WDR62_HUMAN
ID WDR62_HUMAN Reviewed; 1518 AA.
AC O43379; Q63HP9; Q659D7; Q8NBF7; Q96AD9;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 4.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=WD repeat-containing protein 62;
GN Name=WDR62; Synonyms=C19orf14;
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 3).
RC TISSUE=Glial tumor;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 865-1518 (ISOFORM 1), AND VARIANTS LEU-1305 AND
RP PHE-1385.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS SER-850 AND
RP PHE-1385.
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 735-1518 (ISOFORM 1), AND VARIANTS SER-850; LEU-1305;
RP SER-1370 AND PHE-1385.
RC TISSUE=Muscle;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; THR-50; SER-52; SER-501;
RP THR-1053; SER-1123; SER-1228 AND THR-1268, AND IDENTIFICATION BY MASS
RP 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1248 AND SER-1249, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANTS MCPH2 MET-65; HIS-438
RP AND ASN-511, VARIANT MCPH2 THR-1078 (ISOFORM 4), AND CHARACTERIZATION OF
RP VARIANT MCPH2 HIS-438.
RX PubMed=20890279; DOI=10.1038/ng.682;
RA Nicholas A.K., Khurshid M., Desir J., Carvalho O.P., Cox J.J., Thornton G.,
RA Kausar R., Ansar M., Ahmad W., Verloes A., Passemard S., Misson J.P.,
RA Lindsay S., Gergely F., Dobyns W.B., Roberts E., Abramowicz M., Woods C.G.;
RT "WDR62 is associated with the spindle pole and is mutated in human
RT microcephaly.";
RL Nat. Genet. 42:1010-1014(2010).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND VARIANT MCPH2 MET-65.
RX PubMed=20890278; DOI=10.1038/ng.683;
RA Yu T.W., Mochida G.H., Tischfield D.J., Sgaier S.K., Flores-Sarnat L.,
RA Sergi C.M., Topcu M., McDonald M.T., Barry B.J., Felie J.M., Sunu C.,
RA Dobyns W.B., Folkerth R.D., Barkovich A.J., Walsh C.A.;
RT "Mutations in WDR62, encoding a centrosome-associated protein, cause
RT microcephaly with simplified gyri and abnormal cortical architecture.";
RL Nat. Genet. 42:1015-1020(2010).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND VARIANTS MCPH2 SER-224 AND LYS-526.
RX PubMed=20729831; DOI=10.1038/nature09327;
RA Bilguvar K., Ozturk A.K., Louvi A., Kwan K.Y., Choi M., Tatli B.,
RA Yalnizoglu D., Tuysuz B., Caglayan A.O., Gokben S., Kaymakcalan H.,
RA Barak T., Bakircioglu M., Yasuno K., Ho W., Sanders S., Zhu Y., Yilmaz S.,
RA Dincer A., Johnson M.H., Bronen R.A., Kocer N., Per H., Mane S.,
RA Pamir M.N., Yalcinkaya C., Kumandas S., Topcu M., Ozmen M., Sestan N.,
RA Lifton R.P., State M.W., Gunel M.;
RT "Whole-exome sequencing identifies recessive WDR62 mutations in severe
RT brain malformations.";
RL Nature 467:207-210(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-501; SER-1093 AND
RP SER-1101, AND IDENTIFICATION BY 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 INVOLVEMENT IN MCPH2, AND SUBCELLULAR LOCATION.
RX PubMed=21496009; DOI=10.1111/j.1399-0004.2011.01686.x;
RA Bhat V., Girimaji S.C., Mohan G., Arvinda H.R., Singhmar P., Duvvari M.R.,
RA Kumar A.;
RT "Mutations in WDR62, encoding a centrosomal and nuclear protein, in Indian
RT primary microcephaly families with cortical malformations.";
RL Clin. Genet. 80:532-540(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-46 AND SER-49, AND
RP IDENTIFICATION BY 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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP SUBUNIT, AND INTERACTION WITH MAPKBP1.
RX PubMed=23341463; DOI=10.1074/jbc.m112.422055;
RA Cohen-Katsenelson K., Wasserman T., Darlyuk-Saadon I., Rabner A.,
RA Glaser F., Aronheim A.;
RT "Identification and analysis of a novel dimerization domain shared by
RT various members of c-Jun N-terminal kinase (JNK) scaffold proteins.";
RL J. Biol. Chem. 288:7294-7304(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-49; THR-50; SER-501;
RP SER-1070; SER-1123; SER-1144 AND SER-1228, AND IDENTIFICATION BY MASS
RP 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 FUNCTION, INTERACTION WITH CDK5RAP2; CEP152; CEP63 AND KIAA0753, AND
RP SUBCELLULAR LOCATION.
RX PubMed=26297806; DOI=10.7554/elife.07519;
RA Kodani A., Yu T.W., Johnson J.R., Jayaraman D., Johnson T.L., Al-Gazali L.,
RA Sztriha L., Partlow J.N., Kim H., Krup A.L., Dammermann A., Krogan N.,
RA Walsh C.A., Reiter J.F.;
RT "Centriolar satellites assemble centrosomal microcephaly proteins to
RT recruit CDK2 and promote centriole duplication.";
RL Elife 4:0-0(2015).
RN [19]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MAPKBP1.
RX PubMed=28089251; DOI=10.1016/j.ajhg.2016.12.011;
RA Macia M.S., Halbritter J., Delous M., Bredrup C., Gutter A., Filhol E.,
RA Mellgren A.E., Leh S., Bizet A., Braun D.A., Gee H.Y., Silbermann F.,
RA Henry C., Krug P., Bole-Feysot C., Nitschke P., Joly D., Nicoud P.,
RA Paget A., Haugland H., Brackmann D., Ahmet N., Sandford R., Cengiz N.,
RA Knappskog P.M., Boman H., Linghu B., Yang F., Oakeley E.J.,
RA Saint Mezard P., Sailer A.W., Johansson S., Roedahl E., Saunier S.,
RA Hildebrandt F., Benmerah A.;
RT "Mutations in MAPKBP1 cause juvenile or late-onset cilia-independent
RT nephronophthisis.";
RL Am. J. Hum. Genet. 100:323-333(2017).
RN [20]
RP ERRATUM OF PUBMED:28089251.
RX PubMed=28157543; DOI=10.1016/j.ajhg.2017.01.025;
RA Macia M.S., Halbritter J., Delous M., Bredrup C., Gutter A., Filhol E.,
RA Mellgren A.E., Leh S., Bizet A., Braun D.A., Gee H.Y., Silbermann F.,
RA Henry C., Krug P., Bole-Feysot C., Nitschke P., Joly D., Nicoud P.,
RA Paget A., Haugland H., Brackmann D., Ahmet N., Sandford R., Cengiz N.,
RA Knappskog P.M., Boman H., Linghu B., Yang F., Oakeley E.J.,
RA Saint Mezard P., Sailer A.W., Johansson S., Roedahl E., Saunier S.,
RA Hildebrandt F., Benmerah A.;
RL Am. J. Hum. Genet. 100:372-372(2017).
CC -!- FUNCTION: Required for cerebral cortical development. Plays a role in
CC neuronal proliferation and migration (PubMed:20890278,
CC PubMed:20729831). Plays a role in mother-centriole-dependent centriole
CC duplication; the function seems also to involve CEP152, CDK5RAP2 and
CC CEP63 through a stepwise assembled complex at the centrosome that
CC recruits CDK2 required for centriole duplication (PubMed:26297806).
CC {ECO:0000269|PubMed:20729831, ECO:0000269|PubMed:20890278,
CC ECO:0000269|PubMed:26297806}.
CC -!- SUBUNIT: Can form homodimers (via C-terminus) (PubMed:23341463).
CC Interacts (via C-terminus) with MAPKBP1 (via C-terminus)
CC (PubMed:23341463, PubMed:28089251). Interacts with CDK5RAP2, CEP152,
CC CEP63 and KIAA0753 (PubMed:26297806). CEP63, CDK5RAP2, CEP152, WDR62
CC are proposed to form a stepwise assembled complex at the centrosome
CC forming a ring near parental centrioles (PubMed:26297806).
CC {ECO:0000269|PubMed:23341463, ECO:0000269|PubMed:26297806,
CC ECO:0000269|PubMed:28089251}.
CC -!- INTERACTION:
CC O43379; Q92630: DYRK2; NbExp=3; IntAct=EBI-714790, EBI-749432;
CC O43379; Q9H0I2: ENKD1; NbExp=4; IntAct=EBI-714790, EBI-744099;
CC O43379; Q2KHM9: KIAA0753; NbExp=3; IntAct=EBI-714790, EBI-2805604;
CC O43379; O15481: MAGEB4; NbExp=3; IntAct=EBI-714790, EBI-751857;
CC O43379; P45984: MAPK9; NbExp=5; IntAct=EBI-714790, EBI-713568;
CC O43379; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-714790, EBI-10181968;
CC O43379; Q9NUY8: TBC1D23; NbExp=3; IntAct=EBI-714790, EBI-2853126;
CC O43379; Q9NUY8-2: TBC1D23; NbExp=3; IntAct=EBI-714790, EBI-10314276;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20729831,
CC ECO:0000269|PubMed:21496009}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:20890278, ECO:0000269|PubMed:20890279,
CC ECO:0000269|PubMed:28089251}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:20890278,
CC ECO:0000269|PubMed:21496009, ECO:0000269|PubMed:26297806}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:26297806}. Note=Shows cell cycle-dependent
CC localization. Accumulates to the spindle pole during mitosis.
CC Colocalizes with CDK5RAP2, CEP152 and WDR62 in a discrete ring around
CC the proximal end of the parental centriole. At this site, a cohesive
CC structure is predicted to engage parental centrioles and procentrioles.
CC {ECO:0000269|PubMed:20890278, ECO:0000269|PubMed:26297806}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O43379-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43379-2; Sequence=VSP_024079, VSP_024080;
CC Name=3;
CC IsoId=O43379-3; Sequence=VSP_024077, VSP_024078;
CC Name=4;
CC IsoId=O43379-4; Sequence=VSP_039906;
CC -!- TISSUE SPECIFICITY: Present in fetal brain, enriched within the
CC ventricular and subventricular zone (at protein level). In the
CC embryonic brain it is expressed in mitotic neural precursor cells.
CC {ECO:0000269|PubMed:20890279}.
CC -!- DISEASE: Microcephaly 2, primary, autosomal recessive, with or without
CC cortical malformations (MCPH2) [MIM:604317]: A disease characterized by
CC microcephaly, moderate to severe intellectual disability, and various
CC type of cortical malformations in most patients. Microcephaly is
CC defined as a head circumference more than 3 standard deviations below
CC the age-related mean. Cortical malformations include pachygyria with
CC cortical thickening, microgyria, lissencephaly, hypoplasia of the
CC corpus callosum, schizencephaly. All affected individuals have delayed
CC psychomotor development. Some patients have seizures.
CC {ECO:0000269|PubMed:20729831, ECO:0000269|PubMed:20890278,
CC ECO:0000269|PubMed:20890279, ECO:0000269|PubMed:21496009}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC27979.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAH17261.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK090617; BAC03488.1; -; mRNA.
DR EMBL; BX647726; CAH56191.1; -; mRNA.
DR EMBL; AL133651; CAH56390.1; -; mRNA.
DR EMBL; AD000813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004144; AAC27979.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC017261; AAH17261.1; ALT_INIT; mRNA.
DR EMBL; BC058939; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS33001.1; -. [O43379-1]
DR CCDS; CCDS46059.1; -. [O43379-4]
DR PIR; T01437; T01437.
DR RefSeq; NP_001077430.1; NM_001083961.1. [O43379-4]
DR RefSeq; NP_775907.4; NM_173636.4. [O43379-1]
DR RefSeq; XP_016882154.1; XM_017026665.1. [O43379-4]
DR AlphaFoldDB; O43379; -.
DR SMR; O43379; -.
DR BioGRID; 129863; 92.
DR DIP; DIP-56792N; -.
DR IntAct; O43379; 59.
DR MINT; O43379; -.
DR STRING; 9606.ENSP00000384792; -.
DR GlyGen; O43379; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43379; -.
DR PhosphoSitePlus; O43379; -.
DR BioMuta; WDR62; -.
DR EPD; O43379; -.
DR jPOST; O43379; -.
DR MassIVE; O43379; -.
DR MaxQB; O43379; -.
DR PaxDb; O43379; -.
DR PeptideAtlas; O43379; -.
DR PRIDE; O43379; -.
DR ProteomicsDB; 48915; -. [O43379-1]
DR ProteomicsDB; 48916; -. [O43379-2]
DR ProteomicsDB; 48917; -. [O43379-3]
DR ProteomicsDB; 48918; -. [O43379-4]
DR Antibodypedia; 29678; 63 antibodies from 14 providers.
DR DNASU; 284403; -.
DR Ensembl; ENST00000270301.12; ENSP00000270301.6; ENSG00000075702.19. [O43379-1]
DR Ensembl; ENST00000378860.8; ENSP00000504870.1; ENSG00000075702.19. [O43379-3]
DR Ensembl; ENST00000401500.7; ENSP00000384792.1; ENSG00000075702.19. [O43379-4]
DR Ensembl; ENST00000587391.6; ENSP00000465525.1; ENSG00000075702.19. [O43379-2]
DR GeneID; 284403; -.
DR KEGG; hsa:284403; -.
DR MANE-Select; ENST00000401500.7; ENSP00000384792.1; NM_001083961.2; NP_001077430.1. [O43379-4]
DR UCSC; uc002odc.3; human. [O43379-1]
DR CTD; 284403; -.
DR DisGeNET; 284403; -.
DR GeneCards; WDR62; -.
DR GeneReviews; WDR62; -.
DR HGNC; HGNC:24502; WDR62.
DR HPA; ENSG00000075702; Tissue enhanced (skeletal muscle, testis, tongue).
DR MalaCards; WDR62; -.
DR MIM; 604317; phenotype.
DR MIM; 613583; gene.
DR neXtProt; NX_O43379; -.
DR OpenTargets; ENSG00000075702; -.
DR Orphanet; 2512; Autosomal recessive primary microcephaly.
DR PharmGKB; PA134963627; -.
DR VEuPathDB; HostDB:ENSG00000075702; -.
DR eggNOG; KOG1408; Eukaryota.
DR GeneTree; ENSGT00940000160719; -.
DR HOGENOM; CLU_056306_0_0_1; -.
DR InParanoid; O43379; -.
DR OMA; YHLMVSS; -.
DR OrthoDB; 1017450at2759; -.
DR PhylomeDB; O43379; -.
DR TreeFam; TF323254; -.
DR PathwayCommons; O43379; -.
DR SignaLink; O43379; -.
DR BioGRID-ORCS; 284403; 26 hits in 1082 CRISPR screens.
DR ChiTaRS; WDR62; human.
DR GeneWiki; WDR62; -.
DR GenomeRNAi; 284403; -.
DR Pharos; O43379; Tbio.
DR PRO; PR:O43379; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O43379; protein.
DR Bgee; ENSG00000075702; Expressed in left testis and 163 other tissues.
DR ExpressionAtlas; O43379; baseline and differential.
DR Genevisible; O43379; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0007099; P:centriole replication; IMP:UniProtKB.
DR GO; GO:0021987; P:cerebral cortex development; IMP:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:MGI.
DR GO; GO:0022008; P:neurogenesis; IMP:UniProtKB.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IEA:Ensembl.
DR GO; GO:2001224; P:positive regulation of neuron migration; IEA:Ensembl.
DR GO; GO:0046605; P:regulation of centrosome cycle; IEA:Ensembl.
DR GO; GO:0045664; P:regulation of neuron differentiation; IEA:Ensembl.
DR Gene3D; 2.130.10.10; -; 4.
DR InterPro; IPR024977; Apc4_WD40_dom.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM00320; WD40; 12.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Disease variant; Intellectual disability; Neurogenesis; Nucleus;
KW Phosphoprotein; Primary microcephaly; Reference proteome; Repeat;
KW WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..1518
FT /note="WD repeat-containing protein 62"
FT /id="PRO_0000281879"
FT REPEAT 109..150
FT /note="WD 1"
FT REPEAT 153..194
FT /note="WD 2"
FT REPEAT 196..234
FT /note="WD 3"
FT REPEAT 291..330
FT /note="WD 4"
FT REPEAT 357..396
FT /note="WD 5"
FT REPEAT 402..450
FT /note="WD 6"
FT REPEAT 490..529
FT /note="WD 7"
FT REPEAT 532..574
FT /note="WD 8"
FT REPEAT 578..618
FT /note="WD 9"
FT REPEAT 626..665
FT /note="WD 10"
FT REPEAT 671..713
FT /note="WD 11"
FT REPEAT 714..752
FT /note="WD 12"
FT REPEAT 803..846
FT /note="WD 13"
FT REPEAT 1132..1173
FT /note="WD 14"
FT REPEAT 1255..1293
FT /note="WD 15"
FT REGION 762..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1339..1377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1362
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 46
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 50
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 944
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U3T8"
FT MOD_RES 1053
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1070
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1093
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1268
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 412..414
FT /note="VYP -> ALS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024077"
FT VAR_SEQ 415..1518
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024078"
FT VAR_SEQ 458..483
FT /note="TLLKVVYVENDIQHLQDMSHFPDRGS -> LAPALQMCGRGHSRQPNTPSPG
FT EIAS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_024079"
FT VAR_SEQ 484..1518
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_024080"
FT VAR_SEQ 1073
FT /note="R -> RELFPA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039906"
FT VARIANT 65
FT /note="V -> M (in MCPH2; dbSNP:rs387907084)"
FT /evidence="ECO:0000269|PubMed:20890278,
FT ECO:0000269|PubMed:20890279"
FT /id="VAR_065843"
FT VARIANT 224
FT /note="W -> S (in MCPH2; dbSNP:rs267607176)"
FT /evidence="ECO:0000269|PubMed:20729831"
FT /id="VAR_063702"
FT VARIANT 289
FT /note="K -> R (in dbSNP:rs12327568)"
FT /id="VAR_055014"
FT VARIANT 438
FT /note="R -> H (in MCPH2; the mutant protein does not
FT localize to the spindle pole during mitosis;
FT dbSNP:rs387907082)"
FT /evidence="ECO:0000269|PubMed:20890279"
FT /id="VAR_065844"
FT VARIANT 511
FT /note="D -> N (in MCPH2; dbSNP:rs387907083)"
FT /evidence="ECO:0000269|PubMed:20890279"
FT /id="VAR_065845"
FT VARIANT 526
FT /note="E -> K (in MCPH2; dbSNP:rs147875659)"
FT /evidence="ECO:0000269|PubMed:20729831"
FT /id="VAR_063703"
FT VARIANT 850
FT /note="L -> S (in dbSNP:rs2285745)"
FT /evidence="ECO:0000269|PubMed:15057824,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_031299"
FT VARIANT 1305
FT /note="Q -> L (in dbSNP:rs2074435)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_055015"
FT VARIANT 1311
FT /note="Q -> E (in dbSNP:rs35811023)"
FT /id="VAR_057629"
FT VARIANT 1370
FT /note="G -> S (in dbSNP:rs17851503)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031300"
FT VARIANT 1385
FT /note="L -> F (in dbSNP:rs1008328)"
FT /evidence="ECO:0000269|PubMed:15057824,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_031301"
FT CONFLICT 370
FT /note="I -> T (in Ref. 1; BAC03488)"
FT /evidence="ECO:0000305"
FT CONFLICT 1174
FT /note="Missing (in Ref. 2; CAH56390)"
FT /evidence="ECO:0000305"
FT VARIANT O43379-4:1078
FT /note="A -> T (in MCPH2; uncertain pathological
FT significance; dbSNP:rs373781801)"
FT /evidence="ECO:0000305"
FT /id="VAR_082935"
SQ SEQUENCE 1518 AA; 165954 MW; 6E60A95B5774EF18 CRC64;
MAAVGSGGYA RNDAGEKLPS VMAGVPARRG QSSPPPAPPI CLRRRTRLST ASEETVQNRV
SLEKVLGITA QNSSGLTCDP GTGHVAYLAG CVVVILDPKE NKQQHIFNTA RKSLSALAFS
PDGKYIVTGE NGHRPAVRIW DVEEKNQVAE MLGHKYGVAC VAFSPNMKHI VSMGYQHDMV
LNVWDWKKDI VVASNKVSCR VIALSFSEDS SYFVTVGNRH VRFWFLEVST ETKVTSTVPL
VGRSGILGEL HNNIFCGVAC GRGRMAGSTF CVSYSGLLCQ FNEKRVLEKW INLKVSLSSC
LCVSQELIFC GCTDGIVRIF QAHSLHYLAN LPKPHYLGVD VAQGLEPSFL FHRKAEAVYP
DTVALTFDPI HQWLSCVYKD HSIYIWDVKD INRVGKVWSE LFHSSYVWNV EVYPEFEDQR
ACLPSGSFLT CSSDNTIRFW NLDSSPDSHW QKNIFSNTLL KVVYVENDIQ HLQDMSHFPD
RGSENGTPMD VKAGVRVMQV SPDGQHLASG DRSGNLRIHE LHFMDELVKV EAHDAEVLCL
EYSKPETGLT LLASASRDRL IHVLNVEKNY NLEQTLDDHS SSITAIKFAG NRDIQMISCG
ADKSIYFRSA QQGSDGLHFV RTHHVAEKTT LYDMDIDITQ KYVAVACQDR NVRVYNTVNG
KQKKCYKGSQ GDEGSLLKVH VDPSGTFLAT SCSDKSISVI DFYSGECIAK MFGHSEIITS
MKFTYDCHHL ITVSGDSCVF IWHLGPEITN CMKQHLLEID HRQQQQHTND KKRSGHPRQD
TYVSTPSEIH SLSPGEQTED DLEEECEPEE MLKTPSKDSL DPDPRCLLTN GKLPLWAKRL
LGDDDVADGL AFHAKRSYQP HGRWAERAGQ EPLKTILDAQ DLDCYFTPMK PESLENSILD
SLEPQSLASL LSESESPQEA GRGHPSFLPQ QKESSEASEL ILYSLEAEVT VTGTDSQYCR
KEVEAGPGDQ QGDSYLRVSS DSPKDQSPPE DSGESEADLE CSFAAIHSPA PPPDPAPRFA
TSLPHFPGCA GPTEDELSLP EGPSVPSSSL PQTPEQEKFL RHHFETLTES PCRALGDVEA
SEAEDHFFNP RLSISTQFLS SLQKASRFTH TFPPRATQCL VKSPEVKLMD RGGSQPRAGT
GYASPDRTHV LAAGKAEETL EAWRPPPPCL TSLASCVPAS SVLPTDRNLP TPTSAPTPGL
AQGVHAPSTC SYMEATASSR ARISRSISLG DSEGPIVATL AQPLRRPSSV GELASLGQEL
QAITTATTPS LDSEGQEPAL RSWGNHEARA NLRLTLSSAC DGLLQPPVDT QPGVTVPAVS
FPAPSPVEES ALRLHGSAFR PSLPAPESPG LPAHPSNPQL PEARPGIPGG TASLLEPTSG
ALGLLQGSPA RWSEPWVPVE ALPPSPLELS RVGNILHRLQ TTFQEALDLY RVLVSSGQVD
TGQQQARTEL VSTFLWIHSQ LEAECLVGTS VAPAQALPSP GPPSPPTLYP LASPDLQALL
EHYSELLVQA VRRKARGH
