GenomeNet

Database: UniProt/SWISS-PROT
Entry: WDR62_HUMAN
LinkDB: WDR62_HUMAN
Original site: 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   17-JUN-2020, entry version 167.
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=4; 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 mental retardation, and various type
CC       of cortical malformations in most patients. Microcephaly is defined as
CC       a head circumference more than 3 standard deviations below the age-
CC       related mean. Cortical malformations include pachygyria with cortical
CC       thickening, microgyria, lissencephaly, hypoplasia of the corpus
CC       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 mutations affecting the gene represented in this
CC       entry.
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};
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   BioGRID; 129863; 57.
DR   DIP; DIP-56792N; -.
DR   IntAct; O43379; 58.
DR   MINT; O43379; -.
DR   STRING; 9606.ENSP00000384792; -.
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; 52 antibodies.
DR   DNASU; 284403; -.
DR   Ensembl; ENST00000270301; ENSP00000270301; ENSG00000075702. [O43379-1]
DR   Ensembl; ENST00000401500; ENSP00000384792; ENSG00000075702. [O43379-4]
DR   Ensembl; ENST00000587391; ENSP00000465525; ENSG00000075702. [O43379-2]
DR   GeneID; 284403; -.
DR   KEGG; hsa:284403; -.
DR   UCSC; uc002odc.3; human. [O43379-1]
DR   CTD; 284403; -.
DR   DisGeNET; 284403; -.
DR   EuPathDB; HostDB:ENSG00000075702.16; -.
DR   GeneCards; WDR62; -.
DR   HGNC; HGNC:24502; WDR62.
DR   HPA; ENSG00000075702; Group enriched (skeletal muscle, testis).
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   eggNOG; KOG1408; Eukaryota.
DR   eggNOG; ENOG410Y87A; LUCA.
DR   GeneTree; ENSGT00940000160719; -.
DR   HOGENOM; CLU_056306_0_0_1; -.
DR   InParanoid; O43379; -.
DR   KO; K21762; -.
DR   OMA; HTFPPRA; -.
DR   OrthoDB; 1017450at2759; -.
DR   PhylomeDB; O43379; -.
DR   TreeFam; TF323254; -.
DR   SignaLink; O43379; -.
DR   BioGRID-ORCS; 284403; 15 hits in 789 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 right testis and 187 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: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   Gene3D; 2.130.10.10; -; 3.
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; IPR017986; WD40_repeat_dom.
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 mutation; Mental retardation; Neurogenesis; Nucleus;
KW   Phosphoprotein; Polymorphism; Primary microcephaly; Reference proteome;
KW   Repeat; WD repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000244|PubMed:19413330,
FT                   ECO:0000244|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   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000244|PubMed:19413330,
FT                   ECO:0000244|PubMed:22814378"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         46
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         50
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         52
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648"
FT   MOD_RES         501
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|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:0000244|PubMed:18669648"
FT   MOD_RES         1070
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         1093
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231"
FT   MOD_RES         1101
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:20068231"
FT   MOD_RES         1123
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         1144
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         1228
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         1248
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:19690332"
FT   MOD_RES         1249
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:19690332"
FT   MOD_RES         1268
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|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)"
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
//
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