WDR62_MOUSE
ID WDR62_MOUSE Reviewed; 1523 AA.
AC Q3U3T8; Q6PGG0; Q7TQE9;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=WD repeat-containing protein 62;
GN Name=Wdr62;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 446-1523 (ISOFORM 3).
RC STRAIN=C57BL/6J; 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-966; SER-972 AND
RP SER-1143, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Required for cerebral cortical development. Plays a role in
CC neuronal proliferation and migration (By similarity). Plays a role in
CC mother-centriole-dependent centriole duplication; the function seems
CC also to involve CEP152, CDK5RAP2 and CEP63 through a stepwise assembled
CC complex at the centrosome that recruits CDK2 required for centriole
CC duplication (By similarity). {ECO:0000250|UniProtKB:O43379}.
CC -!- SUBUNIT: Can form homodimers (via C-terminus). Interacts (via C-
CC terminus) with MAPKBP1 (via C-terminus). Interacts with CDK5RAP2,
CC CEP152, CEP63 and KIAA0753. CEP63, CDK5RAP2, CEP152, WDR62 are proposed
CC to form a stepwise assembled complex at the centrosome forming a ring
CC near parental centrioles. {ECO:0000250|UniProtKB:O43379}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43379}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:O43379}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:O43379}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:O43379}. Note=Shows cell cycle-dependent
CC localization. Accumulates to the spindle pole during mitosis (By
CC similarity). Colocalizes with CDK5RAP2, CEP152 and WDR62 in a discrete
CC ring around the proximal end of the parental centriole. At this site, a
CC cohesive structure is predicted to engage parental centrioles and
CC procentrioles (By similarity). {ECO:0000250|UniProtKB:O43379}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3U3T8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U3T8-2; Sequence=VSP_024082, VSP_024084;
CC Name=3;
CC IsoId=Q3U3T8-3; Sequence=VSP_024081, VSP_024083;
CC -!- TISSUE SPECIFICITY: Prominent in neural crest lineages from 9.5 dpc to
CC 11.5 dpc. Also expressed in the ventricular and subventricular zones
CC during the period of cerebral cortical neurogenesis (11.5-16.5 dpc),
CC with expression decreasing in intensity by 17.5 dpc. In the cerebellum,
CC it is strongly expressed in precursors of granule neurons at late
CC embryonic and early postnatal stages; by postnatal day 9 (P9). Present
CC in fetal brain, enriched within the ventricular and subventricular zone
CC (at protein level). {ECO:0000269|PubMed:20729831}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH57041.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE32697.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK154592; BAE32697.1; ALT_INIT; mRNA.
DR EMBL; BC054747; AAH54747.1; -; mRNA.
DR EMBL; BC057041; AAH57041.1; ALT_INIT; mRNA.
DR CCDS; CCDS52178.1; -. [Q3U3T8-1]
DR AlphaFoldDB; Q3U3T8; -.
DR SMR; Q3U3T8; -.
DR IntAct; Q3U3T8; 3.
DR MINT; Q3U3T8; -.
DR STRING; 10090.ENSMUSP00000103825; -.
DR iPTMnet; Q3U3T8; -.
DR PhosphoSitePlus; Q3U3T8; -.
DR EPD; Q3U3T8; -.
DR jPOST; Q3U3T8; -.
DR MaxQB; Q3U3T8; -.
DR PaxDb; Q3U3T8; -.
DR PRIDE; Q3U3T8; -.
DR ProteomicsDB; 299746; -. [Q3U3T8-1]
DR ProteomicsDB; 299747; -. [Q3U3T8-2]
DR ProteomicsDB; 299748; -. [Q3U3T8-3]
DR MGI; MGI:1923696; Wdr62.
DR eggNOG; KOG1408; Eukaryota.
DR InParanoid; Q3U3T8; -.
DR PhylomeDB; Q3U3T8; -.
DR ChiTaRS; Wdr62; mouse.
DR PRO; PR:Q3U3T8; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3U3T8; protein.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISO:MGI.
DR GO; GO:0007099; P:centriole replication; ISO:MGI.
DR GO; GO:0021987; P:cerebral cortex development; ISS:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; ISO:MGI.
DR GO; GO:0022008; P:neurogenesis; ISO:MGI.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; ISO:MGI.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISO:MGI.
DR GO; GO:2001224; P:positive regulation of neuron migration; ISO:MGI.
DR GO; GO:0046605; P:regulation of centrosome cycle; ISO:MGI.
DR GO; GO:0045664; P:regulation of neuron differentiation; ISO:MGI.
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 Pfam; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM00320; WD40; 12.
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; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O43379"
FT CHAIN 2..1523
FT /note="WD repeat-containing protein 62"
FT /id="PRO_0000281880"
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 411..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 REGION 762..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O43379"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 46
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43379"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43379"
FT MOD_RES 966
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 972
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1072
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43379"
FT MOD_RES 1117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43379"
FT MOD_RES 1143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43379"
FT MOD_RES 1234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43379"
FT VAR_SEQ 913..934
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024081"
FT VAR_SEQ 1046..1075
FT /note="GKPEYPSTEELSQPELPGLGNGSLPQTPEQ -> ASSAVTQSADKSSPPCLP
FT SRVPKYRRAFPA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024082"
FT VAR_SEQ 1046..1048
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024083"
FT VAR_SEQ 1076..1523
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024084"
FT CONFLICT 136
FT /note="T -> A (in Ref. 2; AAH54747)"
FT /evidence="ECO:0000305"
FT CONFLICT 647
FT /note="C -> F (in Ref. 2; AAH57041)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1523 AA; 167283 MW; 28F92D7F102F9D08 CRC64;
MAALAAGGYT RSDTIEKLSS VMAGVPARRN QSSPPPAPPL CLRRRTRLAA APEDTVQNRV
TLEKVLGITA QNSSGLTCDP GTGHVAYLAG CVVVVLNPKE NKQQHIFNTT RKSLSALAFS
PDGKYIVTGE NGHRPTVRIW DVEEKTQVAE MLGHKYGVAC VAFSPNMKHI VSMGYQHDMV
LNVWDWKKDI VVASNKVSCR VIALSFSEDS SYFVTVGNRH VRFWFLEAST EAKVTSTVPL
VGRSGILGEL HNNIFCGVAC GRGRMAGNTF CVSYSGLLCQ FNEKRVLDKW INLKVSLSSC
LCVSDELIFC GCTDGIVRIF QAHSLLYLTN LPKPHYLGVD VAHGLDSSFL FHRKAEAVYP
DTVALTFDPV HQWLSCVYKD HSIYIWDVKD IDEVSKIWSE LFHSSFVWNV EVYPEFEDQR
ACLPSGTFLT CSSDNTIRFW NLDSASDTRW QKNIFSDSLL KVVYVENDIQ HLQDLSHFPD
RGSENGTPMD MKAGVRVMQV SPDGQHLASG DRSGNLRIHE LHFMDELIKV EAHDAEVLCL
EYSKPETGVT LLASASRDRL IHVLNVEKNY NLEQTLDDHS SSITAIKFAG TRDVQMISCG
ADKSIYFRSA QQASDGLHFV RTHHVAEKTT LYDMDIDITQ KYVAVACQDR NVRVYNTVSG
KQKKCYKGSQ GDEGSLLKVH VDPSGTFLAT SCSDKSISLI DFYSGECVAK MFGHSEIVTG
MKFTYDCRHL ITVSGDSCVF IWHLGPEITT CMKQHLLEIN HQEQQQQPKD QKWSGPPSQE
TYASTPSEIR SLSPGEQTED EMEEECEPEE LLKTPSKDSL DPDPRCLLTN GKLPLWAKRL
LGDDDVADSS AFHAKRSYQP HGRWAERAEQ EPLKTILDAW SLDSYFTPMK PENLQDSVLD
SVEPQNLAGL LSECSLGNGH TSPGEGLVSY LLHPELGSPK EDNRGHPSYL PLQREATEAS
ELILCSPEAE VSLTGMHREY YEEETEAGPE DQQGDTYLRV SSVSSKDQSP PEDSGESEAE
LECSFAAAHS SAPQTDPGPH LTMTAGKPEY PSTEELSQPE LPGLGNGSLP QTPEQEKFLR
HHFETLTDAP TEELFHGSLG DIKISETEDY FFNPRLSIST QFLSRLQKTS RCPPRLPLHL
MKSPEAQPVG QGGNQPKAGP LRAGTGYMSS DGTNVLSGQK AEETQEALSL LDRKPPTPTS
VLTTGREQSI SAPSSCSYLE STTSSHAKTT RSISLGDSEG PVTAELPQSL HKPLSPGQEL
QAIPTTVALT SSIKDHEPAP LSWGNHEARA SLKLTLSSVC EQLLSPPPQE PPITHVWSQE
PVDVPPSMAV TVASFCAPSP VDMSTLGLHS SMFLPKTSAS GPLTPPAHLQ LLETRSRVPG
STAALLEPTP DASGVIADSP GHWDTEVPTP ELLGSVESVL HRLQTAFQEA LDLYRMLVSS
SQLGPEQQQA QTELASTFHW ILNQLEASNC MAAANLAPPQ TLPSPDPLSL PTLCPLASPN
LQALLEHYSE LLVQAVRRKA RGD
