WDR55_HUMAN
ID WDR55_HUMAN Reviewed; 383 AA.
AC Q9H6Y2; Q9NXK4;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=WD repeat-containing protein 55;
GN Name=WDR55;
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] (ISOFORMS 1 AND 2), AND VARIANT
RP ARG-151.
RC TISSUE=Colon, and Colon mucosa;
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 GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-151.
RC TISSUE=Placenta;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; THR-378 AND SER-382, AND
RP IDENTIFICATION BY 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, 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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-354, 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).
CC -!- FUNCTION: Nucleolar protein that acts as a modulator of rRNA synthesis.
CC Plays a central role during organogenesis (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H6Y2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H6Y2-2; Sequence=VSP_037275;
CC -!- SIMILARITY: Belongs to the WD repeat WDR55 family. {ECO:0000305}.
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DR EMBL; AK000202; BAA91006.1; -; mRNA.
DR EMBL; AK025355; BAB15118.1; -; mRNA.
DR EMBL; AC116353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC068485; AAH68485.1; -; mRNA.
DR CCDS; CCDS4235.1; -. [Q9H6Y2-1]
DR RefSeq; NP_060176.2; NM_017706.4. [Q9H6Y2-1]
DR RefSeq; XP_005268526.1; XM_005268469.2. [Q9H6Y2-1]
DR PDB; 7KQQ; X-ray; 1.80 A; A/B=21-334.
DR PDBsum; 7KQQ; -.
DR AlphaFoldDB; Q9H6Y2; -.
DR SMR; Q9H6Y2; -.
DR BioGRID; 120203; 91.
DR IntAct; Q9H6Y2; 27.
DR MINT; Q9H6Y2; -.
DR STRING; 9606.ENSP00000351100; -.
DR GlyGen; Q9H6Y2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H6Y2; -.
DR PhosphoSitePlus; Q9H6Y2; -.
DR BioMuta; WDR55; -.
DR DMDM; 296453035; -.
DR EPD; Q9H6Y2; -.
DR jPOST; Q9H6Y2; -.
DR MassIVE; Q9H6Y2; -.
DR MaxQB; Q9H6Y2; -.
DR PaxDb; Q9H6Y2; -.
DR PeptideAtlas; Q9H6Y2; -.
DR PRIDE; Q9H6Y2; -.
DR ProteomicsDB; 81057; -. [Q9H6Y2-1]
DR ProteomicsDB; 81058; -. [Q9H6Y2-2]
DR Antibodypedia; 45472; 34 antibodies from 15 providers.
DR DNASU; 54853; -.
DR Ensembl; ENST00000358337.10; ENSP00000351100.5; ENSG00000120314.19. [Q9H6Y2-1]
DR GeneID; 54853; -.
DR KEGG; hsa:54853; -.
DR MANE-Select; ENST00000358337.10; ENSP00000351100.5; NM_017706.5; NP_060176.3.
DR UCSC; uc003lgr.5; human. [Q9H6Y2-1]
DR CTD; 54853; -.
DR DisGeNET; 54853; -.
DR GeneCards; WDR55; -.
DR HGNC; HGNC:25971; WDR55.
DR HPA; ENSG00000120314; Low tissue specificity.
DR neXtProt; NX_Q9H6Y2; -.
DR OpenTargets; ENSG00000120314; -.
DR PharmGKB; PA142670590; -.
DR VEuPathDB; HostDB:ENSG00000120314; -.
DR eggNOG; KOG2444; Eukaryota.
DR GeneTree; ENSGT00940000153727; -.
DR HOGENOM; CLU_035848_0_1_1; -.
DR InParanoid; Q9H6Y2; -.
DR OMA; QTHHPHD; -.
DR OrthoDB; 1173229at2759; -.
DR PhylomeDB; Q9H6Y2; -.
DR TreeFam; TF315175; -.
DR PathwayCommons; Q9H6Y2; -.
DR SignaLink; Q9H6Y2; -.
DR BioGRID-ORCS; 54853; 588 hits in 1088 CRISPR screens.
DR ChiTaRS; WDR55; human.
DR GenomeRNAi; 54853; -.
DR Pharos; Q9H6Y2; Tdark.
DR PRO; PR:Q9H6Y2; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9H6Y2; protein.
DR Bgee; ENSG00000120314; Expressed in granulocyte and 160 other tissues.
DR ExpressionAtlas; Q9H6Y2; baseline and differential.
DR Genevisible; Q9H6Y2; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0006364; P:rRNA processing; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR024977; Apc4_WD40_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR017422; WDR55.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF00400; WD40; 1.
DR PIRSF; PIRSF038169; WD_repeat_p55; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; rRNA processing; WD repeat.
FT CHAIN 1..383
FT /note="WD repeat-containing protein 55"
FT /id="PRO_0000237598"
FT REPEAT 36..75
FT /note="WD 1"
FT REPEAT 82..121
FT /note="WD 2"
FT REPEAT 125..163
FT /note="WD 3"
FT REPEAT 166..205
FT /note="WD 4"
FT REPEAT 208..247
FT /note="WD 5"
FT REPEAT 250..289
FT /note="WD 6"
FT REPEAT 293..332
FT /note="WD 7"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 378
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..218
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037275"
FT VARIANT 50
FT /note="R -> C (in dbSNP:rs34342435)"
FT /id="VAR_037056"
FT VARIANT 151
FT /note="C -> R (in dbSNP:rs2530245)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_037057"
FT VARIANT 210
FT /note="S -> F (in dbSNP:rs2286394)"
FT /id="VAR_037058"
FT VARIANT 235
FT /note="Y -> C (in dbSNP:rs35983033)"
FT /id="VAR_037059"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:7KQQ"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:7KQQ"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:7KQQ"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 232..238
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 258..270
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:7KQQ"
FT TURN 281..284
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 307..314
FT /evidence="ECO:0007829|PDB:7KQQ"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:7KQQ"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:7KQQ"
FT HELIX 324..327
FT /evidence="ECO:0007829|PDB:7KQQ"
SQ SEQUENCE 383 AA; 42070 MW; 757962232E1034EB CRC64;
MDRTCEERPA EDGSDEEDPD SMEAPTRIRD TPEDIVLEAP ASGLAFHPAR DLLAAGDVDG
DVFVFSYSCQ EGETKELWSS GHHLKACRAV AFSEDGQKLI TVSKDKAIHV LDVEQGQLER
RVSKAHGAPI NSLLLVDENV LATGDDTGGI CLWDQRKEGP LMDMRQHEEY IADMALDPAK
KLLLTASGDG CLGIFNIKRR RFELLSEPQS GDLTSVTLMK WGKKVACGSS EGTIYLFNWN
GFGATSDRFA LRAESIDCMV PVTESLLCTG STDGVIRAVN ILPNRVVGSV GQHTGEPVEE
LALSHCGRFL ASSGHDQRLK FWDMAQLRAV VVDDYRRRKK KGGPLRALSS KTWSTDDFFA
GLREEGEDSM AQEEKEETGD DSD
