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WD repeat-containing protein 5 (BMP2-induced 3-kb gene protein) (WD repeat-containing protein BIG-3)

 WDR5_MOUSE              Reviewed;         334 AA.
P61965; Q91VA5; Q922C9; Q9NWX7; Q9UGP9;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 1.
22-NOV-2017, entry version 139.
RecName: Full=WD repeat-containing protein 5;
AltName: Full=BMP2-induced 3-kb gene protein;
AltName: Full=WD repeat-containing protein BIG-3;
Name=Wdr5; Synonyms=Big, Big3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
STRAIN=C57BL/6J;
PubMed=11551928; DOI=10.1074/jbc.M105757200;
Gori F., Divieti P., Demay M.B.;
"Cloning and characterization of a novel WD-40 repeat protein that
dramatically accelerates osteoblastic differentiation.";
J. Biol. Chem. 276:46515-46522(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II, and FVB/N;
TISSUE=Liver, Mammary tumor, and Salivary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=15860628; DOI=10.1126/science.1107373;
Brown S.A., Ripperger J., Kadener S., Fleury-Olela F., Vilbois F.,
Rosbash M., Schibler U.;
"PERIOD1-associated proteins modulate the negative limb of the
mammalian circadian oscillator.";
Science 308:693-696(2005).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
IDENTIFICATION IN THE MLL COMPLEX, AND INTERACTION WITH ASH2L; DPY30;
KMT2A; KMT2D AND RRBP5.
PubMed=21335234; DOI=10.1016/j.cell.2011.01.020;
Jiang H., Shukla A., Wang X., Chen W.Y., Bernstein B.E., Roeder R.G.;
"Role for Dpy-30 in ES cell-fate specification by regulation of H3K4
methylation within bivalent domains.";
Cell 144:513-525(2011).
[7]
INTERACTION WITH ZNF335.
PubMed=23178126; DOI=10.1016/j.cell.2012.10.043;
Yang Y.J., Baltus A.E., Mathew R.S., Murphy E.A., Evrony G.D.,
Gonzalez D.M., Wang E.P., Marshall-Walker C.A., Barry B.J., Murn J.,
Tatarakis A., Mahajan M.A., Samuels H.H., Shi Y., Golden J.A.,
Mahajnah M., Shenhav R., Walsh C.A.;
"Microcephaly gene links trithorax and REST/NRSF to control neural
stem cell proliferation and differentiation.";
Cell 151:1097-1112(2012).
[8]
INTERACTION WITH PAXBP1.
PubMed=22862948; DOI=10.1016/j.stem.2012.05.022;
Diao Y., Guo X., Li Y., Sun K., Lu L., Jiang L., Fu X., Zhu H.,
Sun H., Wang H., Wu Z.;
"Pax3/7BP is a Pax7- and Pax3-binding protein that regulates the
proliferation of muscle precursor cells by an epigenetic mechanism.";
Cell Stem Cell 11:231-241(2012).
-!- FUNCTION: Contributes to histone modification. May position the N-
terminus of histone H3 for efficient trimethylation at 'Lys-4'. As
part of the MLL1/MLL complex it is involved in methylation and
dimethylation at 'Lys-4' of histone H3. H3 'Lys-4' methylation
represents a specific tag for epigenetic transcriptional
activation. As part of the NSL complex it may be involved in
acetylation of nucleosomal histone H4 on several lysine residues.
May regulate osteoblasts differentiation (By similarity).
{ECO:0000250, ECO:0000269|PubMed:11551928}.
-!- SUBUNIT: Interacts with PAXBP1; the interaction is direct and
links a WDR5-containing histone methyltransferase complex to PAX7
and PAX3. Interacts with HCFC1. Component of the ATAC complex, a
complex with histone acetyltransferase activity on histones H3 and
H4. Component of the SET1 complex, at least composed of the
catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5,
ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30. Core component of several
methyltransferase-containing complexes including MLL1/MLL, MLL2/3
(also named ASCOM complex) and MLL4/WBP7. Each complex is at least
composed of ASH2L, RBBP5, WDR5, DPY30, one or more specific
histone methyltransferases (KMT2A/MLL1, KMT2D/MLL2, KMT2C/MLL3 and
KMT2B/MLL4), and the facultative components PAGR1, BAP18, CHD8,
E2F6, HCFC1, HCFC2, HSP70, INO80C, KDM6A, KANSL1, LAS1L, MAX,
MCRS1, MEN1, MGA, MYST1/MOF, NCOA6, PAXIP1/PTIP, PELP1, PHF20,
PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6,
TAF7, TAF9, TEX10 and alpha- and beta-tubulin. Component of the
NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3,
MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1. Interacts with KMT2A/MLL1
and RBBP5; the interaction is direct. Component ofthe ADA2A-
containing complex (ATAC), composed of KAT14, KAT2A, TADA2L,
TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1. In the complex,
it probably interacts directly with KAT2A, MBIP and KAT14.
Interacts with histone H3. Interacts with SETD1A. Part of a
complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2,
MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may
have a histone H3-specific methyltransferase activity. Interacts
with PER1. {ECO:0000269|PubMed:21335234,
ECO:0000269|PubMed:22862948, ECO:0000269|PubMed:23178126}.
-!- INTERACTION:
P20263:Pou5f1; NbExp=7; IntAct=EBI-1247084, EBI-1606219;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15860628}.
-!- TISSUE SPECIFICITY: Expressed in liver (at protein level).
Detected in brain, testis and kidney.
{ECO:0000269|PubMed:15860628}.
-!- SIMILARITY: Belongs to the WD repeat WDR5/wds family.
{ECO:0000305}.
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EMBL; AF416510; AAL27006.1; -; mRNA.
EMBL; AK075937; BAC36067.1; -; mRNA.
EMBL; BC008547; AAH08547.1; -; mRNA.
EMBL; BC016103; AAH16103.1; -; mRNA.
EMBL; BC025801; AAH25801.1; -; mRNA.
CCDS; CCDS15829.1; -.
RefSeq; NP_543124.1; NM_080848.2.
RefSeq; XP_006497735.1; XM_006497672.3.
UniGene; Mm.28265; -.
PDB; 2XL2; X-ray; 2.40 A; A/B=1-334.
PDB; 2XL3; X-ray; 2.70 A; A/B=1-334.
PDBsum; 2XL2; -.
PDBsum; 2XL3; -.
ProteinModelPortal; P61965; -.
SMR; P61965; -.
BioGrid; 228326; 50.
CORUM; P61965; -.
DIP; DIP-38618N; -.
ELM; P61965; -.
IntAct; P61965; 46.
MINT; MINT-4140361; -.
STRING; 10090.ENSMUSP00000109585; -.
iPTMnet; P61965; -.
PhosphoSitePlus; P61965; -.
EPD; P61965; -.
MaxQB; P61965; -.
PaxDb; P61965; -.
PeptideAtlas; P61965; -.
PRIDE; P61965; -.
Ensembl; ENSMUST00000113952; ENSMUSP00000109585; ENSMUSG00000026917.
GeneID; 140858; -.
KEGG; mmu:140858; -.
UCSC; uc012bsw.2; mouse.
CTD; 11091; -.
MGI; MGI:2155884; Wdr5.
eggNOG; KOG0266; Eukaryota.
eggNOG; ENOG410XP3K; LUCA.
GeneTree; ENSGT00810000125363; -.
HOGENOM; HOG000091642; -.
HOVERGEN; HBG055117; -.
InParanoid; P61965; -.
KO; K14963; -.
OMA; DNPICSH; -.
OrthoDB; EOG091G0CM2; -.
PhylomeDB; P61965; -.
TreeFam; TF314125; -.
Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
Reactome; R-MMU-3214847; HATs acetylate histones.
Reactome; R-MMU-3214858; RMTs methylate histone arginines.
Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-MMU-8951664; Neddylation.
EvolutionaryTrace; P61965; -.
PRO; PR:P61965; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026917; -.
CleanEx; MM_WDR5; -.
ExpressionAtlas; P61965; baseline and differential.
Genevisible; P61965; MM.
GO; GO:0005671; C:Ada2/Gcn5/Ada3 transcription activator complex; IDA:MGI.
GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
GO; GO:0035097; C:histone methyltransferase complex; ISS:UniProtKB.
GO; GO:0005622; C:intracellular; IDA:MGI.
GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
GO; GO:0044666; C:MLL3/4 complex; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048188; C:Set1C/COMPASS complex; ISS:UniProtKB.
GO; GO:0046972; F:histone acetyltransferase activity (H4-K16 specific); IEA:Ensembl.
GO; GO:0043995; F:histone acetyltransferase activity (H4-K5 specific); IEA:Ensembl.
GO; GO:0043996; F:histone acetyltransferase activity (H4-K8 specific); IEA:Ensembl.
GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IEA:Ensembl.
GO; GO:0035064; F:methylated histone binding; ISO:MGI.
GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
GO; GO:0051568; P:histone H3-K4 methylation; IMP:MGI.
GO; GO:0043984; P:histone H4-K16 acetylation; ISS:UniProtKB.
GO; GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
GO; GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
GO; GO:0035948; P:positive regulation of gluconeogenesis by positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
GO; GO:0001501; P:skeletal system development; IDA:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF00400; WD40; 7.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 7.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 4.
PROSITE; PS50082; WD_REPEATS_2; 6.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chromatin regulator; Complete proteome;
Isopeptide bond; Nucleus; Reference proteome; Repeat; Transcription;
Transcription regulation; Ubl conjugation; WD repeat.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P61964}.
CHAIN 2 334 WD repeat-containing protein 5.
/FTId=PRO_0000051351.
REPEAT 43 82 WD 1.
REPEAT 85 126 WD 2.
REPEAT 128 168 WD 3.
REPEAT 169 208 WD 4.
REPEAT 212 253 WD 5.
REPEAT 256 296 WD 6.
REPEAT 299 333 WD 7.
SITE 107 107 Important for interaction with histone
H3. {ECO:0000250}.
SITE 133 133 Important for interaction with histone
H3. {ECO:0000250}.
SITE 263 263 Important for interaction with histone
H3. {ECO:0000250}.
SITE 322 322 Important for interaction with histone
H3. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P61964}.
MOD_RES 112 112 N6-acetyllysine.
{ECO:0000250|UniProtKB:P61964}.
CROSSLNK 7 7 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P61964}.
CROSSLNK 27 27 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P61964}.
CROSSLNK 46 46 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P61964}.
STRAND 36 41 {ECO:0000244|PDB:2XL2}.
STRAND 48 53 {ECO:0000244|PDB:2XL2}.
STRAND 57 64 {ECO:0000244|PDB:2XL2}.
STRAND 69 73 {ECO:0000244|PDB:2XL2}.
TURN 74 76 {ECO:0000244|PDB:2XL2}.
STRAND 79 83 {ECO:0000244|PDB:2XL2}.
STRAND 90 95 {ECO:0000244|PDB:2XL2}.
STRAND 99 106 {ECO:0000244|PDB:2XL2}.
STRAND 109 115 {ECO:0000244|PDB:2XL2}.
TURN 116 119 {ECO:0000244|PDB:2XL2}.
STRAND 120 126 {ECO:0000244|PDB:2XL2}.
STRAND 132 137 {ECO:0000244|PDB:2XL2}.
STRAND 142 148 {ECO:0000244|PDB:2XL2}.
STRAND 153 157 {ECO:0000244|PDB:2XL2}.
TURN 158 160 {ECO:0000244|PDB:2XL2}.
STRAND 163 167 {ECO:0000244|PDB:2XL2}.
STRAND 174 179 {ECO:0000244|PDB:2XL2}.
STRAND 183 190 {ECO:0000244|PDB:2XL2}.
STRAND 195 199 {ECO:0000244|PDB:2XL2}.
TURN 200 203 {ECO:0000244|PDB:2XL2}.
STRAND 204 209 {ECO:0000244|PDB:2XL2}.
STRAND 217 222 {ECO:0000244|PDB:2XL2}.
STRAND 226 233 {ECO:0000244|PDB:2XL2}.
TURN 234 236 {ECO:0000244|PDB:2XL2}.
STRAND 237 242 {ECO:0000244|PDB:2XL2}.
TURN 243 246 {ECO:0000244|PDB:2XL2}.
STRAND 247 252 {ECO:0000244|PDB:2XL2}.
STRAND 258 260 {ECO:0000244|PDB:2XL2}.
STRAND 264 267 {ECO:0000244|PDB:2XL2}.
STRAND 269 271 {ECO:0000244|PDB:2XL2}.
STRAND 273 276 {ECO:0000244|PDB:2XL2}.
STRAND 283 287 {ECO:0000244|PDB:2XL2}.
TURN 288 290 {ECO:0000244|PDB:2XL2}.
STRAND 293 297 {ECO:0000244|PDB:2XL2}.
STRAND 304 309 {ECO:0000244|PDB:2XL2}.
STRAND 311 320 {ECO:0000244|PDB:2XL2}.
TURN 322 324 {ECO:0000244|PDB:2XL2}.
STRAND 327 331 {ECO:0000244|PDB:2XL2}.
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


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EIAAB47428 CAG repeat protein 1,CAGH1,CAS-interacting zinc finger protein,CIZ,Homo sapiens,Human,NMP4,Nuclear matrix protein 4,Nuclear matrix transcription factor 4,TNRC1,Trinucleotide repeat-containing gene 1 p
EIAAB46368 DXImx38e,Mouse,Mus musculus,WD repeat domain phosphoinositide-interacting protein 4,WD repeat domain X-linked 1,WD repeat-containing protein 45,Wdr45,Wdrx1,Wipi4,WIPI-4
26-993 WDR21A is a WD repeat-containing protein. The function of WDR21A remains unknown.This gene encodes a WD repeat-containing protein. Multiple alternatively spliced transcript variants have been found fo 0.05 mg
18-003-43690 Guanine nucleotide-binding protein subunit beta-like protein 1 - G protein subunit beta-like protein 1; WD40 repeat-containing protein deleted in VCFS; Protein WDVCF; WD repeat-containing protein 14; 0.1 mg Protein A
EIAAB44365 Kiaa1992,Mouse,Mus musculus,Tetratricopeptide repeat protein 21B,Tetratricopeptide repeat-containing hedgehog modulator 1,Thm1,TPR repeat protein 21B,Ttc21b


 

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