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Protein

DCN1-like protein 3

Gene

DCUN1D3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).1 Publication

GO - Molecular functioni

GO - Biological processi

  • negative regulation of cell growth Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of ubiquitin-protein transferase activity Source: GO_Central
  • protein neddylation Source: GO_Central
  • response to gamma radiation Source: UniProtKB
  • response to UV-C Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
DCN1-like protein 3
Alternative name(s):
DCUN1 domain-containing protein 3
Defective in cullin neddylation protein 1-like protein 3
Squamous cell carcinoma-related oncogene 31 Publication
Gene namesi
Name:DCUN1D3
Synonyms:SCCRO31 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:28734. DCUN1D3.

Subcellular locationi

GO - Cellular componenti

  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
  • ubiquitin ligase complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 2626Missing : No effect on CAND1-, CUL1-, CUL3- and RBX1-binding. 1 PublicationAdd
BLAST
Mutagenesisi2 – 21G → 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. 1 Publication
Mutagenesisi241 – 2411D → 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. 1 Publication
Mutagenesisi265 – 2651A → 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. 1 Publication
Mutagenesisi271 – 2711D → 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. 1 Publication

Organism-specific databases

PharmGKBiPA142672009.

Polymorphism and mutation databases

BioMutaiDCUN1D3.
DMDMi74728175.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedSequence analysis
Chaini2 – 304303DCN1-like protein 3PRO_0000320048Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineSequence analysis

Keywords - PTMi

Lipoprotein, Myristate

Proteomic databases

MaxQBiQ8IWE4.
PaxDbiQ8IWE4.
PRIDEiQ8IWE4.

PTM databases

iPTMnetiQ8IWE4.
PhosphoSiteiQ8IWE4.
SwissPalmiQ8IWE4.

Expressioni

Tissue specificityi

Tends to be down-regulated in different type of cancers, including lung neuroendocrine carcinoma, thyroid Huerthle cell carcinoma and lung squamous cell carcinoma.1 Publication

Gene expression databases

BgeeiQ8IWE4.
CleanExiHS_DCUN1D3.
GenevisibleiQ8IWE4. HS.

Organism-specific databases

HPAiHPA041983.
HPA043511.

Interactioni

Subunit structurei

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).2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi125841. 12 interactions.
DIPiDIP-60769N.
STRINGi9606.ENSP00000319482.

Structurei

Secondary structure

1
304
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi90 – 967Combined sources
Beta strandi101 – 1066Combined sources
Helixi108 – 11710Combined sources
Helixi125 – 1339Combined sources
Helixi144 – 15310Combined sources
Helixi159 – 17214Combined sources
Helixi176 – 19015Combined sources
Turni193 – 1964Combined sources
Beta strandi198 – 2014Combined sources
Helixi202 – 21211Combined sources
Turni213 – 2153Combined sources
Helixi221 – 23010Combined sources
Helixi240 – 25213Combined sources
Helixi268 – 28215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GBAX-ray2.40A/B86-304[»]
ProteinModelPortaliQ8IWE4.
SMRiQ8IWE4. Positions 89-294.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini86 – 278193DCUN1PROSITE-ProRule annotationAdd
BLAST

Domaini

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.2 Publications

Sequence similaritiesi

Contains 1 DCUN1 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3077. Eukaryota.
ENOG410XTIJ. LUCA.
GeneTreeiENSGT00550000074529.
HOGENOMiHOG000241761.
HOVERGENiHBG099655.
InParanoidiQ8IWE4.
KOiK17823.
OMAiWRLVFTQ.
OrthoDBiEOG7QG44H.
PhylomeDBiQ8IWE4.
TreeFamiTF313332.

Family and domain databases

InterProiIPR014764. DCN-prot.
IPR005176. PONY_dom.
[Graphical view]
PANTHERiPTHR12281. PTHR12281. 1 hit.
PfamiPF03556. Cullin_binding. 1 hit.
[Graphical view]
PROSITEiPS51229. DCUN1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8IWE4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQCVTKCKN PSSTLGSKNG DREPSNKSHS RRGAGHREEQ VPPCGKPGGD
60 70 80 90 100
ILVNGTKKAE AATEACQLPT SSGDAGRESK SNAEESSLQR LEELFRRYKD
110 120 130 140 150
EREDAILEEG MERFCNDLCV DPTEFRVLLL AWKFQAATMC KFTRKEFFDG
160 170 180 190 200
CKAISADSID GICARFPSLL TEAKQEDKFK DLYRFTFQFG LDSEEGQRSL
210 220 230 240 250
HREIAIALWK LVFTQNNPPV LDQWLNFLTE NPSGIKGISR DTWNMFLNFT
260 270 280 290 300
QVIGPDLSNY SEDEAWPSLF DTFVEWEMER RKREGEGRGA LSSGPEGLCP

EEQT
Length:304
Mass (Da):34,291
Last modified:March 1, 2003 - v1
Checksum:i4B190AEAE7557A78
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21G → S in a cancer; unknown pathological significance. 1 Publication
VAR_072689
Natural varianti239 – 2391S → F in a cancer; unknown pathological significance. 1 Publication
VAR_072690

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY364247 mRNA. Translation: AAQ76806.1.
AK123719 mRNA. Translation: BAG53946.1.
CH471228 Genomic DNA. Translation: EAW66842.1.
BC040442 mRNA. Translation: AAH40442.1.
CCDSiCCDS10592.1.
RefSeqiNP_775746.1. NM_173475.3.
UniGeneiHs.101007.
Hs.592571.

Genome annotation databases

EnsembliENST00000324344; ENSP00000319482; ENSG00000188215.
ENST00000563934; ENSP00000454762; ENSG00000188215.
GeneIDi123879.
KEGGihsa:123879.
UCSCiuc002dhz.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY364247 mRNA. Translation: AAQ76806.1.
AK123719 mRNA. Translation: BAG53946.1.
CH471228 Genomic DNA. Translation: EAW66842.1.
BC040442 mRNA. Translation: AAH40442.1.
CCDSiCCDS10592.1.
RefSeqiNP_775746.1. NM_173475.3.
UniGeneiHs.101007.
Hs.592571.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GBAX-ray2.40A/B86-304[»]
ProteinModelPortaliQ8IWE4.
SMRiQ8IWE4. Positions 89-294.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125841. 12 interactions.
DIPiDIP-60769N.
STRINGi9606.ENSP00000319482.

PTM databases

iPTMnetiQ8IWE4.
PhosphoSiteiQ8IWE4.
SwissPalmiQ8IWE4.

Polymorphism and mutation databases

BioMutaiDCUN1D3.
DMDMi74728175.

Proteomic databases

MaxQBiQ8IWE4.
PaxDbiQ8IWE4.
PRIDEiQ8IWE4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000324344; ENSP00000319482; ENSG00000188215.
ENST00000563934; ENSP00000454762; ENSG00000188215.
GeneIDi123879.
KEGGihsa:123879.
UCSCiuc002dhz.4. human.

Organism-specific databases

CTDi123879.
GeneCardsiDCUN1D3.
HGNCiHGNC:28734. DCUN1D3.
HPAiHPA041983.
HPA043511.
MIMi616167. gene.
neXtProtiNX_Q8IWE4.
PharmGKBiPA142672009.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3077. Eukaryota.
ENOG410XTIJ. LUCA.
GeneTreeiENSGT00550000074529.
HOGENOMiHOG000241761.
HOVERGENiHBG099655.
InParanoidiQ8IWE4.
KOiK17823.
OMAiWRLVFTQ.
OrthoDBiEOG7QG44H.
PhylomeDBiQ8IWE4.
TreeFamiTF313332.

Miscellaneous databases

GenomeRNAii123879.
PROiQ8IWE4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IWE4.
CleanExiHS_DCUN1D3.
GenevisibleiQ8IWE4. HS.

Family and domain databases

InterProiIPR014764. DCN-prot.
IPR005176. PONY_dom.
[Graphical view]
PANTHERiPTHR12281. PTHR12281. 1 hit.
PfamiPF03556. Cullin_binding. 1 hit.
[Graphical view]
PROSITEiPS51229. DCUN1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "NovelFam3000 -- uncharacterized human protein domains conserved across model organisms."
    Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P., Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.
    BMC Genomics 7:48-48(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.
  5. "SCCRO3 (DCUN1D3) antagonizes the neddylation and oncogenic activity of SCCRO (DCUN1D1)."
    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.
    J. Biol. Chem. 289:34728-34742(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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, VARIANTS SER-2 AND PHE-239.
  6. "Structural conservation of distinctive N-terminal acetylation-dependent interactions across a family of mammalian NEDD8 ligation enzymes."
    Monda J.K., Scott D.C., Miller D.J., Lydeard J., King D., Harper J.W., Bennett E.J., Schulman B.A.
    Structure 21:42-53(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 86-304 IN COMPLEX WITH UBE2F PEPTIDE, INTERACTION OF THE DCUN1 DOMAIN WITH UBE2F AND UBE2M.

Entry informationi

Entry nameiDCNL3_HUMAN
AccessioniPrimary (citable) accession number: Q8IWE4
Secondary accession number(s): B3KVY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.