Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9NXF7 (DCA16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DDB1- and CUL4-associated factor 16
Gene names
Name:DCAF16
Synonyms:C4orf30
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length216 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex. Ref.4

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with DDB1 and CUL4A. Ref.4

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Coding sequence diversityPolymorphism
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein ubiquitination

Inferred by curator Ref.4. Source: UniProtKB

   Cellular_componentCul4-RING ubiquitin ligase complex

Inferred from direct assay Ref.4. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

tatP046082EBI-2559096,EBI-6164389From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 216216DDB1- and CUL4-associated factor 16
PRO_0000301964

Regions

Compositional bias13 – 208Poly-Glu

Amino acid modifications

Modified residue611N6-acetyllysine Ref.5

Natural variations

Natural variant451N → S.
Corresponds to variant rs34085539 [ dbSNP | Ensembl ].
VAR_034917
Natural variant1291T → I.
Corresponds to variant rs7690457 [ dbSNP | Ensembl ].
VAR_034918

Experimental info

Sequence conflict1811W → R in BAG51629. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9NXF7 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: D34295DCBC579986

FASTA21624,193
        10         20         30         40         50         60 
MGPRNPSPDH LSESESEEEE NISYLNESSG EEWDSSEEED SMVPNLSPLE SLAWQVKCLL 

        70         80         90        100        110        120 
KYSTTWKPLN PNSWLYHAKL LDPSTPVHIL REIGLRLSHC SHCVPKLEPI PEWPPLASCG 

       130        140        150        160        170        180 
VPPFQKPLTS PSRLSRDHAT LNGALQFATK QLSRTLSRAT PIPEYLKQIP NSCVSGCCCG 

       190        200        210 
WLTKTVKETT RTEPINTTYS YTDFQKAVNK LLTASL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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].
[2]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. expand/collapse author list , 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
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].
Tissue: Heart, Kidney, Lung and Testis.
[4]"A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1."
Jin J., Arias E.E., Chen J., Harper J.W., Walter J.C.
Mol. Cell 23:709-721(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DDB1 AND CUL4A, IDENTIFICATION BY MASS SPECTROMETRY.
[5]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-61, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK000287 mRNA. Translation: BAA91056.1.
AK056116 mRNA. Translation: BAG51629.1.
CH471069 Genomic DNA. Translation: EAW92784.1.
BC050697 mRNA. Translation: AAH50697.1.
BC068025 mRNA. Translation: AAH68025.1.
BC101716 mRNA. Translation: AAI01717.1.
BC101718 mRNA. Translation: AAI01719.1.
RefSeqNP_060211.3. NM_017741.3.
XP_005248226.1. XM_005248169.1.
XP_005248227.1. XM_005248170.1.
XP_005248228.1. XM_005248171.1.
UniGeneHs.614787.

3D structure databases

ProteinModelPortalQ9NXF7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120224. 14 interactions.
IntActQ9NXF7. 5 interactions.
MINTMINT-8417635.
STRING9606.ENSP00000371682.

PTM databases

PhosphoSiteQ9NXF7.

Polymorphism databases

DMDM74719452.

Proteomic databases

PaxDbQ9NXF7.
PRIDEQ9NXF7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000382247; ENSP00000371682; ENSG00000163257.
ENST00000536863; ENSP00000445736; ENSG00000163257.
GeneID54876.
KEGGhsa:54876.
UCSCuc003gpn.3. human.

Organism-specific databases

CTD54876.
GeneCardsGC04M017802.
HGNCHGNC:25987. DCAF16.
HPAHPA042487.
neXtProtNX_Q9NXF7.
PharmGKBPA165663579.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG70631.
HOGENOMHOG000111466.
HOVERGENHBG101583.
InParanoidQ9NXF7.
OMAEDPVVPN.
OrthoDBEOG7SR4NJ.
PhylomeDBQ9NXF7.
TreeFamTF341783.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

BgeeQ9NXF7.
CleanExHS_C4orf30.
GenevestigatorQ9NXF7.

Family and domain databases

InterProIPR028216. DCAF16.
[Graphical view]
PANTHERPTHR16194:SF0. PTHR16194:SF0. 1 hit.
PfamPF15349. DCA16. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDCAF16. human.
GenomeRNAi54876.
NextBio35469191.
PROQ9NXF7.

Entry information

Entry nameDCA16_HUMAN
AccessionPrimary (citable) accession number: Q9NXF7
Secondary accession number(s): B3KPB7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM