DCNL2_MOUSE
ID DCNL2_MOUSE Reviewed; 259 AA.
AC Q8BZJ7; Q3U1U0; Q7TMX3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=DCN1-like protein 2;
DE Short=DCNL2 {ECO:0000250|UniProtKB:Q6PH85};
DE AltName: Full=DCUN1 domain-containing protein 2;
DE AltName: Full=Defective in cullin neddylation protein 1-like protein 2;
GN Name=Dcun1d2 {ECO:0000312|MGI:MGI:2142792}; Synonyms=Dcun1l2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Dendritic cell, and Diencephalon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C3H/He; TISSUE=Mesenchymal stem cell;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Contributes to the neddylation of all cullins by transferring
CC NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to
CC different cullin C-terminal domain-RBX complexes and plays an essential
CC role in the regulation of SCF (SKP1-CUL1-F-box protein)-type complexes
CC activity. {ECO:0000250|UniProtKB:Q6PH85}.
CC -!- SUBUNIT: Interacts (via the DCUN1 domain) with the unneddylated
CC cullins: interacts with CUL1, CUL2, CUL3, CUL4A, CUL4B and CUL5; these
CC interactions promote the cullin neddylation and the identity of the
CC cullin dictates the affinity of the interaction. May also interact with
CC regulators or subunits of cullin-RING ligases such as RBX1, RNF7, ELOB
CC and DDB1; these interactions are bridged by cullins. Interacts with
CC CAND1; this interaction is bridged by cullins such as CUL3 and strongly
CC inhibits the neddylation of CUL3. These CAND-cullin-DCNL complexes can
CC only be neddylated in the presence of a substrate adapter. Interacts
CC (via DCUN1 domain) with the N-terminally acetylated form of UBE2M and
CC UBE2F. {ECO:0000250|UniProtKB:Q6PH85}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6PH85}. Nucleus
CC {ECO:0000250|UniProtKB:Q6PH85}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BZJ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BZJ7-2; Sequence=VSP_015318;
CC Name=3;
CC IsoId=Q8BZJ7-4; Sequence=VSP_027370;
CC -!- DOMAIN: The DCUN1 domain, also known as PONY domain, mediates the
CC interaction with different cullins. The DCUN1 domain mediates the
CC interaction with the N-terminally acetylated NEDD8-conjugating E2s
CC enzyme leading to the NEDD8 transfer from N-terminally acetylated
CC NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX
CC complexes; the neddylation efficiency correlates with the DCUN1D5-
CC cullin and DCUN1D5-E2 interaction affinities.
CC {ECO:0000250|UniProtKB:Q6PH85}.
CC -!- MISCELLANEOUS: [Isoform 2]: Splicing donor and acceptor site not
CC canonical. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC052676; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK034394; BAC28695.1; -; mRNA.
DR EMBL; AK155726; BAE33403.1; -; mRNA.
DR EMBL; AC130818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052676; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS40227.1; -. [Q8BZJ7-4]
DR CCDS; CCDS40228.1; -. [Q8BZJ7-1]
DR RefSeq; NP_001019675.2; NM_001024504.2. [Q8BZJ7-1]
DR RefSeq; NP_001036114.1; NM_001042649.1.
DR RefSeq; NP_001036115.1; NM_001042650.1. [Q8BZJ7-4]
DR RefSeq; NP_001036116.1; NM_001042651.1.
DR AlphaFoldDB; Q8BZJ7; -.
DR SMR; Q8BZJ7; -.
DR BioGRID; 221842; 1.
DR STRING; 10090.ENSMUSP00000047208; -.
DR iPTMnet; Q8BZJ7; -.
DR PhosphoSitePlus; Q8BZJ7; -.
DR EPD; Q8BZJ7; -.
DR MaxQB; Q8BZJ7; -.
DR PaxDb; Q8BZJ7; -.
DR PeptideAtlas; Q8BZJ7; -.
DR PRIDE; Q8BZJ7; -.
DR ProteomicsDB; 279503; -. [Q8BZJ7-1]
DR ProteomicsDB; 279504; -. [Q8BZJ7-2]
DR ProteomicsDB; 279505; -. [Q8BZJ7-4]
DR Antibodypedia; 48901; 98 antibodies from 15 providers.
DR DNASU; 102323; -.
DR Ensembl; ENSMUST00000045366; ENSMUSP00000047208; ENSMUSG00000038506. [Q8BZJ7-1]
DR Ensembl; ENSMUST00000110840; ENSMUSP00000106464; ENSMUSG00000038506. [Q8BZJ7-4]
DR GeneID; 102323; -.
DR KEGG; mmu:102323; -.
DR UCSC; uc009kxg.1; mouse. [Q8BZJ7-1]
DR UCSC; uc009kxj.1; mouse. [Q8BZJ7-4]
DR CTD; 55208; -.
DR MGI; MGI:2142792; Dcun1d2.
DR VEuPathDB; HostDB:ENSMUSG00000038506; -.
DR eggNOG; KOG3077; Eukaryota.
DR GeneTree; ENSGT00940000157453; -.
DR HOGENOM; CLU_047042_0_1_1; -.
DR InParanoid; Q8BZJ7; -.
DR OMA; NEDQAWP; -.
DR OrthoDB; 1418097at2759; -.
DR PhylomeDB; Q8BZJ7; -.
DR TreeFam; TF313332; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR BioGRID-ORCS; 102323; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Dcun1d2; mouse.
DR PRO; PR:Q8BZJ7; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BZJ7; protein.
DR Bgee; ENSMUSG00000038506; Expressed in knee joint and 219 other tissues.
DR ExpressionAtlas; Q8BZJ7; baseline and differential.
DR Genevisible; Q8BZJ7; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0097602; F:cullin family protein binding; ISS:UniProtKB.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0032182; F:ubiquitin-like protein binding; IBA:GO_Central.
DR GO; GO:2000436; P:positive regulation of protein neddylation; ISS:UniProtKB.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0045116; P:protein neddylation; IBA:GO_Central.
DR GO; GO:2000434; P:regulation of protein neddylation; ISS:UniProtKB.
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 Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..259
FT /note="DCN1-like protein 2"
FT /id="PRO_0000129502"
FT DOMAIN 8..45
FT /note="UBA-like"
FT DOMAIN 60..248
FT /note="DCUN1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00574"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 174..233
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027370"
FT VAR_SEQ 202..259
FT /note="EHHKRSIPRDTWNLLLDFGNMIADDLSNYDEEGAWPVLIDDFVEYARPVVTG
FT GRRSPF -> LVSDCFLPFVPNQKEAFLV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015318"
SQ SEQUENCE 259 AA; 30068 MW; 1D032DC36C2D3393 CRC64;
MHKLKSAQKD KVRQFMACTQ ASERTAIYCL TQNEWKLDEA TDSFFQNPEA FHRESMKSSV
DQKKLEQLYS RYKDPQDENK IGIDGIQQFC DDLSLDPASI SVLVIAWKFR AATQCEFSKK
EFVDGMTELG CDSTERLKAL LPRLEQELKD PAKFKDLYQF TFTFAKNPGQ KGLDLEMAVA
YWKLVLSGRF KFLDLWNTFL LEHHKRSIPR DTWNLLLDFG NMIADDLSNY DEEGAWPVLI
DDFVEYARPV VTGGRRSPF
