DCN1_YEAST
ID DCN1_YEAST Reviewed; 269 AA.
AC Q12395; D6VYC3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Defective in cullin neddylation protein 1;
GN Name=DCN1; OrderedLocusNames=YLR128W; ORFNames=L3111;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 90840 / EAY235 / FY23;
RX PubMed=9090053;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<241::aid-yea61>3.0.co;2-#;
RA Verhasselt P., Volckaert G.;
RT "Sequence analysis of a 37.6 kbp cosmid clone from the right arm of
RT Saccharomyces cerevisiae chromosome XII, carrying YAP3, HOG1, SNR6, tRNA-
RT Arg3 and 23 new open reading frames, among which several homologies to
RT proteins involved in cell division control and to mammalian growth factors
RT and other animal proteins are found.";
RL Yeast 13:241-250(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [4]
RP INTERACTION WITH CDC53.
RX PubMed=11283612; DOI=10.1038/35070067;
RA Seol J.H., Shevchenko A., Shevchenko A., Deshaies R.J.;
RT "Skp1 forms multiple protein complexes, including RAVE, a regulator of V-
RT ATPase assembly.";
RL Nat. Cell Biol. 3:384-391(2001).
RN [5]
RP FUNCTION, AND INTERACTION WITH UBIQUITIN AND NEDD8.
RX PubMed=15988528; DOI=10.1038/nature03662;
RA Kurz T., Oezlue N., Rudolf F., O'Rourke S.M., Luke B., Hofmann K.,
RA Hyman A.A., Bowerman B., Peter M.;
RT "The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C.
RT elegans and S. cerevisiae.";
RL Nature 435:1257-1261(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 70-269 IN COMPLEX WITH UBC12.
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: Required for neddylation of cullin components of SCF-type E3
CC ubiquitin ligase complexes. Neddylation of cullins play an essential
CC role in the regulation of SCF-type complexes activity. Does not act by
CC preventing deneddylation, but rather facilitates neddylation, possibly
CC by acting with HRT1/RBX1 to recruit the Nedd8-charged E2 UBC12 to the
CC cullin component of SCF-type complexes. {ECO:0000269|PubMed:15988528}.
CC -!- SUBUNIT: Interacts with the cullin CDC53. Interacts with ubiquitin via
CC its UBA-like domain. Interacts with RUB1/NEDD8.
CC {ECO:0000269|PubMed:11283612, ECO:0000269|PubMed:15988528,
CC ECO:0000269|PubMed:21940857}.
CC -!- INTERACTION:
CC Q12395; Q12018: CDC53; NbExp=3; IntAct=EBI-29871, EBI-4321;
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DR EMBL; X89514; CAA61706.1; -; Genomic_DNA.
DR EMBL; Z73300; CAA97697.1; -; Genomic_DNA.
DR EMBL; U53877; AAB82374.1; -; Genomic_DNA.
DR EMBL; X91258; CAA62639.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09439.1; -; Genomic_DNA.
DR PIR; S59316; S59316.
DR RefSeq; NP_013229.1; NM_001182015.1.
DR PDB; 2IS9; X-ray; 1.92 A; A=66-269.
DR PDB; 2L4E; NMR; -; A=6-62.
DR PDB; 2L4F; NMR; -; A=6-62.
DR PDB; 3BQ3; X-ray; 1.90 A; A=1-269.
DR PDB; 3O2P; X-ray; 2.23 A; A=70-269.
DR PDB; 3O6B; X-ray; 3.10 A; A/C/E/G/I=70-269.
DR PDB; 3TDI; X-ray; 2.30 A; A/B=70-269.
DR PDBsum; 2IS9; -.
DR PDBsum; 2L4E; -.
DR PDBsum; 2L4F; -.
DR PDBsum; 3BQ3; -.
DR PDBsum; 3O2P; -.
DR PDBsum; 3O6B; -.
DR PDBsum; 3TDI; -.
DR AlphaFoldDB; Q12395; -.
DR BMRB; Q12395; -.
DR SMR; Q12395; -.
DR BioGRID; 31397; 40.
DR DIP; DIP-1238N; -.
DR IntAct; Q12395; 1.
DR MINT; Q12395; -.
DR STRING; 4932.YLR128W; -.
DR iPTMnet; Q12395; -.
DR MaxQB; Q12395; -.
DR PaxDb; Q12395; -.
DR PRIDE; Q12395; -.
DR EnsemblFungi; YLR128W_mRNA; YLR128W; YLR128W.
DR GeneID; 850819; -.
DR KEGG; sce:YLR128W; -.
DR SGD; S000004118; DCN1.
DR VEuPathDB; FungiDB:YLR128W; -.
DR eggNOG; KOG3077; Eukaryota.
DR GeneTree; ENSGT00940000154944; -.
DR HOGENOM; CLU_047042_0_0_1; -.
DR InParanoid; Q12395; -.
DR OMA; FTQTGEQ; -.
DR BioCyc; YEAST:G3O-32270-MON; -.
DR BRENDA; 2.3.2.32; 984.
DR EvolutionaryTrace; Q12395; -.
DR PRO; PR:Q12395; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12395; protein.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0097602; F:cullin family protein binding; IMP:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:SGD.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IDA:SGD.
DR GO; GO:0032182; F:ubiquitin-like protein binding; IDA:SGD.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IMP:SGD.
DR GO; GO:0045116; P:protein neddylation; IDA:SGD.
DR Gene3D; 1.10.238.200; -; 1.
DR InterPro; IPR014764; DCN-prot.
DR InterPro; IPR042460; DCN1-like_PONY.
DR InterPro; IPR005176; PONY_dom.
DR InterPro; IPR009060; UBA-like_sf.
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; Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..269
FT /note="Defective in cullin neddylation protein 1"
FT /id="PRO_0000129518"
FT DOMAIN 14..51
FT /note="UBA-like"
FT DOMAIN 70..266
FT /note="DCUN1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00574"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:3BQ3"
FT HELIX 29..37
FT /evidence="ECO:0007829|PDB:3BQ3"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:3BQ3"
FT HELIX 43..54
FT /evidence="ECO:0007829|PDB:3BQ3"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:2L4F"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:3BQ3"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:3BQ3"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:3BQ3"
FT HELIX 127..136
FT /evidence="ECO:0007829|PDB:3BQ3"
FT HELIX 142..158
FT /evidence="ECO:0007829|PDB:3BQ3"
FT HELIX 160..174
FT /evidence="ECO:0007829|PDB:3BQ3"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:3BQ3"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:3BQ3"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:3O2P"
FT HELIX 205..218
FT /evidence="ECO:0007829|PDB:3BQ3"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:3BQ3"
FT HELIX 225..237
FT /evidence="ECO:0007829|PDB:3BQ3"
FT HELIX 241..247
FT /evidence="ECO:0007829|PDB:3BQ3"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:3O2P"
FT HELIX 256..267
FT /evidence="ECO:0007829|PDB:3BQ3"
SQ SEQUENCE 269 AA; 32204 MW; CBD829C941466180 CRC64;
MSNNKIKRKD ASPEQEAIES FTSLTKCDPK VSRKYLQRNH WNINYALNDY YDKEIGTFTD
EVSTVAHPPV YPKELTQVFE HYINNNLFDI DSLVKFIEEL GYNLEDLATL CLAHLLGYKK
LEEPLKREDF LSTWFMQGCS TISDMQECIK TLDVKLHEDL QYFTQIYNYA FNLILDPNRK
DIDTDEGIQY WKLFFQPEYP VRMEPDLLEA WFRFLRDEGK TTISKDTWRM LLLFFKRYPT
IQKIISDYDE TAAWPFIIDE FYECLQDQQ
