Full text data of RNF7
RNF7
(RBX2, ROC2, SAG)
[Confidence: low (only semi-automatic identification from reviews)]
RING-box protein 2; Rbx2 (CKII beta-binding protein 1; CKBBP1; RING finger protein 7; Regulator of cullins 2; Sensitive to apoptosis gene protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
RING-box protein 2; Rbx2 (CKII beta-binding protein 1; CKBBP1; RING finger protein 7; Regulator of cullins 2; Sensitive to apoptosis gene protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UBF6
ID RBX2_HUMAN Reviewed; 113 AA.
AC Q9UBF6; A8K1H9; A8MTB5; C9JYL3; D3DNF7; D3DNF8; Q9BXN8; Q9Y5M7;
read moreDT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 117.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT an 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;
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
RT apoptosis 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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA 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.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Sun Y.;
RT "Yeast homolog of human SAG/ROC2/Rbx2/Hrt2 is essential for cell
RT growth, but not for germination: chip profiling implicates its role in
RT cell cycle 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
RT kinase 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, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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.,
RA Scott D.C., Borg L.A., Neale G., Murray P.J., Roussel M.F.,
RA 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 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
RT 2.";
RL Submitted (AUG-2007) to the PDB data bank.
CC -!- FUNCTION: Probable component of the SCF (SKP1-CUL1-F-box protein)
CC E3 ubiquitin ligase complex which mediates the ubiquitination and
CC subsequent proteasomal degradation of target proteins involved in
CC cell cycle progression, signal transduction and transcription.
CC Through the RING-type zinc finger, seems to recruit the E2
CC ubiquitination enzyme to the complex and brings it into close
CC proximity to the substrate. Promotes the neddylation of CUL5 via
CC its interaction with UBE2F. May play a role in protecting cells
CC from apoptosis induced by redox agents.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Probable part of SCF complexes, which consist of SKP1,
CC CUL1, RNF7/RBX2 and a F-box protein. Interacts (preferentially)
CC with CUL5. Also interacts (with lower preference) with CUL1, CUL2,
CC CUL3, CUL4A and CUL4B. Interacts with UBE2F. Interacts with
CC CSNK2B, the interaction is not affected by phosphorylation by CK2.
CC -!- INTERACTION:
CC Q96Q27:ASB2; NbExp=2; IntAct=EBI-398632, EBI-2880677;
CC Q9Y6K9:IKBKG; NbExp=3; IntAct=EBI-398632, EBI-81279;
CC P12504:vif (xeno); NbExp=4; IntAct=EBI-398632, EBI-779991;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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 Note=Inactive;
CC Name=3;
CC IsoId=Q9UBF6-3; Sequence=VSP_041444;
CC Name=4;
CC IsoId=Q9UBF6-4; Sequence=VSP_044525;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in heart, liver, skeletal muscle and
CC pancreas. At very low levels expressed in brain, placenta and
CC lung.
CC -!- INDUCTION: By 1,10-phenanthroline.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for
CC ubiquitin ligase activity. It coordinates an additional third zinc
CC ion.
CC -!- PTM: Phosphorylation by CK2 is required for efficient degradation
CC of NFKBIA and CDKN1B.
CC -!- SIMILARITY: Belongs to the RING-box family.
CC -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and 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 RefSeq; NP_001188299.1; NM_001201370.1.
DR RefSeq; NP_055060.1; NM_014245.4.
DR RefSeq; NP_899060.1; NM_183237.2.
DR UniGene; Hs.134623; -.
DR PDB; 2ECL; NMR; -; A=40-113.
DR PDBsum; 2ECL; -.
DR ProteinModelPortal; Q9UBF6; -.
DR SMR; Q9UBF6; 40-113.
DR IntAct; Q9UBF6; 28.
DR MINT; MINT-1470812; -.
DR STRING; 9606.ENSP00000273480; -.
DR PhosphoSite; Q9UBF6; -.
DR DMDM; 37538003; -.
DR PaxDb; Q9UBF6; -.
DR PRIDE; Q9UBF6; -.
DR DNASU; 9616; -.
DR Ensembl; ENST00000273480; ENSP00000273480; ENSG00000114125.
DR Ensembl; ENST00000393000; ENSP00000376725; ENSG00000114125.
DR Ensembl; ENST00000477012; ENSP00000419339; ENSG00000114125.
DR Ensembl; ENST00000480908; ENSP00000419084; ENSG00000114125.
DR GeneID; 9616; -.
DR KEGG; hsa:9616; -.
DR UCSC; uc003eud.3; human.
DR CTD; 9616; -.
DR GeneCards; GC03P141457; -.
DR HGNC; HGNC:10070; RNF7.
DR HPA; HPA036995; -.
DR MIM; 603863; gene.
DR neXtProt; NX_Q9UBF6; -.
DR PharmGKB; PA34444; -.
DR eggNOG; COG5194; -.
DR HOVERGEN; HBG001507; -.
DR InParanoid; Q9UBF6; -.
DR KO; K10611; -.
DR OMA; DICAICR; -.
DR OrthoDB; EOG7CG721; -.
DR PhylomeDB; Q9UBF6; -.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; Q9UBF6; -.
DR GeneWiki; RNF7; -.
DR GenomeRNAi; 9616; -.
DR NextBio; 36073; -.
DR PRO; PR:Q9UBF6; -.
DR ArrayExpress; Q9UBF6; -.
DR Bgee; Q9UBF6; -.
DR CleanEx; HS_RNF7; -.
DR CleanEx; HS_SAG; -.
DR Genevestigator; Q9UBF6; -.
DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; TAS:ProtInc.
DR GO; GO:0019788; F:NEDD8 ligase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; TAS:ProtInc.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc.
DR GO; GO:0045116; P:protein neddylation; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0051775; P:response to redox state; TAS:ProtInc.
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 SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 113 RING-box protein 2.
FT /FTId=PRO_0000056023.
FT ZN_FING 61 103 RING-type.
FT METAL 50 50 Zinc 1 (By similarity).
FT METAL 53 53 Zinc 1 (By similarity).
FT METAL 61 61 Zinc 3 (By similarity).
FT METAL 64 64 Zinc 3 (By similarity).
FT METAL 73 73 Zinc 3 (By similarity).
FT METAL 80 80 Zinc 2 (By similarity).
FT METAL 82 82 Zinc 2 (By similarity).
FT METAL 85 85 Zinc 1 (By similarity).
FT METAL 87 87 Zinc 3 (By similarity).
FT METAL 88 88 Zinc 1 (By similarity).
FT METAL 99 99 Zinc 2 (By similarity).
FT METAL 102 102 Zinc 2 (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 10 10 Phosphothreonine; by CK2.
FT VAR_SEQ 57 113 VMDACLRCQAENKQEDCVVVWGECNHSFHNCCMSLWVKQNN
FT RCPLCQQDWVVQRIGK -> MPVLDVKLKTNKRTVLWSGEN
FT VIIPSTTAACPCG (in isoform 3).
FT /FTId=VSP_041444.
FT VAR_SEQ 59 74 Missing (in isoform 4).
FT /FTId=VSP_044525.
FT VAR_SEQ 60 113 ACLRCQAENKQEDCVVVWGECNHSFHNCCMSLWVKQNNRCP
FT LCQQDWVVQRIGK -> EGIGVRNWSEALNLINASEMGFDC
FT RSGSTALAVPSVSLASHQPCLDDHR (in isoform 2).
FT /FTId=VSP_008449.
FT CONFLICT 23 23 K -> T (in Ref. 2; AAD30147).
FT TURN 51 54
FT HELIX 64 67
FT TURN 70 72
FT STRAND 75 78
FT STRAND 83 85
FT HELIX 86 92
FT TURN 93 95
FT TURN 100 102
FT STRAND 108 112
SQ SEQUENCE 113 AA; 12683 MW; CE1E6CAC940C8257 CRC64;
MADVEDGEET CALASHSGSS GSKSGGDKMF SLKKWNAVAM WSWDVECDTC AICRVQVMDA
CLRCQAENKQ EDCVVVWGEC NHSFHNCCMS LWVKQNNRCP LCQQDWVVQR IGK
//
ID RBX2_HUMAN Reviewed; 113 AA.
AC Q9UBF6; A8K1H9; A8MTB5; C9JYL3; D3DNF7; D3DNF8; Q9BXN8; Q9Y5M7;
read moreDT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 117.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT an 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;
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
RT apoptosis 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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA 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.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Sun Y.;
RT "Yeast homolog of human SAG/ROC2/Rbx2/Hrt2 is essential for cell
RT growth, but not for germination: chip profiling implicates its role in
RT cell cycle 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
RT kinase 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, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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.,
RA Scott D.C., Borg L.A., Neale G., Murray P.J., Roussel M.F.,
RA 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 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
RT 2.";
RL Submitted (AUG-2007) to the PDB data bank.
CC -!- FUNCTION: Probable component of the SCF (SKP1-CUL1-F-box protein)
CC E3 ubiquitin ligase complex which mediates the ubiquitination and
CC subsequent proteasomal degradation of target proteins involved in
CC cell cycle progression, signal transduction and transcription.
CC Through the RING-type zinc finger, seems to recruit the E2
CC ubiquitination enzyme to the complex and brings it into close
CC proximity to the substrate. Promotes the neddylation of CUL5 via
CC its interaction with UBE2F. May play a role in protecting cells
CC from apoptosis induced by redox agents.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Probable part of SCF complexes, which consist of SKP1,
CC CUL1, RNF7/RBX2 and a F-box protein. Interacts (preferentially)
CC with CUL5. Also interacts (with lower preference) with CUL1, CUL2,
CC CUL3, CUL4A and CUL4B. Interacts with UBE2F. Interacts with
CC CSNK2B, the interaction is not affected by phosphorylation by CK2.
CC -!- INTERACTION:
CC Q96Q27:ASB2; NbExp=2; IntAct=EBI-398632, EBI-2880677;
CC Q9Y6K9:IKBKG; NbExp=3; IntAct=EBI-398632, EBI-81279;
CC P12504:vif (xeno); NbExp=4; IntAct=EBI-398632, EBI-779991;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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 Note=Inactive;
CC Name=3;
CC IsoId=Q9UBF6-3; Sequence=VSP_041444;
CC Name=4;
CC IsoId=Q9UBF6-4; Sequence=VSP_044525;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Expressed in heart, liver, skeletal muscle and
CC pancreas. At very low levels expressed in brain, placenta and
CC lung.
CC -!- INDUCTION: By 1,10-phenanthroline.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for
CC ubiquitin ligase activity. It coordinates an additional third zinc
CC ion.
CC -!- PTM: Phosphorylation by CK2 is required for efficient degradation
CC of NFKBIA and CDKN1B.
CC -!- SIMILARITY: Belongs to the RING-box family.
CC -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RNF7ID44108ch3q22.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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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 RefSeq; NP_001188299.1; NM_001201370.1.
DR RefSeq; NP_055060.1; NM_014245.4.
DR RefSeq; NP_899060.1; NM_183237.2.
DR UniGene; Hs.134623; -.
DR PDB; 2ECL; NMR; -; A=40-113.
DR PDBsum; 2ECL; -.
DR ProteinModelPortal; Q9UBF6; -.
DR SMR; Q9UBF6; 40-113.
DR IntAct; Q9UBF6; 28.
DR MINT; MINT-1470812; -.
DR STRING; 9606.ENSP00000273480; -.
DR PhosphoSite; Q9UBF6; -.
DR DMDM; 37538003; -.
DR PaxDb; Q9UBF6; -.
DR PRIDE; Q9UBF6; -.
DR DNASU; 9616; -.
DR Ensembl; ENST00000273480; ENSP00000273480; ENSG00000114125.
DR Ensembl; ENST00000393000; ENSP00000376725; ENSG00000114125.
DR Ensembl; ENST00000477012; ENSP00000419339; ENSG00000114125.
DR Ensembl; ENST00000480908; ENSP00000419084; ENSG00000114125.
DR GeneID; 9616; -.
DR KEGG; hsa:9616; -.
DR UCSC; uc003eud.3; human.
DR CTD; 9616; -.
DR GeneCards; GC03P141457; -.
DR HGNC; HGNC:10070; RNF7.
DR HPA; HPA036995; -.
DR MIM; 603863; gene.
DR neXtProt; NX_Q9UBF6; -.
DR PharmGKB; PA34444; -.
DR eggNOG; COG5194; -.
DR HOVERGEN; HBG001507; -.
DR InParanoid; Q9UBF6; -.
DR KO; K10611; -.
DR OMA; DICAICR; -.
DR OrthoDB; EOG7CG721; -.
DR PhylomeDB; Q9UBF6; -.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; Q9UBF6; -.
DR GeneWiki; RNF7; -.
DR GenomeRNAi; 9616; -.
DR NextBio; 36073; -.
DR PRO; PR:Q9UBF6; -.
DR ArrayExpress; Q9UBF6; -.
DR Bgee; Q9UBF6; -.
DR CleanEx; HS_RNF7; -.
DR CleanEx; HS_SAG; -.
DR Genevestigator; Q9UBF6; -.
DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; TAS:ProtInc.
DR GO; GO:0019788; F:NEDD8 ligase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; TAS:ProtInc.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc.
DR GO; GO:0045116; P:protein neddylation; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0051775; P:response to redox state; TAS:ProtInc.
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 SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 113 RING-box protein 2.
FT /FTId=PRO_0000056023.
FT ZN_FING 61 103 RING-type.
FT METAL 50 50 Zinc 1 (By similarity).
FT METAL 53 53 Zinc 1 (By similarity).
FT METAL 61 61 Zinc 3 (By similarity).
FT METAL 64 64 Zinc 3 (By similarity).
FT METAL 73 73 Zinc 3 (By similarity).
FT METAL 80 80 Zinc 2 (By similarity).
FT METAL 82 82 Zinc 2 (By similarity).
FT METAL 85 85 Zinc 1 (By similarity).
FT METAL 87 87 Zinc 3 (By similarity).
FT METAL 88 88 Zinc 1 (By similarity).
FT METAL 99 99 Zinc 2 (By similarity).
FT METAL 102 102 Zinc 2 (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 10 10 Phosphothreonine; by CK2.
FT VAR_SEQ 57 113 VMDACLRCQAENKQEDCVVVWGECNHSFHNCCMSLWVKQNN
FT RCPLCQQDWVVQRIGK -> MPVLDVKLKTNKRTVLWSGEN
FT VIIPSTTAACPCG (in isoform 3).
FT /FTId=VSP_041444.
FT VAR_SEQ 59 74 Missing (in isoform 4).
FT /FTId=VSP_044525.
FT VAR_SEQ 60 113 ACLRCQAENKQEDCVVVWGECNHSFHNCCMSLWVKQNNRCP
FT LCQQDWVVQRIGK -> EGIGVRNWSEALNLINASEMGFDC
FT RSGSTALAVPSVSLASHQPCLDDHR (in isoform 2).
FT /FTId=VSP_008449.
FT CONFLICT 23 23 K -> T (in Ref. 2; AAD30147).
FT TURN 51 54
FT HELIX 64 67
FT TURN 70 72
FT STRAND 75 78
FT STRAND 83 85
FT HELIX 86 92
FT TURN 93 95
FT TURN 100 102
FT STRAND 108 112
SQ SEQUENCE 113 AA; 12683 MW; CE1E6CAC940C8257 CRC64;
MADVEDGEET CALASHSGSS GSKSGGDKMF SLKKWNAVAM WSWDVECDTC AICRVQVMDA
CLRCQAENKQ EDCVVVWGEC NHSFHNCCMS LWVKQNNRCP LCQQDWVVQR IGK
//
MIM
603863
*RECORD*
*FIELD* NO
603863
*FIELD* TI
*603863 RING FINGER PROTEIN 7; RNF7
;;REGULATOR OF CULLINS 2; ROC2;;
RBX2;;
SENSITIVE TO APOPTOSIS GENE; SAG
read more*FIELD* TX
CLONING
Reactive oxygen species (ROS), a group of very reactive, short-lived
chemicals produced during normal respiratory processes or after
oxidative insults, may mediate apoptosis. Metal chelators and metal ions
are redox-sensitive agents that can mediate ROS generation. The metal
chelator 1,10-phenanthroline (OP) induces or suppresses apoptosis in a
cell line-dependent manner. Using differential display, Duan et al.
(1999) isolated mouse cDNAs associated with OP-induced apoptosis. One
cDNA encoded Gss (601002), and the other encoded a novel protein
produced by a gene that they designated Sag. The authors used the mouse
Sag cDNA to identify a HeLa cell cDNA corresponding to human SAG. The
predicted 113-amino acid human SAG protein is 97% identical to mouse
Sag. The C-terminal half of SAG consists of a zinc RING finger domain.
Northern blot analysis revealed that SAG was ubiquitously expressed,
with the highest levels in heart, skeletal muscle, and testis.
Immunofluorescent staining indicated that SAG localized in both the
cytoplasm and nuclei of mammalian cells.
By searching databases for homologs of ROC1 (RBX1; 603814), followed by
PCR of a HeLa cell cDNA library, Ohta et al. (1999) cloned RNF7, which
they called ROC2. The deduced 85-amino acid ROC2 protein shares 51%
identity with ROC1 and 35% identity with human APC11 (ANAPC11; 614534),
a subunit of the anaphase-promoting complex. Both ROC proteins are
highly evolutionarily conserved. ROC1 and ROC2 both contain a RING
finger domain and are rich in tryptophan.
GENE FUNCTION
Duan et al. (1999) found that, in vitro, recombinant human SAG bound to
zinc and copper metal ions and prevented lipid peroxidation induced by
copper or a free radical generator. When overexpressed in human cell
lines, SAG protected cells from apoptosis induced by redox agents such
as OP. Duan et al. (1999) concluded that SAG is a cellular protective
molecule that appears to act as an antioxidant to inhibit apoptosis
induced by metal ions and ROS.
By yeast 2-hybrid and immunoprecipitation analyses, Ohta et al. (1999)
found that human ROC1 and ROC2 commonly interacted with all cullins (see
603134). They concluded that combinations of ROC/APC11 and cullin
proteins potentially constitute a wide variety of ubiquitin ligases.
MAPPING
By fluorescence in situ hybridization, Duan et al. (1999) mapped the SAG
gene to chromosome 3q22-q24.
*FIELD* RF
1. Duan, H.; Wang, Y.; Aviram, M.; Swaroop, M.; Loo, J. A.; Bian,
J.; Tian, Y.; Mueller, T.; Bisgaier, C. L.; Sun, Y.: SAG, a novel
zinc RING finger protein that protects cells from apoptosis induced
by redox agents. Molec. Cell. Biol. 19: 3145-3155, 1999.
2. Ohta, T.; Michel, J. J.; Schottelius, A. J.; Xiong, Y.: ROC1,
a homolog of APC11, represents a family of cullin partners with an
associated ubiquitin ligase activity. Molec. Cell 3: 535-541, 1999.
*FIELD* CN
Matthew B. Gross - updated: 3/16/2012
Patricia A. Hartz - updated: 2/10/2012
Rebekah S. Rasooly - updated: 6/22/1999
*FIELD* CD
Stylianos E. Antonarakis: 6/2/1999
*FIELD* ED
mgross: 01/30/2013
mgross: 3/16/2012
mgross: 3/15/2012
terry: 2/10/2012
jlewis: 6/22/1999
jlewis: 6/21/1999
mgross: 6/3/1999
mgross: 6/2/1999
*RECORD*
*FIELD* NO
603863
*FIELD* TI
*603863 RING FINGER PROTEIN 7; RNF7
;;REGULATOR OF CULLINS 2; ROC2;;
RBX2;;
SENSITIVE TO APOPTOSIS GENE; SAG
read more*FIELD* TX
CLONING
Reactive oxygen species (ROS), a group of very reactive, short-lived
chemicals produced during normal respiratory processes or after
oxidative insults, may mediate apoptosis. Metal chelators and metal ions
are redox-sensitive agents that can mediate ROS generation. The metal
chelator 1,10-phenanthroline (OP) induces or suppresses apoptosis in a
cell line-dependent manner. Using differential display, Duan et al.
(1999) isolated mouse cDNAs associated with OP-induced apoptosis. One
cDNA encoded Gss (601002), and the other encoded a novel protein
produced by a gene that they designated Sag. The authors used the mouse
Sag cDNA to identify a HeLa cell cDNA corresponding to human SAG. The
predicted 113-amino acid human SAG protein is 97% identical to mouse
Sag. The C-terminal half of SAG consists of a zinc RING finger domain.
Northern blot analysis revealed that SAG was ubiquitously expressed,
with the highest levels in heart, skeletal muscle, and testis.
Immunofluorescent staining indicated that SAG localized in both the
cytoplasm and nuclei of mammalian cells.
By searching databases for homologs of ROC1 (RBX1; 603814), followed by
PCR of a HeLa cell cDNA library, Ohta et al. (1999) cloned RNF7, which
they called ROC2. The deduced 85-amino acid ROC2 protein shares 51%
identity with ROC1 and 35% identity with human APC11 (ANAPC11; 614534),
a subunit of the anaphase-promoting complex. Both ROC proteins are
highly evolutionarily conserved. ROC1 and ROC2 both contain a RING
finger domain and are rich in tryptophan.
GENE FUNCTION
Duan et al. (1999) found that, in vitro, recombinant human SAG bound to
zinc and copper metal ions and prevented lipid peroxidation induced by
copper or a free radical generator. When overexpressed in human cell
lines, SAG protected cells from apoptosis induced by redox agents such
as OP. Duan et al. (1999) concluded that SAG is a cellular protective
molecule that appears to act as an antioxidant to inhibit apoptosis
induced by metal ions and ROS.
By yeast 2-hybrid and immunoprecipitation analyses, Ohta et al. (1999)
found that human ROC1 and ROC2 commonly interacted with all cullins (see
603134). They concluded that combinations of ROC/APC11 and cullin
proteins potentially constitute a wide variety of ubiquitin ligases.
MAPPING
By fluorescence in situ hybridization, Duan et al. (1999) mapped the SAG
gene to chromosome 3q22-q24.
*FIELD* RF
1. Duan, H.; Wang, Y.; Aviram, M.; Swaroop, M.; Loo, J. A.; Bian,
J.; Tian, Y.; Mueller, T.; Bisgaier, C. L.; Sun, Y.: SAG, a novel
zinc RING finger protein that protects cells from apoptosis induced
by redox agents. Molec. Cell. Biol. 19: 3145-3155, 1999.
2. Ohta, T.; Michel, J. J.; Schottelius, A. J.; Xiong, Y.: ROC1,
a homolog of APC11, represents a family of cullin partners with an
associated ubiquitin ligase activity. Molec. Cell 3: 535-541, 1999.
*FIELD* CN
Matthew B. Gross - updated: 3/16/2012
Patricia A. Hartz - updated: 2/10/2012
Rebekah S. Rasooly - updated: 6/22/1999
*FIELD* CD
Stylianos E. Antonarakis: 6/2/1999
*FIELD* ED
mgross: 01/30/2013
mgross: 3/16/2012
mgross: 3/15/2012
terry: 2/10/2012
jlewis: 6/22/1999
jlewis: 6/21/1999
mgross: 6/3/1999
mgross: 6/2/1999