ID WDR5_RAT Reviewed; 334 AA. AC Q498M4; DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 142. DE RecName: Full=WD repeat-containing protein 5; GN Name=Wdr5; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; 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 [2] RP INTERACTION WITH PER1. RX PubMed=15860628; DOI=10.1126/science.1107373; RA Brown S.A., Ripperger J., Kadener S., Fleury-Olela F., Vilbois F., RA Rosbash M., Schibler U.; RT "PERIOD1-associated proteins modulate the negative limb of the mammalian RT circadian oscillator."; RL Science 308:693-696(2005). CC -!- FUNCTION: Contributes to histone modification (By similarity). May CC position the N-terminus of histone H3 for efficient trimethylation at CC 'Lys-4' (By similarity). As part of the MLL1/MLL complex it is involved CC in methylation and dimethylation at 'Lys-4' of histone H3 (By CC similarity). H3 'Lys-4' methylation represents a specific tag for CC epigenetic transcriptional activation (By similarity). As part of the CC NSL complex it may be involved in acetylation of nucleosomal histone H4 CC on several lysine residues (By similarity). May regulate osteoblasts CC differentiation (By similarity). In association with RBBP5 and ASH2L, CC stimulates the histone methyltransferase activities of KMT2A, KMT2B, CC KMT2C, KMT2D, SETD1A and SETD1B (By similarity). CC {ECO:0000250|UniProtKB:P61964, ECO:0000250|UniProtKB:P61965}. CC -!- SUBUNIT: Interacts with PAXBP1; the interaction is direct and links a CC WDR5-containing histone methyltransferase complex to PAX7 and PAX3 (By CC similarity). Interacts with HCFC1 (By similarity). Component of the CC ATAC complex, a complex with histone acetyltransferase activity on CC histones H3 and H4 (By similarity). Component of the SET1 complex, at CC least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, CC WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30 (By similarity). CC Core component of several methyltransferase-containing complexes CC including MLL1/MLL, MLL2/3 (also named ASCOM complex) and MLL4/WBP7 (By CC similarity). Each complex is at least composed of ASH2L, RBBP5, WDR5, CC DPY30, one or more specific histone methyltransferases (KMT2A/MLL1, CC KMT2D/MLL2, KMT2C/MLL3 and KMT2B/MLL4), and the facultative components CC PAGR1, BAP18, CHD8, E2F6, HCFC1, HCFC2, HSP70, INO80C, KDM6A, KANSL1, CC LAS1L, MAX, MCRS1, MEN1, MGA, MYST1/MOF, NCOA6, PAXIP1/PTIP, PELP1, CC PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, CC TAF6, TAF7, TAF9, TEX10 and alpha- and beta-tubulin (By similarity). CC Component of the NSL complex at least composed of MOF/KAT8, KANSL1, CC KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1 (By similarity). CC Interacts with KMT2A/MLL1 (via WIN motif) and RBBP5; the interaction is CC direct (By similarity). Component ofthe ADA2A-containing complex CC (ATAC), composed of KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, CC YEATS2, CCDC101 and DR1 (By similarity). In the complex, it probably CC interacts directly with KAT2A, MBIP and KAT14 (By similarity). CC Interacts with histone H3 (By similarity). Interacts with SETD1A (via CC WIN motif) (By similarity). Component of a histone methylation complex CC composed of at least ZNF335, RBBP5, ASH2L and WDR5; the complex may CC have histone H3-specific methyltransferase activity, however does not CC have specificity for 'Lys-4' of histone H3 (By similarity). Interacts CC with ZNF335 (By similarity). Components of this complex may associate CC with components of the ZNF335-CCAR2-EMSY nuclear receptor-mediated CC transcription complex to form a complex at least composed of ZNF335, CC HCFC1, CCAR2, EMSY, MKI67, RBBP5, ASH2L and WDR5 (By similarity). CC Interacts with PER1 (PubMed:15860628). Interacts with KMT2B (via WIN CC motif), KMT2C (via WIN motif), KMT2D (via WIN motif) and SETD1B (via CC WIN motif) (By similarity). {ECO:0000250|UniProtKB:P61964, CC ECO:0000269|PubMed:15860628}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- SIMILARITY: Belongs to the WD repeat WDR5/wds 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; BC100156; AAI00157.1; -; mRNA. DR RefSeq; NP_001034123.1; NM_001039034.1. DR RefSeq; XP_006233893.1; XM_006233831.2. DR PDB; 4QQE; X-ray; 1.80 A; A=24-334. DR PDBsum; 4QQE; -. DR AlphaFoldDB; Q498M4; -. DR SMR; Q498M4; -. DR CORUM; Q498M4; -. DR IntAct; Q498M4; 1. DR STRING; 10116.ENSRNOP00000011556; -. DR iPTMnet; Q498M4; -. DR PhosphoSitePlus; Q498M4; -. DR jPOST; Q498M4; -. DR PaxDb; 10116-ENSRNOP00000011556; -. DR Ensembl; ENSRNOT00055010160; ENSRNOP00055007850; ENSRNOG00055006265. DR Ensembl; ENSRNOT00060045554; ENSRNOP00060037820; ENSRNOG00060026298. DR Ensembl; ENSRNOT00065035363; ENSRNOP00065028473; ENSRNOG00065020830. DR GeneID; 362093; -. DR KEGG; rno:362093; -. DR UCSC; RGD:1305159; rat. DR AGR; RGD:1305159; -. DR CTD; 11091; -. DR RGD; 1305159; Wdr5. DR VEuPathDB; HostDB:ENSRNOG00000008212; -. DR eggNOG; KOG0266; Eukaryota. DR HOGENOM; CLU_000288_57_1_1; -. DR InParanoid; Q498M4; -. DR OrthoDB; 989707at2759; -. DR PhylomeDB; Q498M4; -. DR TreeFam; TF314125; -. DR Reactome; R-RNO-3214841; PKMTs methylate histone lysines. DR Reactome; R-RNO-3214847; HATs acetylate histones. DR Reactome; R-RNO-3214858; RMTs methylate histone arginines. DR Reactome; R-RNO-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function. DR Reactome; R-RNO-8951664; Neddylation. DR Reactome; R-RNO-9772755; Formation of WDR5-containing histone-modifying complexes. DR PRO; PR:Q498M4; -. DR Proteomes; UP000002494; Chromosome 3. DR Bgee; ENSRNOG00000008212; Expressed in thymus and 20 other cell types or tissues. DR GO; GO:0140672; C:ATAC complex; ISO:RGD. DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB. DR GO; GO:0035097; C:histone methyltransferase complex; ISS:UniProtKB. DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB. DR GO; GO:0044665; C:MLL1/2 complex; ISO:RGD. DR GO; GO:0044666; C:MLL3/4 complex; ISO:RGD. DR GO; GO:0044545; C:NSL complex; ISO:RGD. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0048188; C:Set1C/COMPASS complex; ISS:UniProtKB. DR GO; GO:0042393; F:histone binding; IBA:GO_Central. DR GO; GO:0042800; F:histone H3K4 methyltransferase activity; ISO:RGD. DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB. DR GO; GO:0006094; P:gluconeogenesis; ISO:RGD. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0031175; P:neuron projection development; IDA:RGD. DR GO; GO:0045722; P:positive regulation of gluconeogenesis; ISO:RGD. DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISO:RGD. DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD. DR GO; GO:0051302; P:regulation of cell division; ISO:RGD. DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:RGD. DR GO; GO:0045995; P:regulation of embryonic development; ISO:RGD. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0090043; P:regulation of tubulin deacetylation; ISO:RGD. DR GO; GO:0001501; P:skeletal system development; ISO:RGD. DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; ISS:UniProtKB. DR CDD; cd00200; WD40; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR020472; G-protein_beta_WD-40_rep. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR19879:SF1; CANNONBALL-RELATED; 1. DR PANTHER; PTHR19879; TRANSCRIPTION INITIATION FACTOR TFIID; 1. DR Pfam; PF00400; WD40; 7. DR PIRSF; PIRSF002394; GN-bd_beta; 1. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 7. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS00678; WD_REPEATS_1; 4. DR PROSITE; PS50082; WD_REPEATS_2; 6. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR Genevisible; Q498M4; RN. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Chromatin regulator; Isopeptide bond; Nucleus; KW Reference proteome; Repeat; Transcription; Transcription regulation; KW Ubl conjugation; WD repeat. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P61964" FT CHAIN 2..334 FT /note="WD repeat-containing protein 5" FT /id="PRO_0000278192" FT REPEAT 43..82 FT /note="WD 1" FT REPEAT 85..126 FT /note="WD 2" FT REPEAT 128..168 FT /note="WD 3" FT REPEAT 169..208 FT /note="WD 4" FT REPEAT 212..253 FT /note="WD 5" FT REPEAT 256..296 FT /note="WD 6" FT REPEAT 299..333 FT /note="WD 7" FT REGION 1..31 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 14..31 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 107 FT /note="Important for interaction with histone H3" FT /evidence="ECO:0000250" FT SITE 133 FT /note="Important for interaction with histone H3" FT /evidence="ECO:0000250" FT SITE 263 FT /note="Important for interaction with histone H3" FT /evidence="ECO:0000250" FT SITE 322 FT /note="Important for interaction with histone H3" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P61964" FT MOD_RES 112 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P61964" FT CROSSLNK 7 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P61964" FT CROSSLNK 27 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P61964" FT CROSSLNK 46 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P61964" FT STRAND 36..41 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 48..53 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 57..64 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 67..73 FT /evidence="ECO:0007829|PDB:4QQE" FT TURN 74..76 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 79..84 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 90..95 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 99..106 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 111..115 FT /evidence="ECO:0007829|PDB:4QQE" FT TURN 116..118 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 121..125 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 132..137 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 139..148 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 153..157 FT /evidence="ECO:0007829|PDB:4QQE" FT TURN 158..160 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 163..167 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 174..179 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 183..190 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 195..199 FT /evidence="ECO:0007829|PDB:4QQE" FT TURN 200..202 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 205..209 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 217..222 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 226..233 FT /evidence="ECO:0007829|PDB:4QQE" FT TURN 234..236 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 237..242 FT /evidence="ECO:0007829|PDB:4QQE" FT TURN 243..246 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 247..252 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 258..260 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 264..267 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 269..271 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 273..276 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 283..287 FT /evidence="ECO:0007829|PDB:4QQE" FT TURN 288..290 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 293..297 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 304..309 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 311..320 FT /evidence="ECO:0007829|PDB:4QQE" FT TURN 322..324 FT /evidence="ECO:0007829|PDB:4QQE" FT STRAND 327..331 FT /evidence="ECO:0007829|PDB:4QQE" SQ SEQUENCE 334 AA; 36588 MW; 4BF30914A2250286 CRC64; MATEEKKPET EAARAQPTPS SSATQSKPTP VKPNYALKFT LAGHTKAVSS VKFSPNGEWL ASSSADKLIK IWGAYDGKFE KTISGHKLGI SDVAWSSDSN LLVSASDDKT LKIWDVSSGK CLKTLKGHSN YVFCCNFNPQ SNLIVSGSFD ESVRIWDVKT GKCLKTLPAH SDPVSAVHFN RDGSLIVSSS YDGLCRIWDT ASGQCLKTLI DDDNPPVSFV KFSPNGKYIL AATLDNTLKL WDYSKGKCLK TYTGHKNEKY CIFANFSVTG GKWIVSGSED NLVYIWNLQT KEIVQKLQGH TDVVISTACH PTENIIASAA LENDKTIKLW KSDC //