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Protein

DCN1-like protein 2

Gene

DCUN1D2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Potently stimulates the neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes from the NEDD8-conjugating E2 enzyme UBC12. Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
DCN1-like protein 2
Alternative name(s):
DCUN1 domain-containing protein 2
Defective in cullin neddylation protein 1-like protein 2
Gene namesi
Name:DCUN1D2
Synonyms:C13orf17, DCUN1L2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:20328. DCUN1D2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134941036.

Polymorphism and mutation databases

BioMutaiDCUN1D2.
DMDMi73919224.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 259259DCN1-like protein 2PRO_0000129501Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ6PH85.
MaxQBiQ6PH85.
PaxDbiQ6PH85.
PeptideAtlasiQ6PH85.
PRIDEiQ6PH85.

PTM databases

iPTMnetiQ6PH85.
PhosphoSiteiQ6PH85.

Expressioni

Gene expression databases

BgeeiQ6PH85.
CleanExiHS_DCUN1D2.
ExpressionAtlasiQ6PH85. baseline and differential.
GenevisibleiQ6PH85. HS.

Organism-specific databases

HPAiHPA039349.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi120504. 11 interactions.
DIPiDIP-60768N.
IntActiQ6PH85. 4 interactions.
STRINGi9606.ENSP00000417706.

Structurei

Secondary structure

1
259
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi62 – 709Combined sources
Beta strandi77 – 815Combined sources
Helixi83 – 9210Combined sources
Helixi100 – 10910Combined sources
Helixi119 – 12810Combined sources
Helixi134 – 14613Combined sources
Helixi147 – 1493Combined sources
Helixi151 – 16515Combined sources
Beta strandi171 – 1744Combined sources
Helixi175 – 18511Combined sources
Turni187 – 1893Combined sources
Helixi193 – 20210Combined sources
Helixi210 – 22213Combined sources
Helixi238 – 24710Combined sources
Helixi249 – 2513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GAOX-ray3.28A/B/D/G62-259[»]
ProteinModelPortaliQ6PH85.
SMRiQ6PH85. Positions 6-252.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 4538UBA-likeAdd
BLAST
Domaini60 – 248189DCUN1PROSITE-ProRule annotationAdd
BLAST

Domaini

The DCUN1 domain, also known as PONY domain mediates recognition of the N-terminally acetylated NEDD8-conjugating E2 enzyme.1 Publication

Sequence similaritiesi

Contains 1 DCUN1 domain.PROSITE-ProRule annotation
Contains 1 UBA-like domain.Curated

Phylogenomic databases

eggNOGiKOG3077. Eukaryota.
ENOG410XTIJ. LUCA.
GeneTreeiENSGT00550000074529.
HOGENOMiHOG000241761.
HOVERGENiHBG055256.
InParanoidiQ6PH85.
KOiK17822.
OMAiSFHRESM.
OrthoDBiEOG7S4X6Q.
PhylomeDBiQ6PH85.
TreeFamiTF313332.

Family and domain databases

InterProiIPR014764. DCN-prot.
IPR005176. PONY_dom.
IPR009060. UBA-like.
[Graphical view]
PANTHERiPTHR12281. PTHR12281. 1 hit.
PfamiPF03556. Cullin_binding. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
PROSITEiPS51229. DCUN1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6PH85-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MHKLKSSQKD KVRQFMACTQ AGERTAIYCL TQNEWRLDEA TDSFFQNPDS
60 70 80 90 100
LHRESMRNAV DKKKLERLYG RYKDPQDENK IGVDGIQQFC DDLSLDPASI
110 120 130 140 150
SVLVIAWKFR AATQCEFSRK EFLDGMTELG CDSMEKLKAL LPRLEQELKD
160 170 180 190 200
TAKFKDFYQF TFTFAKNPGQ KGLDLEMAVA YWKLVLSGRF KFLDLWNTFL
210 220 230 240 250
MEHHKRSIPR DTWNLLLDFG NMIADDMSNY DEEGAWPVLI DDFVEYARPV

VTGGKRSLF
Length:259
Mass (Da):30,179
Last modified:July 5, 2004 - v1
Checksum:iB12A33F80D419A28
GO
Isoform 2 (identifier: Q6PH85-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     174-186: DLEMAVAYWKLVL → GSPPFLNVKALHH
     187-259: Missing.

Note: No experimental confirmation available.
Show »
Length:186
Mass (Da):21,467
Checksum:iBDFE4F388A59A041
GO

Sequence cautioni

The sequence BAA90944.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAI39428.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI39429.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI39777.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI39778.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI39779.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei174 – 18613DLEMA…WKLVL → GSPPFLNVKALHH in isoform 2. 1 PublicationVSP_015315Add
BLAST
Alternative sequencei187 – 25973Missing in isoform 2. 1 PublicationVSP_015316Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000099 mRNA. Translation: BAA90944.1. Different initiation.
AK001566 mRNA. Translation: BAA91760.1.
AL160251, AL442125 Genomic DNA. Translation: CAI39428.1. Sequence problems.
AL160251, AL442125 Genomic DNA. Translation: CAI39429.1. Sequence problems.
AL442125, AL160251 Genomic DNA. Translation: CAI39777.1. Sequence problems.
AL442125 Genomic DNA. Translation: CAI39778.1. Sequence problems.
AL442125, AL160251 Genomic DNA. Translation: CAI39779.1. Sequence problems.
BC056669 mRNA. Translation: AAH56669.1.
CCDSiCCDS32013.1. [Q6PH85-1]
RefSeqiNP_001014305.1. NM_001014283.1. [Q6PH85-1]
UniGeneiHs.682987.

Genome annotation databases

EnsembliENST00000375403; ENSP00000364552; ENSG00000150401. [Q6PH85-2]
ENST00000478244; ENSP00000417706; ENSG00000150401. [Q6PH85-1]
GeneIDi55208.
KEGGihsa:55208.
UCSCiuc001vtr.2. human. [Q6PH85-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000099 mRNA. Translation: BAA90944.1. Different initiation.
AK001566 mRNA. Translation: BAA91760.1.
AL160251, AL442125 Genomic DNA. Translation: CAI39428.1. Sequence problems.
AL160251, AL442125 Genomic DNA. Translation: CAI39429.1. Sequence problems.
AL442125, AL160251 Genomic DNA. Translation: CAI39777.1. Sequence problems.
AL442125 Genomic DNA. Translation: CAI39778.1. Sequence problems.
AL442125, AL160251 Genomic DNA. Translation: CAI39779.1. Sequence problems.
BC056669 mRNA. Translation: AAH56669.1.
CCDSiCCDS32013.1. [Q6PH85-1]
RefSeqiNP_001014305.1. NM_001014283.1. [Q6PH85-1]
UniGeneiHs.682987.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GAOX-ray3.28A/B/D/G62-259[»]
ProteinModelPortaliQ6PH85.
SMRiQ6PH85. Positions 6-252.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120504. 11 interactions.
DIPiDIP-60768N.
IntActiQ6PH85. 4 interactions.
STRINGi9606.ENSP00000417706.

PTM databases

iPTMnetiQ6PH85.
PhosphoSiteiQ6PH85.

Polymorphism and mutation databases

BioMutaiDCUN1D2.
DMDMi73919224.

Proteomic databases

EPDiQ6PH85.
MaxQBiQ6PH85.
PaxDbiQ6PH85.
PeptideAtlasiQ6PH85.
PRIDEiQ6PH85.

Protocols and materials databases

DNASUi55208.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375403; ENSP00000364552; ENSG00000150401. [Q6PH85-2]
ENST00000478244; ENSP00000417706; ENSG00000150401. [Q6PH85-1]
GeneIDi55208.
KEGGihsa:55208.
UCSCiuc001vtr.2. human. [Q6PH85-1]

Organism-specific databases

CTDi55208.
GeneCardsiDCUN1D2.
HGNCiHGNC:20328. DCUN1D2.
HPAiHPA039349.
neXtProtiNX_Q6PH85.
PharmGKBiPA134941036.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3077. Eukaryota.
ENOG410XTIJ. LUCA.
GeneTreeiENSGT00550000074529.
HOGENOMiHOG000241761.
HOVERGENiHBG055256.
InParanoidiQ6PH85.
KOiK17822.
OMAiSFHRESM.
OrthoDBiEOG7S4X6Q.
PhylomeDBiQ6PH85.
TreeFamiTF313332.

Miscellaneous databases

ChiTaRSiDCUN1D2. human.
GenomeRNAii55208.
PROiQ6PH85.

Gene expression databases

BgeeiQ6PH85.
CleanExiHS_DCUN1D2.
ExpressionAtlasiQ6PH85. baseline and differential.
GenevisibleiQ6PH85. HS.

Family and domain databases

InterProiIPR014764. DCN-prot.
IPR005176. PONY_dom.
IPR009060. UBA-like.
[Graphical view]
PANTHERiPTHR12281. PTHR12281. 1 hit.
PfamiPF03556. Cullin_binding. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
PROSITEiPS51229. DCUN1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORM 2).
    Tissue: Colon and Teratocarcinoma.
  2. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] (ISOFORM 1).
  4. "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 (3.28 ANGSTROMS) OF 62-259 IN COMPLEX WITH UBC12 PEPTIDE, FUNCTION.

Entry informationi

Entry nameiDCNL2_HUMAN
AccessioniPrimary (citable) accession number: Q6PH85
Secondary accession number(s): Q5JSA5
, Q5JSA6, Q5JSA7, Q9NVJ1, Q9NXR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: July 5, 2004
Last modified: July 6, 2016
This is version 109 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 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.