Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

WD repeat-containing protein 5

Gene

Wdr5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei107 – 1071Important for interaction with histone H3By similarity
Sitei133 – 1331Important for interaction with histone H3By similarity
Sitei263 – 2631Important for interaction with histone H3By similarity
Sitei322 – 3221Important for interaction with histone H3By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
WD repeat-containing protein 5
Alternative name(s):
BMP2-induced 3-kb gene protein
WD repeat-containing protein BIG-3
Gene namesi
Name:Wdr5
Synonyms:Big, Big3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:2155884. Wdr5.

Subcellular locationi

GO - Cellular componenti

  • Ada2/Gcn5/Ada3 transcription activator complex Source: MGI
  • histone acetyltransferase complex Source: UniProtKB
  • histone methyltransferase complex Source: UniProtKB
  • intracellular Source: MGI
  • MLL1 complex Source: UniProtKB
  • MLL3/4 complex Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: UniProtKB
  • Set1C/COMPASS complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 334333WD repeat-containing protein 5PRO_0000051351Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei112 – 1121N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP61965.
MaxQBiP61965.
PaxDbiP61965.
PRIDEiP61965.

PTM databases

iPTMnetiP61965.
PhosphoSiteiP61965.

Expressioni

Tissue specificityi

Expressed in liver (at protein level). Detected in brain, testis and kidney.1 Publication

Gene expression databases

BgeeiP61965.
CleanExiMM_WDR5.
ExpressionAtlasiP61965. baseline and differential.
GenevisibleiP61965. MM.

Interactioni

Subunit structurei

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 CSRP2BP, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1. In the complex, it probably interacts directly with KAT2A, MBIP and CSRP2BP. 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 PER1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Pou5f1P202637EBI-1247084,EBI-1606219

GO - Molecular functioni

Protein-protein interaction databases

BioGridi228326. 47 interactions.
DIPiDIP-38618N.
IntActiP61965. 44 interactions.
MINTiMINT-4140361.
STRINGi10090.ENSMUSP00000109585.

Structurei

Secondary structure

1
334
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 416Combined sources
Beta strandi48 – 536Combined sources
Beta strandi57 – 648Combined sources
Beta strandi69 – 735Combined sources
Turni74 – 763Combined sources
Beta strandi79 – 835Combined sources
Beta strandi90 – 956Combined sources
Beta strandi99 – 1068Combined sources
Beta strandi109 – 1157Combined sources
Turni116 – 1194Combined sources
Beta strandi120 – 1267Combined sources
Beta strandi132 – 1376Combined sources
Beta strandi142 – 1487Combined sources
Beta strandi153 – 1575Combined sources
Turni158 – 1603Combined sources
Beta strandi163 – 1675Combined sources
Beta strandi174 – 1796Combined sources
Beta strandi183 – 1908Combined sources
Beta strandi195 – 1995Combined sources
Turni200 – 2034Combined sources
Beta strandi204 – 2096Combined sources
Beta strandi217 – 2226Combined sources
Beta strandi226 – 2338Combined sources
Turni234 – 2363Combined sources
Beta strandi237 – 2426Combined sources
Turni243 – 2464Combined sources
Beta strandi247 – 2526Combined sources
Beta strandi258 – 2603Combined sources
Beta strandi264 – 2674Combined sources
Beta strandi269 – 2713Combined sources
Beta strandi273 – 2764Combined sources
Beta strandi283 – 2875Combined sources
Turni288 – 2903Combined sources
Beta strandi293 – 2975Combined sources
Beta strandi304 – 3096Combined sources
Beta strandi311 – 32010Combined sources
Turni322 – 3243Combined sources
Beta strandi327 – 3315Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XL2X-ray2.40A/B1-334[»]
2XL3X-ray2.70A/B1-334[»]
ProteinModelPortaliP61965.
SMRiP61965. Positions 31-334.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61965.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati43 – 8240WD 1Add
BLAST
Repeati85 – 12642WD 2Add
BLAST
Repeati128 – 16841WD 3Add
BLAST
Repeati169 – 20840WD 4Add
BLAST
Repeati212 – 25342WD 5Add
BLAST
Repeati256 – 29641WD 6Add
BLAST
Repeati299 – 33335WD 7Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat WDR5/wds family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0266. Eukaryota.
ENOG410XP3K. LUCA.
GeneTreeiENSGT00810000125363.
HOGENOMiHOG000091642.
HOVERGENiHBG055117.
InParanoidiP61965.
KOiK14963.
OMAiCIKTLPA.
OrthoDBiEOG7MH0ZD.
PhylomeDBiP61965.
TreeFamiTF314125.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 7 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P61965-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATEEKKPET EAARAQPTPS SSATQSKPTP VKPNYALKFT LAGHTKAVSS
60 70 80 90 100
VKFSPNGEWL ASSSADKLIK IWGAYDGKFE KTISGHKLGI SDVAWSSDSN
110 120 130 140 150
LLVSASDDKT LKIWDVSSGK CLKTLKGHSN YVFCCNFNPQ SNLIVSGSFD
160 170 180 190 200
ESVRIWDVKT GKCLKTLPAH SDPVSAVHFN RDGSLIVSSS YDGLCRIWDT
210 220 230 240 250
ASGQCLKTLI DDDNPPVSFV KFSPNGKYIL AATLDNTLKL WDYSKGKCLK
260 270 280 290 300
TYTGHKNEKY CIFANFSVTG GKWIVSGSED NLVYIWNLQT KEIVQKLQGH
310 320 330
TDVVISTACH PTENIIASAA LENDKTIKLW KSDC
Length:334
Mass (Da):36,588
Last modified:June 7, 2004 - v1
Checksum:i4BF30914A2250286
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF416510 mRNA. Translation: AAL27006.1.
AK075937 mRNA. Translation: BAC36067.1.
BC008547 mRNA. Translation: AAH08547.1.
BC016103 mRNA. Translation: AAH16103.1.
BC025801 mRNA. Translation: AAH25801.1.
CCDSiCCDS15829.1.
RefSeqiNP_543124.1. NM_080848.2.
XP_006497735.1. XM_006497672.2.
UniGeneiMm.28265.

Genome annotation databases

EnsembliENSMUST00000113952; ENSMUSP00000109585; ENSMUSG00000026917.
GeneIDi140858.
KEGGimmu:140858.
UCSCiuc012bsw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF416510 mRNA. Translation: AAL27006.1.
AK075937 mRNA. Translation: BAC36067.1.
BC008547 mRNA. Translation: AAH08547.1.
BC016103 mRNA. Translation: AAH16103.1.
BC025801 mRNA. Translation: AAH25801.1.
CCDSiCCDS15829.1.
RefSeqiNP_543124.1. NM_080848.2.
XP_006497735.1. XM_006497672.2.
UniGeneiMm.28265.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XL2X-ray2.40A/B1-334[»]
2XL3X-ray2.70A/B1-334[»]
ProteinModelPortaliP61965.
SMRiP61965. Positions 31-334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi228326. 47 interactions.
DIPiDIP-38618N.
IntActiP61965. 44 interactions.
MINTiMINT-4140361.
STRINGi10090.ENSMUSP00000109585.

PTM databases

iPTMnetiP61965.
PhosphoSiteiP61965.

Proteomic databases

EPDiP61965.
MaxQBiP61965.
PaxDbiP61965.
PRIDEiP61965.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000113952; ENSMUSP00000109585; ENSMUSG00000026917.
GeneIDi140858.
KEGGimmu:140858.
UCSCiuc012bsw.2. mouse.

Organism-specific databases

CTDi11091.
MGIiMGI:2155884. Wdr5.

Phylogenomic databases

eggNOGiKOG0266. Eukaryota.
ENOG410XP3K. LUCA.
GeneTreeiENSGT00810000125363.
HOGENOMiHOG000091642.
HOVERGENiHBG055117.
InParanoidiP61965.
KOiK14963.
OMAiCIKTLPA.
OrthoDBiEOG7MH0ZD.
PhylomeDBiP61965.
TreeFamiTF314125.

Enzyme and pathway databases

ReactomeiR-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.

Miscellaneous databases

EvolutionaryTraceiP61965.
PROiP61965.
SOURCEiSearch...

Gene expression databases

BgeeiP61965.
CleanExiMM_WDR5.
ExpressionAtlasiP61965. baseline and differential.
GenevisibleiP61965. MM.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 7 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 4 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a novel WD-40 repeat protein that dramatically accelerates osteoblastic differentiation."
    Gori F., Divieti P., Demay M.B.
    J. Biol. Chem. 276:46515-46522(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Strain: C57BL/6J.
  2. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryonic stem cell.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II and FVB/N.
    Tissue: Liver, Mammary tumor and Salivary gland.
  4. "PERIOD1-associated proteins modulate the negative limb of the mammalian circadian oscillator."
    Brown S.A., Ripperger J., Kadener S., Fleury-Olela F., Vilbois F., Rosbash M., Schibler U.
    Science 308:693-696(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Lung, Spleen and Testis.
  6. "Role for Dpy-30 in ES cell-fate specification by regulation of H3K4 methylation within bivalent domains."
    Jiang H., Shukla A., Wang X., Chen W.Y., Bernstein B.E., Roeder R.G.
    Cell 144:513-525(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL COMPLEX, INTERACTION WITH ASH2L; DPY30; KMT2A; KMT2D AND RRBP5.
  7. Cited for: INTERACTION WITH ZNF335.
  8. "Pax3/7BP is a Pax7- and Pax3-binding protein that regulates the proliferation of muscle precursor cells by an epigenetic mechanism."
    Diao Y., Guo X., Li Y., Sun K., Lu L., Jiang L., Fu X., Zhu H., Sun H., Wang H., Wu Z.
    Cell Stem Cell 11:231-241(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAXBP1.

Entry informationi

Entry nameiWDR5_MOUSE
AccessioniPrimary (citable) accession number: P61965
Secondary accession number(s): Q91VA5
, Q922C9, Q9NWX7, Q9UGP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: June 8, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.