RBX2_HUMAN
ID RBX2_HUMAN Reviewed; 113 AA.
AC Q9UBF6; A8K1H9; A8MTB5; C9JYL3; D3DNF7; D3DNF8; Q9BXN8; Q9Y5M7;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=RING-box protein 2;
DE Short=Rbx2;
DE AltName: Full=CKII beta-binding protein 1;
DE Short=CKBBP1;
DE AltName: Full=RING finger protein 7;
DE AltName: Full=Regulator of cullins 2;
DE AltName: Full=Sensitive to apoptosis gene protein;
GN Name=RNF7; Synonyms=RBX2, ROC2, SAG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=10512750; DOI=10.1006/bbrc.1999.1460;
RA Son M.-Y., Park J.-W., Kim Y.-S., Kang S.-W., Marshak D.R., Park W.,
RA Bae Y.-S.;
RT "Protein kinase CKII interacts with and phosphorylates the SAG protein
RT containing ring-H2 finger motif.";
RL Biochem. Biophys. Res. Commun. 263:743-748(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH CULLINS.
RX PubMed=10230407; DOI=10.1016/s1097-2765(00)80482-7;
RA Ohta T., Michel J.J., Schottelius A.J., Xiong Y.;
RT "ROC1, a homolog of APC11, represents a family of cullin partners with an
RT associated ubiquitin ligase activity.";
RL Mol. Cell 3:535-541(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, AND SUBCELLULAR
RP LOCATION.
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=11506706; DOI=10.1089/104454901750361488;
RA Swaroop M., Gosink M., Sun Y.;
RT "SAG/ROC2/Rbx2/Hrt2, a component of SCF E3 ubiquitin ligase: genomic
RT structure, a splicing variant, and two family pseudogenes.";
RL DNA Cell Biol. 20:425-434(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Corpus callosum, and Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Kidney;
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).
RN [10]
RP INTERACTION WITH CUL1, AND FUNCTION.
RX PubMed=10851089; DOI=10.1038/sj.onc.1203635;
RA Swaroop M., Wang Y., Miller P., Duan H., Jatkoe T., Madore S.J., Sun Y.;
RT "Yeast homolog of human SAG/ROC2/Rbx2/Hrt2 is essential for cell growth,
RT but not for germination: chip profiling implicates its role in cell cycle
RT regulation.";
RL Oncogene 19:2855-2866(2000).
RN [11]
RP PHOSPHORYLATION AT THR-10 BY CK2.
RX PubMed=12748192; DOI=10.1074/jbc.m302584200;
RA Kim Y.-S., Lee J.-Y., Son M.-Y., Park W., Bae Y.-S.;
RT "Phosphorylation of threonine 10 on CKBBP1/SAG/ROC2/Rbx2 by protein kinase
RT CKII promotes the degradation of IkappaBalpha and p27Kip1.";
RL J. Biol. Chem. 278:28462-28469(2003).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP INTERACTION WITH UBE2F.
RX PubMed=19250909; DOI=10.1016/j.molcel.2009.01.011;
RA Huang D.T., Ayrault O., Hunt H.W., Taherbhoy A.M., Duda D.M., Scott D.C.,
RA Borg L.A., Neale G., Murray P.J., Roussel M.F., Schulman B.A.;
RT "E2-RING expansion of the NEDD8 cascade confers specificity to cullin
RT modification.";
RL Mol. Cell 33:483-495(2009).
RN [14]
RP INTERACTION WITH DCUN1D1; DCUN1D2; DCUN1D3; DCUN1D4 AND DCUN1D5.
RX PubMed=26906416; DOI=10.1242/jcs.181784;
RA Keuss M.J., Thomas Y., Mcarthur R., Wood N.T., Knebel A., Kurz T.;
RT "Characterization of the mammalian family of DCN-type NEDD8 E3 ligases.";
RL J. Cell Sci. 129:1441-1454(2016).
RN [15]
RP STRUCTURE BY NMR OF 40-113.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RING domain of the human RING-box protein 2.";
RL Submitted (AUG-2007) to the PDB data bank.
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
CC (PubMed:10851089). CRLs complexes and ARIH1 collaborate in tandem to
CC mediate ubiquitination of target proteins, ARIH1 mediating addition of
CC the first ubiquitin on CRLs targets (By similarity). Through the RING-
CC type 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.
CC {ECO:0000250|UniProtKB:P62877, ECO:0000269|PubMed:10851089}.
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. Interacts with CSNK2B, the interaction is
CC not affected by phosphorylation by CK2. May also interact with DCUN1D1,
CC DCUN1D2, DCUN1D3, DCUN1D4 and DCUN1D5 (PubMed:26906416).
CC {ECO:0000269|PubMed:10230407, ECO:0000269|PubMed:10851089,
CC ECO:0000269|PubMed:19250909, ECO:0000269|PubMed:26906416}.
CC -!- INTERACTION:
CC Q9UBF6; Q93034: CUL5; NbExp=8; IntAct=EBI-398632, EBI-1057139;
CC Q9UBF6; Q9Y6K9: IKBKG; NbExp=3; IntAct=EBI-398632, EBI-81279;
CC Q9UBF6; P12004: PCNA; NbExp=3; IntAct=EBI-398632, EBI-358311;
CC Q9UBF6; P12504: vif; Xeno; NbExp=4; IntAct=EBI-398632, EBI-779991;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10082581}. Nucleus
CC {ECO:0000269|PubMed:10082581}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9UBF6-1; Sequence=Displayed;
CC Name=2; Synonyms=SAG-v;
CC IsoId=Q9UBF6-2; Sequence=VSP_008449;
CC Name=3;
CC IsoId=Q9UBF6-3; Sequence=VSP_041444;
CC Name=4;
CC IsoId=Q9UBF6-4; Sequence=VSP_044525;
CC -!- TISSUE SPECIFICITY: Expressed in heart, liver, skeletal muscle and
CC pancreas. At very low levels expressed in brain, placenta and lung.
CC {ECO:0000269|PubMed:10512750}.
CC -!- INDUCTION: By 1,10-phenanthroline. {ECO:0000269|PubMed:10082581}.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC ligase activity. It coordinates an additional third zinc ion.
CC -!- PTM: Phosphorylation by CK2 is required for efficient degradation of
CC NFKBIA and CDKN1B. {ECO:0000269|PubMed:12748192}.
CC -!- MISCELLANEOUS: [Isoform 2]: Inactive. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RING-box family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RNF7ID44108ch3q22.html";
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DR EMBL; AF164679; AAD55984.1; -; mRNA.
DR EMBL; AF142060; AAD30147.1; -; mRNA.
DR EMBL; AF092878; AAD25962.1; -; mRNA.
DR EMBL; AF312226; AAK37450.1; -; mRNA.
DR EMBL; BT007348; AAP36012.1; -; mRNA.
DR EMBL; AK289894; BAF82583.1; -; mRNA.
DR EMBL; DB272382; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC112771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78991.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78992.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78994.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78995.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78996.1; -; Genomic_DNA.
DR EMBL; BC005966; AAH05966.1; -; mRNA.
DR EMBL; BC008627; AAH08627.1; -; mRNA.
DR CCDS; CCDS3118.1; -. [Q9UBF6-1]
DR CCDS; CCDS43158.1; -. [Q9UBF6-3]
DR CCDS; CCDS56283.1; -. [Q9UBF6-4]
DR RefSeq; NP_001188299.1; NM_001201370.1. [Q9UBF6-4]
DR RefSeq; NP_055060.1; NM_014245.4. [Q9UBF6-1]
DR RefSeq; NP_899060.1; NM_183237.2. [Q9UBF6-3]
DR PDB; 2ECL; NMR; -; A=40-113.
DR PDB; 7ONI; EM; 3.40 A; R=5-113.
DR PDBsum; 2ECL; -.
DR PDBsum; 7ONI; -.
DR AlphaFoldDB; Q9UBF6; -.
DR BMRB; Q9UBF6; -.
DR SMR; Q9UBF6; -.
DR BioGRID; 114977; 121.
DR CORUM; Q9UBF6; -.
DR IntAct; Q9UBF6; 30.
DR MINT; Q9UBF6; -.
DR STRING; 9606.ENSP00000273480; -.
DR GlyGen; Q9UBF6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UBF6; -.
DR MetOSite; Q9UBF6; -.
DR PhosphoSitePlus; Q9UBF6; -.
DR BioMuta; RNF7; -.
DR DMDM; 37538003; -.
DR EPD; Q9UBF6; -.
DR jPOST; Q9UBF6; -.
DR MassIVE; Q9UBF6; -.
DR MaxQB; Q9UBF6; -.
DR PaxDb; Q9UBF6; -.
DR PeptideAtlas; Q9UBF6; -.
DR PRIDE; Q9UBF6; -.
DR ProteomicsDB; 12270; -.
DR ProteomicsDB; 83956; -. [Q9UBF6-1]
DR ProteomicsDB; 83957; -. [Q9UBF6-2]
DR ProteomicsDB; 83958; -. [Q9UBF6-3]
DR Antibodypedia; 18025; 193 antibodies from 32 providers.
DR DNASU; 9616; -.
DR Ensembl; ENST00000273480.4; ENSP00000273480.3; ENSG00000114125.14. [Q9UBF6-1]
DR Ensembl; ENST00000393000.3; ENSP00000376725.3; ENSG00000114125.14. [Q9UBF6-3]
DR Ensembl; ENST00000477012.5; ENSP00000419339.1; ENSG00000114125.14. [Q9UBF6-2]
DR Ensembl; ENST00000480908.1; ENSP00000419084.1; ENSG00000114125.14. [Q9UBF6-4]
DR GeneID; 9616; -.
DR KEGG; hsa:9616; -.
DR MANE-Select; ENST00000273480.4; ENSP00000273480.3; NM_014245.5; NP_055060.1.
DR UCSC; uc003euc.4; human. [Q9UBF6-1]
DR CTD; 9616; -.
DR DisGeNET; 9616; -.
DR GeneCards; RNF7; -.
DR HGNC; HGNC:10070; RNF7.
DR HPA; ENSG00000114125; Low tissue specificity.
DR MIM; 603863; gene.
DR neXtProt; NX_Q9UBF6; -.
DR OpenTargets; ENSG00000114125; -.
DR PharmGKB; PA34444; -.
DR VEuPathDB; HostDB:ENSG00000114125; -.
DR eggNOG; KOG2930; Eukaryota.
DR GeneTree; ENSGT00940000155481; -.
DR HOGENOM; CLU_115512_2_2_1; -.
DR InParanoid; Q9UBF6; -.
DR OMA; RQNNRCP; -.
DR OrthoDB; 1587140at2759; -.
DR PhylomeDB; Q9UBF6; -.
DR TreeFam; TF351049; -.
DR PathwayCommons; Q9UBF6; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9UBF6; -.
DR SIGNOR; Q9UBF6; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 9616; 46 hits in 1131 CRISPR screens.
DR ChiTaRS; RNF7; human.
DR EvolutionaryTrace; Q9UBF6; -.
DR GeneWiki; RNF7; -.
DR GenomeRNAi; 9616; -.
DR Pharos; Q9UBF6; Tbio.
DR PRO; PR:Q9UBF6; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9UBF6; protein.
DR Bgee; ENSG00000114125; Expressed in left adrenal gland and 195 other tissues.
DR ExpressionAtlas; Q9UBF6; baseline and differential.
DR Genevisible; Q9UBF6; HS.
DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; IDA:MGI.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; TAS:ProtInc.
DR GO; GO:0097602; F:cullin family protein binding; IDA:MGI.
DR GO; GO:0061663; F:NEDD8 ligase activity; IDA:UniProtKB.
DR GO; GO:0019788; F:NEDD8 transferase activity; TAS:Reactome.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR GO; GO:0045116; P:protein neddylation; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0051775; P:response to redox state; TAS:ProtInc.
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; Alternative splicing; Cytoplasm; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..113
FT /note="RING-box protein 2"
FT /id="PRO_0000056023"
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:0007744|PubMed:19413330"
FT MOD_RES 10
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000269|PubMed:12748192"
FT VAR_SEQ 57..113
FT /note="VMDACLRCQAENKQEDCVVVWGECNHSFHNCCMSLWVKQNNRCPLCQQDWVV
FT QRIGK -> MPVLDVKLKTNKRTVLWSGENVIIPSTTAACPCG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041444"
FT VAR_SEQ 59..74
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_044525"
FT VAR_SEQ 60..113
FT /note="ACLRCQAENKQEDCVVVWGECNHSFHNCCMSLWVKQNNRCPLCQQDWVVQRI
FT GK -> EGIGVRNWSEALNLINASEMGFDCRSGSTALAVPSVSLASHQPCLDDHR (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:11506706,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_008449"
FT CONFLICT 23
FT /note="K -> T (in Ref. 2; AAD30147)"
FT /evidence="ECO:0000305"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:7ONI"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:7ONI"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:7ONI"
FT HELIX 62..67
FT /evidence="ECO:0007829|PDB:7ONI"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:2ECL"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:7ONI"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2ECL"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:7ONI"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:7ONI"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:7ONI"
SQ SEQUENCE 113 AA; 12683 MW; CE1E6CAC940C8257 CRC64;
MADVEDGEET CALASHSGSS GSKSGGDKMF SLKKWNAVAM WSWDVECDTC AICRVQVMDA
CLRCQAENKQ EDCVVVWGEC NHSFHNCCMS LWVKQNNRCP LCQQDWVVQR IGK
