WDR26_HUMAN
ID WDR26_HUMAN Reviewed; 661 AA.
AC Q9H7D7; A0MNN3; Q4G100; Q59EC4; Q5GLZ9; Q86UY4; Q9H3C2;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=WD repeat-containing protein 26;
DE AltName: Full=CUL4- and DDB1-associated WDR protein 2;
DE AltName: Full=Myocardial ischemic preconditioning up-regulated protein 2;
GN Name=WDR26; Synonyms=CDW2, MIP2; ORFNames=PRO0852;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Endothelial cell;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-661 (ISOFORM 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 138-661 (ISOFORM 1).
RC TISSUE=Lung, Testis, and Uterus;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 25-661 (ISOFORM 2).
RA Yuan C., Xiao X., Zhang H.;
RT "Human myocardial ischemic preconditioning upregulated gene 2.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 84-661 (ISOFORM 1), TISSUE SPECIFICITY,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Heart;
RX PubMed=15378603; DOI=10.1002/jcb.20175;
RA Zhu Y., Wang Y., Xia C., Li D., Li Y., Zeng W., Yuan W., Liu H., Zhu C.,
RA Wu X., Liu M.;
RT "WDR26: a novel Gbeta-like protein, suppresses MAPK signaling pathway.";
RL J. Cell. Biochem. 93:579-587(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 86-661 (ISOFORM 4).
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y., Xu W.,
RA Gao F., Liu M., He F.;
RT "Functional prediction of the coding sequences of 75 new genes deduced by
RT analysis of cDNA clones from human fetal liver.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 138-661 (ISOFORM 1), INTERACTION WITH CUL4,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17041588; DOI=10.1038/ncb1490;
RA Higa L.A., Wu M., Ye T., Kobayashi R., Sun H., Zhang H.;
RT "CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins
RT and regulates histone methylation.";
RL Nat. Cell Biol. 8:1277-1283(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 265-661 (ISOFORM 1).
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP INDUCTION, AND FUNCTION.
RX PubMed=19446606; DOI=10.1016/j.neulet.2009.05.024;
RA Zhao J., Liu Y., Wei X., Yuan C., Yuan X., Xiao X.;
RT "A novel WD-40 repeat protein WDR26 suppresses H2O2-induced cell death in
RT neural cells.";
RL Neurosci. Lett. 460:66-71(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP FUNCTION, AND INTERACTION WITH A G-BETA:GAMMA UNIT.
RX PubMed=22065575; DOI=10.1074/jbc.m111.301382;
RA Sun Z., Tang X., Lin F., Chen S.;
RT "The WD40 repeat protein WDR26 binds Gbetagamma and promotes Gbetagamma-
RT dependent signal transduction and leukocyte migration.";
RL J. Biol. Chem. 286:43902-43912(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH PLCB2 AND A G-BETA:GAMMA UNIT.
RX PubMed=23625927; DOI=10.1074/jbc.m113.462564;
RA Sun Z., Smrcka A.V., Chen S.;
RT "WDR26 functions as a scaffolding protein to promote Gbetagamma-mediated
RT phospholipase C beta2 (PLCbeta2) activation in leukocytes.";
RL J. Biol. Chem. 288:16715-16725(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121 AND SER-123, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121 AND SER-123, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP INTERACTION WITH AXIN1, AND FUNCTION.
RX PubMed=27098453; DOI=10.1002/1873-3468.12180;
RA Goto T., Matsuzawa J., Iemura S., Natsume T., Shibuya H.;
RT "WDR26 is a new partner of Axin1 in the canonical Wnt signaling pathway.";
RL FEBS Lett. 590:1291-1303(2016).
RN [20]
RP FUNCTION.
RX PubMed=26895380; DOI=10.18632/oncotarget.7439;
RA Ye Y., Tang X., Sun Z., Chen S.;
RT "Upregulated WDR26 serves as a scaffold to coordinate PI3K/ AKT pathway-
RT driven breast cancer cell growth, migration, and invasion.";
RL Oncotarget 7:17854-17869(2016).
RN [21]
RP FUNCTION, IDENTIFICATION IN THE CTLH COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=29911972; DOI=10.7554/elife.35528;
RA Lampert F., Stafa D., Goga A., Soste M.V., Gilberto S., Olieric N.,
RA Picotti P., Stoffel M., Peter M.;
RT "The multi-subunit GID/CTLH E3 ligase promotes proliferation and targets
RT the transcription factor Hbp1 for degradation.";
RL Elife 7:0-0(2018).
RN [22]
RP VARIANTS SKDEAS 46-SER--SER-661 DEL; ARG-172; PRO-215; ARG-254;
RP 279-ARG--SER-661 DEL; ASN-284; 426-GLU--SER-661 DEL; 428-TRP--SER-661 DEL
RP AND 524-GLN--SER-661 DEL, AND CHARACTERIZATION OF VARIANT SKDEAS ASN-284.
RX PubMed=28686853; DOI=10.1016/j.ajhg.2017.06.002;
RA Skraban C.M., Wells C.F., Markose P., Cho M.T., Nesbitt A.I., Au P.Y.B.,
RA Begtrup A., Bernat J.A., Bird L.M., Cao K., de Brouwer A.P.M.,
RA Denenberg E.H., Douglas G., Gibson K.M., Grand K., Goldenberg A.,
RA Innes A.M., Juusola J., Kempers M., Kinning E., Markie D.M., Owens M.M.,
RA Payne K., Person R., Pfundt R., Stocco A., Turner C.L.S., Verbeek N.E.,
RA Walsh L.E., Warner T.C., Wheeler P.G., Wieczorek D., Wilkens A.B.,
RA Zonneveld-Huijssoon E., Kleefstra T., Robertson S.P., Santani A.,
RA van Gassen K.L.I., Deardorff M.A.;
RT "WDR26 haploinsufficiency causes a recognizable syndrome of intellectual
RT disability, seizures, abnormal gait, and distinctive facial features.";
RL Am. J. Hum. Genet. 101:139-148(2017).
CC -!- FUNCTION: G-beta-like protein involved in cell signal transduction
CC (PubMed:15378603, PubMed:19446606, PubMed:22065575, PubMed:23625927,
CC PubMed:27098453, PubMed:26895380). Acts as a negative regulator in MAPK
CC signaling pathway (PubMed:15378603). Functions as a scaffolding protein
CC to promote G beta:gamma-mediated PLCB2 plasma membrane translocation
CC and subsequent activation in leukocytes (PubMed:22065575,
CC PubMed:23625927). Core component of the CTLH E3 ubiquitin-protein
CC ligase complex that selectively accepts ubiquitin from UBE2H and
CC mediates ubiquitination and subsequent proteasomal degradation of the
CC transcription factor HBP1 (PubMed:29911972). Acts as a negative
CC regulator of the canonical Wnt signaling pathway through preventing
CC ubiquitination of beta-catenin CTNNB1 by the beta-catenin destruction
CC complex, thus negatively regulating CTNNB1 degradation
CC (PubMed:27098453). Serves as a scaffold to coordinate PI3K/AKT pathway-
CC driven cell growth and migration (PubMed:26895380). Protects cells from
CC oxidative stress-induced apoptosis via the down-regulation of AP-1
CC transcriptional activity as well as by inhibiting cytochrome c release
CC from mitochondria (PubMed:19446606). Protects also cells by promoting
CC hypoxia-mediated autophagy and mitophagy (By similarity).
CC {ECO:0000250|UniProtKB:F1LTR1, ECO:0000269|PubMed:15378603,
CC ECO:0000269|PubMed:19446606, ECO:0000269|PubMed:23625927,
CC ECO:0000269|PubMed:26895380, ECO:0000269|PubMed:27098453,
CC ECO:0000269|PubMed:29911972}.
CC -!- SUBUNIT: Forms homooligomers (PubMed:23625927). Identified in the CTLH
CC complex that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A
CC (or alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5
CC (PubMed:29911972). Within this complex, MAEA, RMND5A (or alternatively
CC its paralog RMND5B), GID8, WDR26, and RANBP9 and/or RANBP10 form the
CC catalytic core, while GID4, MKLN1, ARMC8 and YPEL5 have ancillary roles
CC (PubMed:29911972). Interacts with DDB1-CUL4A/B E3 ligase complexes
CC (PubMed:17041588). Forms a complex composed of at least WDR26, a G-
CC beta:gamma unit, and PLCB2 (PubMed:22065575, PubMed:23625927).
CC Interacts with AXIN1 (PubMed:27098453). {ECO:0000269|PubMed:17041588,
CC ECO:0000269|PubMed:22065575, ECO:0000269|PubMed:23625927,
CC ECO:0000269|PubMed:27098453, ECO:0000269|PubMed:29911972}.
CC -!- INTERACTION:
CC Q9H7D7; O15169: AXIN1; NbExp=4; IntAct=EBI-1046864, EBI-710484;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15378603}. Nucleus
CC {ECO:0000269|PubMed:29911972}. Mitochondrion
CC {ECO:0000250|UniProtKB:F1LTR1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9H7D7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H7D7-2; Sequence=VSP_023895;
CC Name=3;
CC IsoId=Q9H7D7-3; Sequence=VSP_023896, VSP_023898;
CC Name=4;
CC IsoId=Q9H7D7-4; Sequence=VSP_023897, VSP_023899;
CC -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in heart and
CC skeletal muscle. {ECO:0000269|PubMed:15378603}.
CC -!- INDUCTION: Expression is significantly up-regulated by oxidative stress
CC (PubMed:19446606). {ECO:0000269|PubMed:19446606}.
CC -!- DISEASE: Skraban-Deardorff syndrome (SKDEAS) [MIM:617616]: An autosomal
CC dominant syndrome characterized by psychomotor developmental delay,
CC intellectual disability with delayed speech, febrile and non-febrile
CC seizures, abnormal gait, and facial dysmorphism. Facial features
CC include a prominent maxilla and upper lip that readily reveal the upper
CC gingiva, widely spaced teeth, and a broad nasal tip.
CC {ECO:0000269|PubMed:28686853}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG35477.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH52301.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH63817.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO67709.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAQ74770.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABK41102.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14955.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD93124.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB209887; BAD93124.1; ALT_INIT; mRNA.
DR EMBL; AC099790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031471; AAH31471.2; -; mRNA.
DR EMBL; BC034498; AAH34498.1; -; mRNA.
DR EMBL; BC052301; AAH52301.2; ALT_INIT; mRNA.
DR EMBL; BC063817; AAH63817.2; ALT_INIT; mRNA.
DR EMBL; AY221751; AAO67709.1; ALT_INIT; mRNA.
DR EMBL; AY304473; AAQ74770.1; ALT_INIT; mRNA.
DR EMBL; AF130049; AAG35477.1; ALT_INIT; mRNA.
DR EMBL; EF011612; ABK41102.1; ALT_INIT; mRNA.
DR EMBL; AK024669; BAB14955.1; ALT_SEQ; mRNA.
DR CCDS; CCDS31037.2; -. [Q9H7D7-1]
DR RefSeq; NP_001108585.2; NM_001115113.2. [Q9H7D7-2]
DR RefSeq; NP_079436.4; NM_025160.6. [Q9H7D7-1]
DR AlphaFoldDB; Q9H7D7; -.
DR SMR; Q9H7D7; -.
DR BioGRID; 123195; 162.
DR CORUM; Q9H7D7; -.
DR IntAct; Q9H7D7; 69.
DR MINT; Q9H7D7; -.
DR STRING; 9606.ENSP00000408108; -.
DR GlyGen; Q9H7D7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H7D7; -.
DR PhosphoSitePlus; Q9H7D7; -.
DR BioMuta; WDR26; -.
DR DMDM; 134047967; -.
DR EPD; Q9H7D7; -.
DR jPOST; Q9H7D7; -.
DR MassIVE; Q9H7D7; -.
DR MaxQB; Q9H7D7; -.
DR PaxDb; Q9H7D7; -.
DR PeptideAtlas; Q9H7D7; -.
DR PRIDE; Q9H7D7; -.
DR ProteomicsDB; 81109; -. [Q9H7D7-1]
DR ProteomicsDB; 81110; -. [Q9H7D7-2]
DR ProteomicsDB; 81111; -. [Q9H7D7-3]
DR ProteomicsDB; 81112; -. [Q9H7D7-4]
DR Antibodypedia; 34639; 97 antibodies from 18 providers.
DR DNASU; 80232; -.
DR Ensembl; ENST00000678917.1; ENSP00000504428.1; ENSG00000162923.17. [Q9H7D7-1]
DR GeneID; 80232; -.
DR KEGG; hsa:80232; -.
DR UCSC; uc001hop.4; human. [Q9H7D7-1]
DR CTD; 80232; -.
DR DisGeNET; 80232; -.
DR GeneCards; WDR26; -.
DR GeneReviews; WDR26; -.
DR HGNC; HGNC:21208; WDR26.
DR HPA; ENSG00000162923; Low tissue specificity.
DR MalaCards; WDR26; -.
DR MIM; 617424; gene.
DR MIM; 617616; phenotype.
DR neXtProt; NX_Q9H7D7; -.
DR OpenTargets; ENSG00000162923; -.
DR Orphanet; 513456; Intellectual disability-seizures-abnormal gait-facial dysmorphism syndrome.
DR PharmGKB; PA134907873; -.
DR VEuPathDB; HostDB:ENSG00000162923; -.
DR eggNOG; KOG0293; Eukaryota.
DR GeneTree; ENSGT00940000153634; -.
DR HOGENOM; CLU_000288_57_25_1; -.
DR InParanoid; Q9H7D7; -.
DR OrthoDB; 349428at2759; -.
DR PhylomeDB; Q9H7D7; -.
DR TreeFam; TF314869; -.
DR PathwayCommons; Q9H7D7; -.
DR SignaLink; Q9H7D7; -.
DR BioGRID-ORCS; 80232; 306 hits in 1078 CRISPR screens.
DR ChiTaRS; WDR26; human.
DR GeneWiki; WDR26; -.
DR GenomeRNAi; 80232; -.
DR Pharos; Q9H7D7; Tbio.
DR PRO; PR:Q9H7D7; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H7D7; protein.
DR Bgee; ENSG00000162923; Expressed in sperm and 198 other tissues.
DR ExpressionAtlas; Q9H7D7; baseline and differential.
DR Genevisible; Q9H7D7; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0034657; C:GID complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR006594; LisH.
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; 4.
DR SMART; SM00668; CTLH; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Disease variant; Intellectual disability;
KW Mitochondrion; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..661
FT /note="WD repeat-containing protein 26"
FT /id="PRO_0000051373"
FT DOMAIN 123..155
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 156..231
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT REPEAT 353..392
FT /note="WD 1"
FT REPEAT 399..438
FT /note="WD 2"
FT REPEAT 444..484
FT /note="WD 3"
FT REPEAT 524..563
FT /note="WD 4"
FT REPEAT 566..608
FT /note="WD 5"
FT REPEAT 611..651
FT /note="WD 6"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 192..207
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_023895"
FT VAR_SEQ 194..216
FT /note="VRGALEISQTLLGIIVRMKFLLL -> AQTFSETSINFFPLTAAFCHVRG
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023896"
FT VAR_SEQ 210..223
FT /note="RMKFLLLQQKYLEY -> VNTLLFLVSHLCLF (in isoform 4)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_023897"
FT VAR_SEQ 217..661
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023898"
FT VAR_SEQ 224..661
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_023899"
FT VARIANT 46..661
FT /note="Missing (in SKDEAS)"
FT /evidence="ECO:0000269|PubMed:28686853"
FT /id="VAR_079297"
FT VARIANT 172
FT /note="W -> R (in SKDEAS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28686853"
FT /id="VAR_079298"
FT VARIANT 215
FT /note="L -> P (in SKDEAS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28686853"
FT /id="VAR_079299"
FT VARIANT 254
FT /note="S -> R (in SKDEAS; unknown pathological
FT significance; dbSNP:rs150512167)"
FT /evidence="ECO:0000269|PubMed:28686853"
FT /id="VAR_079300"
FT VARIANT 279..661
FT /note="Missing (in SKDEAS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28686853"
FT /id="VAR_079301"
FT VARIANT 284
FT /note="D -> N (in SKDEAS; unknown pathological
FT significance; slightly decreased protein expression;;
FT dbSNP:rs1553359384)"
FT /evidence="ECO:0000269|PubMed:28686853"
FT /id="VAR_079302"
FT VARIANT 426..661
FT /note="Missing (in SKDEAS)"
FT /evidence="ECO:0000269|PubMed:28686853"
FT /id="VAR_079303"
FT VARIANT 428..661
FT /note="Missing (in SKDEAS)"
FT /evidence="ECO:0000269|PubMed:28686853"
FT /id="VAR_079304"
FT VARIANT 524..661
FT /note="Missing (in SKDEAS)"
FT /evidence="ECO:0000269|PubMed:28686853"
FT /id="VAR_079305"
FT CONFLICT 8
FT /note="G -> A (in Ref. 3; AAH34498)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 661 AA; 72124 MW; E0B8AAFF44CB7DF7 CRC64;
MQANGAGGGG GGGGGGGGGG GGGGGQGQTP ELACLSAQNG ESSPSSSSSA GDLAHANGLL
PSAPSAASNN SNSLNVNNGV PGGAAAASSA TVAAASATTA ASSSLATPEL GSSLKKKKRL
SQSDEDVIRL IGQHLNGLGL NQTVDLLMQE SGCRLEHPSA TKFRNHVMEG DWDKAENDLN
ELKPLVHSPH AIVVRGALEI SQTLLGIIVR MKFLLLQQKY LEYLEDGKVL EALQVLRCEL
TPLKYNTERI HVLSGYLMCS HAEDLRAKAE WEGKGTASRS KLLDKLQTYL PPSVMLPPRR
LQTLLRQAVE LQRDRCLYHN TKLDNNLDSV SLLIDHVCSR RQFPCYTQQI LTEHCNEVWF
CKFSNDGTKL ATGSKDTTVI IWQVDPDTHL LKLLKTLEGH AYGVSYIAWS PDDNYLVACG
PDDCSELWLW NVQTGELRTK MSQSHEDSLT SVAWNPDGKR FVTGGQRGQF YQCDLDGNLL
DSWEGVRVQC LWCLSDGKTV LASDTHQRIR GYNFEDLTDR NIVQEDHPIM SFTISKNGRL
ALLNVATQGV HLWDLQDRVL VRKYQGVTQG FYTIHSCFGG HNEDFIASGS EDHKVYIWHK
RSELPIAELT GHTRTVNCVS WNPQIPSMMA SASDDGTVRI WGPAPFIDHQ NIEEECSSMD
S
