WDR82_MOUSE
ID WDR82_MOUSE Reviewed; 313 AA.
AC Q8BFQ4; Q8K2G5; Q8VEE8;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=WD repeat-containing protein 82 {ECO:0000305};
GN Name=Wdr82 {ECO:0000303|PubMed:17041588, ECO:0000312|MGI:MGI:1924555};
GN Synonyms=Cdw5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-313, AND INTERACTION WITH CUL4B.
RX PubMed=17041588; DOI=10.1038/ncb1490;
RA Higa L.A., Wu M., Ye T., Kobayashi R., Sun H., Zhang H.;
RT "CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins
RT and regulates histone methylation.";
RL Nat. Cell Biol. 8:1277-1283(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-313.
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ZC3H4.
RX PubMed=33767452; DOI=10.1038/s41594-021-00572-y;
RA Austenaa L.M.I., Piccolo V., Russo M., Prosperini E., Polletti S.,
RA Polizzese D., Ghisletti S., Barozzi I., Diaferia G.R., Natoli G.;
RT "A first exon termination checkpoint preferentially suppresses extragenic
RT transcription.";
RL Nat. Struct. Mol. Biol. 28:337-346(2021).
CC -!- FUNCTION: Regulatory component of the SET1 complex implicated in the
CC tethering of this complex to transcriptional start sites of active
CC genes (By similarity). Facilitates histone H3 'Lys-4' methylation
CC (H3K4me) via recruitment of the SETD1A or SETD1B to the 'Ser-5'
CC phosphorylated C-terminal domain (CTD) of RNA polymerase II large
CC subunit (POLR2A) (By similarity). Component of PTW/PP1 phosphatase
CC complex, which plays a role in the control of chromatin structure and
CC cell cycle progression during the transition from mitosis into
CC interphase (By similarity). Together with ZC3H4, but independently of
CC the SET1 complex, part of a transcription termination checkpoint that
CC promotes transcription termination of long non-coding RNAs (lncRNAs)
CC (PubMed:33767452). The transcription termination checkpoint is
CC activated by the inefficiently spliced first exon of lncRNAs and
CC promotes transcription termination of lncRNAs and their subsequent
CC degradation by the exosome (PubMed:33767452).
CC {ECO:0000250|UniProtKB:Q6UXN9, ECO:0000269|PubMed:33767452}.
CC -!- SUBUNIT: Component of the SET1 complex, at least composed of the
CC catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2,
CC CXXC1/CFP1, HCFC1 and DPY30 (By similarity). Component of the PTW/PP1
CC phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA
CC or PPP1CB or PPP1CC (By similarity). Associated with multiple protein
CC complexes including an RNA polymerase II complex, MLL3/MLL4 complex and
CC a chaperonin-containing TCP1 complex (By similarity). Interacts with
CC CUL4B (PubMed:17041588). Interacts with RBBP5 and SETD1B (By
CC similarity). Interacts with SETD1A (via RRM domain) (By similarity).
CC Interacts with POLR2B (By similarity). Interacts with
CC hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II large
CC subunit (POLR2A) (By similarity). Binds specifically to CTD heptad
CC repeats phosphorylated on 'Ser-5' of each heptad (By similarity).
CC SETD1A enhances its interaction with POLR2A (By similarity). Interacts
CC with PPP1R10/PNUTS (By similarity). Interacts with PPP1CA in the
CC presence of PPP1R10/PNUTS (By similarity). Interacts with ZC3H4;
CC interaction is independent of the SET1 complex and promotes
CC transcription termination of long non-coding RNAs (lncRNAs)
CC (PubMed:33767452). {ECO:0000250|UniProtKB:Q6UXN9,
CC ECO:0000269|PubMed:17041588, ECO:0000269|PubMed:33767452}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6UXN9}.
CC Chromosome {ECO:0000269|PubMed:33767452}. Note=Associates with
CC chromatin (By similarity). Recruited at sites of high RNA polymerase II
CC occupancy (PubMed:33767452). {ECO:0000250|UniProtKB:Q6UXN9,
CC ECO:0000269|PubMed:33767452}.
CC -!- SIMILARITY: Belongs to the WD repeat SWD2 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; AK035109; BAC28947.1; -; mRNA.
DR EMBL; AK037620; BAC29836.1; -; mRNA.
DR EMBL; AK149692; BAE29029.1; -; mRNA.
DR EMBL; EF011615; ABK41105.1; -; mRNA.
DR EMBL; BC019115; AAH19115.1; -; mRNA.
DR EMBL; BC031502; AAH31502.1; -; mRNA.
DR CCDS; CCDS40754.1; -.
DR RefSeq; NP_084172.1; NM_029896.1.
DR AlphaFoldDB; Q8BFQ4; -.
DR SMR; Q8BFQ4; -.
DR BioGRID; 218612; 53.
DR IntAct; Q8BFQ4; 2.
DR MINT; Q8BFQ4; -.
DR STRING; 10090.ENSMUSP00000020490; -.
DR iPTMnet; Q8BFQ4; -.
DR PhosphoSitePlus; Q8BFQ4; -.
DR REPRODUCTION-2DPAGE; Q8BFQ4; -.
DR EPD; Q8BFQ4; -.
DR MaxQB; Q8BFQ4; -.
DR PaxDb; Q8BFQ4; -.
DR PRIDE; Q8BFQ4; -.
DR ProteomicsDB; 299973; -.
DR Antibodypedia; 56045; 85 antibodies from 20 providers.
DR Ensembl; ENSMUST00000020490; ENSMUSP00000020490; ENSMUSG00000020257.
DR GeneID; 77305; -.
DR KEGG; mmu:77305; -.
DR UCSC; uc009rjc.1; mouse.
DR CTD; 80335; -.
DR MGI; MGI:1924555; Wdr82.
DR VEuPathDB; HostDB:ENSMUSG00000020257; -.
DR eggNOG; KOG1446; Eukaryota.
DR GeneTree; ENSGT00530000063965; -.
DR HOGENOM; CLU_044117_3_0_1; -.
DR InParanoid; Q8BFQ4; -.
DR OMA; CVLNGDH; -.
DR OrthoDB; 1146727at2759; -.
DR PhylomeDB; Q8BFQ4; -.
DR TreeFam; TF313497; -.
DR BioGRID-ORCS; 77305; 32 hits in 71 CRISPR screens.
DR ChiTaRS; Wdr82; mouse.
DR PRO; PR:Q8BFQ4; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BFQ4; protein.
DR Bgee; ENSMUSG00000020257; Expressed in mandibular prominence and 260 other tissues.
DR ExpressionAtlas; Q8BFQ4; baseline and differential.
DR Genevisible; Q8BFQ4; MM.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0035097; C:histone methyltransferase complex; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
DR GO; GO:0048188; C:Set1C/COMPASS complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); ISO:MGI.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR GO; GO:0051568; P:histone H3-K4 methylation; IMP:MGI.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IBA:GO_Central.
DR GO; GO:0110064; P:lncRNA catabolic process; IDA:UniProtKB.
DR GO; GO:0032785; P:negative regulation of DNA-templated transcription, elongation; IDA:UniProtKB.
DR GO; GO:0140744; P:negative regulation of lncRNA transcription; IDA:UniProtKB.
DR GO; GO:0071027; P:nuclear RNA surveillance; IDA:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR037867; Swd2/WDR82.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19861; PTHR19861; 1.
DR Pfam; PF00400; WD40; 3.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
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 Chromosome; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Transcription termination; WD repeat.
FT CHAIN 1..313
FT /note="WD repeat-containing protein 82"
FT /id="PRO_0000279686"
FT REPEAT 19..58
FT /note="WD 1"
FT REPEAT 105..144
FT /note="WD 2"
FT REPEAT 146..184
FT /note="WD 3"
FT REPEAT 192..231
FT /note="WD 4"
FT REPEAT 236..276
FT /note="WD 5"
FT REPEAT 280..313
FT /note="WD 6"
FT CONFLICT 63..65
FT /note="KYG -> TRP (in Ref. 3; AAH19115)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 313 AA; 35079 MW; FD3505A9B89863A0 CRC64;
MKLTDSVLRS FRVAKVFREN SDKINCFDFS PNGETVISSS DDDSIVLYDC QEGKPKRTLY
SKKYGVDLIR YTHAANTVVY SSNKIDDTIR YLSLHDNKYI RYFPGHSKRV VALSMSPVDD
TFISGSLDKT IRLWDLRSPN CQGLMHLQGK PVCSFDPEGL IFAAGVNSEM VKLYDLRSFD
KGPFATFKMQ YDRTCEWTGL KFSNDGKLIL ISTNGSFIRL IDAFKGVVMH TFGGYANSKA
VTLEASFTPD SQFIMIGSED GKIHVWNGES GIKVAVLDGK HTGPITCLQF NPKFMTFASA
CSNMAFWLPT IDD
