WDR33_HUMAN
ID WDR33_HUMAN Reviewed; 1336 AA.
AC Q9C0J8; Q05DP8; Q53FG9; Q587J1; Q69YF7; Q6NUQ0; Q9NUL1;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=pre-mRNA 3' end processing protein WDR33;
DE AltName: Full=WD repeat-containing protein 33;
DE AltName: Full=WD repeat-containing protein of 146 kDa {ECO:0000303|PubMed:11162572};
GN Name=WDR33; Synonyms=WDC146 {ECO:0000303|PubMed:11162572};
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 [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11162572; DOI=10.1006/bbrc.2000.4163;
RA Ito S., Sakai A., Nomura T., Miki Y., Ouchida M., Sasaki J., Shimizu K.;
RT "A novel WD40 repeat protein, WDC146, highly expressed during
RT spermatogenesis in a stage-specific manner.";
RL Biochem. Biophys. Res. Commun. 280:656-663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
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 2).
RC TISSUE=Small intestine;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain, Pancreas, and Placenta;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1187-1336 (ISOFORM 1).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1210, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP FUNCTION, IDENTIFICATION IN THE 3' PRE-MRNA END PROCESSING COMPLEX,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CPSF3.
RX PubMed=19217410; DOI=10.1016/j.molcel.2008.12.028;
RA Shi Y., Di Giammartino D.C., Taylor D., Sarkeshik A., Rice W.J.,
RA Yates J.R. III, Frank J., Manley J.L.;
RT "Molecular architecture of the human pre-mRNA 3' processing complex.";
RL Mol. Cell 33:365-376(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-46, 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-7 AND SER-1210, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-7, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1210, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-782; ARG-915 AND ARG-1315, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-530, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-526; LYS-530 AND LYS-560, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Essential for both cleavage and polyadenylation of pre-mRNA
CC 3' ends. {ECO:0000269|PubMed:19217410}.
CC -!- SUBUNIT: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) module of the pre-mRNA 3'-end processing complex.
CC Interacts with CPSF3/CPSF73. {ECO:0000269|PubMed:19217410}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11162572,
CC ECO:0000269|PubMed:19217410}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9C0J8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C0J8-2; Sequence=VSP_041333, VSP_041334;
CC Name=3;
CC IsoId=Q9C0J8-3; Sequence=VSP_042684, VSP_042685, VSP_041334;
CC -!- TISSUE SPECIFICITY: Most highly expressed in testis.
CC {ECO:0000269|PubMed:11162572}.
CC -!- SIMILARITY: Belongs to the WD repeat WDR33 family. {ECO:0000305}.
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; AB044749; BAB32435.1; -; mRNA.
DR EMBL; AK002156; BAA92113.1; -; mRNA.
DR EMBL; AK223319; BAD97039.1; -; mRNA.
DR EMBL; AC006011; AAX82033.1; -; Genomic_DNA.
DR EMBL; CH471103; EAW95342.1; -; Genomic_DNA.
DR EMBL; CH471103; EAW95343.1; -; Genomic_DNA.
DR EMBL; BC005401; AAH05401.1; ALT_TERM; mRNA.
DR EMBL; BC013990; AAH13990.1; -; mRNA.
DR EMBL; BC068484; AAH68484.1; -; mRNA.
DR EMBL; AL834365; CAH10688.1; -; mRNA.
DR CCDS; CCDS2150.1; -. [Q9C0J8-1]
DR CCDS; CCDS42746.1; -. [Q9C0J8-3]
DR CCDS; CCDS46407.1; -. [Q9C0J8-2]
DR RefSeq; NP_001006623.1; NM_001006622.2. [Q9C0J8-2]
DR RefSeq; NP_001006624.1; NM_001006623.2. [Q9C0J8-3]
DR RefSeq; NP_060853.3; NM_018383.4. [Q9C0J8-1]
DR RefSeq; XP_011509738.1; XM_011511436.1. [Q9C0J8-1]
DR PDB; 6BLY; EM; 3.36 A; B=1-572.
DR PDB; 6BM0; EM; 3.80 A; B=1-572.
DR PDB; 6DNH; EM; 3.40 A; B=1-572.
DR PDB; 6F9N; X-ray; 2.50 A; B=35-410.
DR PDB; 6FBS; EM; 3.07 A; B=1-410.
DR PDB; 6FUW; EM; 3.07 A; B=1-410.
DR PDB; 6URG; EM; 3.00 A; B=1-572.
DR PDB; 6URO; EM; 3.60 A; B=1-572.
DR PDBsum; 6BLY; -.
DR PDBsum; 6BM0; -.
DR PDBsum; 6DNH; -.
DR PDBsum; 6F9N; -.
DR PDBsum; 6FBS; -.
DR PDBsum; 6FUW; -.
DR PDBsum; 6URG; -.
DR PDBsum; 6URO; -.
DR AlphaFoldDB; Q9C0J8; -.
DR SMR; Q9C0J8; -.
DR BioGRID; 120620; 126.
DR IntAct; Q9C0J8; 50.
DR MINT; Q9C0J8; -.
DR STRING; 9606.ENSP00000325377; -.
DR iPTMnet; Q9C0J8; -.
DR MetOSite; Q9C0J8; -.
DR PhosphoSitePlus; Q9C0J8; -.
DR SwissPalm; Q9C0J8; -.
DR BioMuta; WDR33; -.
DR DMDM; 209572695; -.
DR EPD; Q9C0J8; -.
DR jPOST; Q9C0J8; -.
DR MassIVE; Q9C0J8; -.
DR MaxQB; Q9C0J8; -.
DR PaxDb; Q9C0J8; -.
DR PeptideAtlas; Q9C0J8; -.
DR PRIDE; Q9C0J8; -.
DR ProteomicsDB; 80062; -. [Q9C0J8-1]
DR ProteomicsDB; 80063; -. [Q9C0J8-2]
DR ProteomicsDB; 80064; -. [Q9C0J8-3]
DR Antibodypedia; 18487; 102 antibodies from 20 providers.
DR DNASU; 55339; -.
DR Ensembl; ENST00000322313.9; ENSP00000325377.3; ENSG00000136709.12. [Q9C0J8-1]
DR Ensembl; ENST00000393006.5; ENSP00000376730.1; ENSG00000136709.12. [Q9C0J8-3]
DR Ensembl; ENST00000409658.7; ENSP00000387186.3; ENSG00000136709.12. [Q9C0J8-2]
DR GeneID; 55339; -.
DR KEGG; hsa:55339; -.
DR MANE-Select; ENST00000322313.9; ENSP00000325377.3; NM_018383.5; NP_060853.3.
DR UCSC; uc002tpg.3; human. [Q9C0J8-1]
DR CTD; 55339; -.
DR GeneCards; WDR33; -.
DR HGNC; HGNC:25651; WDR33.
DR HPA; ENSG00000136709; Low tissue specificity.
DR MIM; 618082; gene.
DR neXtProt; NX_Q9C0J8; -.
DR OpenTargets; ENSG00000136709; -.
DR PharmGKB; PA134943440; -.
DR VEuPathDB; HostDB:ENSG00000136709; -.
DR eggNOG; KOG0284; Eukaryota.
DR GeneTree; ENSGT00730000111130; -.
DR HOGENOM; CLU_000288_77_3_1; -.
DR OMA; DHREMEA; -.
DR OrthoDB; 604979at2759; -.
DR PhylomeDB; Q9C0J8; -.
DR TreeFam; TF317659; -.
DR PathwayCommons; Q9C0J8; -.
DR Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-HSA-77595; Processing of Intronless Pre-mRNAs.
DR SignaLink; Q9C0J8; -.
DR BioGRID-ORCS; 55339; 673 hits in 1057 CRISPR screens.
DR ChiTaRS; WDR33; human.
DR GeneWiki; WDR33; -.
DR GenomeRNAi; 55339; -.
DR Pharos; Q9C0J8; Tbio.
DR PRO; PR:Q9C0J8; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9C0J8; protein.
DR Bgee; ENSG00000136709; Expressed in gingival epithelium and 186 other tissues.
DR ExpressionAtlas; Q9C0J8; baseline and differential.
DR Genevisible; Q9C0J8; HS.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0006301; P:postreplication repair; NAS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; NAS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR045245; Pfs2-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR22836; PTHR22836; 2.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Collagen; Isopeptide bond;
KW Methylation; mRNA processing; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ubl conjugation; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT CHAIN 2..1336
FT /note="pre-mRNA 3' end processing protein WDR33"
FT /id="PRO_0000051382"
FT REPEAT 117..156
FT /note="WD 1"
FT REPEAT 159..198
FT /note="WD 2"
FT REPEAT 200..239
FT /note="WD 3"
FT REPEAT 242..283
FT /note="WD 4"
FT REPEAT 286..325
FT /note="WD 5"
FT REPEAT 329..369
FT /note="WD 6"
FT REPEAT 373..412
FT /note="WD 7"
FT DOMAIN 618..770
FT /note="Collagen-like"
FT REGION 568..1336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..592
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..730
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..751
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..982
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1042
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 46
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 782
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 915
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 987
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4P0"
FT MOD_RES 1035
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4P0"
FT MOD_RES 1210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 1262
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8K4P0"
FT MOD_RES 1315
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1315
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 526
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 530
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 560
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 209..326
FT /note="SFSPTDNKFATCSDDGTVRIWDFLRCHEERILRGHGADVKCVDWHPTKGLVV
FT SGSKDSQQPIKFWDPKTGQSLATLHAHKNTVMEVKLNLNGNWLLTASRDHLCKLFDIRN
FT LKEELQV -> RFIHNIPFSVVPIVMVKLFSKCILGAEMHGLCQFLGNFLHPINTIFFF
FT VFTHSPFCWHLSEVVLSRYQPLQYVRDVLSAAFCTGFLFSFMINNVYTLFLFIIYCVRQ
FT EYFIPNKEFSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_041333"
FT VAR_SEQ 242..257
FT /note="GHGADVKCVDWHPTKG -> DTCFHHCRCYFLSVKR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042684"
FT VAR_SEQ 258..326
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042685"
FT VAR_SEQ 327..1336
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_041334"
FT VARIANT 33
FT /note="A -> S (in dbSNP:rs11557686)"
FT /id="VAR_046717"
FT VARIANT 711
FT /note="P -> R (in dbSNP:rs12615078)"
FT /id="VAR_053427"
FT CONFLICT 113
FT /note="T -> A (in Ref. 3; BAD97039)"
FT /evidence="ECO:0000305"
FT CONFLICT 715
FT /note="G -> S (in Ref. 1; BAB32435)"
FT /evidence="ECO:0000305"
FT HELIX 60..70
FT /evidence="ECO:0007829|PDB:6F9N"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:6F9N"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:6URG"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:6F9N"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:6F9N"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:6URG"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 214..221
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:6F9N"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:6F9N"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 300..307
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 310..318
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 334..339
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:6BLY"
FT STRAND 344..354
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 371..374
FT /evidence="ECO:0007829|PDB:6URG"
FT STRAND 378..383
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 387..397
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 399..403
FT /evidence="ECO:0007829|PDB:6F9N"
FT TURN 414..417
FT /evidence="ECO:0007829|PDB:6URG"
FT CONFLICT Q9C0J8-2:274
FT /note="R -> Q (in Ref. 3; BAD97039)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9C0J8-2:306
FT /note="F -> S (in Ref. 6; AAH05401)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1336 AA; 145891 MW; DE45F510F93BB783 CRC64;
MATEIGSPPR FFHMPRFQHQ APRQLFYKRP DFAQQQAMQQ LTFDGKRMRK AVNRKTIDYN
PSVIKYLENR IWQRDQRDMR AIQPDAGYYN DLVPPIGMLN NPMNAVTTKF VRTSTNKVKC
PVFVVRWTPE GRRLVTGASS GEFTLWNGLT FNFETILQAH DSPVRAMTWS HNDMWMLTAD
HGGYVKYWQS NMNNVKMFQA HKEAIREASF SPTDNKFATC SDDGTVRIWD FLRCHEERIL
RGHGADVKCV DWHPTKGLVV SGSKDSQQPI KFWDPKTGQS LATLHAHKNT VMEVKLNLNG
NWLLTASRDH LCKLFDIRNL KEELQVFRGH KKEATAVAWH PVHEGLFASG GSDGSLLFWH
VGVEKEVGGM EMAHEGMIWS LAWHPLGHIL CSGSNDHTSK FWTRNRPGDK MRDRYNLNLL
PGMSEDGVEY DDLEPNSLAV IPGMGIPEQL KLAMEQEQMG KDESNEIEMT IPGLDWGMEE
VMQKDQKKVP QKKVPYAKPI PAQFQQAWMQ NKVPIPAPNE VLNDRKEDIK LEEKKKTQAE
IEQEMATLQY TNPQLLEQLK IERLAQKQVE QIQPPPSSGT PLLGPQPFPG QGPMSQIPQG
FQQPHPSQQM PMNMAQMGPP GPQGQFRPPG PQGQMGPQGP PLHQGGGGPQ GFMGPQGPQG
PPQGLPRPQD MHGPQGMQRH PGPHGPLGPQ GPPGPQGSSG PQGHMGPQGP PGPQGHIGPQ
GPPGPQGHLG PQGPPGTQGM QGPPGPRGMQ GPPHPHGIQG GPGSQGIQGP VSQGPLMGLN
PRGMQGPPGP RENQGPAPQG MIMGHPPQEM RGPHPPGGLL GHGPQEMRGP QEIRGMQGPP
PQGSMLGPPQ ELRGPPGSQS QQGPPQGSLG PPPQGGMQGP PGPQGQQNPA RGPHPSQGPI
PFQQQKTPLL GDGPRAPFNQ EGQSTGPPPL IPGLGQQGAQ GRIPPLNPGQ GPGPNKGDSR
GPPNHHMGPM SERRHEQSGG PEHGPERGPF RGGQDCRGPP DRRGPHPDFP DDFSRPDDFH
PDKRFGHRLR EFEGRGGPLP QEEKWRRGGP GPPFPPDHRE FSEGDGRGAA RGPPGAWEGR
RPGDERFPRD PEDPRFRGRR EESFRRGAPP RHEGRAPPRG RDGFPGPEDF GPEENFDASE
EAARGRDLRG RGRGTPRGGR KGLLPTPDEF PRFEGGRKPD SWDGNREPGP GHEHFRDTPR
PDHPPHDGHS PASRERSSSL QGMDMASLPP RKRPWHDGPG TSEHREMEAP GGPSEDRGGK
GRGGPGPAQR VPKSGRSSSL DGEHHDGYHR DEPFGGPPGS GTPSRGGRSG SNWGRGSNMN
SGPPRRGASR GGGRGR
