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DCN1-like protein 3 (DCUN1 domain-containing protein 3) (Defective in cullin neddylation protein 1-like protein 3) (Squamous cell carcinoma-related oncogene 3)

 DCNL3_HUMAN             Reviewed;         304 AA.
Q8IWE4; B3KVY4;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
25-OCT-2017, entry version 110.
RecName: Full=DCN1-like protein 3;
AltName: Full=DCUN1 domain-containing protein 3;
AltName: Full=Defective in cullin neddylation protein 1-like protein 3;
AltName: Full=Squamous cell carcinoma-related oncogene 3 {ECO:0000303|PubMed:25349211};
Name=DCUN1D3; Synonyms=SCCRO3 {ECO:0000303|PubMed:25349211};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=16533400; DOI=10.1186/1471-2164-7-48;
Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P.,
Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.;
"NovelFam3000 -- uncharacterized human protein domains conserved
across model organisms.";
BMC Genomics 7:48-48(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, INTERACTION WITH CAND1; CUL1; CUL3 AND RBX1, LACK OF
INTERACTION WITH UBE2M, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
MUTAGENESIS OF 1-MET--ASN-26; GLY-2; ASP-241; ALA-265 AND ASP-271, AND
VARIANTS SER-2 AND PHE-239.
PubMed=25349211; DOI=10.1074/jbc.M114.585505;
Huang G., Stock C., Bommelje C.C., Weeda V.B., Shah K., Bains S.,
Buss E., Shaha M., Rechler W., Ramanathan S.Y., Singh B.;
"SCCRO3 (DCUN1D3) antagonizes the neddylation and oncogenic activity
of SCCRO (DCUN1D1).";
J. Biol. Chem. 289:34728-34742(2014).
[6]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 86-304 IN COMPLEX WITH UBE2F
PEPTIDE, AND INTERACTION OF THE DCUN1 DOMAIN WITH UBE2F AND UBE2M.
PubMed=23201271; DOI=10.1016/j.str.2012.10.013;
Monda J.K., Scott D.C., Miller D.J., Lydeard J., King D., Harper J.W.,
Bennett E.J., Schulman B.A.;
"Structural conservation of distinctive N-terminal acetylation-
dependent interactions across a family of mammalian NEDD8 ligation
enzymes.";
Structure 21:42-53(2013).
-!- FUNCTION: Antagonizes DCUN1D1-mediated CUL1 neddylation by
sequestering CUL1 at the cell membrane (PubMed:25349211). When
overexpressed in transformed cells, may promote mesenchymal to
epithelial-like changes and inhibit colony formation in soft agar
(PubMed:25349211). {ECO:0000269|PubMed:25349211}.
-!- SUBUNIT: Interacts with CAND1, CUL1, CUL3 and RBX1 through the
DCUN1 domain. In vitro, the DCUN1/PONY domain binds UBE2F and,
with lower affinity, UBE2M (PubMed:23201271). This interaction is
not detected in vivo with full-length protein (PubMed:25349211).
{ECO:0000269|PubMed:23201271, ECO:0000269|PubMed:25349211}.
-!- INTERACTION:
Q13618:CUL3; NbExp=2; IntAct=EBI-15794102, EBI-456129;
Q13618-1:CUL3; NbExp=3; IntAct=EBI-15794102, EBI-15794202;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25349211}.
-!- TISSUE SPECIFICITY: Tends to be down-regulated in different type
of cancers, including lung neuroendocrine carcinoma, thyroid
Huerthle cell carcinoma and lung squamous cell carcinoma.
{ECO:0000269|PubMed:25349211}.
-!- DOMAIN: The DCUN1 domain, also known as PONY domain, mediates
recognition of the N-terminally acetylated NEDD8-conjugating E2
enzyme. This domain is also involved in CAND1-, CUL1-, CUL3- and
RBX1-binding. {ECO:0000269|PubMed:23201271,
ECO:0000269|PubMed:25349211}.
-----------------------------------------------------------------------
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EMBL; AY364247; AAQ76806.1; -; mRNA.
EMBL; AK123719; BAG53946.1; -; mRNA.
EMBL; CH471228; EAW66842.1; -; Genomic_DNA.
EMBL; BC040442; AAH40442.1; -; mRNA.
CCDS; CCDS10592.1; -.
RefSeq; NP_775746.1; NM_173475.3.
UniGene; Hs.101007; -.
UniGene; Hs.592571; -.
PDB; 4GBA; X-ray; 2.40 A; A/B=86-304.
PDBsum; 4GBA; -.
ProteinModelPortal; Q8IWE4; -.
SMR; Q8IWE4; -.
BioGrid; 125841; 15.
DIP; DIP-60769N; -.
ELM; Q8IWE4; -.
IntAct; Q8IWE4; 5.
STRING; 9606.ENSP00000319482; -.
iPTMnet; Q8IWE4; -.
PhosphoSitePlus; Q8IWE4; -.
SwissPalm; Q8IWE4; -.
BioMuta; DCUN1D3; -.
DMDM; 74728175; -.
EPD; Q8IWE4; -.
MaxQB; Q8IWE4; -.
PaxDb; Q8IWE4; -.
PeptideAtlas; Q8IWE4; -.
PRIDE; Q8IWE4; -.
Ensembl; ENST00000324344; ENSP00000319482; ENSG00000188215.
Ensembl; ENST00000563934; ENSP00000454762; ENSG00000188215.
GeneID; 123879; -.
KEGG; hsa:123879; -.
UCSC; uc002dhz.4; human.
CTD; 123879; -.
EuPathDB; HostDB:ENSG00000188215.9; -.
GeneCards; DCUN1D3; -.
HGNC; HGNC:28734; DCUN1D3.
HPA; HPA041983; -.
HPA; HPA043511; -.
MIM; 616167; gene.
neXtProt; NX_Q8IWE4; -.
OpenTargets; ENSG00000188215; -.
PharmGKB; PA142672009; -.
eggNOG; KOG3077; Eukaryota.
eggNOG; ENOG410XTIJ; LUCA.
GeneTree; ENSGT00550000074529; -.
HOGENOM; HOG000241761; -.
HOVERGEN; HBG099655; -.
InParanoid; Q8IWE4; -.
KO; K17823; -.
OMA; VLAWKFQ; -.
OrthoDB; EOG091G091X; -.
PhylomeDB; Q8IWE4; -.
TreeFam; TF313332; -.
Reactome; R-HSA-8951664; Neddylation.
GenomeRNAi; 123879; -.
PRO; PR:Q8IWE4; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000188215; -.
CleanEx; HS_DCUN1D3; -.
Genevisible; Q8IWE4; HS.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
GO; GO:0032182; F:ubiquitin-like protein binding; IBA:GO_Central.
GO; GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IBA:GO_Central.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0045116; P:protein neddylation; IBA:GO_Central.
GO; GO:0010332; P:response to gamma radiation; IDA:UniProtKB.
GO; GO:0010225; P:response to UV-C; IDA:UniProtKB.
InterPro; IPR014764; DCN-prot.
InterPro; IPR005176; PONY_dom.
PANTHER; PTHR12281; PTHR12281; 1.
Pfam; PF03556; Cullin_binding; 1.
PROSITE; PS51229; DCUN1; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Lipoprotein; Membrane;
Myristate; Polymorphism; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000255}.
CHAIN 2 304 DCN1-like protein 3.
/FTId=PRO_0000320048.
DOMAIN 86 278 DCUN1. {ECO:0000255|PROSITE-
ProRule:PRU00574}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000255}.
VARIANT 2 2 G -> S (in a cancer; unknown pathological
significance).
{ECO:0000269|PubMed:25349211}.
/FTId=VAR_072689.
VARIANT 239 239 S -> F (in a cancer; unknown pathological
significance).
{ECO:0000269|PubMed:25349211}.
/FTId=VAR_072690.
MUTAGEN 1 26 Missing: No effect on CAND1-, CUL1-,
CUL3- and RBX1-binding.
{ECO:0000269|PubMed:25349211}.
MUTAGEN 2 2 G->A: No effect on CAND1-, CUL1-,
CUL3- and RBX1-binding. Loss of
localization at the cell membrane. Loss
of function of inhibition of DCUN1D1-
mediated CUL1 neddylation.
{ECO:0000269|PubMed:25349211}.
MUTAGEN 241 241 D->N: Loss of CAND1-, CUL1-, CUL3- and
RBX1-binding. Loss of function of
inhibition of DCUN1D1-mediated CUL1
neddylation, but no effect on
localization at the cell membrane; when
associated with R-265 and N-271.
{ECO:0000269|PubMed:25349211}.
MUTAGEN 265 265 A->R: Loss of CAND1-, CUL1-, CUL3- and
RBX1-binding. Loss of function of
inhibition of DCUN1D1-mediated CUL1
neddylation, but no effect on
localization at the cell membrane; when
associated with N-241 and N-271.
{ECO:0000269|PubMed:25349211}.
MUTAGEN 271 271 D->N: Loss of CAND1-, CUL1-, CUL3- and
RBX1-binding. Loss of function of
inhibition of DCUN1D1-mediated CUL1
neddylation, but no effect on
localization at the cell membrane; when
associated with N-241 and R-265.
{ECO:0000269|PubMed:25349211}.
HELIX 90 96 {ECO:0000244|PDB:4GBA}.
STRAND 101 106 {ECO:0000244|PDB:4GBA}.
HELIX 108 117 {ECO:0000244|PDB:4GBA}.
HELIX 125 133 {ECO:0000244|PDB:4GBA}.
HELIX 144 153 {ECO:0000244|PDB:4GBA}.
HELIX 159 172 {ECO:0000244|PDB:4GBA}.
HELIX 176 190 {ECO:0000244|PDB:4GBA}.
TURN 193 196 {ECO:0000244|PDB:4GBA}.
STRAND 198 201 {ECO:0000244|PDB:4GBA}.
HELIX 202 212 {ECO:0000244|PDB:4GBA}.
TURN 213 215 {ECO:0000244|PDB:4GBA}.
HELIX 221 230 {ECO:0000244|PDB:4GBA}.
HELIX 240 252 {ECO:0000244|PDB:4GBA}.
HELIX 268 282 {ECO:0000244|PDB:4GBA}.
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


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