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   17-JUN-2020, entry version 148.
DE   RecName: Full=WD repeat-containing protein 82;
DE   AltName: Full=Protein TMEM113;
DE   AltName: Full=Swd2;
GN   Name=WDR82; Synonyms=TMEM113, WDR82A; ORFNames=UNQ9342/PRO34047;
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).
CC   -!- FUNCTION: Regulatory component of the SET1 complex implicated in the
CC       tethering of this complex to transcriptional start sites of active
CC       genes. Facilitates histone H3 'Lys-4' methylation via recruitment of
CC       the SETD1A or SETD1B to the 'Ser-5' phosphorylated C-terminal domain
CC       (CTD) of RNA polymerase II large subunit (POLR2A). Component of PTW/PP1
CC       phosphatase complex, which plays a role in the control of chromatin
CC       structure and cell cycle progression during the transition from mitosis
CC       into interphase. {ECO:0000269|PubMed:17998332,
CC       ECO:0000269|PubMed:18838538, ECO:0000269|PubMed:20516061}.
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. Component of the PTW/PP1 phosphatase
CC       complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB
CC       or PPP1CC. Associated with multiple protein complexes including an RNA
CC       polymerase II complex, MLL3/MLL4 complex and a chaperonin-containing
CC       TCP1 complex. Interacts with CUL4B. Interacts with RBBP5 and SETD1B.
CC       Interacts with SETD1A (via RRM domain). Interacts with POLR2B.
CC       Interacts with hyperphosphorylated C-terminal domain (CTD) of RNA
CC       polymerase II large subunit (POLR2A). Binds specifically to CTD heptad
CC       repeats phosphorylated on 'Ser-5' of each heptad. SETD1A enhances its
CC       interaction with POLR2A. Interacts with PPP1R10/PNUTS. Interacts with
CC       PPP1CA in the presence of PPP1R10/PNUTS. {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}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16253997,
CC       ECO:0000269|PubMed:17355966, ECO:0000269|PubMed:20516061}.
CC       Note=Associates with chromatin.
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   SMR; Q6UXN9; -.
DR   BioGRID; 123245; 81.
DR   CORUM; Q6UXN9; -.
DR   IntAct; Q6UXN9; 35.
DR   MINT; Q6UXN9; -.
DR   STRING; 9606.ENSP00000296490; -.
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; 80 antibodies.
DR   Ensembl; ENST00000296490; ENSP00000296490; ENSG00000164091.
DR   GeneID; 80335; -.
DR   KEGG; hsa:80335; -.
DR   UCSC; uc003ddl.3; human.
DR   CTD; 80335; -.
DR   EuPathDB; HostDB:ENSG00000164091.11; -.
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   eggNOG; KOG1446; Eukaryota.
DR   eggNOG; ENOG410XT9X; LUCA.
DR   GeneTree; ENSGT00530000063965; -.
DR   HOGENOM; CLU_044117_3_0_1; -.
DR   InParanoid; Q6UXN9; -.
DR   KO; K14962; -.
DR   OMA; CVLNGDH; -.
DR   OrthoDB; 1146727at2759; -.
DR   PhylomeDB; Q6UXN9; -.
DR   TreeFam; TF313497; -.
DR   SignaLink; Q6UXN9; -.
DR   BioGRID-ORCS; 80335; 705 hits in 798 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 frontal cortex and 247 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:0051568; P:histone H3-K4 methylation; IDA:UniProtKB.
DR   GO; GO:0080182; P:histone H3-K4 trimethylation; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 1.
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; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR19861:SF0; PTHR19861:SF0; 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   Nucleus; Reference proteome; Repeat; 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
//