DCA13_HUMAN
ID DCA13_HUMAN Reviewed; 445 AA.
AC Q9NV06; Q3MII9; Q8NCH8; Q8TC51; Q96JY7; Q9NZX3;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=DDB1- and CUL4-associated factor 13;
DE AltName: Full=WD repeat and SOF domain-containing protein 1;
GN Name=DCAF13; Synonyms=WDSOF1; ORFNames=HSPC064;
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] (ISOFORM 2).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-42.
RC TISSUE=Placenta, and Teratocarcinoma;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-42.
RC TISSUE=Brain, 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 IDENTIFICATION BY MASS 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-49, 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=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=24754225; DOI=10.1139/bcb-2014-0007;
RA Wada K., Sato M., Araki N., Kumeta M., Hirai Y., Takeyasu K., Furukawa K.,
RA Horigome T.;
RT "Dynamics of WD-repeat containing proteins in SSU processome components.";
RL Biochem. Cell Biol. 92:191-199(2014).
RN [8]
RP INTERACTION WITH ESR1 AND LATS1.
RX PubMed=28068668; DOI=10.1038/nature20829;
RA Britschgi A., Duss S., Kim S., Couto J.P., Brinkhaus H., Koren S.,
RA De Silva D., Mertz K.D., Kaup D., Varga Z., Voshol H., Vissieres A.,
RA Leroy C., Roloff T., Stadler M.B., Scheel C.H., Miraglia L.J., Orth A.P.,
RA Bonamy G.M., Reddy V.A., Bentires-Alj M.;
RT "The Hippo kinases LATS1 and 2 control human breast cell fate via crosstalk
RT with ERalpha.";
RL Nature 541:541-545(2017).
CC -!- FUNCTION: Possible role in ribosomal RNA processing (By similarity).
CC May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein
CC ligase complex. {ECO:0000250, ECO:0000269|PubMed:16949367}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with DDB1 (PubMed:16949367). Interacts with ESR1 and
CC LATS1 (PubMed:28068668). {ECO:0000269|PubMed:16949367,
CC ECO:0000269|PubMed:28068668}.
CC -!- INTERACTION:
CC Q9NV06; P03372: ESR1; NbExp=2; IntAct=EBI-7402939, EBI-78473;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:24754225}.
CC Note=In the nucleolus, localizes predominantly in the granular
CC component, but also detected in the fibrillar center and dense
CC fibrillar component. {ECO:0000269|PubMed:24754225}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NV06-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NV06-2; Sequence=VSP_029283, VSP_029284;
CC -!- SIMILARITY: Belongs to the WD repeat DCAF13/WDSOF1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26067.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI01811.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI12043.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB55377.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC11163.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF161549; AAF29036.1; -; mRNA.
DR EMBL; AK001874; BAA91955.1; -; mRNA.
DR EMBL; AK027799; BAB55377.1; ALT_INIT; mRNA.
DR EMBL; AK074725; BAC11163.1; ALT_INIT; mRNA.
DR EMBL; BC026067; AAH26067.2; ALT_INIT; mRNA.
DR EMBL; BC101810; AAI01811.1; ALT_INIT; mRNA.
DR EMBL; BC112042; AAI12043.1; ALT_INIT; mRNA.
DR CCDS; CCDS34934.1; -. [Q9NV06-1]
DR RefSeq; NP_056235.4; NM_015420.6. [Q9NV06-1]
DR PDB; 7MQ8; EM; 3.60 A; LU=1-445.
DR PDB; 7MQ9; EM; 3.87 A; LU=1-445.
DR PDB; 7MQA; EM; 2.70 A; LU=1-445.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; Q9NV06; -.
DR SMR; Q9NV06; -.
DR BioGRID; 117393; 189.
DR IntAct; Q9NV06; 22.
DR MINT; Q9NV06; -.
DR STRING; 9606.ENSP00000297579; -.
DR iPTMnet; Q9NV06; -.
DR PhosphoSitePlus; Q9NV06; -.
DR SwissPalm; Q9NV06; -.
DR BioMuta; DCAF13; -.
DR DMDM; 160358731; -.
DR EPD; Q9NV06; -.
DR jPOST; Q9NV06; -.
DR MassIVE; Q9NV06; -.
DR MaxQB; Q9NV06; -.
DR PaxDb; Q9NV06; -.
DR PeptideAtlas; Q9NV06; -.
DR PRIDE; Q9NV06; -.
DR ProteomicsDB; 82733; -. [Q9NV06-1]
DR ProteomicsDB; 82734; -. [Q9NV06-2]
DR Antibodypedia; 26392; 107 antibodies from 15 providers.
DR DNASU; 25879; -.
DR Ensembl; ENST00000612750.5; ENSP00000484962.1; ENSG00000164934.14. [Q9NV06-1]
DR Ensembl; ENST00000618975.1; ENSP00000480810.1; ENSG00000164934.14. [Q9NV06-2]
DR GeneID; 25879; -.
DR KEGG; hsa:25879; -.
DR MANE-Select; ENST00000612750.5; ENSP00000484962.1; NM_015420.7; NP_056235.5.
DR UCSC; uc064pix.1; human. [Q9NV06-1]
DR CTD; 25879; -.
DR DisGeNET; 25879; -.
DR GeneCards; DCAF13; -.
DR HGNC; HGNC:24535; DCAF13.
DR HPA; ENSG00000164934; Low tissue specificity.
DR MIM; 616196; gene.
DR neXtProt; NX_Q9NV06; -.
DR OpenTargets; ENSG00000164934; -.
DR PharmGKB; PA165585440; -.
DR VEuPathDB; HostDB:ENSG00000164934; -.
DR eggNOG; KOG0268; Eukaryota.
DR GeneTree; ENSGT00390000005711; -.
DR HOGENOM; CLU_033999_0_0_1; -.
DR InParanoid; Q9NV06; -.
DR OrthoDB; 418107at2759; -.
DR PhylomeDB; Q9NV06; -.
DR TreeFam; TF300844; -.
DR PathwayCommons; Q9NV06; -.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-8951664; Neddylation.
DR SignaLink; Q9NV06; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 25879; 63 hits in 1124 CRISPR screens.
DR ChiTaRS; DCAF13; human.
DR GenomeRNAi; 25879; -.
DR Pharos; Q9NV06; Tbio.
DR PRO; PR:Q9NV06; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9NV06; protein.
DR Bgee; ENSG00000164934; Expressed in secondary oocyte and 183 other tissues.
DR ExpressionAtlas; Q9NV06; baseline and differential.
DR Genevisible; Q9NV06; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR007287; Sof1.
DR InterPro; IPR013979; TIF_beta_prop-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF08662; eIF2A; 1.
DR Pfam; PF04158; Sof1; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Nucleus;
KW Reference proteome; Repeat; Ribonucleoprotein; Ribosome biogenesis;
KW rRNA processing; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..445
FT /note="DDB1- and CUL4-associated factor 13"
FT /id="PRO_0000310428"
FT REPEAT 64..104
FT /note="WD 1"
FT REPEAT 107..146
FT /note="WD 2"
FT REPEAT 149..191
FT /note="WD 3"
FT REPEAT 194..234
FT /note="WD 4"
FT REPEAT 236..276
FT /note="WD 5"
FT REPEAT 280..319
FT /note="WD 6"
FT REPEAT 323..362
FT /note="WD 7"
FT MOD_RES 49
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 91..96
FT /note="VRIWNL -> LVMTKL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11042152"
FT /id="VSP_029283"
FT VAR_SEQ 97..445
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11042152"
FT /id="VSP_029284"
FT VARIANT 42
FT /note="I -> V (in dbSNP:rs3134253)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_037035"
FT VARIANT 70
FT /note="N -> S (in dbSNP:rs13272825)"
FT /id="VAR_037036"
FT CONFLICT 38
FT /note="P -> S (in Ref. 2; BAC11163)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="A -> S (in Ref. 3; AAH26067)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="K -> E (in Ref. 2; BAC11163)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 51402 MW; 33F6079364A0F0A3 CRC64;
MKVKMLSRNP DNYVRETKLD LQRVPRNYDP ALHPFEVPRE YIRALNATKL ERVFAKPFLA
SLDGHRDGVN CLAKHPEKLA TVLSGACDGE VRIWNLTQRN CIRTIQAHEG FVRGICTRFC
GTSFFTVGDD KTVKQWKMDG PGYGDEEEPL HTILGKTVYT GIDHHWKEAV FATCGQQVDI
WDEQRTNPIC SMTWGFDSIS SVKFNPIETF LLGSCASDRN IVLYDMRQAT PLKKVILDMR
TNTICWNPME AFIFTAANED YNLYTFDMRA LDTPVMVHMD HVSAVLDVDY SPTGKEFVSA
SFDKSIRIFP VDKSRSREVY HTKRMQHVIC VKWTSDSKYI MCGSDEMNIR LWKANASEKL
GVLTSREKAA KDYNQKLKEK FQHYPHIKRI ARHRHLPKSI YSQIQEQRIM KEARRRKEVN
RIKHSKPGSV PLVSEKKKHV VAVVK
