Full text data of DCUN1D1
DCUN1D1
(DCUN1L1, RP42, SCCRO)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
DCN1-like protein 1 (DCUN1 domain-containing protein 1; Defective in cullin neddylation protein 1-like protein 1; Squamous cell carcinoma-related oncogene)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
DCN1-like protein 1 (DCUN1 domain-containing protein 1; Defective in cullin neddylation protein 1-like protein 1; Squamous cell carcinoma-related oncogene)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00291893
IPI00291893 RP42 protein Hypothetical protein FLJ22111 soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
IPI00291893 RP42 protein Hypothetical protein FLJ22111 soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
UniProt
Q96GG9
ID DCNL1_HUMAN Reviewed; 259 AA.
AC Q96GG9; B2RB37; Q7L3G9; Q8TEX7; Q9H6M1; Q9HCT3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 93.
DE RecName: Full=DCN1-like protein 1;
DE AltName: Full=DCUN1 domain-containing protein 1;
DE AltName: Full=Defective in cullin neddylation protein 1-like protein 1;
DE AltName: Full=Squamous cell carcinoma-related oncogene;
GN Name=DCUN1D1; Synonyms=DCUN1L1, RP42, SCCRO;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Telencephalon;
RX PubMed=10777668; DOI=10.1006/geno.2000.6126;
RA Mas C., Bourgeois F., Bulfone A., Levacher B., Mugnier C.,
RA Simonneau M.;
RT "Cloning and expression analysis of a novel gene, RP42, mapping to an
RT autism susceptibility locus on 6q16.";
RL Genomics 65:70-74(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung carcinoma, and Squamous cell carcinoma;
RX PubMed=17018598; DOI=10.1158/0008-5472.CAN-06-2074;
RA Sarkaria I., O-charoenrat P., Talbot S.G., Reddy P.G., Ngai I.,
RA Maghami E., Patel K.N., Lee B., Yonekawa Y., Dudas M., Kaufman A.,
RA Ryan R., Ghossein R., Rao P.H., Stoffel A., Ramanathan Y., Singh B.;
RT "Squamous cell carcinoma related oncogene/DCUN1D1 is highly conserved
RT and activated by amplification in squamous cell carcinomas.";
RL Cancer Res. 66:9437-9444(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Skin;
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 [6]
RP OVEREXPRESSION IN SQUAMOUS CELL CARCINOMAS.
RX PubMed=12796399;
RA Estilo C.L., O-Charoenrat P., Ngai I., Patel S.G., Reddy P.G., Dao S.,
RA Shaha A.R., Kraus D.H., Boyle J.O., Wong R.J., Pfister D.G.,
RA Huryn J.M., Zlotolow I.M., Shah J.P., Singh B.;
RT "The role of novel oncogenes squamous cell carcinoma-related oncogene
RT and phosphatidylinositol 3-kinase p110alpha in squamous cell carcinoma
RT of the oral tongue.";
RL Clin. Cancer Res. 9:2300-2306(2003).
RN [7]
RP OVEREXPRESSION IN SQUAMOUS CELL CARCINOMAS.
RX PubMed=15123463; DOI=10.1245/ASO.2004.03.014;
RA Talbot S.G., O-charoenrat P., Sarkaria I.S., Ghossein R., Reddy P.,
RA Ngai I., Cordeiro C.N., Wong R.J., Kris M.G., Rusch V.W., Singh B.;
RT "Squamous cell carcinoma related oncogene regulates angiogenesis
RT through vascular endothelial growth factor-A.";
RL Ann. Surg. Oncol. 11:530-534(2004).
RN [8]
RP OVEREXPRESSION IN BRONCHIOLOALVEOLAR CARCINOMAS.
RX PubMed=15511464; DOI=10.1016/j.athoracsur.2004.05.056;
RA Sarkaria I.S., Pham D., Ghossein R.A., Talbot S.G., Hezel M.,
RA Dudas M.E., Ebright M.I., Chuai S., Memoli N., Venkatraman E.S.,
RA Miller V.A., Kris M.G., Zakowski M.F., Rusch V.W., Singh B.;
RT "SCCRO expression correlates with invasive progression in
RT bronchioloalveolar carcinoma.";
RL Ann. Thorac. Surg. 78:1734-1741(2004).
RN [9]
RP LACK OF OVEREXPRESSION IN ADRENOCORTICAL CARCINOMAS.
RX PubMed=15657565; DOI=10.1016/j.surg.2004.06.041;
RA Sarkaria I.S., Stojadinovic A., Talbot S.G., Hoos A., Dudas M.E.,
RA Brennan M.F., Ghossein R.A., Singh B.;
RT "Squamous cell carcinoma-related oncogene is highly expressed in
RT developing, normal, and adenomatous adrenal tissue but not in
RT aggressive adrenocortical carcinomas.";
RL Surgery 136:1122-1128(2004).
RN [10]
RP OVEREXPRESSION IN THYROID CANCERS.
RX PubMed=15623817; DOI=10.1210/jc.2004-1337;
RA Jacques C., Baris O., Prunier-Mirebeau D., Savagner F., Rodien P.,
RA Rohmer V., Franc B., Guyetant S., Malthiery Y., Reynier P.;
RT "Two-step differential expression analysis reveals a new set of genes
RT involved in thyroid oncocytic tumors.";
RL J. Clin. Endocrinol. Metab. 90:2314-2320(2005).
RN [11]
RP IDENTIFICATION IN AN E3 LIGASE COMPLEX FOR NEDDYLATION, INTERACTION
RP WITH CUL1; CUL2; CUL3; CUL4; CUL5; UBE2M; CAND1 AND RBX1, AND
RP MUTAGENESIS OF ASP-241.
RX PubMed=18826954; DOI=10.1074/jbc.M804440200;
RA Kim A.Y., Bommelje C.C., Lee B.E., Yonekawa Y., Choi L., Morris L.G.,
RA Huang G., Kaufman A., Ryan R.J., Hao B., Ramanathan Y., Singh B.;
RT "SCCRO (DCUN1D1) is an essential component of the E3 complex for
RT neddylation.";
RL J. Biol. Chem. 283:33211-33220(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 62-259 IN COMPLEX WITH CUL1
RP AND UBE2M.
RX PubMed=21940857; DOI=10.1126/science.1209307;
RA Scott D.C., Monda J.K., Bennett E.J., Harper J.W., Schulman B.A.;
RT "N-terminal acetylation acts as an avidity enhancer within an
RT interconnected multiprotein complex.";
RL Science 334:674-678(2011).
CC -!- FUNCTION: Part of an E3 ubiquitin ligase complex for neddylation.
CC Required for neddylation of cullin components of E3 cullin-RING
CC ubiquitin ligase complexes by enhancing the rate of cullins
CC neddylation. Functions to recruit the NEDD8-charged E2 enzyme to
CC the cullin component. Involved in the release of inhibitory effets
CC of CAND1 on cullin-RING ligase E3 complex assembly and activity.
CC Acts also as an oncogene facilitating malignant transformation and
CC carcinogenic progression (By similarity).
CC -!- SUBUNIT: Part of an E3 complex for neddylation composed of
CC cullins, RBX1, UBE2M and CAND1. Interacts (via the C-terminus 50
CC AA) with CUL1, CUL2, CUL3, CUL4 and CUL5. Binds neddylated CUL1.
CC Interacts (via the C-terminus 50 AA) directly with RBX1. Interacts
CC preferentially with UBE2M-NEDD8 thioester (via N-terminus 1-26 AA)
CC than with free UBE2M. Interacts with CAND1 when in complex with
CC CUL1-RBX1.
CC -!- TISSUE SPECIFICITY: Expressed in pancreas, kidney, placenta, brain
CC and heart. Weakly or not expressed in liver, skeletal muscle and
CC lung. Strongly overexpressed in thyroid tumors, bronchioloalveolar
CC carcinomas, and malignant tissues of squamous cell carcinoma of
CC the oral tongue. Not overexpressed in aggressive adrenocortical
CC carcinomas.
CC -!- SIMILARITY: Contains 1 DCUN1 domain.
CC -!- SIMILARITY: Contains 1 UBA-like domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15235.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AF292100; AAG00606.2; -; mRNA.
DR EMBL; AF456425; AAL78672.1; -; mRNA.
DR EMBL; AF456426; AAL78673.1; -; mRNA.
DR EMBL; AK025764; BAB15235.1; ALT_INIT; mRNA.
DR EMBL; AK056335; BAG51680.1; -; mRNA.
DR EMBL; AK314480; BAG37084.1; -; mRNA.
DR EMBL; CH471052; EAW78342.1; -; Genomic_DNA.
DR EMBL; BC009478; AAH09478.1; -; mRNA.
DR EMBL; BC013163; AAH13163.2; -; mRNA.
DR RefSeq; NP_065691.2; NM_020640.2.
DR UniGene; Hs.744153; -.
DR PDB; 3TDU; X-ray; 1.50 A; A/B=62-259.
DR PDB; 3TDZ; X-ray; 2.00 A; A/B=62-259.
DR PDBsum; 3TDU; -.
DR PDBsum; 3TDZ; -.
DR ProteinModelPortal; Q96GG9; -.
DR SMR; Q96GG9; 6-253.
DR IntAct; Q96GG9; 5.
DR MINT; MINT-1182942; -.
DR STRING; 9606.ENSP00000292782; -.
DR PhosphoSite; Q96GG9; -.
DR DMDM; 73919222; -.
DR PaxDb; Q96GG9; -.
DR PRIDE; Q96GG9; -.
DR DNASU; 54165; -.
DR Ensembl; ENST00000292782; ENSP00000292782; ENSG00000043093.
DR GeneID; 54165; -.
DR KEGG; hsa:54165; -.
DR UCSC; uc003fld.1; human.
DR CTD; 54165; -.
DR GeneCards; GC03M182655; -.
DR HGNC; HGNC:18184; DCUN1D1.
DR HPA; HPA035911; -.
DR MIM; 605905; gene.
DR neXtProt; NX_Q96GG9; -.
DR PharmGKB; PA142672008; -.
DR eggNOG; NOG273293; -.
DR HOGENOM; HOG000241761; -.
DR HOVERGEN; HBG055256; -.
DR InParanoid; Q96GG9; -.
DR OMA; AQAYISS; -.
DR OrthoDB; EOG7S4X6Q; -.
DR PhylomeDB; Q96GG9; -.
DR ChiTaRS; DCUN1D1; human.
DR GeneWiki; DCUN1D1; -.
DR GenomeRNAi; 54165; -.
DR NextBio; 56518; -.
DR PRO; PR:Q96GG9; -.
DR ArrayExpress; Q96GG9; -.
DR Bgee; Q96GG9; -.
DR CleanEx; HS_DCUN1D1; -.
DR Genevestigator; Q96GG9; -.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR InterPro; IPR014764; DCN-prot.
DR InterPro; IPR005176; PONY_dom.
DR InterPro; IPR009060; UBA-like.
DR PANTHER; PTHR12281; PTHR12281; 1.
DR Pfam; PF03556; Cullin_binding; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS51229; DCUN1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Proto-oncogene;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1 259 DCN1-like protein 1.
FT /FTId=PRO_0000129498.
FT DOMAIN 8 45 UBA-like.
FT DOMAIN 60 248 DCUN1.
FT MOD_RES 1 1 N-acetylmethionine.
FT MUTAGEN 241 241 D->N: Loss of binding to CAND1 and CUL-
FT RBX1 complex but retains binding to
FT UBE2M.
FT CONFLICT 134 134 I -> T (in Ref. 2; AAL78673).
FT CONFLICT 136 136 K -> Q (in Ref. 1; AAG00606).
FT CONFLICT 191 192 KF -> RL (in Ref. 2; AAL78673).
FT HELIX 62 72
FT STRAND 77 81
FT HELIX 83 93
FT HELIX 100 108
FT HELIX 119 129
FT HELIX 134 139
FT HELIX 141 147
FT HELIX 151 165
FT STRAND 171 174
FT HELIX 175 185
FT TURN 187 189
FT HELIX 193 202
FT HELIX 210 222
FT HELIX 238 250
SQ SEQUENCE 259 AA; 30124 MW; F3709235E0610C54 CRC64;
MNKLKSSQKD KVRQFMIFTQ SSEKTAVSCL SQNDWKLDVA TDNFFQNPEL YIRESVKGSL
DRKKLEQLYN RYKDPQDENK IGIDGIQQFC DDLALDPASI SVLIIAWKFR AATQCEFSKQ
EFMDGMTELG CDSIEKLKAQ IPKMEQELKE PGRFKDFYQF TFNFAKNPGQ KGLDLEMAIA
YWNLVLNGRF KFLDLWNKFL LEHHKRSIPK DTWNLLLDFS TMIADDMSNY DEEGAWPVLI
DDFVEFARPQ IAGTKSTTV
//
ID DCNL1_HUMAN Reviewed; 259 AA.
AC Q96GG9; B2RB37; Q7L3G9; Q8TEX7; Q9H6M1; Q9HCT3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 93.
DE RecName: Full=DCN1-like protein 1;
DE AltName: Full=DCUN1 domain-containing protein 1;
DE AltName: Full=Defective in cullin neddylation protein 1-like protein 1;
DE AltName: Full=Squamous cell carcinoma-related oncogene;
GN Name=DCUN1D1; Synonyms=DCUN1L1, RP42, SCCRO;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Telencephalon;
RX PubMed=10777668; DOI=10.1006/geno.2000.6126;
RA Mas C., Bourgeois F., Bulfone A., Levacher B., Mugnier C.,
RA Simonneau M.;
RT "Cloning and expression analysis of a novel gene, RP42, mapping to an
RT autism susceptibility locus on 6q16.";
RL Genomics 65:70-74(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung carcinoma, and Squamous cell carcinoma;
RX PubMed=17018598; DOI=10.1158/0008-5472.CAN-06-2074;
RA Sarkaria I., O-charoenrat P., Talbot S.G., Reddy P.G., Ngai I.,
RA Maghami E., Patel K.N., Lee B., Yonekawa Y., Dudas M., Kaufman A.,
RA Ryan R., Ghossein R., Rao P.H., Stoffel A., Ramanathan Y., Singh B.;
RT "Squamous cell carcinoma related oncogene/DCUN1D1 is highly conserved
RT and activated by amplification in squamous cell carcinomas.";
RL Cancer Res. 66:9437-9444(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Skin;
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 [6]
RP OVEREXPRESSION IN SQUAMOUS CELL CARCINOMAS.
RX PubMed=12796399;
RA Estilo C.L., O-Charoenrat P., Ngai I., Patel S.G., Reddy P.G., Dao S.,
RA Shaha A.R., Kraus D.H., Boyle J.O., Wong R.J., Pfister D.G.,
RA Huryn J.M., Zlotolow I.M., Shah J.P., Singh B.;
RT "The role of novel oncogenes squamous cell carcinoma-related oncogene
RT and phosphatidylinositol 3-kinase p110alpha in squamous cell carcinoma
RT of the oral tongue.";
RL Clin. Cancer Res. 9:2300-2306(2003).
RN [7]
RP OVEREXPRESSION IN SQUAMOUS CELL CARCINOMAS.
RX PubMed=15123463; DOI=10.1245/ASO.2004.03.014;
RA Talbot S.G., O-charoenrat P., Sarkaria I.S., Ghossein R., Reddy P.,
RA Ngai I., Cordeiro C.N., Wong R.J., Kris M.G., Rusch V.W., Singh B.;
RT "Squamous cell carcinoma related oncogene regulates angiogenesis
RT through vascular endothelial growth factor-A.";
RL Ann. Surg. Oncol. 11:530-534(2004).
RN [8]
RP OVEREXPRESSION IN BRONCHIOLOALVEOLAR CARCINOMAS.
RX PubMed=15511464; DOI=10.1016/j.athoracsur.2004.05.056;
RA Sarkaria I.S., Pham D., Ghossein R.A., Talbot S.G., Hezel M.,
RA Dudas M.E., Ebright M.I., Chuai S., Memoli N., Venkatraman E.S.,
RA Miller V.A., Kris M.G., Zakowski M.F., Rusch V.W., Singh B.;
RT "SCCRO expression correlates with invasive progression in
RT bronchioloalveolar carcinoma.";
RL Ann. Thorac. Surg. 78:1734-1741(2004).
RN [9]
RP LACK OF OVEREXPRESSION IN ADRENOCORTICAL CARCINOMAS.
RX PubMed=15657565; DOI=10.1016/j.surg.2004.06.041;
RA Sarkaria I.S., Stojadinovic A., Talbot S.G., Hoos A., Dudas M.E.,
RA Brennan M.F., Ghossein R.A., Singh B.;
RT "Squamous cell carcinoma-related oncogene is highly expressed in
RT developing, normal, and adenomatous adrenal tissue but not in
RT aggressive adrenocortical carcinomas.";
RL Surgery 136:1122-1128(2004).
RN [10]
RP OVEREXPRESSION IN THYROID CANCERS.
RX PubMed=15623817; DOI=10.1210/jc.2004-1337;
RA Jacques C., Baris O., Prunier-Mirebeau D., Savagner F., Rodien P.,
RA Rohmer V., Franc B., Guyetant S., Malthiery Y., Reynier P.;
RT "Two-step differential expression analysis reveals a new set of genes
RT involved in thyroid oncocytic tumors.";
RL J. Clin. Endocrinol. Metab. 90:2314-2320(2005).
RN [11]
RP IDENTIFICATION IN AN E3 LIGASE COMPLEX FOR NEDDYLATION, INTERACTION
RP WITH CUL1; CUL2; CUL3; CUL4; CUL5; UBE2M; CAND1 AND RBX1, AND
RP MUTAGENESIS OF ASP-241.
RX PubMed=18826954; DOI=10.1074/jbc.M804440200;
RA Kim A.Y., Bommelje C.C., Lee B.E., Yonekawa Y., Choi L., Morris L.G.,
RA Huang G., Kaufman A., Ryan R.J., Hao B., Ramanathan Y., Singh B.;
RT "SCCRO (DCUN1D1) is an essential component of the E3 complex for
RT neddylation.";
RL J. Biol. Chem. 283:33211-33220(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 62-259 IN COMPLEX WITH CUL1
RP AND UBE2M.
RX PubMed=21940857; DOI=10.1126/science.1209307;
RA Scott D.C., Monda J.K., Bennett E.J., Harper J.W., Schulman B.A.;
RT "N-terminal acetylation acts as an avidity enhancer within an
RT interconnected multiprotein complex.";
RL Science 334:674-678(2011).
CC -!- FUNCTION: Part of an E3 ubiquitin ligase complex for neddylation.
CC Required for neddylation of cullin components of E3 cullin-RING
CC ubiquitin ligase complexes by enhancing the rate of cullins
CC neddylation. Functions to recruit the NEDD8-charged E2 enzyme to
CC the cullin component. Involved in the release of inhibitory effets
CC of CAND1 on cullin-RING ligase E3 complex assembly and activity.
CC Acts also as an oncogene facilitating malignant transformation and
CC carcinogenic progression (By similarity).
CC -!- SUBUNIT: Part of an E3 complex for neddylation composed of
CC cullins, RBX1, UBE2M and CAND1. Interacts (via the C-terminus 50
CC AA) with CUL1, CUL2, CUL3, CUL4 and CUL5. Binds neddylated CUL1.
CC Interacts (via the C-terminus 50 AA) directly with RBX1. Interacts
CC preferentially with UBE2M-NEDD8 thioester (via N-terminus 1-26 AA)
CC than with free UBE2M. Interacts with CAND1 when in complex with
CC CUL1-RBX1.
CC -!- TISSUE SPECIFICITY: Expressed in pancreas, kidney, placenta, brain
CC and heart. Weakly or not expressed in liver, skeletal muscle and
CC lung. Strongly overexpressed in thyroid tumors, bronchioloalveolar
CC carcinomas, and malignant tissues of squamous cell carcinoma of
CC the oral tongue. Not overexpressed in aggressive adrenocortical
CC carcinomas.
CC -!- SIMILARITY: Contains 1 DCUN1 domain.
CC -!- SIMILARITY: Contains 1 UBA-like domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15235.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AF292100; AAG00606.2; -; mRNA.
DR EMBL; AF456425; AAL78672.1; -; mRNA.
DR EMBL; AF456426; AAL78673.1; -; mRNA.
DR EMBL; AK025764; BAB15235.1; ALT_INIT; mRNA.
DR EMBL; AK056335; BAG51680.1; -; mRNA.
DR EMBL; AK314480; BAG37084.1; -; mRNA.
DR EMBL; CH471052; EAW78342.1; -; Genomic_DNA.
DR EMBL; BC009478; AAH09478.1; -; mRNA.
DR EMBL; BC013163; AAH13163.2; -; mRNA.
DR RefSeq; NP_065691.2; NM_020640.2.
DR UniGene; Hs.744153; -.
DR PDB; 3TDU; X-ray; 1.50 A; A/B=62-259.
DR PDB; 3TDZ; X-ray; 2.00 A; A/B=62-259.
DR PDBsum; 3TDU; -.
DR PDBsum; 3TDZ; -.
DR ProteinModelPortal; Q96GG9; -.
DR SMR; Q96GG9; 6-253.
DR IntAct; Q96GG9; 5.
DR MINT; MINT-1182942; -.
DR STRING; 9606.ENSP00000292782; -.
DR PhosphoSite; Q96GG9; -.
DR DMDM; 73919222; -.
DR PaxDb; Q96GG9; -.
DR PRIDE; Q96GG9; -.
DR DNASU; 54165; -.
DR Ensembl; ENST00000292782; ENSP00000292782; ENSG00000043093.
DR GeneID; 54165; -.
DR KEGG; hsa:54165; -.
DR UCSC; uc003fld.1; human.
DR CTD; 54165; -.
DR GeneCards; GC03M182655; -.
DR HGNC; HGNC:18184; DCUN1D1.
DR HPA; HPA035911; -.
DR MIM; 605905; gene.
DR neXtProt; NX_Q96GG9; -.
DR PharmGKB; PA142672008; -.
DR eggNOG; NOG273293; -.
DR HOGENOM; HOG000241761; -.
DR HOVERGEN; HBG055256; -.
DR InParanoid; Q96GG9; -.
DR OMA; AQAYISS; -.
DR OrthoDB; EOG7S4X6Q; -.
DR PhylomeDB; Q96GG9; -.
DR ChiTaRS; DCUN1D1; human.
DR GeneWiki; DCUN1D1; -.
DR GenomeRNAi; 54165; -.
DR NextBio; 56518; -.
DR PRO; PR:Q96GG9; -.
DR ArrayExpress; Q96GG9; -.
DR Bgee; Q96GG9; -.
DR CleanEx; HS_DCUN1D1; -.
DR Genevestigator; Q96GG9; -.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR InterPro; IPR014764; DCN-prot.
DR InterPro; IPR005176; PONY_dom.
DR InterPro; IPR009060; UBA-like.
DR PANTHER; PTHR12281; PTHR12281; 1.
DR Pfam; PF03556; Cullin_binding; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS51229; DCUN1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Proto-oncogene;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1 259 DCN1-like protein 1.
FT /FTId=PRO_0000129498.
FT DOMAIN 8 45 UBA-like.
FT DOMAIN 60 248 DCUN1.
FT MOD_RES 1 1 N-acetylmethionine.
FT MUTAGEN 241 241 D->N: Loss of binding to CAND1 and CUL-
FT RBX1 complex but retains binding to
FT UBE2M.
FT CONFLICT 134 134 I -> T (in Ref. 2; AAL78673).
FT CONFLICT 136 136 K -> Q (in Ref. 1; AAG00606).
FT CONFLICT 191 192 KF -> RL (in Ref. 2; AAL78673).
FT HELIX 62 72
FT STRAND 77 81
FT HELIX 83 93
FT HELIX 100 108
FT HELIX 119 129
FT HELIX 134 139
FT HELIX 141 147
FT HELIX 151 165
FT STRAND 171 174
FT HELIX 175 185
FT TURN 187 189
FT HELIX 193 202
FT HELIX 210 222
FT HELIX 238 250
SQ SEQUENCE 259 AA; 30124 MW; F3709235E0610C54 CRC64;
MNKLKSSQKD KVRQFMIFTQ SSEKTAVSCL SQNDWKLDVA TDNFFQNPEL YIRESVKGSL
DRKKLEQLYN RYKDPQDENK IGIDGIQQFC DDLALDPASI SVLIIAWKFR AATQCEFSKQ
EFMDGMTELG CDSIEKLKAQ IPKMEQELKE PGRFKDFYQF TFNFAKNPGQ KGLDLEMAIA
YWNLVLNGRF KFLDLWNKFL LEHHKRSIPK DTWNLLLDFS TMIADDMSNY DEEGAWPVLI
DDFVEFARPQ IAGTKSTTV
//
MIM
605905
*RECORD*
*FIELD* NO
605905
*FIELD* TI
*605905 DCN1 DOMAIN-CONTAINING PROTEIN 1; DCUN1D1
;;RP42 HOMOLOG; RP42
*FIELD* TX
read moreCLONING
In a systematic search for genes expressed in proliferating neuroblasts
whose human orthologs map to susceptibility loci for autism (209850),
Mas et al. (2000) isolated a novel mouse gene, which they designated
RP42. They obtained the human homolog by combining contigs of human ESTs
and RT-PCR of human embryonic mRNAs. The deduced human and mouse RP42
proteins contain 259 amino acids and differ by only 2 residues. They
show 30 to 36% overall sequence identity to an S. pombe and a C. elegans
protein, suggesting that the RP42 protein has an important cellular
function. Northern blot analysis in the mouse embryo demonstrated
expression of 2 transcripts, with the larger transcript reaching peak
expression from E11 to E15, and the smaller transcript showing high
expression from E7 to E15, indicating developmentally regulated
expression, which was found particularly in proliferating neuroblasts.
In mouse adult tissues, 3 transcripts were expressed in testis, kidney,
liver, skeletal muscle, and heart, with weaker expression in brain.
Northern blot analysis of adult human tissues detected 2 RP42
transcripts of approximately 3.7 and 2.7 kb at lower levels of
expression than in mouse. RT-PCR showed that RP42 is expressed in the
human embryo telencephalon.
By searching databases for sequences similar to S. cerevisiae and C.
elegans Dcn1, Kurz et al. (2005) identified mouse and human DCUN1D1.
Like Dcn1, DCUN1D1 contains a DUF298 domain and a UBA-like ubiquitin
(see 191339)-binding domain.
GENE FUNCTION
Kurz et al. (2005) found that Dcn1 was required for cullin (see CUL1;
603134) neddylation in C. elegans and S. cerevisiae. Dcn1 from both
species bound cullin directly, and overexpression of Dcn1 in yeast
resulted in accumulation of Nedd8 (603171)-modified Cdc53, a Cul1
ortholog.
Scott et al. (2011) found that N-terminal acetylation of the E2 enzyme
UBC12 (603173) dictates distinctive E3-dependent ligation of the
ubiquitin-like protein NEDD8 (603171) to CUL1 (603134). Structural,
biochemical, biophysical, and genetic analyses revealed how complete
burial of UBC12's N-acetyl-methionine in a hydrophobic pocket in the E3
DCN1 promotes cullin neddylation. The results suggested that the
N-terminal acetyl both directs UBC12's interactions with DCN1 and
prevents repulsion of a charged N terminus. Scott et al. (2011)
concluded that their data provided a link between acetylation and
ubiquitin-like protein conjugation and defined a mechanism for
N-terminal acetylation-dependent recognition.
MAPPING
Mas et al. (2000) identified the human RP42 sequence in a cluster of
embryonic neuronally expressed genes on a PAC mapping to 6q16, making it
a candidate gene for the susceptibility autism locus previously assigned
to this region.
*FIELD* RF
1. Kurz, T.; Ozlu, N.; Rudolf, F.; O'Rourke, S. M.; Luke, B.; Hofmann,
K.; Hyman, A. A.; Bowerman, B.; Peter, M.: The conserved protein
DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S.
cerevisiae. Nature 435: 1257-1261, 2005.
2. Mas, C.; Bourgeois, F.; Bulfone, A.; Levacher, B.; Mugnier, C.;
Simonneau, M.: Cloning and expression analysis of a novel gene, RP42,
mapping to an autism susceptibility locus on 6q16. Genomics 65:
70-74, 2000.
3. Scott, D. C.; Monda, J. K.; Bennett, E. J.; Harper, J. W.; Schulman,
B. A.: N-terminal acetylation acts as an avidity enhancer within
an interconnected multiprotein complex. Science 334: 674-678, 2011.
*FIELD* CN
Ada Hamosh - updated: 11/29/2011
Patricia A. Hartz - updated: 8/25/2009
*FIELD* CD
Tara S. Marathe: 5/3/2001
*FIELD* ED
alopez: 11/30/2011
terry: 11/29/2011
mgross: 8/25/2009
carol: 7/27/2006
carol: 3/8/2002
carol: 5/3/2001
*RECORD*
*FIELD* NO
605905
*FIELD* TI
*605905 DCN1 DOMAIN-CONTAINING PROTEIN 1; DCUN1D1
;;RP42 HOMOLOG; RP42
*FIELD* TX
read moreCLONING
In a systematic search for genes expressed in proliferating neuroblasts
whose human orthologs map to susceptibility loci for autism (209850),
Mas et al. (2000) isolated a novel mouse gene, which they designated
RP42. They obtained the human homolog by combining contigs of human ESTs
and RT-PCR of human embryonic mRNAs. The deduced human and mouse RP42
proteins contain 259 amino acids and differ by only 2 residues. They
show 30 to 36% overall sequence identity to an S. pombe and a C. elegans
protein, suggesting that the RP42 protein has an important cellular
function. Northern blot analysis in the mouse embryo demonstrated
expression of 2 transcripts, with the larger transcript reaching peak
expression from E11 to E15, and the smaller transcript showing high
expression from E7 to E15, indicating developmentally regulated
expression, which was found particularly in proliferating neuroblasts.
In mouse adult tissues, 3 transcripts were expressed in testis, kidney,
liver, skeletal muscle, and heart, with weaker expression in brain.
Northern blot analysis of adult human tissues detected 2 RP42
transcripts of approximately 3.7 and 2.7 kb at lower levels of
expression than in mouse. RT-PCR showed that RP42 is expressed in the
human embryo telencephalon.
By searching databases for sequences similar to S. cerevisiae and C.
elegans Dcn1, Kurz et al. (2005) identified mouse and human DCUN1D1.
Like Dcn1, DCUN1D1 contains a DUF298 domain and a UBA-like ubiquitin
(see 191339)-binding domain.
GENE FUNCTION
Kurz et al. (2005) found that Dcn1 was required for cullin (see CUL1;
603134) neddylation in C. elegans and S. cerevisiae. Dcn1 from both
species bound cullin directly, and overexpression of Dcn1 in yeast
resulted in accumulation of Nedd8 (603171)-modified Cdc53, a Cul1
ortholog.
Scott et al. (2011) found that N-terminal acetylation of the E2 enzyme
UBC12 (603173) dictates distinctive E3-dependent ligation of the
ubiquitin-like protein NEDD8 (603171) to CUL1 (603134). Structural,
biochemical, biophysical, and genetic analyses revealed how complete
burial of UBC12's N-acetyl-methionine in a hydrophobic pocket in the E3
DCN1 promotes cullin neddylation. The results suggested that the
N-terminal acetyl both directs UBC12's interactions with DCN1 and
prevents repulsion of a charged N terminus. Scott et al. (2011)
concluded that their data provided a link between acetylation and
ubiquitin-like protein conjugation and defined a mechanism for
N-terminal acetylation-dependent recognition.
MAPPING
Mas et al. (2000) identified the human RP42 sequence in a cluster of
embryonic neuronally expressed genes on a PAC mapping to 6q16, making it
a candidate gene for the susceptibility autism locus previously assigned
to this region.
*FIELD* RF
1. Kurz, T.; Ozlu, N.; Rudolf, F.; O'Rourke, S. M.; Luke, B.; Hofmann,
K.; Hyman, A. A.; Bowerman, B.; Peter, M.: The conserved protein
DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S.
cerevisiae. Nature 435: 1257-1261, 2005.
2. Mas, C.; Bourgeois, F.; Bulfone, A.; Levacher, B.; Mugnier, C.;
Simonneau, M.: Cloning and expression analysis of a novel gene, RP42,
mapping to an autism susceptibility locus on 6q16. Genomics 65:
70-74, 2000.
3. Scott, D. C.; Monda, J. K.; Bennett, E. J.; Harper, J. W.; Schulman,
B. A.: N-terminal acetylation acts as an avidity enhancer within
an interconnected multiprotein complex. Science 334: 674-678, 2011.
*FIELD* CN
Ada Hamosh - updated: 11/29/2011
Patricia A. Hartz - updated: 8/25/2009
*FIELD* CD
Tara S. Marathe: 5/3/2001
*FIELD* ED
alopez: 11/30/2011
terry: 11/29/2011
mgross: 8/25/2009
carol: 7/27/2006
carol: 3/8/2002
carol: 5/3/2001