Full text data of RNF14
RNF14
(ARA54)
[Confidence: low (only semi-automatic identification from reviews)]
E3 ubiquitin-protein ligase RNF14; 6.3.2.- (Androgen receptor-associated protein 54; HFB30; RING finger protein 14; Triad2 protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
E3 ubiquitin-protein ligase RNF14; 6.3.2.- (Androgen receptor-associated protein 54; HFB30; RING finger protein 14; Triad2 protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UBS8
ID RNF14_HUMAN Reviewed; 474 AA.
AC Q9UBS8; A0AV26; A6NMR2; A8MTW5; B3KN72; B7ZLV2; D3DQE4; O94793;
read moreAC Q6IBV0;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=E3 ubiquitin-protein ligase RNF14;
DE EC=6.3.2.-;
DE AltName: Full=Androgen receptor-associated protein 54;
DE AltName: Full=HFB30;
DE AltName: Full=RING finger protein 14;
DE AltName: Full=Triad2 protein;
GN Name=RNF14; Synonyms=ARA54; ORFNames=HRIHFB2038;
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).
RC TISSUE=Fetal brain;
RX PubMed=10320776; DOI=10.1016/S0167-4781(99)00045-7;
RA Ueki N., Seki N., Yano K., Masuho Y., Saito T., Muramatsu M.-A.;
RT "Isolation and characterization of a novel human gene (HFB30) which
RT encodes a protein with a RING finger motif.";
RL Biochim. Biophys. Acta 1445:232-236(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
RC TISSUE=Prostate;
RX PubMed=10085091; DOI=10.1074/jbc.274.13.8570;
RA Kang H.-Y., Yeh S., Fujimoto N., Chang C.;
RT "Cloning and characterization of human prostate coactivator ARA54, a
RT novel protein that associates with the androgen receptor.";
RL J. Biol. Chem. 274:8570-8576(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Thyroid;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 286-474 (ISOFORM 1), AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Fetal brain;
RX PubMed=9853615; DOI=10.1038/4315;
RA Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.;
RT "Selection system for genes encoding nuclear-targeted proteins.";
RL Nat. Biotechnol. 16:1338-1342(1998).
RN [9]
RP MUTAGENESIS OF CYS-220.
RX PubMed=11322894; DOI=10.1046/j.1432-1327.2001.02169.x;
RA Ito K., Adachi S., Iwakami R., Yasuda H., Muto Y., Seki N., Okano Y.;
RT "N-terminally extended human ubiquitin-conjugating enzymes (E2s)
RT mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8.";
RL Eur. J. Biochem. 268:2725-2732(2001).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP FUNCTION, AND INTERACTION WITH AR.
RX PubMed=19345326; DOI=10.1016/j.ccr.2009.02.021;
RA Xu K., Shimelis H., Linn D.E., Jiang R., Yang X., Sun F., Guo Z.,
RA Chen H., Li W., Chen H., Kong X., Melamed J., Fang S., Xiao Z.,
RA Veenstra T.D., Qiu Y.;
RT "Regulation of androgen receptor transcriptional activity and
RT specificity by RNF6-induced ubiquitination.";
RL Cancer Cell 15:270-282(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
CC -!- FUNCTION: Might act as an E3 ubiquitin-protein ligase which
CC accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes
CC and then transfers it to substrates, which could be nuclear
CC proteins. Could play a role as a coactivator for androgen- and, to
CC a lesser extent, progesterone-dependent transcription.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with the ubiquitin-conjugating enzymes UBE2E1
CC and UBE2E2. Interacts with AR/androgen receptor; testosterone- and
CC RNF6-regulated it promotes AR transcriptional activity.
CC -!- INTERACTION:
CC P10275:AR; NbExp=2; IntAct=EBI-2130308, EBI-608057;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UBS8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UBS8-2; Sequence=VSP_045780;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DOMAIN: The N-terminal destruction box (D-box) acts as a
CC recognition signal for degradation via the ubiquitin-proteasome
CC pathway (By similarity).
CC -!- DOMAIN: The RING-type zinc finger is essential for the interaction
CC with UBE2E2.
CC -!- PTM: RING-type zinc finger-dependent and UBE2E2-dependent
CC autoubiquitination.
CC -!- SIMILARITY: Belongs to the RBR family. RNF14 subfamily.
CC -!- SIMILARITY: Contains 1 IBR-type zinc finger.
CC -!- SIMILARITY: Contains 2 RING-type zinc fingers.
CC -!- SIMILARITY: Contains 1 RWD domain.
CC -!- CAUTION: Lacks the His residue in the RING-type domain 2 that is
CC one of the conserved features of the family.
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DR EMBL; AB022663; BAA78677.1; -; mRNA.
DR EMBL; AF060544; AAD21842.1; -; mRNA.
DR EMBL; AK023884; BAG51234.1; -; mRNA.
DR EMBL; AK057868; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CR456702; CAG32983.1; -; mRNA.
DR EMBL; AC005740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61895.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61896.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61897.1; -; Genomic_DNA.
DR EMBL; BC126185; AAI26186.1; -; mRNA.
DR EMBL; BC144061; AAI44062.1; -; mRNA.
DR EMBL; AB015333; BAA34792.1; -; mRNA.
DR RefSeq; NP_001188294.1; NM_001201365.1.
DR RefSeq; NP_004281.1; NM_004290.4.
DR RefSeq; NP_899645.1; NM_183398.2.
DR RefSeq; NP_899646.1; NM_183399.2.
DR RefSeq; NP_899647.1; NM_183400.2.
DR RefSeq; NP_899648.1; NM_183401.2.
DR RefSeq; XP_005268593.1; XM_005268536.1.
DR RefSeq; XP_005268594.1; XM_005268537.1.
DR RefSeq; XP_005268595.1; XM_005268538.1.
DR RefSeq; XP_005268596.1; XM_005268539.1.
DR RefSeq; XP_005268597.1; XM_005268540.1.
DR RefSeq; XP_005268598.1; XM_005268541.1.
DR UniGene; Hs.483616; -.
DR ProteinModelPortal; Q9UBS8; -.
DR SMR; Q9UBS8; 188-448.
DR IntAct; Q9UBS8; 14.
DR MINT; MINT-1187964; -.
DR STRING; 9606.ENSP00000324956; -.
DR PhosphoSite; Q9UBS8; -.
DR DMDM; 17380293; -.
DR PaxDb; Q9UBS8; -.
DR PRIDE; Q9UBS8; -.
DR DNASU; 9604; -.
DR Ensembl; ENST00000347642; ENSP00000324956; ENSG00000013561.
DR Ensembl; ENST00000356143; ENSP00000348462; ENSG00000013561.
DR Ensembl; ENST00000394514; ENSP00000378022; ENSG00000013561.
DR Ensembl; ENST00000394519; ENSP00000378027; ENSG00000013561.
DR Ensembl; ENST00000394520; ENSP00000378028; ENSG00000013561.
DR GeneID; 9604; -.
DR KEGG; hsa:9604; -.
DR UCSC; uc003lly.3; human.
DR CTD; 9604; -.
DR GeneCards; GC05P141358; -.
DR HGNC; HGNC:10058; RNF14.
DR HPA; HPA008716; -.
DR MIM; 605675; gene.
DR neXtProt; NX_Q9UBS8; -.
DR PharmGKB; PA34423; -.
DR eggNOG; NOG266709; -.
DR HOVERGEN; HBG057296; -.
DR InParanoid; Q9UBS8; -.
DR KO; K11971; -.
DR OMA; QYFCWLC; -.
DR PhylomeDB; Q9UBS8; -.
DR UniPathway; UPA00143; -.
DR ChiTaRS; RNF14; human.
DR GeneWiki; RNF14; -.
DR GenomeRNAi; 9604; -.
DR NextBio; 36027; -.
DR PRO; PR:Q9UBS8; -.
DR ArrayExpress; Q9UBS8; -.
DR Bgee; Q9UBS8; -.
DR CleanEx; HS_RNF14; -.
DR Genevestigator; Q9UBS8; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019787; F:small conjugating protein ligase activity; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; NAS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEP:UniProtKB.
DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:UniProtKB.
DR GO; GO:0032355; P:response to estradiol stimulus; IDA:BHF-UCL.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR006575; RWD-domain.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR002867; Znf_C6HC.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF01485; IBR; 2.
DR Pfam; PF05773; RWD; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 1.
DR SMART; SM00591; RWD; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50908; RWD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
KW Ligase; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1 474 E3 ubiquitin-protein ligase RNF14.
FT /FTId=PRO_0000056057.
FT DOMAIN 11 137 RWD.
FT ZN_FING 220 270 RING-type 1; atypical.
FT ZN_FING 289 350 IBR-type.
FT ZN_FING 404 433 RING-type 2; degenerate.
FT REGION 361 474 Interaction with androgen receptor.
FT COILED 351 395 Potential.
FT MOTIF 37 45 D-box.
FT MOD_RES 348 348 Phosphoserine.
FT VAR_SEQ 1 126 Missing (in isoform 2).
FT /FTId=VSP_045780.
FT MUTAGEN 220 220 C->S: Loss of interaction with UBE2E2 and
FT of autoubiquitination.
FT CONFLICT 32 32 Q -> R (in Ref. 4; CAG32983).
SQ SEQUENCE 474 AA; 53837 MW; 529E3F5AF38A5DAD CRC64;
MSSEDREAQE DELLALASIY DGDEFRKAES VQGGETRIYL DLPQNFKIFV SGNSNECLQN
SGFEYTICFL PPLVLNFELP PDYPSSSPPS FTLSGKWLSP TQLSALCKHL DNLWEEHRGS
VVLFAWMQFL KEETLAYLNI VSPFELKIGS QKKVQRRTAQ ASPNTELDFG GAAGSDVDQE
EIVDERAVQD VESLSNLIQE ILDFDQAQQI KCFNSKLFLC SICFCEKLGS ECMYFLECRH
VYCKACLKDY FEIQIRDGQV QCLNCPEPKC PSVATPGQVK ELVEAELFAR YDRLLLQSSL
DLMADVVYCP RPCCQLPVMQ EPGCTMGICS SCNFAFCTLC RLTYHGVSPC KVTAEKLMDL
RNEYLQADEA NKRLLDQRYG KRVIQKALEE MESKEWLEKN SKSCPCCGTP IEKLDGCNKM
TCTGCMQYFC WICMGSLSRA NPYKHFNDPG SPCFNRLFYA VDVDDDIWED EVED
//
ID RNF14_HUMAN Reviewed; 474 AA.
AC Q9UBS8; A0AV26; A6NMR2; A8MTW5; B3KN72; B7ZLV2; D3DQE4; O94793;
read moreAC Q6IBV0;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=E3 ubiquitin-protein ligase RNF14;
DE EC=6.3.2.-;
DE AltName: Full=Androgen receptor-associated protein 54;
DE AltName: Full=HFB30;
DE AltName: Full=RING finger protein 14;
DE AltName: Full=Triad2 protein;
GN Name=RNF14; Synonyms=ARA54; ORFNames=HRIHFB2038;
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).
RC TISSUE=Fetal brain;
RX PubMed=10320776; DOI=10.1016/S0167-4781(99)00045-7;
RA Ueki N., Seki N., Yano K., Masuho Y., Saito T., Muramatsu M.-A.;
RT "Isolation and characterization of a novel human gene (HFB30) which
RT encodes a protein with a RING finger motif.";
RL Biochim. Biophys. Acta 1445:232-236(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
RC TISSUE=Prostate;
RX PubMed=10085091; DOI=10.1074/jbc.274.13.8570;
RA Kang H.-Y., Yeh S., Fujimoto N., Chang C.;
RT "Cloning and characterization of human prostate coactivator ARA54, a
RT novel protein that associates with the androgen receptor.";
RL J. Biol. Chem. 274:8570-8576(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Thyroid;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 286-474 (ISOFORM 1), AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Fetal brain;
RX PubMed=9853615; DOI=10.1038/4315;
RA Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.;
RT "Selection system for genes encoding nuclear-targeted proteins.";
RL Nat. Biotechnol. 16:1338-1342(1998).
RN [9]
RP MUTAGENESIS OF CYS-220.
RX PubMed=11322894; DOI=10.1046/j.1432-1327.2001.02169.x;
RA Ito K., Adachi S., Iwakami R., Yasuda H., Muto Y., Seki N., Okano Y.;
RT "N-terminally extended human ubiquitin-conjugating enzymes (E2s)
RT mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8.";
RL Eur. J. Biochem. 268:2725-2732(2001).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP FUNCTION, AND INTERACTION WITH AR.
RX PubMed=19345326; DOI=10.1016/j.ccr.2009.02.021;
RA Xu K., Shimelis H., Linn D.E., Jiang R., Yang X., Sun F., Guo Z.,
RA Chen H., Li W., Chen H., Kong X., Melamed J., Fang S., Xiao Z.,
RA Veenstra T.D., Qiu Y.;
RT "Regulation of androgen receptor transcriptional activity and
RT specificity by RNF6-induced ubiquitination.";
RL Cancer Cell 15:270-282(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
CC -!- FUNCTION: Might act as an E3 ubiquitin-protein ligase which
CC accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes
CC and then transfers it to substrates, which could be nuclear
CC proteins. Could play a role as a coactivator for androgen- and, to
CC a lesser extent, progesterone-dependent transcription.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with the ubiquitin-conjugating enzymes UBE2E1
CC and UBE2E2. Interacts with AR/androgen receptor; testosterone- and
CC RNF6-regulated it promotes AR transcriptional activity.
CC -!- INTERACTION:
CC P10275:AR; NbExp=2; IntAct=EBI-2130308, EBI-608057;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UBS8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UBS8-2; Sequence=VSP_045780;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DOMAIN: The N-terminal destruction box (D-box) acts as a
CC recognition signal for degradation via the ubiquitin-proteasome
CC pathway (By similarity).
CC -!- DOMAIN: The RING-type zinc finger is essential for the interaction
CC with UBE2E2.
CC -!- PTM: RING-type zinc finger-dependent and UBE2E2-dependent
CC autoubiquitination.
CC -!- SIMILARITY: Belongs to the RBR family. RNF14 subfamily.
CC -!- SIMILARITY: Contains 1 IBR-type zinc finger.
CC -!- SIMILARITY: Contains 2 RING-type zinc fingers.
CC -!- SIMILARITY: Contains 1 RWD domain.
CC -!- CAUTION: Lacks the His residue in the RING-type domain 2 that is
CC one of the conserved features of the family.
CC -----------------------------------------------------------------------
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DR EMBL; AB022663; BAA78677.1; -; mRNA.
DR EMBL; AF060544; AAD21842.1; -; mRNA.
DR EMBL; AK023884; BAG51234.1; -; mRNA.
DR EMBL; AK057868; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CR456702; CAG32983.1; -; mRNA.
DR EMBL; AC005740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61895.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61896.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61897.1; -; Genomic_DNA.
DR EMBL; BC126185; AAI26186.1; -; mRNA.
DR EMBL; BC144061; AAI44062.1; -; mRNA.
DR EMBL; AB015333; BAA34792.1; -; mRNA.
DR RefSeq; NP_001188294.1; NM_001201365.1.
DR RefSeq; NP_004281.1; NM_004290.4.
DR RefSeq; NP_899645.1; NM_183398.2.
DR RefSeq; NP_899646.1; NM_183399.2.
DR RefSeq; NP_899647.1; NM_183400.2.
DR RefSeq; NP_899648.1; NM_183401.2.
DR RefSeq; XP_005268593.1; XM_005268536.1.
DR RefSeq; XP_005268594.1; XM_005268537.1.
DR RefSeq; XP_005268595.1; XM_005268538.1.
DR RefSeq; XP_005268596.1; XM_005268539.1.
DR RefSeq; XP_005268597.1; XM_005268540.1.
DR RefSeq; XP_005268598.1; XM_005268541.1.
DR UniGene; Hs.483616; -.
DR ProteinModelPortal; Q9UBS8; -.
DR SMR; Q9UBS8; 188-448.
DR IntAct; Q9UBS8; 14.
DR MINT; MINT-1187964; -.
DR STRING; 9606.ENSP00000324956; -.
DR PhosphoSite; Q9UBS8; -.
DR DMDM; 17380293; -.
DR PaxDb; Q9UBS8; -.
DR PRIDE; Q9UBS8; -.
DR DNASU; 9604; -.
DR Ensembl; ENST00000347642; ENSP00000324956; ENSG00000013561.
DR Ensembl; ENST00000356143; ENSP00000348462; ENSG00000013561.
DR Ensembl; ENST00000394514; ENSP00000378022; ENSG00000013561.
DR Ensembl; ENST00000394519; ENSP00000378027; ENSG00000013561.
DR Ensembl; ENST00000394520; ENSP00000378028; ENSG00000013561.
DR GeneID; 9604; -.
DR KEGG; hsa:9604; -.
DR UCSC; uc003lly.3; human.
DR CTD; 9604; -.
DR GeneCards; GC05P141358; -.
DR HGNC; HGNC:10058; RNF14.
DR HPA; HPA008716; -.
DR MIM; 605675; gene.
DR neXtProt; NX_Q9UBS8; -.
DR PharmGKB; PA34423; -.
DR eggNOG; NOG266709; -.
DR HOVERGEN; HBG057296; -.
DR InParanoid; Q9UBS8; -.
DR KO; K11971; -.
DR OMA; QYFCWLC; -.
DR PhylomeDB; Q9UBS8; -.
DR UniPathway; UPA00143; -.
DR ChiTaRS; RNF14; human.
DR GeneWiki; RNF14; -.
DR GenomeRNAi; 9604; -.
DR NextBio; 36027; -.
DR PRO; PR:Q9UBS8; -.
DR ArrayExpress; Q9UBS8; -.
DR Bgee; Q9UBS8; -.
DR CleanEx; HS_RNF14; -.
DR Genevestigator; Q9UBS8; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019787; F:small conjugating protein ligase activity; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; NAS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEP:UniProtKB.
DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:UniProtKB.
DR GO; GO:0032355; P:response to estradiol stimulus; IDA:BHF-UCL.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR006575; RWD-domain.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR002867; Znf_C6HC.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF01485; IBR; 2.
DR Pfam; PF05773; RWD; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 1.
DR SMART; SM00591; RWD; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50908; RWD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
KW Ligase; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1 474 E3 ubiquitin-protein ligase RNF14.
FT /FTId=PRO_0000056057.
FT DOMAIN 11 137 RWD.
FT ZN_FING 220 270 RING-type 1; atypical.
FT ZN_FING 289 350 IBR-type.
FT ZN_FING 404 433 RING-type 2; degenerate.
FT REGION 361 474 Interaction with androgen receptor.
FT COILED 351 395 Potential.
FT MOTIF 37 45 D-box.
FT MOD_RES 348 348 Phosphoserine.
FT VAR_SEQ 1 126 Missing (in isoform 2).
FT /FTId=VSP_045780.
FT MUTAGEN 220 220 C->S: Loss of interaction with UBE2E2 and
FT of autoubiquitination.
FT CONFLICT 32 32 Q -> R (in Ref. 4; CAG32983).
SQ SEQUENCE 474 AA; 53837 MW; 529E3F5AF38A5DAD CRC64;
MSSEDREAQE DELLALASIY DGDEFRKAES VQGGETRIYL DLPQNFKIFV SGNSNECLQN
SGFEYTICFL PPLVLNFELP PDYPSSSPPS FTLSGKWLSP TQLSALCKHL DNLWEEHRGS
VVLFAWMQFL KEETLAYLNI VSPFELKIGS QKKVQRRTAQ ASPNTELDFG GAAGSDVDQE
EIVDERAVQD VESLSNLIQE ILDFDQAQQI KCFNSKLFLC SICFCEKLGS ECMYFLECRH
VYCKACLKDY FEIQIRDGQV QCLNCPEPKC PSVATPGQVK ELVEAELFAR YDRLLLQSSL
DLMADVVYCP RPCCQLPVMQ EPGCTMGICS SCNFAFCTLC RLTYHGVSPC KVTAEKLMDL
RNEYLQADEA NKRLLDQRYG KRVIQKALEE MESKEWLEKN SKSCPCCGTP IEKLDGCNKM
TCTGCMQYFC WICMGSLSRA NPYKHFNDPG SPCFNRLFYA VDVDDDIWED EVED
//
MIM
605675
*RECORD*
*FIELD* NO
605675
*FIELD* TI
*605675 RING FINGER PROTEIN 14; RNF14
;;ANDROGEN RECEPTOR-ASSOCIATED PROTEIN 54; ARA54
read more*FIELD* TX
The RING finger motif is a unique zinc-chelating domain involved in
mediating protein-DNA and protein-protein interactions. Using the
sequence of the partial cDNA clone HFB30 isolated by Ueki et al. (1998)
to screen a human fetal brain cDNA library, Ueki et al. (1999) cloned
the full-length cDNA, which encoded a novel ring finger protein, RNF14.
The deduced 474-amino acid protein has a calculated molecular mass of
approximately 53 kD. RT-PCR analysis revealed ubiquitous expression of
RNF14 in a wide variety of human tissues.
Kang et al. (1999) independently cloned RNF14, which they called ARA54
(androgen receptor-associated protein-54), by a yeast 2-hybrid screen of
a prostate cDNA library. Northern blot analysis detected a major 3-kb
transcript, with highest expression in testis, followed by thymus,
spleen, colon, prostate, and uterus. Low expression was detected in
small intestine and blood leukocytes. The RNF14 transcript was also
strongly detected in 2 other prostate cell lines. A second transcript of
2 kb was detected in testis only. Kang et al. (1999) demonstrated that
RNF14 can function as a coactivator for androgen-dependent transcription
on both wildtype and mutant androgen receptor (313700). They also showed
that in the presence of a certain amount of 17-beta-estradiol or
hydroxyflutamide, the transcriptional activity of a specific AR mutant
was significantly enhanced, whereas that of wildtype and another AR
mutant was not. The authors suggested that both RNF14 and the positions
of the AR mutation might contribute to the specificity of AR-mediated
transactivation.
Ueki et al. (1999) determined that the RNF14 gene contains 9 exons and
spans approximately 20 kb of genomic DNA. By somatic cell hybrid and
radiation hybrid analyses, Ueki et al. (1999) mapped the RNF14 gene to
chromosome 5q23.3-q31.1.
*FIELD* RF
1. Kang, H.-Y.; Yeh, S.; Fujimoto, N.; Chang, C.: Cloning and characterization
of human prostate coactivator ARA54, a novel protein that associates
with the androgen receptor. J. Biol. Chem. 274: 8570-8576, 1999.
2. Ueki, N.; Oda, T.; Kondo, M.; Yano, K.; Noguchi, T.; Muramatsu,
M.: Selection system for genes encoding nuclear-targeted proteins. Nature
Biotech. 16: 1338-1342, 1998.
3. Ueki, N.; Seki, N.; Yano, K.; Masuho, Y.; Saito, T.; Muramatsu,
M.: Isolation and characterization of a novel human gene (HFB30)
which encodes a protein with a RING finger motif. Biochim. Biophys.
Acta 1445: 232-236, 1999.
*FIELD* CD
Carol A. Bocchini: 2/22/2001
*FIELD* ED
terry: 10/13/2010
cwells: 9/17/2003
mcapotos: 3/13/2001
mcapotos: 2/22/2001
carol: 2/22/2001
*RECORD*
*FIELD* NO
605675
*FIELD* TI
*605675 RING FINGER PROTEIN 14; RNF14
;;ANDROGEN RECEPTOR-ASSOCIATED PROTEIN 54; ARA54
read more*FIELD* TX
The RING finger motif is a unique zinc-chelating domain involved in
mediating protein-DNA and protein-protein interactions. Using the
sequence of the partial cDNA clone HFB30 isolated by Ueki et al. (1998)
to screen a human fetal brain cDNA library, Ueki et al. (1999) cloned
the full-length cDNA, which encoded a novel ring finger protein, RNF14.
The deduced 474-amino acid protein has a calculated molecular mass of
approximately 53 kD. RT-PCR analysis revealed ubiquitous expression of
RNF14 in a wide variety of human tissues.
Kang et al. (1999) independently cloned RNF14, which they called ARA54
(androgen receptor-associated protein-54), by a yeast 2-hybrid screen of
a prostate cDNA library. Northern blot analysis detected a major 3-kb
transcript, with highest expression in testis, followed by thymus,
spleen, colon, prostate, and uterus. Low expression was detected in
small intestine and blood leukocytes. The RNF14 transcript was also
strongly detected in 2 other prostate cell lines. A second transcript of
2 kb was detected in testis only. Kang et al. (1999) demonstrated that
RNF14 can function as a coactivator for androgen-dependent transcription
on both wildtype and mutant androgen receptor (313700). They also showed
that in the presence of a certain amount of 17-beta-estradiol or
hydroxyflutamide, the transcriptional activity of a specific AR mutant
was significantly enhanced, whereas that of wildtype and another AR
mutant was not. The authors suggested that both RNF14 and the positions
of the AR mutation might contribute to the specificity of AR-mediated
transactivation.
Ueki et al. (1999) determined that the RNF14 gene contains 9 exons and
spans approximately 20 kb of genomic DNA. By somatic cell hybrid and
radiation hybrid analyses, Ueki et al. (1999) mapped the RNF14 gene to
chromosome 5q23.3-q31.1.
*FIELD* RF
1. Kang, H.-Y.; Yeh, S.; Fujimoto, N.; Chang, C.: Cloning and characterization
of human prostate coactivator ARA54, a novel protein that associates
with the androgen receptor. J. Biol. Chem. 274: 8570-8576, 1999.
2. Ueki, N.; Oda, T.; Kondo, M.; Yano, K.; Noguchi, T.; Muramatsu,
M.: Selection system for genes encoding nuclear-targeted proteins. Nature
Biotech. 16: 1338-1342, 1998.
3. Ueki, N.; Seki, N.; Yano, K.; Masuho, Y.; Saito, T.; Muramatsu,
M.: Isolation and characterization of a novel human gene (HFB30)
which encodes a protein with a RING finger motif. Biochim. Biophys.
Acta 1445: 232-236, 1999.
*FIELD* CD
Carol A. Bocchini: 2/22/2001
*FIELD* ED
terry: 10/13/2010
cwells: 9/17/2003
mcapotos: 3/13/2001
mcapotos: 2/22/2001
carol: 2/22/2001