WDR61_MOUSE
ID WDR61_MOUSE Reviewed; 305 AA.
AC Q9ERF3; Q3U562; Q9CZP1;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=WD repeat-containing protein 61;
DE AltName: Full=Meiotic recombination REC14 protein homolog;
DE Contains:
DE RecName: Full=WD repeat-containing protein 61, N-terminally processed;
GN Name=Wdr61;
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 [MRNA].
RC STRAIN=BALB/cJ;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Placenta, and Stomach;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; 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 FUNCTION.
RX PubMed=19345177; DOI=10.1016/j.stem.2009.03.009;
RA Ding L., Paszkowski-Rogacz M., Nitzsche A., Slabicki M.M., Heninger A.K.,
RA de Vries I., Kittler R., Junqueira M., Shevchenko A., Schulz H., Hubner N.,
RA Doss M.X., Sachinidis A., Hescheler J., Iacone R., Anastassiadis K.,
RA Stewart A.F., Pisabarro M.T., Caldarelli A., Poser I., Theis M.,
RA Buchholz F.;
RT "A genome-scale RNAi screen for Oct4 modulators defines a role of the Paf1
RT complex for embryonic stem cell identity.";
RL Cell Stem Cell 4:403-415(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PHF5A, AND SUBUNIT.
RX PubMed=27749823; DOI=10.1038/ncb3424;
RA Strikoudis A., Lazaris C., Trimarchi T., Galvao Neto A.L., Yang Y.,
RA Ntziachristos P., Rothbart S., Buckley S., Dolgalev I., Stadtfeld M.,
RA Strahl B.D., Dynlacht B.D., Tsirigos A., Aifantis I.;
RT "Regulation of transcriptional elongation in pluripotency and cell
RT differentiation by the PHD-finger protein Phf5a.";
RL Nat. Cell Biol. 18:1127-1138(2016).
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.
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. 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 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:19345177}.
CC -!- SUBUNIT: Component of the PAF1 complex, which consists of CDC73, PAF1,
CC LEO1, CTR9, RTF1 and WDR61. The PAF1 complex interacts with PHF5A
CC (PubMed:27749823). Within the PAF1 complex interacts directly with
CC PHF5A (PubMed:27749823). Component of the SKI complex which consists of
CC WDR61, SKIV2L and TTC37 (By similarity). {ECO:0000250|UniProtKB:Q9GZS3,
CC ECO:0000269|PubMed:27749823}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9GZS3}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9GZS3}.
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; AF309554; AAG31640.1; -; mRNA.
DR EMBL; AK012342; BAB28173.1; -; mRNA.
DR EMBL; AK013114; BAB28657.1; -; mRNA.
DR EMBL; AK142498; BAE25087.1; -; mRNA.
DR EMBL; AK153862; BAE32218.1; -; mRNA.
DR EMBL; AK167706; BAE39750.1; -; mRNA.
DR EMBL; BC023026; AAH23026.1; -; mRNA.
DR CCDS; CCDS23194.1; -.
DR RefSeq; NP_001020546.1; NM_001025375.2.
DR RefSeq; NP_075680.1; NM_023191.3.
DR AlphaFoldDB; Q9ERF3; -.
DR SMR; Q9ERF3; -.
DR BioGRID; 211379; 42.
DR IntAct; Q9ERF3; 27.
DR MINT; Q9ERF3; -.
DR STRING; 10090.ENSMUSP00000113560; -.
DR iPTMnet; Q9ERF3; -.
DR PhosphoSitePlus; Q9ERF3; -.
DR EPD; Q9ERF3; -.
DR MaxQB; Q9ERF3; -.
DR PaxDb; Q9ERF3; -.
DR PRIDE; Q9ERF3; -.
DR ProteomicsDB; 275206; -.
DR Antibodypedia; 27601; 308 antibodies from 29 providers.
DR DNASU; 66317; -.
DR Ensembl; ENSMUST00000051822; ENSMUSP00000056359; ENSMUSG00000061559.
DR Ensembl; ENSMUST00000121204; ENSMUSP00000113560; ENSMUSG00000061559.
DR GeneID; 66317; -.
DR KEGG; mmu:66317; -.
DR UCSC; uc009prm.2; mouse.
DR CTD; 80349; -.
DR MGI; MGI:1917493; Wdr61.
DR VEuPathDB; HostDB:ENSMUSG00000061559; -.
DR eggNOG; KOG4155; Eukaryota.
DR GeneTree; ENSGT00940000153533; -.
DR InParanoid; Q9ERF3; -.
DR OMA; VGFSPCN; -.
DR OrthoDB; 1052423at2759; -.
DR PhylomeDB; Q9ERF3; -.
DR TreeFam; TF324549; -.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-429958; mRNA decay by 3' to 5' exoribonuclease.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR BioGRID-ORCS; 66317; 33 hits in 72 CRISPR screens.
DR ChiTaRS; Wdr61; mouse.
DR PRO; PR:Q9ERF3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9ERF3; protein.
DR Bgee; ENSMUSG00000061559; Expressed in metanephric ureteric bud and 260 other tissues.
DR ExpressionAtlas; Q9ERF3; baseline and differential.
DR Genevisible; Q9ERF3; MM.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; IPI:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0055087; C:Ski complex; ISS:UniProtKB.
DR GO; GO:0051568; P:histone H3-K4 methylation; IBA:GO_Central.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; ISS:UniProtKB.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; ISS:UniProtKB.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISS:UniProtKB.
DR GO; GO:2001162; P:positive regulation of histone H3-K79 methylation; ISS:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
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; IPR013979; TIF_beta_prop-like.
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; PF08662; eIF2A; 1.
DR Pfam; PF00400; WD40; 4.
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 Acetylation; Cytoplasm; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; WD repeat; Wnt signaling pathway.
FT CHAIN 1..305
FT /note="WD repeat-containing protein 61"
FT /id="PRO_0000425749"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9GZS3"
FT CHAIN 2..305
FT /note="WD repeat-containing protein 61, N-terminally
FT processed"
FT /id="PRO_0000245852"
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:0000250|UniProtKB:Q9GZS3"
FT MOD_RES 2
FT /note="N-acetylthreonine; in WD repeat-containing protein
FT 61, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:Q9GZS3"
FT CONFLICT 229
FT /note="S -> G (in Ref. 2; BAE32218)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="S -> L (in Ref. 2; BAB28173)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 305 AA; 33773 MW; 18502857097C4081 CRC64;
MTNQYSILFK QEQAHDDAIW SVAWETNKKE NIETVVTGSL DDLVKVWKWR DERLELQWSL
EGHQLGVVSV DISHTLPIAA SSSLDAHIRL WDLENGKQMK SIDAGPVDAW TLAFSPDSQY
LATGTHMGKV NIFGVESGKK EYSLDTRGKF ILSIAYSPDG KYLASGAIDG IINIFDIATG
KLLHTLEGHA MPIRSLTFSP DSQLLVTASD DGYIKIYDVQ HANLAGTLSG HASWVLNVAF
CPDDTHFVSS SSDKSVKVWD VGTRTCIHTF FDHQDQVWGV KYNGNGSKIV SVGDDQEIHV
YDCPI
