Full text data of RNF126
RNF126
[Confidence: low (only semi-automatic identification from reviews)]
E3 ubiquitin-protein ligase RNF126; 6.3.2.- (RING finger protein 126)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
E3 ubiquitin-protein ligase RNF126; 6.3.2.- (RING finger protein 126)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9BV68
ID RN126_HUMAN Reviewed; 326 AA.
AC Q9BV68; Q9NWX1;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=E3 ubiquitin-protein ligase RNF126;
DE EC=6.3.2.-;
DE AltName: Full=RING finger protein 126;
GN Name=RNF126;
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 [LARGE SCALE MRNA] (ISOFORM 2).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Placenta;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-5, MASS SPECTROMETRY, AND CLEAVAGE OF INITIATOR
RP METHIONINE.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [5]
RP FUNCTION, AUTOUBIQUITINATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP CYS-229 AND CYS-232.
RX PubMed=23026136; DOI=10.1158/0008-5472.CAN-12-0562;
RA Zhi X., Zhao D., Wang Z., Zhou Z., Wang C., Chen W., Liu R., Chen C.;
RT "E3 ubiquitin ligase RNF126 promotes cancer cell proliferation by
RT targeting the tumor suppressor p21 for ubiquitin-mediated
RT degradation.";
RL Cancer Res. 73:385-394(2013).
CC -!- FUNCTION: E3 ubiquitin-protein ligase. By ubiquitinating
CC CDKN1A/p21 and targeting it for proteasomal degradation, may
CC promote cell proliferation.
CC -!- INTERACTION:
CC P51668:UBE2D1; NbExp=3; IntAct=EBI-357322, EBI-743540;
CC P61077:UBE2D3; NbExp=3; IntAct=EBI-357322, EBI-348268;
CC Q9Y2X8:UBE2D4; NbExp=3; IntAct=EBI-357322, EBI-745527;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BV68-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BV68-2; Sequence=VSP_015693, VSP_015694;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver and testis.
CC -!- PTM: Auto-ubiquitinated.
CC -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK000559; BAA91254.1; -; mRNA.
DR EMBL; BC001442; AAH01442.1; -; mRNA.
DR EMBL; BC025374; AAH25374.1; -; mRNA.
DR RefSeq; NP_919442.1; NM_194460.2.
DR UniGene; Hs.69554; -.
DR ProteinModelPortal; Q9BV68; -.
DR SMR; Q9BV68; 219-288.
DR IntAct; Q9BV68; 20.
DR MINT; MINT-1032305; -.
DR STRING; 9606.ENSP00000292363; -.
DR PhosphoSite; Q9BV68; -.
DR DMDM; 74762712; -.
DR PaxDb; Q9BV68; -.
DR PRIDE; Q9BV68; -.
DR Ensembl; ENST00000292363; ENSP00000292363; ENSG00000070423.
DR GeneID; 55658; -.
DR KEGG; hsa:55658; -.
DR CTD; 55658; -.
DR GeneCards; GC19M000647; -.
DR H-InvDB; HIX0014558; -.
DR HGNC; HGNC:21151; RNF126.
DR HPA; HPA043050; -.
DR MIM; 615177; gene.
DR neXtProt; NX_Q9BV68; -.
DR PharmGKB; PA134876469; -.
DR eggNOG; COG5540; -.
DR HOGENOM; HOG000116417; -.
DR HOVERGEN; HBG059832; -.
DR InParanoid; Q9BV68; -.
DR KO; K11982; -.
DR OMA; PTDQSRP; -.
DR OrthoDB; EOG7353XB; -.
DR PhylomeDB; Q9BV68; -.
DR ChiTaRS; RNF126; human.
DR GenomeRNAi; 55658; -.
DR NextBio; 60383; -.
DR PRO; PR:Q9BV68; -.
DR ArrayExpress; Q9BV68; -.
DR Bgee; Q9BV68; -.
DR CleanEx; HS_RNF126; -.
DR Genevestigator; Q9BV68; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Ligase; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 326 E3 ubiquitin-protein ligase RNF126.
FT /FTId=PRO_0000056093.
FT ZN_FING 229 270 RING-type.
FT COMPBIAS 289 303 Ser-rich.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 5 5 Phosphoserine.
FT VAR_SEQ 309 311 WSP -> SNS (in isoform 2).
FT /FTId=VSP_015693.
FT VAR_SEQ 312 326 Missing (in isoform 2).
FT /FTId=VSP_015694.
FT VARIANT 68 68 V -> M (in dbSNP:rs2285751).
FT /FTId=VAR_057217.
FT MUTAGEN 229 229 C->A: Loss of E3 ligase activity; when
FT associated with A-232.
FT MUTAGEN 232 232 C->A: Loss of E3 ligase activity; when
FT associated with A-229.
SQ SEQUENCE 326 AA; 35585 MW; D422FFB090362F46 CRC64;
MAEASPHPGR YFCHCCSVEI VPRLPDYICP RCESGFIEEL PEETRSTENG SAPSTAPTDQ
SRPPLEHVDQ HLFTLPQGYG QFAFGIFDDS FEIPTFPPGA QADDGRDPES RRERDHPSRH
RYGARQPRAR LTTRRATGRH EGVPTLEGII QQLVNGIITP ATIPSLGPWG VLHSNPMDYA
WGANGLDAII TQLLNQFENT GPPPADKEKI QALPTVPVTE EHVGSGLECP VCKDDYALGE
RVRQLPCNHL FHDGCIVPWL EQHDSCPVCR KSLTGQNTAT NPPGLTGVSF SSSSSSSSSS
SPSNENATWS PLGRPQPPRP LSNLTL
//
ID RN126_HUMAN Reviewed; 326 AA.
AC Q9BV68; Q9NWX1;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=E3 ubiquitin-protein ligase RNF126;
DE EC=6.3.2.-;
DE AltName: Full=RING finger protein 126;
GN Name=RNF126;
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 [LARGE SCALE MRNA] (ISOFORM 2).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Placenta;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-5, MASS SPECTROMETRY, AND CLEAVAGE OF INITIATOR
RP METHIONINE.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [5]
RP FUNCTION, AUTOUBIQUITINATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP CYS-229 AND CYS-232.
RX PubMed=23026136; DOI=10.1158/0008-5472.CAN-12-0562;
RA Zhi X., Zhao D., Wang Z., Zhou Z., Wang C., Chen W., Liu R., Chen C.;
RT "E3 ubiquitin ligase RNF126 promotes cancer cell proliferation by
RT targeting the tumor suppressor p21 for ubiquitin-mediated
RT degradation.";
RL Cancer Res. 73:385-394(2013).
CC -!- FUNCTION: E3 ubiquitin-protein ligase. By ubiquitinating
CC CDKN1A/p21 and targeting it for proteasomal degradation, may
CC promote cell proliferation.
CC -!- INTERACTION:
CC P51668:UBE2D1; NbExp=3; IntAct=EBI-357322, EBI-743540;
CC P61077:UBE2D3; NbExp=3; IntAct=EBI-357322, EBI-348268;
CC Q9Y2X8:UBE2D4; NbExp=3; IntAct=EBI-357322, EBI-745527;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BV68-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BV68-2; Sequence=VSP_015693, VSP_015694;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver and testis.
CC -!- PTM: Auto-ubiquitinated.
CC -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK000559; BAA91254.1; -; mRNA.
DR EMBL; BC001442; AAH01442.1; -; mRNA.
DR EMBL; BC025374; AAH25374.1; -; mRNA.
DR RefSeq; NP_919442.1; NM_194460.2.
DR UniGene; Hs.69554; -.
DR ProteinModelPortal; Q9BV68; -.
DR SMR; Q9BV68; 219-288.
DR IntAct; Q9BV68; 20.
DR MINT; MINT-1032305; -.
DR STRING; 9606.ENSP00000292363; -.
DR PhosphoSite; Q9BV68; -.
DR DMDM; 74762712; -.
DR PaxDb; Q9BV68; -.
DR PRIDE; Q9BV68; -.
DR Ensembl; ENST00000292363; ENSP00000292363; ENSG00000070423.
DR GeneID; 55658; -.
DR KEGG; hsa:55658; -.
DR CTD; 55658; -.
DR GeneCards; GC19M000647; -.
DR H-InvDB; HIX0014558; -.
DR HGNC; HGNC:21151; RNF126.
DR HPA; HPA043050; -.
DR MIM; 615177; gene.
DR neXtProt; NX_Q9BV68; -.
DR PharmGKB; PA134876469; -.
DR eggNOG; COG5540; -.
DR HOGENOM; HOG000116417; -.
DR HOVERGEN; HBG059832; -.
DR InParanoid; Q9BV68; -.
DR KO; K11982; -.
DR OMA; PTDQSRP; -.
DR OrthoDB; EOG7353XB; -.
DR PhylomeDB; Q9BV68; -.
DR ChiTaRS; RNF126; human.
DR GenomeRNAi; 55658; -.
DR NextBio; 60383; -.
DR PRO; PR:Q9BV68; -.
DR ArrayExpress; Q9BV68; -.
DR Bgee; Q9BV68; -.
DR CleanEx; HS_RNF126; -.
DR Genevestigator; Q9BV68; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Ligase; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 326 E3 ubiquitin-protein ligase RNF126.
FT /FTId=PRO_0000056093.
FT ZN_FING 229 270 RING-type.
FT COMPBIAS 289 303 Ser-rich.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 5 5 Phosphoserine.
FT VAR_SEQ 309 311 WSP -> SNS (in isoform 2).
FT /FTId=VSP_015693.
FT VAR_SEQ 312 326 Missing (in isoform 2).
FT /FTId=VSP_015694.
FT VARIANT 68 68 V -> M (in dbSNP:rs2285751).
FT /FTId=VAR_057217.
FT MUTAGEN 229 229 C->A: Loss of E3 ligase activity; when
FT associated with A-232.
FT MUTAGEN 232 232 C->A: Loss of E3 ligase activity; when
FT associated with A-229.
SQ SEQUENCE 326 AA; 35585 MW; D422FFB090362F46 CRC64;
MAEASPHPGR YFCHCCSVEI VPRLPDYICP RCESGFIEEL PEETRSTENG SAPSTAPTDQ
SRPPLEHVDQ HLFTLPQGYG QFAFGIFDDS FEIPTFPPGA QADDGRDPES RRERDHPSRH
RYGARQPRAR LTTRRATGRH EGVPTLEGII QQLVNGIITP ATIPSLGPWG VLHSNPMDYA
WGANGLDAII TQLLNQFENT GPPPADKEKI QALPTVPVTE EHVGSGLECP VCKDDYALGE
RVRQLPCNHL FHDGCIVPWL EQHDSCPVCR KSLTGQNTAT NPPGLTGVSF SSSSSSSSSS
SPSNENATWS PLGRPQPPRP LSNLTL
//
MIM
615177
*RECORD*
*FIELD* NO
615177
*FIELD* TI
*615177 RING FINGER PROTEIN 126; RNF126
*FIELD* TX
DESCRIPTION
RNF126 is an E3 ubiquitin ligase that ubiquitinates proteins and thereby
read moretargets them for proteasome-mediated degradation (Zhi et al., 2012).
CLONING
Using a small interfering RNA library to screen for E3 ubiquitin ligases
that, upon knockdown, reduced the viability of MDA-MB-231 breast cancer
and PC3 prostate cancer cell lines, Zhi et al. (2012) identified RNF126.
The deduced 311-amino acid protein has an N-terminal zinc finger domain
and a C-terminal RING finger domain. Analysis of 48 human tissues showed
that RNF126 mRNA was highly expressed in liver and testis.
Epitope-tagged RNF126 localized to both the cytoplasm and nucleus of
transfected PC3 cells and TSU-Pr1 bladder cancer cells.
GENE FUNCTION
Zhi et al. (2012) found that RNF126 was highly expressed in a subset of
breast cancer cell lines and that its upregulation negatively correlated
with expression of the cell cycle regulator p21 (CDKN1A; 116899).
Knockdown of RNF126 reduced viability in several human cancer cell
lines, increased p21 protein stability, caused G1 cell cycle arrest, and
reduced tumorigenicity following injection in nude mice. Protein
interaction assays revealed that the N-terminal and middle domains of
RNF126, but not the C-terminal RING domain, interacted directly with p21
in a p53 (TP53 191170)-independent manner. RNF126 ubiquitinated p21 in
vitro in the presence of E1 (see 314370), UBCH5B (602962), ATP, and
ubiquitin (191339). RNF126 was heavily ubiquitinated in cells and was
subject to autoubiquitination in vitro; however, RNF126 had a long
half-life, and ubiquitination did not appear to cause its instability.
MAPPING
Hartz (2013) mapped the RNF126 gene to chromosome 19p13.3 based on an
alignment of the RNF126 sequence (GenBank GENBANK AK000559) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 4/15/2013.
2. Zhi, X.; Zhao, D.; Wang, Z.; Zhou, Z.; Wang, C.; Chen, W.; Liu,
R.; Chen, C.: E3 ubiquitin ligase RNF126 promotes cancer cell proliferation
by targeting the tumor suppressor p21 for ubiquitin-mediated degradation. Cancer
Res. 73: 385-394, 2012.
*FIELD* CD
Patricia A. Hartz: 4/15/2013
*FIELD* ED
mgross: 04/15/2013
*RECORD*
*FIELD* NO
615177
*FIELD* TI
*615177 RING FINGER PROTEIN 126; RNF126
*FIELD* TX
DESCRIPTION
RNF126 is an E3 ubiquitin ligase that ubiquitinates proteins and thereby
read moretargets them for proteasome-mediated degradation (Zhi et al., 2012).
CLONING
Using a small interfering RNA library to screen for E3 ubiquitin ligases
that, upon knockdown, reduced the viability of MDA-MB-231 breast cancer
and PC3 prostate cancer cell lines, Zhi et al. (2012) identified RNF126.
The deduced 311-amino acid protein has an N-terminal zinc finger domain
and a C-terminal RING finger domain. Analysis of 48 human tissues showed
that RNF126 mRNA was highly expressed in liver and testis.
Epitope-tagged RNF126 localized to both the cytoplasm and nucleus of
transfected PC3 cells and TSU-Pr1 bladder cancer cells.
GENE FUNCTION
Zhi et al. (2012) found that RNF126 was highly expressed in a subset of
breast cancer cell lines and that its upregulation negatively correlated
with expression of the cell cycle regulator p21 (CDKN1A; 116899).
Knockdown of RNF126 reduced viability in several human cancer cell
lines, increased p21 protein stability, caused G1 cell cycle arrest, and
reduced tumorigenicity following injection in nude mice. Protein
interaction assays revealed that the N-terminal and middle domains of
RNF126, but not the C-terminal RING domain, interacted directly with p21
in a p53 (TP53 191170)-independent manner. RNF126 ubiquitinated p21 in
vitro in the presence of E1 (see 314370), UBCH5B (602962), ATP, and
ubiquitin (191339). RNF126 was heavily ubiquitinated in cells and was
subject to autoubiquitination in vitro; however, RNF126 had a long
half-life, and ubiquitination did not appear to cause its instability.
MAPPING
Hartz (2013) mapped the RNF126 gene to chromosome 19p13.3 based on an
alignment of the RNF126 sequence (GenBank GENBANK AK000559) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 4/15/2013.
2. Zhi, X.; Zhao, D.; Wang, Z.; Zhou, Z.; Wang, C.; Chen, W.; Liu,
R.; Chen, C.: E3 ubiquitin ligase RNF126 promotes cancer cell proliferation
by targeting the tumor suppressor p21 for ubiquitin-mediated degradation. Cancer
Res. 73: 385-394, 2012.
*FIELD* CD
Patricia A. Hartz: 4/15/2013
*FIELD* ED
mgross: 04/15/2013