ENSMUSG00000051234; -.
DR eggNOG; KOG2930; Eukaryota.
DR GeneTree; ENSGT00940000155481; -.
DR HOGENOM; CLU_115512_2_2_1; -.
DR InParanoid; Q9WTZ1; -.
DR OMA; RQNNRCP; -.
DR OrthoDB; 1587140at2759; -.
DR PhylomeDB; Q9WTZ1; -.
DR TreeFam; TF351049; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 19823; 8 hits in 73 CRISPR screens.
DR ChiTaRS; Rnf7; mouse.
DR PRO; PR:Q9WTZ1; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9WTZ1; protein.
DR Bgee; ENSMUSG00000051234; Expressed in choroid plexus epithelium and 262 other tissues.
DR ExpressionAtlas; Q9WTZ1; baseline and differential.
DR Genevisible; Q9WTZ1; MM.
DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0097602; F:cullin family protein binding; ISO:MGI.
DR GO; GO:0061663; F:NEDD8 ligase activity; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IDA:MGI.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IMP:MGI.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IDA:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
DR GO; GO:0045116; P:protein neddylation; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0021942; P:radial glia guided migration of Purkinje cell; IMP:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR024766; Znf_RING_H2.
DR Pfam; PF12678; zf-rbx1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UBF6"
FT CHAIN 2..113
FT /note="RING-box protein 2"
FT /id="PRO_0000056024"
FT ZN_FING 61..103
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBF6"
SQ SEQUENCE 113 AA; 12707 MW; D6FA02EE6038FDD2 CRC64;
MADVEDGEEP CVLSSHSGSA GSKSGGDKMF SLKKWNAVAM WSWDVECDTC AICRVQVMDA
CLRCQAENKQ EDCVVVWGEC NHSFHNCCMS LWVKQNNRCP LCQQDWVVQR IGK
