DCNL3_HUMAN
ID DCNL3_HUMAN Reviewed; 304 AA.
AC Q8IWE4; B3KVY4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=DCN1-like protein 3;
DE Short=DCNL3 {ECO:0000303|PubMed:23201271};
DE AltName: Full=DCUN1 domain-containing protein 3;
DE AltName: Full=Defective in cullin neddylation protein 1-like protein 3;
DE AltName: Full=Squamous cell carcinoma-related oncogene 3 {ECO:0000303|PubMed:25349211};
GN Name=DCUN1D3 {ECO:0000312|HGNC:HGNC:28734};
GN Synonyms=SCCRO3 {ECO:0000303|PubMed:25349211};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16533400; DOI=10.1186/1471-2164-7-48;
RA Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P.,
RA Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.;
RT "NovelFam3000 -- uncharacterized human protein domains conserved across
RT model organisms.";
RL BMC Genomics 7:48-48(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION, AND FUNCTION.
RX PubMed=18823379; DOI=10.1111/j.1349-7006.2008.00929.x;
RA Ma T., Shi T., Huang J., Wu L., Hu F., He P., Deng W., Gao P., Zhang Y.,
RA Song Q., Ma D., Qiu X.;
RT "DCUN1D3, a novel UVC-responsive gene that is involved in cell cycle
RT progression and cell growth.";
RL Cancer Sci. 99:2128-2135(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 [6]
RP FUNCTION, INTERACTION WITH CUL1; CUL2; CUL3 AND UBE2M, MUTAGENESIS OF
RP GLY-2; CYS-4; CYS-8; ASP-241; ALA-265 AND ASP-271, DOMAIN, MYRISTOYLATION
RP AT GLY-2, AND SUBCELLULAR LOCATION.
RX PubMed=19617556; DOI=10.1073/pnas.0812528106;
RA Meyer-Schaller N., Chou Y.C., Sumara I., Martin D.D., Kurz T., Katheder N.,
RA Hofmann K., Berthiaume L.G., Sicheri F., Peter M.;
RT "The human Dcn1-like protein DCNL3 promotes Cul3 neddylation at
RT membranes.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:12365-12370(2009).
RN [7]
RP FUNCTION, INTERACTION WITH CAND1; CUL1; CUL3 AND RBX1, LACK OF INTERACTION
RP WITH UBE2M, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF
RP 1-MET--ASN-26; GLY-2; ASP-241; ALA-265 AND ASP-271, AND VARIANTS SER-2 AND
RP PHE-239.
RX PubMed=25349211; DOI=10.1074/jbc.m114.585505;
RA Huang G., Stock C., Bommelje C.C., Weeda V.B., Shah K., Bains S., Buss E.,
RA Shaha M., Rechler W., Ramanathan S.Y., Singh B.;
RT "SCCRO3 (DCUN1D3) antagonizes the neddylation and oncogenic activity of
RT SCCRO (DCUN1D1).";
RL J. Biol. Chem. 289:34728-34742(2014).
RN [8]
RP INTERACTION WITH CUL1; CUL2; CUL3; CUL4A; CUL4B; CUL5; CAND1; RBX1; RNF7;
RP ELOB AND DDB1, SUBCELLULAR LOCATION, FUNCTION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF ASP-241; ALA-265 AND ASP-271.
RX PubMed=26906416; DOI=10.1242/jcs.181784;
RA Keuss M.J., Thomas Y., Mcarthur R., Wood N.T., Knebel A., Kurz T.;
RT "Characterization of the mammalian family of DCN-type NEDD8 E3 ligases.";
RL J. Cell Sci. 129:1441-1454(2016).
RN [9]
RP INTERACTION WITH CAND1 AND CUL1, AND FUNCTION.
RX PubMed=27542266; DOI=10.18632/oncotarget.11302;
RA Zhang S., Huang J., Shi T., Hu F., Zhang L., Zhou P.K., Ma D., Ma T.,
RA Qiu X.;
RT "DCUN1D3 activates SCFSKP2 ubiquitin E3 ligase activity and cell cycle
RT progression under UV damage.";
RL Oncotarget 7:58483-58491(2016).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 86-304 IN COMPLEX WITH UBE2F
RP PEPTIDE, INTERACTION OF THE DCUN1 DOMAIN WITH CUL1; CUL2; CUL3; CUL4A;
RP CUL4B; CUL5; UBE2F AND UBE2M, AND FUNCTION.
RX PubMed=23201271; DOI=10.1016/j.str.2012.10.013;
RA Monda J.K., Scott D.C., Miller D.J., Lydeard J., King D., Harper J.W.,
RA Bennett E.J., Schulman B.A.;
RT "Structural conservation of distinctive N-terminal acetylation-dependent
RT interactions across a family of mammalian NEDD8 ligation enzymes.";
RL Structure 21:42-53(2013).
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 may play a role in
CC the cell cycle progression by regulating the SCF ubiquitin E3 ligase
CC complex, after UV damage (PubMed:23201271, PubMed:19617556,
CC PubMed:27542266, PubMed:18823379). At the cell membrane, can promote
CC and as well inhibit cullins neddylation (PubMed:19617556,
CC PubMed:26906416, PubMed:25349211). {ECO:0000269|PubMed:18823379,
CC ECO:0000269|PubMed:19617556, ECO:0000269|PubMed:23201271,
CC ECO:0000269|PubMed:25349211, ECO:0000269|PubMed:26906416,
CC ECO:0000269|PubMed:27542266}.
CC -!- SUBUNIT: Part of a complex containing DCUN1D3, CUL3 and RBX1
CC (PubMed:19617556). Interacts (via the DCUN1 domain) with the
CC unneddylated cullins: interacts with CUL1, CUL2, CUL3, CUL4A, CUL4B and
CC CUL5; these interactions promote the cullin neddylation and the
CC identity of the cullin dictates the affinity of the interaction
CC (PubMed:26906416, PubMed:23201271, PubMed:27542266). Interacts
CC preferentially with CUL3; this interaction triggers the relocalization
CC of CUL3 to the cell membrane where CUL3 is neddylated
CC (PubMed:19617556). Interacts (via DCUN1 domain) with RBX1
CC (PubMed:26906416, PubMed:25349211). May also interact with regulators
CC or subunits of cullin-RING ligases such as RNF7, ELOB and DDB1; these
CC interactions are bridged by cullins (PubMed:26906416). Interacts (via
CC DCUN1 domain) with CAND1; this interaction is bridged by cullins and
CC strongly inhibits cullin neddylation (PubMed:26906416,
CC PubMed:27542266). These CAND-cullin-DCNL complexes can only be
CC neddylated in the presence of a substrate adapter (PubMed:26906416).
CC Interacts (via DCUN1 domain) with the N-terminally acetylated form of
CC UBE2M and UBE2F (PubMed:23201271, PubMed:25349211, PubMed:19617556).
CC {ECO:0000269|PubMed:19617556, ECO:0000269|PubMed:23201271,
CC ECO:0000269|PubMed:25349211, ECO:0000269|PubMed:26906416,
CC ECO:0000269|PubMed:27542266}.
CC -!- INTERACTION:
CC Q8IWE4; Q13618: CUL3; NbExp=2; IntAct=EBI-15794102, EBI-456129;
CC Q8IWE4; Q13618-1: CUL3; NbExp=3; IntAct=EBI-15794102, EBI-15794202;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19617556,
CC ECO:0000269|PubMed:25349211, ECO:0000269|PubMed:26906416}. Cytoplasm
CC {ECO:0000269|PubMed:18823379, ECO:0000269|PubMed:26906416}. Nucleus
CC {ECO:0000269|PubMed:18823379, ECO:0000269|PubMed:26906416}. Cytoplasm,
CC perinuclear region {ECO:0000269|PubMed:18823379}. Note=After UVC
CC treatment, the protein enters to the nucleus gradually
CC (PubMed:18823379). Cell membrane localization is essential for CUL3
CC neddylation (PubMed:19617556). {ECO:0000269|PubMed:18823379,
CC ECO:0000269|PubMed:19617556}.
CC -!- TISSUE SPECIFICITY: Tends to be down-regulated in different type of
CC cancers, including lung neuroendocrine carcinoma, thyroid Huerthle cell
CC carcinoma and lung squamous cell carcinoma (PubMed:25349211). Mostly
CC expressed in testis and brain (PubMed:26906416). Highly expressed in
CC liver, bladder and renal normal tissue than their tumor tissue
CC counterparts (PubMed:18823379). Palmitoylation stabilizes DCUN1D3 at
CC the cell membrane (PubMed:19617556). {ECO:0000269|PubMed:18823379,
CC ECO:0000269|PubMed:19617556, ECO:0000269|PubMed:25349211,
CC ECO:0000269|PubMed:26906416}.
CC -!- INDUCTION: Increases by UVC treatment. {ECO:0000269|PubMed:18823379}.
CC -!- DOMAIN: The DCUN1 domain, also known as PONY domain, mediates the
CC interaction with different cullins (PubMed:23201271, PubMed:19617556).
CC The DCUN1 domain mediates the interaction with the N-terminally
CC acetylated NEDD8-conjugating E2s enzyme leading to the NEDD8 transfer
CC from N-terminally acetylated NEDD8-conjugating E2s enzyme to different
CC cullin C-terminal domain-RBX complexes; the neddylation efficiency
CC correlates with the DCUN1D5-cullin and DCUN1D5-E2 interaction
CC affinities (PubMed:23201271). This domain is also involved in CAND1-,
CC cullins- and RBX1-binding (PubMed:25349211, PubMed:26906416).
CC {ECO:0000269|PubMed:19617556, ECO:0000269|PubMed:23201271,
CC ECO:0000269|PubMed:25349211, ECO:0000269|PubMed:26906416}.
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DR EMBL; AY364247; AAQ76806.1; -; mRNA.
DR EMBL; AK123719; BAG53946.1; -; mRNA.
DR EMBL; CH471228; EAW66842.1; -; Genomic_DNA.
DR EMBL; BC040442; AAH40442.1; -; mRNA.
DR CCDS; CCDS10592.1; -.
DR RefSeq; NP_775746.1; NM_173475.3.
DR PDB; 4GBA; X-ray; 2.40 A; A/B=86-304.
DR PDBsum; 4GBA; -.
DR AlphaFoldDB; Q8IWE4; -.
DR SMR; Q8IWE4; -.
DR BioGRID; 125841; 25.
DR DIP; DIP-60769N; -.
DR ELM; Q8IWE4; -.
DR IntAct; Q8IWE4; 10.
DR MINT; Q8IWE4; -.
DR STRING; 9606.ENSP00000319482; -.
DR BindingDB; Q8IWE4; -.
DR ChEMBL; CHEMBL4295894; -.
DR iPTMnet; Q8IWE4; -.
DR PhosphoSitePlus; Q8IWE4; -.
DR SwissPalm; Q8IWE4; -.
DR BioMuta; DCUN1D3; -.
DR DMDM; 74728175; -.
DR EPD; Q8IWE4; -.
DR jPOST; Q8IWE4; -.
DR MassIVE; Q8IWE4; -.
DR MaxQB; Q8IWE4; -.
DR PaxDb; Q8IWE4; -.
DR PeptideAtlas; Q8IWE4; -.
DR PRIDE; Q8IWE4; -.
DR ProteomicsDB; 70849; -.
DR Antibodypedia; 25634; 65 antibodies from 18 providers.
DR DNASU; 123879; -.
DR Ensembl; ENST00000324344.9; ENSP00000319482.3; ENSG00000188215.10.
DR Ensembl; ENST00000563934.1; ENSP00000454762.1; ENSG00000188215.10.
DR GeneID; 123879; -.
DR KEGG; hsa:123879; -.
DR MANE-Select; ENST00000324344.9; ENSP00000319482.3; NM_173475.4; NP_775746.1.
DR UCSC; uc002dhz.4; human.
DR CTD; 123879; -.
DR DisGeNET; 123879; -.
DR GeneCards; DCUN1D3; -.
DR HGNC; HGNC:28734; DCUN1D3.
DR HPA; ENSG00000188215; Low tissue specificity.
DR MIM; 616167; gene.
DR neXtProt; NX_Q8IWE4; -.
DR OpenTargets; ENSG00000188215; -.
DR PharmGKB; PA142672009; -.
DR VEuPathDB; HostDB:ENSG00000188215; -.
DR eggNOG; KOG3077; Eukaryota.
DR GeneTree; ENSGT00940000154944; -.
DR HOGENOM; CLU_047042_2_0_1; -.
DR InParanoid; Q8IWE4; -.
DR OMA; ILDQWLH; -.
DR OrthoDB; 1418097at2759; -.
DR PhylomeDB; Q8IWE4; -.
DR TreeFam; TF313332; -.
DR PathwayCommons; Q8IWE4; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; Q8IWE4; -.
DR BioGRID-ORCS; 123879; 25 hits in 1087 CRISPR screens.
DR GenomeRNAi; 123879; -.
DR Pharos; Q8IWE4; Tchem.
DR PRO; PR:Q8IWE4; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8IWE4; protein.
DR Bgee; ENSG00000188215; Expressed in secondary oocyte and 172 other tissues.
DR Genevisible; Q8IWE4; HS.
DR GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
DR GO; GO:0005634; C:nucleus; IMP:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0097602; F:cullin family protein binding; IMP: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:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:2000435; P:negative regulation of protein neddylation; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:2000436; P:positive regulation of protein neddylation; IMP: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:0010564; P:regulation of cell cycle process; IMP:UniProtKB.
DR GO; GO:2000434; P:regulation of protein neddylation; IMP:UniProtKB.
DR GO; GO:0010332; P:response to gamma radiation; IDA:UniProtKB.
DR GO; GO:0010225; P:response to UV-C; IDA: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 PANTHER; PTHR12281; PTHR12281; 1.
DR Pfam; PF03556; Cullin_binding; 1.
DR PROSITE; PS51229; DCUN1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm; Lipoprotein; Membrane; Myristate;
KW Nucleus; Palmitate; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..304
FT /note="DCN1-like protein 3"
FT /id="PRO_0000320048"
FT DOMAIN 86..278
FT /note="DCUN1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00574"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:19617556"
FT VARIANT 2
FT /note="G -> S (in a cancer; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:25349211"
FT /id="VAR_072689"
FT VARIANT 239
FT /note="S -> F (in a cancer; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:25349211"
FT /id="VAR_072690"
FT MUTAGEN 1..26
FT /note="Missing: No effect on CAND1-, CUL1-, CUL3- and RBX1-
FT binding."
FT /evidence="ECO:0000269|PubMed:25349211"
FT MUTAGEN 2
FT /note="G->A: No effect on CAND1-, CUL1-, CUL3- and RBX1-
FT binding. Loss of localization at the cell membrane. Loss of
FT function of inhibition of DCUN1D1-mediated CUL1
FT neddylation. Loss of myristoylation. Loss of
FT myristoylation; when associated with A-4. Loss of
FT myristoylation; when associated with A-8. Loss of
FT palmitoylation. Affects cell membrane localization, and
FT localizes throughout the cytoplasm. Does not relocalizes
FT CUL3 to the cell membrane."
FT /evidence="ECO:0000269|PubMed:19617556,
FT ECO:0000269|PubMed:25349211"
FT MUTAGEN 4
FT /note="C->A: Does not affect myristoylation; when
FT associated with A-8. Loss of myristoylation; when
FT associated with A-2. Loss of palmitoylation; when
FT associated with A-8. Reduces cell membrane localization."
FT /evidence="ECO:0000269|PubMed:19617556"
FT MUTAGEN 8
FT /note="C->A: Does not affect myristoylation; when
FT associated with A-4. Loss of myristoylation; when
FT associated with A-2. Loss of palmitoylation; when
FT associated with A-4. Reduces cell membrane localization."
FT /evidence="ECO:0000269|PubMed:19617556"
FT MUTAGEN 241
FT /note="D->A: Loss of interaction with CUL1, CUL2, CUL3,
FT CULA4, CULA5, CAND1 and RBX1; when associated with R-265
FT and A-271. Does not affect both nucleus and cytoplasm
FT localization; when associated with R-265 and A-271. Loss of
FT interaction with CUL3; when associated with R-265 and A-
FT 271."
FT /evidence="ECO:0000269|PubMed:19617556,
FT ECO:0000269|PubMed:26906416"
FT MUTAGEN 241
FT /note="D->N: Loss of CAND1-, CUL1-, CUL3- and RBX1-binding.
FT Loss of function of inhibition of DCUN1D1-mediated CUL1
FT neddylation, but no effect on localization at the cell
FT membrane; when associated with R-265 and N-271."
FT /evidence="ECO:0000269|PubMed:25349211"
FT MUTAGEN 265
FT /note="A->R: Loss of CAND1-, CUL1-, CUL3- and RBX1-binding.
FT Loss of function of inhibition of DCUN1D1-mediated CUL1
FT neddylation, but no effect on localization at the cell
FT membrane; when associated with N-241 and N-271. Loss of
FT interaction with CUL1, CUL2, CUL3, CULA4, CULA5, CAND1 and
FT RBX1; when associated with A-241 and A-271. Does not affect
FT both nucleus and cytoplasm localization; when associated
FT with A-241 and A-271. Loss of interaction with CUL3; when
FT associated with A-241 and A-271."
FT /evidence="ECO:0000269|PubMed:19617556,
FT ECO:0000269|PubMed:25349211, ECO:0000269|PubMed:26906416"
FT MUTAGEN 271
FT /note="D->A: Loss of interaction with CUL1, CUL2, CUL3,
FT CULA4, CULA5 CALD1 and RBX1; when associated with A-241 and
FT R-265. Does not affect both nucleus and cytoplasm
FT localization; when associated with A-241 and R-265. Loss of
FT interaction with CUL3; when associated with A-241 and A-
FT 271."
FT /evidence="ECO:0000269|PubMed:19617556,
FT ECO:0000269|PubMed:26906416"
FT MUTAGEN 271
FT /note="D->N: Loss of CAND1-, CUL1-, CUL3- and RBX1-binding.
FT Loss of function of inhibition of DCUN1D1-mediated CUL1
FT neddylation, but no effect on localization at the cell
FT membrane; when associated with N-241 and R-265."
FT /evidence="ECO:0000269|PubMed:25349211"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:4GBA"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:4GBA"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:4GBA"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:4GBA"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:4GBA"
FT HELIX 159..172
FT /evidence="ECO:0007829|PDB:4GBA"
FT HELIX 176..190
FT /evidence="ECO:0007829|PDB:4GBA"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:4GBA"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:4GBA"
FT HELIX 202..212
FT /evidence="ECO:0007829|PDB:4GBA"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:4GBA"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:4GBA"
FT HELIX 240..252
FT /evidence="ECO:0007829|PDB:4GBA"
FT HELIX 268..282
FT /evidence="ECO:0007829|PDB:4GBA"
SQ SEQUENCE 304 AA; 34291 MW; 4B190AEAE7557A78 CRC64;
MGQCVTKCKN PSSTLGSKNG DREPSNKSHS RRGAGHREEQ VPPCGKPGGD ILVNGTKKAE
AATEACQLPT SSGDAGRESK SNAEESSLQR LEELFRRYKD EREDAILEEG MERFCNDLCV
DPTEFRVLLL AWKFQAATMC KFTRKEFFDG CKAISADSID GICARFPSLL TEAKQEDKFK
DLYRFTFQFG LDSEEGQRSL HREIAIALWK LVFTQNNPPV LDQWLNFLTE NPSGIKGISR
DTWNMFLNFT QVIGPDLSNY SEDEAWPSLF DTFVEWEMER RKREGEGRGA LSSGPEGLCP
EEQT
