ID   DCA16_HUMAN             Reviewed;         216 AA.
AC   Q9NXF7; B3KPB7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 137.
DE   RecName: Full=DDB1- and CUL4-associated factor 16 {ECO:0000305};
GN   Name=DCAF16 {ECO:0000312|HGNC:HGNC:25987}; Synonyms=C4orf30;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart, Kidney, Lung, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, INTERACTION WITH DDB1 AND CUL4A, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=16949367; DOI=10.1016/j.molcel.2006.08.010;
RA   Jin J., Arias E.E., Chen J., Harper J.W., Walter J.C.;
RT   "A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is
RT   required for S phase destruction of the replication factor Cdt1.";
RL   Mol. Cell 23:709-721(2006).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-61, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [7]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=31209349; DOI=10.1038/s41589-019-0279-5;
RA   Zhang X., Crowley V.M., Wucherpfennig T.G., Dix M.M., Cravatt B.F.;
RT   "Electrophilic PROTACs that degrade nuclear proteins by engaging DCAF16.";
RL   Nat. Chem. Biol. 15:737-746(2019).
CC   -!- FUNCTION: Functions as a substrate recognition component for CUL4-DDB1
CC       E3 ubiquitin-protein ligase complex, which mediates ubiquitination and
CC       proteasome-dependent degradation of nuclear proteins.
CC       {ECO:0000269|PubMed:16949367, ECO:0000269|PubMed:31209349}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with DDB1 and CUL4A. {ECO:0000269|PubMed:16949367}.
CC   -!- INTERACTION:
CC       Q9NXF7; P04608: tat; Xeno; NbExp=2; IntAct=EBI-2559096, EBI-6164389;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31209349}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK000287; BAA91056.1; -; mRNA.
DR   EMBL; AK056116; BAG51629.1; -; mRNA.
DR   EMBL; CH471069; EAW92784.1; -; Genomic_DNA.
DR   EMBL; BC050697; AAH50697.1; -; mRNA.
DR   EMBL; BC068025; AAH68025.1; -; mRNA.
DR   EMBL; BC101716; AAI01717.1; -; mRNA.
DR   EMBL; BC101718; AAI01719.1; -; mRNA.
DR   CCDS; CCDS3423.1; -.
DR   RefSeq; NP_001332809.1; NM_001345880.1.
DR   RefSeq; NP_001332810.1; NM_001345881.1.
DR   RefSeq; NP_001332811.1; NM_001345882.1.
DR   RefSeq; NP_001332813.1; NM_001345884.1.
DR   RefSeq; NP_001332814.1; NM_001345885.1.
DR   RefSeq; NP_060211.3; NM_017741.3.
DR   RefSeq; XP_016863816.1; XM_017008327.1.
DR   RefSeq; XP_016863817.1; XM_017008328.1.
DR   PDB; 8G46; EM; 2.20 A; B=1-216.
DR   PDB; 8OV6; EM; 3.77 A; B=1-216.
DR   PDBsum; 8G46; -.
DR   PDBsum; 8OV6; -.
DR   AlphaFoldDB; Q9NXF7; -.
DR   EMDB; EMD-17172; -.
DR   SMR; Q9NXF7; -.
DR   BioGRID; 120224; 67.
DR   ComplexPortal; CPX-2413; CRL4-DCAF16 E3 ubiquitin ligase complex, CUL4A variant.
DR   ComplexPortal; CPX-2414; CRL4-DCAF16 E3 ubiquitin ligase complex, CUL4B variant.
DR   IntAct; Q9NXF7; 26.
DR   MINT; Q9NXF7; -.
DR   STRING; 9606.ENSP00000371682; -.
DR   iPTMnet; Q9NXF7; -.
DR   PhosphoSitePlus; Q9NXF7; -.
DR   BioMuta; DCAF16; -.
DR   DMDM; 74719452; -.
DR   EPD; Q9NXF7; -.
DR   jPOST; Q9NXF7; -.
DR   MassIVE; Q9NXF7; -.
DR   MaxQB; Q9NXF7; -.
DR   PaxDb; 9606-ENSP00000371682; -.
DR   PeptideAtlas; Q9NXF7; -.
DR   ProteomicsDB; 83088; -.
DR   Pumba; Q9NXF7; -.
DR   Antibodypedia; 51178; 19 antibodies from 10 providers.
DR   DNASU; 54876; -.
DR   Ensembl; ENST00000382247.6; ENSP00000371682.1; ENSG00000163257.11.
DR   GeneID; 54876; -.
DR   KEGG; hsa:54876; -.
DR   MANE-Select; ENST00000382247.6; ENSP00000371682.1; NM_017741.4; NP_060211.3.
DR   UCSC; uc003gpn.3; human.
DR   AGR; HGNC:25987; -.
DR   CTD; 54876; -.
DR   DisGeNET; 54876; -.
DR   GeneCards; DCAF16; -.
DR   HGNC; HGNC:25987; DCAF16.
DR   HPA; ENSG00000163257; Low tissue specificity.
DR   MIM; 620524; gene.
DR   neXtProt; NX_Q9NXF7; -.
DR   OpenTargets; ENSG00000163257; -.
DR   PharmGKB; PA165663579; -.
DR   VEuPathDB; HostDB:ENSG00000163257; -.
DR   eggNOG; ENOG502RC7Y; Eukaryota.
DR   GeneTree; ENSGT00390000012430; -.
DR   HOGENOM; CLU_111172_0_0_1; -.
DR   InParanoid; Q9NXF7; -.
DR   OMA; SGQEWDS; -.
DR   OrthoDB; 4732296at2759; -.
DR   PhylomeDB; Q9NXF7; -.
DR   TreeFam; TF341783; -.
DR   PathwayCommons; Q9NXF7; -.
DR   Reactome; R-HSA-8951664; Neddylation.
DR   SignaLink; Q9NXF7; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 54876; 7 hits in 1181 CRISPR screens.
DR   ChiTaRS; DCAF16; human.
DR   GenomeRNAi; 54876; -.
DR   Pharos; Q9NXF7; Tdark.
DR   PRO; PR:Q9NXF7; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q9NXF7; Protein.
DR   Bgee; ENSG00000163257; Expressed in calcaneal tendon and 192 other cell types or tissues.
DR   GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR028216; DCAF16.
DR   PANTHER; PTHR16194; DDB1- AND CUL4-ASSOCIATED FACTOR 16; 1.
DR   PANTHER; PTHR16194:SF0; DDB1- AND CUL4-ASSOCIATED FACTOR 16; 1.
DR   Pfam; PF15349; DCA16; 1.
DR   Genevisible; Q9NXF7; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Nucleus; Reference proteome;
KW   Ubl conjugation pathway.
FT   CHAIN           1..216
FT                   /note="DDB1- and CUL4-associated factor 16"
FT                   /id="PRO_0000301964"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..39
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         61
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VARIANT         45
FT                   /note="N -> S (in dbSNP:rs34085539)"
FT                   /id="VAR_034917"
FT   VARIANT         129
FT                   /note="T -> I (in dbSNP:rs7690457)"
FT                   /id="VAR_034918"
FT   CONFLICT        181
FT                   /note="W -> R (in Ref. 1; BAG51629)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   216 AA;  24193 MW;  D34295DCBC579986 CRC64;
     MGPRNPSPDH LSESESEEEE NISYLNESSG EEWDSSEEED SMVPNLSPLE SLAWQVKCLL
     KYSTTWKPLN PNSWLYHAKL LDPSTPVHIL REIGLRLSHC SHCVPKLEPI PEWPPLASCG
     VPPFQKPLTS PSRLSRDHAT LNGALQFATK QLSRTLSRAT PIPEYLKQIP NSCVSGCCCG
     WLTKTVKETT RTEPINTTYS YTDFQKAVNK LLTASL
//