WDR6_HUMAN
ID WDR6_HUMAN Reviewed; 1121 AA.
AC Q9NNW5; B4DHK2; Q3MIT1; Q9UF63;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=WD repeat-containing protein 6;
GN Name=WDR6;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Heart atrium;
RX PubMed=10903905; DOI=10.1006/bbrc.2000.3012;
RA Li D., Burch P., Gonzalez O., Kashork C.D., Shaffer L.G., Bachinski L.L.,
RA Roberts R.;
RT "Molecular cloning, expression analysis, and chromosome mapping of WDR6, a
RT novel human WD-repeat gene.";
RL Biochem. Biophys. Res. Commun. 274:117-123(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 618-1121.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION, INTERACTION WITH STK11/LKB1, AND SUBCELLULAR LOCATION.
RX PubMed=17216128; DOI=10.1007/s11010-006-9402-5;
RA Xie X., Wang Z., Chen Y.;
RT "Association of LKB1 with a WD-repeat protein WDR6 is implicated in cell
RT growth arrest and p27(Kip1) induction.";
RL Mol. Cell. Biochem. 301:115-122(2007).
RN [7]
RP FUNCTION.
RX PubMed=22354037; DOI=10.1038/emboj.2012.36;
RA McKnight N.C., Jefferies H.B., Alemu E.A., Saunders R.E., Howell M.,
RA Johansen T., Tooze S.A.;
RT "Genome-wide siRNA screen reveals amino acid starvation-induced autophagy
RT requires SCOC and WAC.";
RL EMBO J. 31:1931-1946(2012).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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).
CC -!- FUNCTION: Enhances the STK11/LKB1-induced cell growth suppression
CC activity. Negative regulator of amino acid starvation-induced
CC autophagy. {ECO:0000269|PubMed:17216128, ECO:0000269|PubMed:22354037}.
CC -!- SUBUNIT: Interacts with IRS4 (By similarity). Interacts with
CC STK11/LKB1. {ECO:0000250, ECO:0000269|PubMed:17216128}.
CC -!- INTERACTION:
CC Q9NNW5; Q9Y3R0-3: GRIP1; NbExp=3; IntAct=EBI-1568315, EBI-12193965;
CC Q9NNW5; P26045: PTPN3; NbExp=6; IntAct=EBI-1568315, EBI-1047946;
CC Q9NNW5; Q15831: STK11; NbExp=3; IntAct=EBI-1568315, EBI-306838;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17216128}.
CC Note=Colocalizes in the cytoplasm with STK11/LKB1.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10903905}.
CC -!- SIMILARITY: Belongs to the WD repeat WDR6 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG58164.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF099100; AAF80244.1; -; mRNA.
DR EMBL; AK295145; BAG58164.1; ALT_INIT; mRNA.
DR EMBL; AC137630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC101707; AAI01708.1; -; mRNA.
DR EMBL; BC113467; AAI13468.1; -; mRNA.
DR EMBL; AL133589; CAB63730.1; -; mRNA.
DR CCDS; CCDS2782.2; -.
DR PIR; JC7329; JC7329.
DR PIR; T43496; T43496.
DR RefSeq; NP_001307475.1; NM_001320546.1.
DR RefSeq; NP_001307476.1; NM_001320547.1.
DR RefSeq; NP_060501.3; NM_018031.4.
DR AlphaFoldDB; Q9NNW5; -.
DR BioGRID; 116350; 246.
DR IntAct; Q9NNW5; 82.
DR MINT; Q9NNW5; -.
DR STRING; 9606.ENSP00000378857; -.
DR GlyGen; Q9NNW5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NNW5; -.
DR PhosphoSitePlus; Q9NNW5; -.
DR BioMuta; WDR6; -.
DR DMDM; 12643813; -.
DR EPD; Q9NNW5; -.
DR jPOST; Q9NNW5; -.
DR MassIVE; Q9NNW5; -.
DR MaxQB; Q9NNW5; -.
DR PaxDb; Q9NNW5; -.
DR PeptideAtlas; Q9NNW5; -.
DR PRIDE; Q9NNW5; -.
DR ProteomicsDB; 81856; -.
DR Antibodypedia; 13436; 102 antibodies from 26 providers.
DR DNASU; 11180; -.
DR Ensembl; ENST00000608424.6; ENSP00000477389.1; ENSG00000178252.19.
DR GeneID; 11180; -.
DR KEGG; hsa:11180; -.
DR MANE-Select; ENST00000608424.6; ENSP00000477389.1; NM_018031.6; NP_060501.4.
DR UCSC; uc062job.1; human.
DR CTD; 11180; -.
DR DisGeNET; 11180; -.
DR GeneCards; WDR6; -.
DR HGNC; HGNC:12758; WDR6.
DR HPA; ENSG00000178252; Low tissue specificity.
DR MIM; 606031; gene.
DR neXtProt; NX_Q9NNW5; -.
DR OpenTargets; ENSG00000178252; -.
DR PharmGKB; PA37362; -.
DR VEuPathDB; HostDB:ENSG00000178252; -.
DR eggNOG; KOG0974; Eukaryota.
DR GeneTree; ENSGT00420000029923; -.
DR HOGENOM; CLU_002615_0_0_1; -.
DR InParanoid; Q9NNW5; -.
DR OrthoDB; 555109at2759; -.
DR PhylomeDB; Q9NNW5; -.
DR TreeFam; TF313984; -.
DR PathwayCommons; Q9NNW5; -.
DR Reactome; R-HSA-9013420; RHOU GTPase cycle.
DR Reactome; R-HSA-9013424; RHOV GTPase cycle.
DR Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR Reactome; R-HSA-9696273; RND1 GTPase cycle.
DR SignaLink; Q9NNW5; -.
DR BioGRID-ORCS; 11180; 22 hits in 1086 CRISPR screens.
DR ChiTaRS; WDR6; human.
DR GeneWiki; WDR6; -.
DR GenomeRNAi; 11180; -.
DR Pharos; Q9NNW5; Tbio.
DR PRO; PR:Q9NNW5; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9NNW5; protein.
DR Bgee; ENSG00000178252; Expressed in right uterine tube and 195 other tissues.
DR ExpressionAtlas; Q9NNW5; baseline and differential.
DR Genevisible; Q9NNW5; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0070314; P:G1 to G0 transition; IPI:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP:BHF-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50965; SSF50965; 1.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cytoplasm; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..1121
FT /note="WD repeat-containing protein 6"
FT /id="PRO_0000051352"
FT REPEAT 53..97
FT /note="WD 1"
FT REPEAT 105..143
FT /note="WD 2"
FT REPEAT 147..189
FT /note="WD 3"
FT REPEAT 200..238
FT /note="WD 4"
FT REPEAT 247..285
FT /note="WD 5"
FT REPEAT 289..327
FT /note="WD 6"
FT REPEAT 335..376
FT /note="WD 7"
FT REPEAT 381..422
FT /note="WD 8"
FT REPEAT 425..470
FT /note="WD 9"
FT REPEAT 476..520
FT /note="WD 10"
FT REPEAT 559..598
FT /note="WD 11"
FT REPEAT 604..642
FT /note="WD 12"
FT REPEAT 645..684
FT /note="WD 13"
FT REPEAT 739..785
FT /note="WD 14"
FT REPEAT 848..893
FT /note="WD 15"
FT REPEAT 901..946
FT /note="WD 16"
FT REPEAT 970..1012
FT /note="WD 17"
FT REPEAT 1036..1073
FT /note="WD 18"
FT REPEAT 1079..1121
FT /note="WD 19"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 38
FT /note="D -> N (in Ref. 2; BAG58164)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="S -> R (in Ref. 2; BAG58164)"
FT /evidence="ECO:0000305"
FT CONFLICT 651
FT /note="V -> I (in Ref. 2; BAG58164)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1121 AA; 121725 MW; 4E408D5D893FF005 CRC64;
MDALEDYVWP RATSELILLP VTGLECVGDR LLAGEGPDVL VYSLDFGGHL RMIKRVQNLL
GHYLIHGFRV RPEPNGDLDL EAMVAVFGSK GLRVVKISWG QGHFWELWRS GLWNMSDWIW
DARWLEGNIA LALGHNSVVL YDPVVGCILQ EVPCTDRCTL SSACLIGDAW KELTIVAGAV
SNQLLVWYPA TALADNKPVA PDRRISGHVG IIFSMSYLES KGLLATASED RSVRIWKVGD
LRVPGGRVQN IGHCFGHSAR VWQVKLLENY LISAGEDCVC LVWSHEGEIL QAFRGHQGRG
IRAIAAHERQ AWVITGGDDS GIRLWHLVGR GYRGLGVSAL CFKSRSRPGT LKAVTLAGSW
RLLAVTDTGA LYLYDVEVKC WEQLLEDKHF QSYCLLEAAP GPEGFGLCAM ANGEGRVKVV
PINTPTAAVD QTLFPGKVHS LSWALRGYEE LLLLASGPGG VVACLEISAA PSGKAIFVKE
RCRYLLPPSK QRWHTCSAFL PPGDFLVCGD RRGSVLLFPS RPGLLKDPGV GGKARAGAGA
PVVGSGSSGG GNAFTGLGPV STLPSLHGKQ GVTSVTCHGG YVYTTGRDGA YYQLFVRDGQ
LQPVLRQKSC RGMNWLAGLR IVPDGSMVIL GFHANEFVVW NPRSHEKLHI VNCGGGHRSW
AFSDTEAAMA FAYLKDGDVM LYRALGGCTR PHVILREGLH GREITCVKRV GTITLGPEYG
VPSFMQPDDL EPGSEGPDLT DIVITCSEDT TVCVLALPTT TGSAHALTAV CNHISSVRAV
AVWGIGTPGG PQDPQPGLTA HVVSAGGRAE MHCFSIMVTP DPSTPSRLAC HVMHLSSHRL
DEYWDRQRNR HRMVKVDPET RYMSLAVCEL DQPGLGPLVA AACSDGAVRL FLLQDSGRIL
QLLAETFHHK RCVLKVHSFT HEAPNQRRRL LLCSAATDGS LAFWDLTTML DHDSTVLEPP
VDPGLPYRLG TPSLTLQAHS CGINSLHTLP TREGHHLVAS GSEDGSLHVF VLAVEMLQLE
EAVGEAGLVP QLRVLEEYSV PCAHAAHVTG LKILSPSIMV SASIDQRLTF WRLGHGEPTF
MNSTVFHVPD VADMDCWPVS PEFGHRCALG GQGLEVYNWY D
