WDR61_HUMAN
ID WDR61_HUMAN Reviewed; 305 AA.
AC Q9GZS3; D3DW84; Q6IA22; Q7Z4X4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=WD repeat-containing protein 61;
DE AltName: Full=Meiotic recombination REC14 protein homolog;
DE AltName: Full=SKI8 homolog;
DE Short=Ski8;
DE Contains:
DE RecName: Full=WD repeat-containing protein 61, N-terminally processed;
GN Name=WDR61;
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].
RA Shannon M., Thelen M.P.;
RT "Mammalian homologs of meiotic recombination proteins SpRec14 and
RT ScRec103.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tu Q., Yu L., Hu P.R., Fu Q., Cui Y.Y., Xin Y.R., Xu Z.G., Zhang X.N.,
RA Gong R.M., Wang X.K., Zhao S.Y.;
RT "Cloning and sequencing of a novel human cDNA homologous to S.mansoni G
RT protein beta subunit-like mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE PAF1 COMPLEX, AND
RP IDENTIFICATION IN THE SKI COMPLEX.
RX PubMed=16024656; DOI=10.1101/gad.1292105;
RA Zhu B., Mandal S.S., Pham A.D., Zheng Y., Erdjument-Bromage H., Batra S.K.,
RA Tempst P., Reinberg D.;
RT "The human PAF complex coordinates transcription with events downstream of
RT RNA synthesis.";
RL Genes Dev. 19:1668-1673(2005).
RN [8]
RP FUNCTION.
RX PubMed=16307923; DOI=10.1016/j.molcel.2005.09.025;
RA Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H., Tempst P.,
RA Reinberg D.;
RT "Monoubiquitination of human histone H2B: the factors involved and their
RT roles in HOX gene regulation.";
RL Mol. Cell 20:601-611(2005).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=18445686; DOI=10.1242/jcs.019174;
RA Tegha-Dunghu J., Neumann B., Reber S., Krause R., Erfle H., Walter T.,
RA Held M., Rogers P., Hupfeld K., Ruppert T., Ellenberg J., Gruss O.J.;
RT "EML3 is a nuclear microtubule-binding protein required for the correct
RT alignment of chromosomes in metaphase.";
RL J. Cell Sci. 121:1718-1726(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION IN THE PAF1 COMPLEX, AND FUNCTION OF THE PAF1 COMPLEX.
RX PubMed=19952111; DOI=10.1101/gad.1834709;
RA Chen Y., Yamaguchi Y., Tsugeno Y., Yamamoto J., Yamada T., Nakamura M.,
RA Hisatake K., Handa H.;
RT "DSIF, the Paf1 complex, and Tat-SF1 have nonredundant, cooperative roles
RT in RNA polymerase II elongation.";
RL Genes Dev. 23:2765-2777(2009).
RN [12]
RP IDENTIFICATION IN THE PAF1 COMPLEX, COMPOSITION OF THE PAF1 COMPLEX, AND
RP FUNCTION OF THE PAF1 COMPLEX.
RX PubMed=20178742; DOI=10.1016/j.cell.2009.12.050;
RA Kim J., Guermah M., Roeder R.G.;
RT "The human PAF1 complex acts in chromatin transcription elongation both
RT independently and cooperatively with SII/TFIIS.";
RL Cell 140:491-503(2010).
RN [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP IDENTIFICATION BY 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 [16]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=21468892; DOI=10.1007/s13238-011-1018-1;
RA Xu C., Min J.;
RT "Structure and function of WD40 domain proteins.";
RL Protein Cell 2:202-214(2011).
CC -!- FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple
CC functions during transcription by RNA polymerase II and is implicated
CC in regulation of development and maintenance of embryonic stem cell
CC pluripotency. PAF1C associates with RNA polymerase II through
CC interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-
CC 5'-phosphorylated forms and is involved in transcriptional elongation,
CC acting both independently and synergistically with TCEA1 and in
CC cooperation with the DSIF complex and HTATSF1. PAF1C is required for
CC transcription of Hox and Wnt target genes. PAF1C is involved in
CC hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it
CC promotes leukemogenesis through association with KMT2A/MLL1-rearranged
CC oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL.
CC PAF1C is involved in histone modifications such as ubiquitination of
CC histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C
CC recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2
CC enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of
CC 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B
CC ubiquitination is proposed to be coupled to transcription. PAF1C is
CC involved in mRNA 3' end formation probably through association with
CC cleavage and poly(A) factors. In case of infection by influenza A
CC strain H3N2, PAF1C associates with viral NS1 protein, thereby
CC regulating gene transcription. Required for mono- and trimethylation on
CC histone H3 'Lys-4' (H3K4me3), dimethylation on histone H3 'Lys-79'
CC (H3K4me3). Required for Hox gene transcription. Component of the SKI
CC complex which is thought to be involved in exosome-mediated RNA decay
CC and associates with transcriptionally active genes in a manner
CC dependent on PAF1C. {ECO:0000269|PubMed:16024656,
CC ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:19952111,
CC ECO:0000269|PubMed:20178742}.
CC -!- SUBUNIT: Component of the PAF1 complex, which consists of CDC73, PAF1,
CC LEO1, CTR9, RTF1 and WDR61 (PubMed:16024656, PubMed:19952111,
CC PubMed:20178742). The PAF1 complex interacts with PHF5A. Within the
CC PAF1 complex interacts directly with PHF5A (By similarity). Component
CC of the SKI complex which consists of WDR61, SKIV2L and TTC37
CC (PubMed:16024656). {ECO:0000250|UniProtKB:Q9ERF3,
CC ECO:0000269|PubMed:16024656, ECO:0000269|PubMed:19952111,
CC ECO:0000269|PubMed:20178742}.
CC -!- INTERACTION:
CC Q9GZS3; A0A0S2Z5Q7: ALS2; NbExp=3; IntAct=EBI-358545, EBI-25928834;
CC Q9GZS3; P05067: APP; NbExp=3; IntAct=EBI-358545, EBI-77613;
CC Q9GZS3; P05067-2: APP; NbExp=3; IntAct=EBI-358545, EBI-17264467;
CC Q9GZS3; P54253: ATXN1; NbExp=6; IntAct=EBI-358545, EBI-930964;
CC Q9GZS3; Q9UBB4: ATXN10; NbExp=3; IntAct=EBI-358545, EBI-702390;
CC Q9GZS3; Q96G97-4: BSCL2; NbExp=3; IntAct=EBI-358545, EBI-10178113;
CC Q9GZS3; Q6PD62: CTR9; NbExp=12; IntAct=EBI-358545, EBI-1019583;
CC Q9GZS3; P09172: DBH; NbExp=3; IntAct=EBI-358545, EBI-8589586;
CC Q9GZS3; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-358545, EBI-25840379;
CC Q9GZS3; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-358545, EBI-21603100;
CC Q9GZS3; Q13216-2: ERCC8; NbExp=3; IntAct=EBI-358545, EBI-16466949;
CC Q9GZS3; Q16595: FXN; NbExp=3; IntAct=EBI-358545, EBI-949340;
CC Q9GZS3; Q8TB36: GDAP1; NbExp=3; IntAct=EBI-358545, EBI-11110431;
CC Q9GZS3; P14136: GFAP; NbExp=3; IntAct=EBI-358545, EBI-744302;
CC Q9GZS3; Q53GS7: GLE1; NbExp=3; IntAct=EBI-358545, EBI-1955541;
CC Q9GZS3; P28799: GRN; NbExp=3; IntAct=EBI-358545, EBI-747754;
CC Q9GZS3; P28358: HOXD10; NbExp=3; IntAct=EBI-358545, EBI-12690664;
CC Q9GZS3; P42858: HTT; NbExp=22; IntAct=EBI-358545, EBI-466029;
CC Q9GZS3; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-358545, EBI-1055254;
CC Q9GZS3; P02545-2: LMNA; NbExp=3; IntAct=EBI-358545, EBI-351953;
CC Q9GZS3; Q8IXL7-2: MSRB3; NbExp=3; IntAct=EBI-358545, EBI-10699187;
CC Q9GZS3; P19404: NDUFV2; NbExp=3; IntAct=EBI-358545, EBI-713665;
CC Q9GZS3; P29474: NOS3; NbExp=3; IntAct=EBI-358545, EBI-1391623;
CC Q9GZS3; Q9BZ23-2: PANK2; NbExp=3; IntAct=EBI-358545, EBI-25929070;
CC Q9GZS3; Q99497: PARK7; NbExp=3; IntAct=EBI-358545, EBI-1164361;
CC Q9GZS3; O43933: PEX1; NbExp=3; IntAct=EBI-358545, EBI-988601;
CC Q9GZS3; Q7Z412: PEX26; NbExp=3; IntAct=EBI-358545, EBI-752057;
CC Q9GZS3; O60260-5: PRKN; NbExp=6; IntAct=EBI-358545, EBI-21251460;
CC Q9GZS3; P49768-2: PSEN1; NbExp=6; IntAct=EBI-358545, EBI-11047108;
CC Q9GZS3; P49810: PSEN2; NbExp=3; IntAct=EBI-358545, EBI-2010251;
CC Q9GZS3; P51149: RAB7A; NbExp=3; IntAct=EBI-358545, EBI-1056089;
CC Q9GZS3; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-358545, EBI-396669;
CC Q9GZS3; Q7Z333: SETX; NbExp=3; IntAct=EBI-358545, EBI-1220123;
CC Q9GZS3; P37840: SNCA; NbExp=3; IntAct=EBI-358545, EBI-985879;
CC Q9GZS3; Q16143: SNCB; NbExp=3; IntAct=EBI-358545, EBI-727106;
CC Q9GZS3; P00441: SOD1; NbExp=3; IntAct=EBI-358545, EBI-990792;
CC Q9GZS3; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-358545, EBI-5235340;
CC Q9GZS3; Q6NUL7: SPTLC1; NbExp=3; IntAct=EBI-358545, EBI-25912847;
CC Q9GZS3; Q13148: TARDBP; NbExp=6; IntAct=EBI-358545, EBI-372899;
CC Q9GZS3; Q6IQ55-3: TTBK2; NbExp=3; IntAct=EBI-358545, EBI-25930156;
CC Q9GZS3; O95292: VAPB; NbExp=3; IntAct=EBI-358545, EBI-1188298;
CC Q9GZS3; P40337-2: VHL; NbExp=3; IntAct=EBI-358545, EBI-12157263;
CC Q9GZS3; Q9P1N4; NbExp=3; IntAct=EBI-358545, EBI-25878161;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16024656,
CC ECO:0000269|PubMed:18445686}. Cytoplasm {ECO:0000269|PubMed:18445686,
CC ECO:0000305|PubMed:16024656}.
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DR EMBL; AF309553; AAG31639.1; -; mRNA.
DR EMBL; AF100786; AAP97225.1; -; mRNA.
DR EMBL; AF127799; AAP97249.1; -; mRNA.
DR EMBL; AK024754; BAB14986.1; -; mRNA.
DR EMBL; CR457333; CAG33614.1; -; mRNA.
DR EMBL; CH471136; EAW99174.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99175.1; -; Genomic_DNA.
DR EMBL; BC010080; AAH10080.1; -; mRNA.
DR CCDS; CCDS10300.1; -.
DR RefSeq; NP_001290176.1; NM_001303247.1.
DR RefSeq; NP_001290177.1; NM_001303248.1.
DR RefSeq; NP_079510.1; NM_025234.2.
DR RefSeq; XP_011520396.1; XM_011522094.1.
DR PDB; 3OW8; X-ray; 2.30 A; A/B/C/D=2-305.
DR PDB; 6GMH; EM; 3.10 A; W=1-305.
DR PDB; 6TED; EM; 3.10 A; W=1-305.
DR PDB; 7OOP; EM; 2.90 A; Y=1-305.
DR PDB; 7OPC; EM; 3.00 A; Y=1-305.
DR PDB; 7OPD; EM; 3.00 A; Y=1-305.
DR PDB; 7QDR; EM; 3.70 A; C/D=1-305.
DR PDB; 7QDS; EM; 3.80 A; C/D=1-305.
DR PDB; 7QDY; EM; 3.10 A; C/D=1-305.
DR PDB; 7QDZ; EM; 3.60 A; C/D=1-305.
DR PDBsum; 3OW8; -.
DR PDBsum; 6GMH; -.
DR PDBsum; 6TED; -.
DR PDBsum; 7OOP; -.
DR PDBsum; 7OPC; -.
DR PDBsum; 7OPD; -.
DR PDBsum; 7QDR; -.
DR PDBsum; 7QDS; -.
DR PDBsum; 7QDY; -.
DR PDBsum; 7QDZ; -.
DR AlphaFoldDB; Q9GZS3; -.
DR SMR; Q9GZS3; -.
DR BioGRID; 123255; 190.
DR CORUM; Q9GZS3; -.
DR DIP; DIP-36672N; -.
DR IntAct; Q9GZS3; 96.
DR MINT; Q9GZS3; -.
DR STRING; 9606.ENSP00000267973; -.
DR GlyGen; Q9GZS3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9GZS3; -.
DR PhosphoSitePlus; Q9GZS3; -.
DR BioMuta; WDR61; -.
DR DMDM; 74761365; -.
DR EPD; Q9GZS3; -.
DR jPOST; Q9GZS3; -.
DR MassIVE; Q9GZS3; -.
DR MaxQB; Q9GZS3; -.
DR PaxDb; Q9GZS3; -.
DR PeptideAtlas; Q9GZS3; -.
DR PRIDE; Q9GZS3; -.
DR ProteomicsDB; 80126; -.
DR Antibodypedia; 27601; 308 antibodies from 29 providers.
DR DNASU; 80349; -.
DR Ensembl; ENST00000267973.7; ENSP00000267973.2; ENSG00000140395.9.
DR Ensembl; ENST00000558311.5; ENSP00000453801.1; ENSG00000140395.9.
DR GeneID; 80349; -.
DR KEGG; hsa:80349; -.
DR MANE-Select; ENST00000267973.7; ENSP00000267973.2; NM_025234.3; NP_079510.1.
DR UCSC; uc002bdn.4; human.
DR CTD; 80349; -.
DR DisGeNET; 80349; -.
DR GeneCards; WDR61; -.
DR HGNC; HGNC:30300; WDR61.
DR HPA; ENSG00000140395; Low tissue specificity.
DR MIM; 609540; gene.
DR neXtProt; NX_Q9GZS3; -.
DR OpenTargets; ENSG00000140395; -.
DR PharmGKB; PA142670595; -.
DR VEuPathDB; HostDB:ENSG00000140395; -.
DR eggNOG; KOG4155; Eukaryota.
DR GeneTree; ENSGT00940000153533; -.
DR InParanoid; Q9GZS3; -.
DR OMA; VGFSPCN; -.
DR OrthoDB; 1052423at2759; -.
DR PhylomeDB; Q9GZS3; -.
DR TreeFam; TF324549; -.
DR PathwayCommons; Q9GZS3; -.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-429958; mRNA decay by 3' to 5' exoribonuclease.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR SignaLink; Q9GZS3; -.
DR BioGRID-ORCS; 80349; 619 hits in 1091 CRISPR screens.
DR ChiTaRS; WDR61; human.
DR EvolutionaryTrace; Q9GZS3; -.
DR GenomeRNAi; 80349; -.
DR Pharos; Q9GZS3; Tbio.
DR PRO; PR:Q9GZS3; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9GZS3; protein.
DR Bgee; ENSG00000140395; Expressed in tibia and 208 other tissues.
DR ExpressionAtlas; Q9GZS3; baseline and differential.
DR Genevisible; Q9GZS3; HS.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0055087; C:Ski complex; IDA:UniProtKB.
DR GO; GO:0051568; P:histone H3-K4 methylation; IBA:GO_Central.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:UniProtKB.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IDA:UniProtKB.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:UniProtKB.
DR GO; GO:2001162; P:positive regulation of histone H3-K79 methylation; IMP:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
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; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 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; Cytoplasm; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; WD repeat; Wnt signaling pathway.
FT CHAIN 1..305
FT /note="WD repeat-containing protein 61"
FT /id="PRO_0000425748"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..305
FT /note="WD repeat-containing protein 61, N-terminally
FT processed"
FT /id="PRO_0000245851"
FT REPEAT 14..57
FT /note="WD 1"
FT REPEAT 62..101
FT /note="WD 2"
FT REPEAT 104..143
FT /note="WD 3"
FT REPEAT 146..187
FT /note="WD 4"
FT REPEAT 188..227
FT /note="WD 5"
FT REPEAT 230..269
FT /note="WD 6"
FT REPEAT 272..305
FT /note="WD 7"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 2
FT /note="N-acetylthreonine; in WD repeat-containing protein
FT 61, N-terminally processed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CONFLICT 91
FT /note="W -> R (in Ref. 2; AAP97249)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="D -> A (in Ref. 2; AAP97249)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="S -> G (in Ref. 4; CAG33614)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="S -> N (in Ref. 4; CAG33614)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="W -> R (in Ref. 2; AAP97249)"
FT /evidence="ECO:0000305"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:3OW8"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 74..83
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:3OW8"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:3OW8"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 160..167
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:6TED"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:3OW8"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:3OW8"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 244..251
FT /evidence="ECO:0007829|PDB:3OW8"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:6GMH"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:3OW8"
FT TURN 261..264
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 286..293
FT /evidence="ECO:0007829|PDB:3OW8"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:3OW8"
SQ SEQUENCE 305 AA; 33581 MW; A26C4BBD4F8ADB80 CRC64;
MTNQYGILFK QEQAHDDAIW SVAWGTNKKE NSETVVTGSL DDLVKVWKWR DERLDLQWSL
EGHQLGVVSV DISHTLPIAA SSSLDAHIRL WDLENGKQIK SIDAGPVDAW TLAFSPDSQY
LATGTHVGKV NIFGVESGKK EYSLDTRGKF ILSIAYSPDG KYLASGAIDG IINIFDIATG
KLLHTLEGHA MPIRSLTFSP DSQLLVTASD DGYIKIYDVQ HANLAGTLSG HASWVLNVAF
CPDDTHFVSS SSDKSVKVWD VGTRTCVHTF FDHQDQVWGV KYNGNGSKIV SVGDDQEIHI
YDCPI
