WDR82_HUMAN
ID WDR82_HUMAN Reviewed; 313 AA.
AC Q6UXN9; A8K5R5; Q8TEB2;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=WD repeat-containing protein 82 {ECO:0000305};
GN Name=WDR82 {ECO:0000303|PubMed:17998332, ECO:0000312|HGNC:HGNC:28826};
GN Synonyms=SWD2, TMEM113, WDR82A;
GN ORFNames=UNQ9342/PRO34047 {ECO:0000303|PubMed:12975309};
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=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Hepatoma;
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 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 [4]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE SET1 COMPLEX.
RX PubMed=16253997; DOI=10.1074/jbc.m508312200;
RA Lee J.-H., Skalnik D.G.;
RT "CpG-binding protein (CXXC finger protein 1) is a component of the
RT mammalian Set1 histone H3-Lys4 methyltransferase complex, the analogue of
RT the yeast Set1/COMPASS complex.";
RL J. Biol. Chem. 280:41725-41731(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, 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 [6]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN SET1 COMPLEX.
RX PubMed=17355966; DOI=10.1074/jbc.m609809200;
RA Lee J.-H., Tate C.M., You J.-S., Skalnik D.G.;
RT "Identification and characterization of the human Set1B histone H3-Lys4
RT methyltransferase complex.";
RL J. Biol. Chem. 282:13419-13428(2007).
RN [7]
RP FUNCTION, IDENTIFICATION IN SET1 COMPLEX, AND INTERACTION WITH SETD1A;
RP SETD1B; POLR2A AND POLR2B.
RX PubMed=17998332; DOI=10.1128/mcb.01356-07;
RA Lee J.H., Skalnik D.G.;
RT "Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A
RT Histone H3-Lys4 methyltransferase complex to transcription start sites of
RT transcribed human genes.";
RL Mol. Cell. Biol. 28:609-618(2008).
RN [8]
RP FUNCTION, IDENTIFICATION IN SET1 COMPLEX, AND INTERACTION WITH RBBP5.
RX PubMed=18838538; DOI=10.1128/mcb.00976-08;
RA Wu M., Wang P.F., Lee J.S., Martin-Brown S., Florens L., Washburn M.,
RA Shilatifard A.;
RT "Molecular regulation of H3K4 trimethylation by Wdr82, a component of human
RT Set1/COMPASS.";
RL Mol. Cell. Biol. 28:7337-7344(2008).
RN [9]
RP IDENTIFICATION IN THE PTW/PP1 PHOSPHATASE COMPLEX, FUNCTION, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH PPP1CA AND PPP1R10/PNUTS.
RX PubMed=20516061; DOI=10.1074/jbc.m110.109801;
RA Lee J.H., You J., Dobrota E., Skalnik D.G.;
RT "Identification and characterization of a novel human PP1 phosphatase
RT complex.";
RL J. Biol. Chem. 285:24466-24476(2010).
RN [10]
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 [11]
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 [12]
RP FUNCTION, AND INTERACTION WITH ZC3H4.
RX PubMed=33913806; DOI=10.7554/elife.67305;
RA Estell C., Davidson L., Steketee P.C., Monier A., West S.;
RT "ZC3H4 restricts non-coding transcription in human cells.";
RL Elife 10:0-0(2021).
RN [13]
RP FUNCTION.
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 (PubMed:17998332, PubMed:18838538, PubMed:20516061). Facilitates
CC histone H3 'Lys-4' methylation (H3K4me) via recruitment of the SETD1A
CC or SETD1B to the 'Ser-5' phosphorylated C-terminal domain (CTD) of RNA
CC polymerase II large subunit (POLR2A) (PubMed:17998332,
CC PubMed:18838538). Component of PTW/PP1 phosphatase complex, which plays
CC a role in the control of chromatin structure and cell cycle progression
CC during the transition from mitosis into interphase (PubMed:20516061).
CC Together with ZC3H4, but independently of the SET1 complex, part of a
CC transcription termination checkpoint that promotes transcription
CC termination of long non-coding RNAs (lncRNAs) (PubMed:33913806,
CC PubMed:33767452). The transcription termination checkpoint is activated
CC by the inefficiently spliced first exon of lncRNAs and promotes
CC transcription termination of lncRNAs and their subsequent degradation
CC by the exosome (PubMed:33767452). {ECO:0000269|PubMed:17998332,
CC ECO:0000269|PubMed:18838538, ECO:0000269|PubMed:20516061,
CC ECO:0000269|PubMed:33767452, ECO:0000269|PubMed:33913806}.
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 (PubMed:16253997, PubMed:17355966,
CC PubMed:17998332, PubMed:18838538). Component of the PTW/PP1 phosphatase
CC complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB
CC or PPP1CC (PubMed:20516061). Associated with multiple protein complexes
CC including an RNA polymerase II complex, MLL3/MLL4 complex and a
CC chaperonin-containing TCP1 complex (PubMed:20516061). Interacts with
CC CUL4B (PubMed:17041588). Interacts with RBBP5 and SETD1B
CC (PubMed:17998332, PubMed:18838538). Interacts with SETD1A (via RRM
CC domain) (PubMed:17998332). Interacts with POLR2B (PubMed:17998332).
CC Interacts with hyperphosphorylated C-terminal domain (CTD) of RNA
CC polymerase II large subunit (POLR2A) (PubMed:17998332). Binds
CC specifically to CTD heptad repeats phosphorylated on 'Ser-5' of each
CC heptad (PubMed:17998332). SETD1A enhances its interaction with POLR2A
CC (PubMed:17998332). Interacts with PPP1R10/PNUTS (PubMed:20516061).
CC Interacts with PPP1CA in the presence of PPP1R10/PNUTS
CC (PubMed:20516061). Interacts with ZC3H4; interaction is independent of
CC the SET1 complex and promotes transcription termination of long non-
CC coding RNAs (lncRNAs) (PubMed:33913806). {ECO:0000269|PubMed:16253997,
CC ECO:0000269|PubMed:17041588, ECO:0000269|PubMed:17355966,
CC ECO:0000269|PubMed:17998332, ECO:0000269|PubMed:18838538,
CC ECO:0000269|PubMed:20516061, ECO:0000269|PubMed:33913806}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16253997,
CC ECO:0000269|PubMed:17355966, ECO:0000269|PubMed:20516061}. Chromosome
CC {ECO:0000250|UniProtKB:Q8BFQ4}. Note=Associates with chromatin
CC (PubMed:20516061). Recruited at sites of high RNA polymerase II
CC occupancy (By similarity). {ECO:0000250|UniProtKB:Q8BFQ4,
CC ECO:0000269|PubMed:20516061}.
CC -!- SIMILARITY: Belongs to the WD repeat SWD2 family. {ECO:0000305}.
CC -!- CAUTION: The gene encoding this protein shares one overlapping exon
CC with TMEM113. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB85039.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY358264; AAQ88631.1; -; mRNA.
DR EMBL; AK074290; BAB85039.1; ALT_INIT; mRNA.
DR EMBL; AK291380; BAF84069.1; -; mRNA.
DR EMBL; CH471055; EAW65202.1; -; Genomic_DNA.
DR CCDS; CCDS2851.2; -.
DR RefSeq; NP_079498.2; NM_025222.3.
DR AlphaFoldDB; Q6UXN9; -.
DR SMR; Q6UXN9; -.
DR BioGRID; 123245; 140.
DR ComplexPortal; CPX-7110; Histone-lysine N-methyltransferase complex, SET1A variant.
DR ComplexPortal; CPX-7111; Histone-lysine N-methyltransferase complex, SET1B variant.
DR CORUM; Q6UXN9; -.
DR IntAct; Q6UXN9; 44.
DR MINT; Q6UXN9; -.
DR STRING; 9606.ENSP00000296490; -.
DR GlyGen; Q6UXN9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6UXN9; -.
DR MetOSite; Q6UXN9; -.
DR PhosphoSitePlus; Q6UXN9; -.
DR SwissPalm; Q6UXN9; -.
DR BioMuta; WDR82; -.
DR DMDM; 74758580; -.
DR EPD; Q6UXN9; -.
DR jPOST; Q6UXN9; -.
DR MassIVE; Q6UXN9; -.
DR MaxQB; Q6UXN9; -.
DR PaxDb; Q6UXN9; -.
DR PeptideAtlas; Q6UXN9; -.
DR PRIDE; Q6UXN9; -.
DR ProteomicsDB; 67641; -.
DR Antibodypedia; 56045; 85 antibodies from 20 providers.
DR DNASU; 80335; -.
DR Ensembl; ENST00000296490.8; ENSP00000296490.3; ENSG00000164091.12.
DR GeneID; 80335; -.
DR KEGG; hsa:80335; -.
DR MANE-Select; ENST00000296490.8; ENSP00000296490.3; NM_025222.4; NP_079498.2.
DR UCSC; uc003ddl.3; human.
DR CTD; 80335; -.
DR DisGeNET; 80335; -.
DR GeneCards; WDR82; -.
DR HGNC; HGNC:28826; WDR82.
DR HPA; ENSG00000164091; Low tissue specificity.
DR MIM; 611059; gene.
DR neXtProt; NX_Q6UXN9; -.
DR OpenTargets; ENSG00000164091; -.
DR PharmGKB; PA142670585; -.
DR VEuPathDB; HostDB:ENSG00000164091; -.
DR eggNOG; KOG1446; Eukaryota.
DR GeneTree; ENSGT00530000063965; -.
DR HOGENOM; CLU_044117_3_0_1; -.
DR InParanoid; Q6UXN9; -.
DR OMA; CVLNGDH; -.
DR OrthoDB; 1146727at2759; -.
DR PhylomeDB; Q6UXN9; -.
DR TreeFam; TF313497; -.
DR PathwayCommons; Q6UXN9; -.
DR SignaLink; Q6UXN9; -.
DR BioGRID-ORCS; 80335; 785 hits in 1098 CRISPR screens.
DR ChiTaRS; WDR82; human.
DR GenomeRNAi; 80335; -.
DR Pharos; Q6UXN9; Tbio.
DR PRO; PR:Q6UXN9; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q6UXN9; protein.
DR Bgee; ENSG00000164091; Expressed in cortical plate and 215 other tissues.
DR ExpressionAtlas; Q6UXN9; baseline and differential.
DR Genevisible; Q6UXN9; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0035097; C:histone methyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0072357; C:PTW/PP1 phosphatase complex; IDA:UniProtKB.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR GO; GO:0051568; P:histone H3-K4 methylation; IDA:UniProtKB.
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_0000279685"
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"
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
