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Q9NXF7

- DCA16_HUMAN

UniProt

Q9NXF7 - DCA16_HUMAN

Protein

DDB1- and CUL4-associated factor 16

Gene

DCAF16

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex.1 Publication

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. protein ubiquitination Source: UniProtKB

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DDB1- and CUL4-associated factor 16
    Gene namesi
    Name:DCAF16
    Synonyms:C4orf30
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:25987. DCAF16.

    Subcellular locationi

    GO - Cellular componenti

    1. Cul4-RING E3 ubiquitin ligase complex Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA165663579.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 216216DDB1- and CUL4-associated factor 16PRO_0000301964Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei61 – 611N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9NXF7.
    PaxDbiQ9NXF7.
    PRIDEiQ9NXF7.

    PTM databases

    PhosphoSiteiQ9NXF7.

    Expressioni

    Gene expression databases

    BgeeiQ9NXF7.
    CleanExiHS_C4orf30.
    GenevestigatoriQ9NXF7.

    Organism-specific databases

    HPAiHPA042487.

    Interactioni

    Subunit structurei

    Interacts with DDB1 and CUL4A.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    tatP046082EBI-2559096,EBI-6164389From a different organism.

    Protein-protein interaction databases

    BioGridi120224. 13 interactions.
    IntActiQ9NXF7. 5 interactions.
    MINTiMINT-8417635.
    STRINGi9606.ENSP00000371682.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NXF7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi13 – 208Poly-Glu

    Phylogenomic databases

    eggNOGiNOG70631.
    HOGENOMiHOG000111466.
    HOVERGENiHBG101583.
    InParanoidiQ9NXF7.
    OMAiEDPVVPN.
    OrthoDBiEOG7SR4NJ.
    PhylomeDBiQ9NXF7.
    TreeFamiTF341783.

    Family and domain databases

    InterProiIPR028216. DCAF16.
    [Graphical view]
    PANTHERiPTHR16194:SF0. PTHR16194:SF0. 1 hit.
    PfamiPF15349. DCA16. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9NXF7-1 [UniParc]FASTAAdd to Basket

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    MGPRNPSPDH LSESESEEEE NISYLNESSG EEWDSSEEED SMVPNLSPLE    50
    SLAWQVKCLL KYSTTWKPLN PNSWLYHAKL LDPSTPVHIL REIGLRLSHC 100
    SHCVPKLEPI PEWPPLASCG VPPFQKPLTS PSRLSRDHAT LNGALQFATK 150
    QLSRTLSRAT PIPEYLKQIP NSCVSGCCCG WLTKTVKETT RTEPINTTYS 200
    YTDFQKAVNK LLTASL 216
    Length:216
    Mass (Da):24,193
    Last modified:October 1, 2000 - v1
    Checksum:iD34295DCBC579986
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti181 – 1811W → R in BAG51629. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti45 – 451N → S.
    Corresponds to variant rs34085539 [ dbSNP | Ensembl ].
    VAR_034917
    Natural varianti129 – 1291T → I.
    Corresponds to variant rs7690457 [ dbSNP | Ensembl ].
    VAR_034918

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS3423.1.
    RefSeqiNP_060211.3. NM_017741.3.
    XP_005248226.1. XM_005248169.1.
    XP_005248227.1. XM_005248170.1.
    XP_005248228.1. XM_005248171.1.
    XP_006714029.1. XM_006713966.1.
    UniGeneiHs.614787.

    Genome annotation databases

    EnsembliENST00000382247; ENSP00000371682; ENSG00000163257.
    GeneIDi54876.
    KEGGihsa:54876.
    UCSCiuc003gpn.3. human.

    Polymorphism databases

    DMDMi74719452.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS3423.1.
    RefSeqi NP_060211.3. NM_017741.3.
    XP_005248226.1. XM_005248169.1.
    XP_005248227.1. XM_005248170.1.
    XP_005248228.1. XM_005248171.1.
    XP_006714029.1. XM_006713966.1.
    UniGenei Hs.614787.

    3D structure databases

    ProteinModelPortali Q9NXF7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120224. 13 interactions.
    IntActi Q9NXF7. 5 interactions.
    MINTi MINT-8417635.
    STRINGi 9606.ENSP00000371682.

    PTM databases

    PhosphoSitei Q9NXF7.

    Polymorphism databases

    DMDMi 74719452.

    Proteomic databases

    MaxQBi Q9NXF7.
    PaxDbi Q9NXF7.
    PRIDEi Q9NXF7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000382247 ; ENSP00000371682 ; ENSG00000163257 .
    GeneIDi 54876.
    KEGGi hsa:54876.
    UCSCi uc003gpn.3. human.

    Organism-specific databases

    CTDi 54876.
    GeneCardsi GC04M017802.
    HGNCi HGNC:25987. DCAF16.
    HPAi HPA042487.
    neXtProti NX_Q9NXF7.
    PharmGKBi PA165663579.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG70631.
    HOGENOMi HOG000111466.
    HOVERGENi HBG101583.
    InParanoidi Q9NXF7.
    OMAi EDPVVPN.
    OrthoDBi EOG7SR4NJ.
    PhylomeDBi Q9NXF7.
    TreeFami TF341783.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    ChiTaRSi DCAF16. human.
    GenomeRNAii 54876.
    NextBioi 35469191.
    PROi Q9NXF7.

    Gene expression databases

    Bgeei Q9NXF7.
    CleanExi HS_C4orf30.
    Genevestigatori Q9NXF7.

    Family and domain databases

    InterProi IPR028216. DCAF16.
    [Graphical view ]
    PANTHERi PTHR16194:SF0. PTHR16194:SF0. 1 hit.
    Pfami PF15349. DCA16. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].
    2. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDCA16_HUMAN
    AccessioniPrimary (citable) accession number: Q9NXF7
    Secondary accession number(s): B3KPB7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 84 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways

    External Data

    Dasty 3