DCNL5_HUMAN
ID DCNL5_HUMAN Reviewed; 237 AA.
AC Q9BTE7; Q3ZTT2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=DCN1-like protein 5 {ECO:0000305};
DE Short=DCNL5 {ECO:0000303|PubMed:29958295};
DE AltName: Full=DCUN1 domain-containing protein 5;
DE AltName: Full=Defective in cullin neddylation protein 1-like protein 5;
DE AltName: Full=Squamous cell carcinoma-related oncogene 5 {ECO:0000303|PubMed:24192928};
GN Name=DCUN1D5 {ECO:0000312|HGNC:HGNC:28409};
GN Synonyms=SCCRO5 {ECO:0000303|PubMed:24192928};
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 [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-233.
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 [4]
RP SUBCELLULAR LOCATION.
RX PubMed=18445686; DOI=10.1242/jcs.019174;
RA Tegha-Dunghu J., Neumann B., Reber S., Krause R., Erfle H., Walter T.,
RA Held M., Rogers P., Hupfeld K., Ruppert T., Ellenberg J., Gruss O.J.;
RT "EML3 is a nuclear microtubule-binding protein required for the correct
RT alignment of chromosomes in metaphase.";
RL J. Cell Sci. 121:1718-1726(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [6]
RP FUNCTION.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
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., Buerckstuemmer T.,
RA 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP SUBCELLULAR LOCATION, INDUCTION, AND FUNCTION.
RX PubMed=23098533; DOI=10.7314/apjcp.2012.13.8.4157;
RA Guo W., Li G.J., Xu H.B., Xie J.S., Shi T.P., Zhang S.Z., Chen X.H.,
RA Huang Z.G.;
RT "In vitro biological characterization of DCUN1D5 in DNA damage response.";
RL Asian Pac. J. Cancer Prev. 13:4157-4162(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-41 AND SER-48, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP DOMAIN, INTERACTION WITH CUL1; CUL2; CUL3; CUL4A; CUL4B; CUL5; UBE2M AND
RP UBE2F, 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).
RN [13]
RP INTERACTION WITH UBE2M; RBX1; CUL1; CUL2; CUL3 AND CAND1, MUTAGENESIS OF
RP ASP-195; ALA-219; ASP-225 AND GLU-226, FUNCTION, AND DOMAIN.
RX PubMed=24192928; DOI=10.1158/1078-0432.ccr-13-1252;
RA Bommelje C.C., Weeda V.B., Huang G., Shah K., Bains S., Buss E., Shaha M.,
RA Goenen M., Ghossein R., Ramanathan S.Y., Singh B.;
RT "Oncogenic function of SCCRO5/DCUN1D5 requires its Neddylation E3 activity
RT and nuclear localization.";
RL Clin. Cancer Res. 20:372-381(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP DOMAIN, INTERACTION WITH CUL1; CUL2; CUL3; CUL4A; CUL4B; CUL5; CAND1; RBX1;
RP RNF7, ELOB AND DDB1, MUTAGENESIS OF 5-LYS--LYS-8; ASP-195; ALA-219 AND
RP ASP-225, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
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 [16]
RP PHOSPHORYLATION AT SER-41, AND DOMAIN.
RX PubMed=29958295; DOI=10.1371/journal.pone.0199197;
RA Thomas Y., Scott D.C., Kristariyanto Y.A., Rinehart J., Clark K., Cohen P.,
RA Kurz T.;
RT "The NEDD8 E3 ligase DCNL5 is phosphorylated by IKK alpha during Toll-like
RT receptor activation.";
RL PLoS ONE 13:e0199197-e0199197(2018).
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 which is necessary for
CC the activation of cullin-RING E3 ubiquitin ligases (CRLs)
CC (PubMed:26906416, PubMed:23201271, PubMed:19617556). May play a role in
CC DNA damage response and may participate in cell proliferation and
CC anchorage-independent cell growth (PubMed:23098533, PubMed:24192928).
CC {ECO:0000269|PubMed:19617556, ECO:0000269|PubMed:23098533,
CC ECO:0000269|PubMed:23201271, ECO:0000269|PubMed:24192928,
CC ECO:0000269|PubMed:26906416}.
CC -!- SUBUNIT: Part of a complex that contains DCUN1D5, CUL1 and RBX1; this
CC interaction is bridged by CUL1 (PubMed:24192928, PubMed:26906416).
CC Interacts (via the DCUN1 domain) with the unneddylated cullins:
CC 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 (PubMed:24192928,
CC PubMed:26906416, PubMed:23201271). Interacts (via DCUN1 domain) with
CC UBE2M (N-terminally acetylated form) and probably with UBE2F (N-
CC terminally acetylated form) (PubMed:24192928, PubMed:23201271). May
CC also interact with regulators or subunits of cullin-RING ligases such
CC as RBX1, RNF7, ELOB and DDB1; these interactions are bridged by cullins
CC (PubMed:26906416). Interacts with CAND1; this interaction is bridged by
CC cullins and strongly inhibits the neddylation of cullins. These CAND-
CC cullin-DCNL complexes can only be neddylated in the presence of a
CC substrate adapter (PubMed:24192928, PubMed:26906416).
CC {ECO:0000269|PubMed:23201271, ECO:0000269|PubMed:24192928,
CC ECO:0000269|PubMed:26906416}.
CC -!- INTERACTION:
CC Q9BTE7; Q14204: DYNC1H1; NbExp=3; IntAct=EBI-3924013, EBI-356015;
CC Q9BTE7; O60921: HUS1; NbExp=5; IntAct=EBI-3924013, EBI-1056174;
CC Q9BTE7; Q92876: KLK6; NbExp=3; IntAct=EBI-3924013, EBI-2432309;
CC Q9BTE7; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-3924013, EBI-739832;
CC Q9BTE7; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-3924013, EBI-79165;
CC Q9BTE7; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-3924013, EBI-949255;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18445686,
CC ECO:0000269|PubMed:23098533, ECO:0000269|PubMed:26906416}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:18445686}. Note=Subcellular
CC localization is independent of the interaction with cullins.
CC {ECO:0000269|PubMed:26906416}.
CC -!- TISSUE SPECIFICITY: Weakly expressed in testis, skin and immune tissues
CC (thymus, spleen and lymph nodes). {ECO:0000269|PubMed:26906416}.
CC -!- INDUCTION: Expression is decreased in a time-dependent manner after UVC
CC exposure. {ECO:0000269|PubMed:23098533}.
CC -!- DOMAIN: The DCUN1 domain, also known as PONY domain, mediates the
CC interaction with different cullins (PubMed:23201271, PubMed:24192928).
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). {ECO:0000269|PubMed:23201271,
CC ECO:0000269|PubMed:24192928}.
CC -!- PTM: Phosphorylation at Ser-41 is independent of cullin's interaction
CC and neddylation. Phosphorylated in response to both TICAM1 and MYD88
CC dependent Toll-like receptor (TLR) pathway activation (By similarity).
CC Phosphorylated in response to IL1B stimulation (PubMed:29958295).
CC {ECO:0000250|UniProtKB:Q9CXV9, ECO:0000269|PubMed:29958295}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ76805.1; 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; AK056993; BAB71336.1; -; mRNA.
DR EMBL; BC004169; AAH04169.1; -; mRNA.
DR EMBL; AY364246; AAQ76805.1; ALT_FRAME; mRNA.
DR CCDS; CCDS8325.1; -.
DR RefSeq; NP_115675.1; NM_032299.3.
DR AlphaFoldDB; Q9BTE7; -.
DR SMR; Q9BTE7; -.
DR BioGRID; 123986; 68.
DR IntAct; Q9BTE7; 26.
DR MINT; Q9BTE7; -.
DR STRING; 9606.ENSP00000260247; -.
DR BindingDB; Q9BTE7; -.
DR ChEMBL; CHEMBL4295937; -.
DR GlyGen; Q9BTE7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BTE7; -.
DR MetOSite; Q9BTE7; -.
DR PhosphoSitePlus; Q9BTE7; -.
DR BioMuta; DCUN1D5; -.
DR DMDM; 74733117; -.
DR EPD; Q9BTE7; -.
DR jPOST; Q9BTE7; -.
DR MassIVE; Q9BTE7; -.
DR MaxQB; Q9BTE7; -.
DR PaxDb; Q9BTE7; -.
DR PeptideAtlas; Q9BTE7; -.
DR PRIDE; Q9BTE7; -.
DR ProteomicsDB; 78988; -.
DR Antibodypedia; 45452; 31 antibodies from 17 providers.
DR DNASU; 84259; -.
DR Ensembl; ENST00000260247.10; ENSP00000260247.5; ENSG00000137692.12.
DR GeneID; 84259; -.
DR KEGG; hsa:84259; -.
DR MANE-Select; ENST00000260247.10; ENSP00000260247.5; NM_032299.4; NP_115675.1.
DR UCSC; uc001phm.4; human.
DR CTD; 84259; -.
DR DisGeNET; 84259; -.
DR GeneCards; DCUN1D5; -.
DR HGNC; HGNC:28409; DCUN1D5.
DR HPA; ENSG00000137692; Low tissue specificity.
DR MIM; 616522; gene.
DR neXtProt; NX_Q9BTE7; -.
DR OpenTargets; ENSG00000137692; -.
DR PharmGKB; PA142672011; -.
DR VEuPathDB; HostDB:ENSG00000137692; -.
DR eggNOG; KOG3077; Eukaryota.
DR GeneTree; ENSGT00940000156155; -.
DR HOGENOM; CLU_047042_3_1_1; -.
DR InParanoid; Q9BTE7; -.
DR OMA; HERKCKI; -.
DR OrthoDB; 1418097at2759; -.
DR PhylomeDB; Q9BTE7; -.
DR TreeFam; TF354270; -.
DR BRENDA; 2.3.2.32; 2681.
DR PathwayCommons; Q9BTE7; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; Q9BTE7; -.
DR BioGRID-ORCS; 84259; 18 hits in 1078 CRISPR screens.
DR ChiTaRS; DCUN1D5; human.
DR GenomeRNAi; 84259; -.
DR Pharos; Q9BTE7; Tchem.
DR PRO; PR:Q9BTE7; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9BTE7; protein.
DR Bgee; ENSG00000137692; Expressed in secondary oocyte and 180 other tissues.
DR ExpressionAtlas; Q9BTE7; baseline and differential.
DR Genevisible; Q9BTE7; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; 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:0006974; P:cellular response to DNA damage stimulus; 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:0001558; P:regulation of cell growth; IMP:UniProtKB.
DR GO; GO:2000434; P:regulation of protein neddylation; IMP: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 Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..237
FT /note="DCN1-like protein 5"
FT /id="PRO_0000254171"
FT DOMAIN 46..232
FT /note="DCUN1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00574"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:29958295,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MUTAGEN 5..8
FT /note="KKRK->AAAA: Affects nucleus localization."
FT /evidence="ECO:0000269|PubMed:26906416"
FT MUTAGEN 195
FT /note="D->A: Loss of interaction with CUL1, CUL2, CUL3,
FT CUL4A, CUL5, CAND1 and RBX1; when associated with R-219 and
FT A-225. Does not affect localization at nucleus; when
FT associated with R-219 and A-225."
FT /evidence="ECO:0000269|PubMed:26906416"
FT MUTAGEN 195
FT /note="D->N: Loss of interaction with RBX1, CUL1 and
FT CAND1."
FT /evidence="ECO:0000269|PubMed:24192928"
FT MUTAGEN 219
FT /note="A->R: Loss of interaction with RBX1, CUL1 and CAND1.
FT Loss of interaction with CUL1, CUL2, CUL3, CUL4A, CUL5,
FT CAND1 and RBX1; when associated with A-195 and A-225. Does
FT not affect localization at nucleus; when associated with A-
FT 195 and A-225."
FT /evidence="ECO:0000269|PubMed:24192928,
FT ECO:0000269|PubMed:26906416"
FT MUTAGEN 225
FT /note="D->A: Loss of interaction with CUL1, CUL2, CUL3,
FT CUL4A, CUL5, CAND1 and RBX1; when associated with A-195 and
FT R-219. Does not affect localization at nucleus; when
FT associated with A-195 and R-219."
FT /evidence="ECO:0000269|PubMed:26906416"
FT MUTAGEN 225
FT /note="D->N: Loss of interaction with RBX1, CUL1, CUL2,
FT CUL3 and CAND1. Does not affect interaction with UBE2M and
FT NEDD8. Fails to augment Cul3 neddylation beyond basal
FT levels."
FT /evidence="ECO:0000269|PubMed:24192928"
FT MUTAGEN 226
FT /note="E->A: Loss of interaction with RBX1, CUL1, CUL2,
FT CUL3 and CAND1. Does not affect interaction with UBE2M and
FT NEDD8. Fails to augment Cul3 neddylation beyond basal
FT levels."
FT /evidence="ECO:0000269|PubMed:24192928"
FT CONFLICT 227
FT /note="F -> L (in Ref. 3; AAQ76805)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 237 AA; 27508 MW; 4F507B6E5D81EF79 CRC64;
MPVKKKRKSP GVAAAVAEDG GLKKCKISSY CRSQPPARLI SGEEHFSSKK CLAWFYEYAG
PDEVVGPEGM EKFCEDIGVE PENIIMLVLA WKLEAESMGF FTKEEWLKGM TSLQCDCTEK
LQNKFDFLRS QLNDISSFKN IYRYAFDFAR DKDQRSLDID TAKSMLALLL GRTWPLFSVF
YQYLEQSKYR VMNKDQWYNV LEFSRTVHAD LSNYDEDGAW PVLLDEFVEW QKVRQTS
