Full text data of WDR55
WDR55
[Confidence: low (only semi-automatic identification from reviews)]
WD repeat-containing protein 55
Note: presumably soluble (membrane word is not in UniProt keywords or features)
WD repeat-containing protein 55
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9H6Y2
ID WDR55_HUMAN Reviewed; 383 AA.
AC Q9H6Y2; Q9NXK4;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 2.
DT 22-JAN-2014, entry version 100.
DE RecName: Full=WD repeat-containing protein 55;
GN Name=WDR55;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA 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
RP 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
RT project: 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,
RP AND MASS SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Nucleolar protein that acts as a modulator of rRNA
CC synthesis. Plays a central role during organogenesis (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity).
CC Cytoplasm (By similarity).
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 Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the WD repeat WDR55 family.
CC -!- SIMILARITY: Contains 7 WD repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_060176.2; NM_017706.4.
DR RefSeq; XP_005268526.1; XM_005268469.1.
DR UniGene; Hs.286261; -.
DR ProteinModelPortal; Q9H6Y2; -.
DR SMR; Q9H6Y2; 43-323.
DR IntAct; Q9H6Y2; 2.
DR MINT; MINT-3068722; -.
DR STRING; 9606.ENSP00000351100; -.
DR PhosphoSite; Q9H6Y2; -.
DR DMDM; 296453035; -.
DR PaxDb; Q9H6Y2; -.
DR PRIDE; Q9H6Y2; -.
DR Ensembl; ENST00000358337; ENSP00000351100; ENSG00000120314.
DR GeneID; 54853; -.
DR KEGG; hsa:54853; -.
DR UCSC; uc003lgr.4; human.
DR CTD; 54853; -.
DR GeneCards; GC05P140044; -.
DR HGNC; HGNC:25971; WDR55.
DR HPA; HPA043470; -.
DR HPA; HPA048143; -.
DR neXtProt; NX_Q9H6Y2; -.
DR PharmGKB; PA142670590; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000242496; -.
DR HOVERGEN; HBG054778; -.
DR InParanoid; Q9H6Y2; -.
DR OMA; IFNWNGF; -.
DR PhylomeDB; Q9H6Y2; -.
DR SignaLink; Q9H6Y2; -.
DR ChiTaRS; WDR55; human.
DR GenomeRNAi; 54853; -.
DR NextBio; 57710; -.
DR PRO; PR:Q9H6Y2; -.
DR ArrayExpress; Q9H6Y2; -.
DR Bgee; Q9H6Y2; -.
DR CleanEx; HS_WDR55; -.
DR Genevestigator; Q9H6Y2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR InterPro; IPR017422; WD_repeat_p55.
DR Pfam; PF00400; WD40; 4.
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 Alternative splicing; Complete proteome; Cytoplasm; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW rRNA processing; WD repeat.
FT CHAIN 1 383 WD repeat-containing protein 55.
FT /FTId=PRO_0000237598.
FT REPEAT 36 75 WD 1.
FT REPEAT 82 121 WD 2.
FT REPEAT 125 163 WD 3.
FT REPEAT 166 205 WD 4.
FT REPEAT 208 247 WD 5.
FT REPEAT 250 289 WD 6.
FT REPEAT 293 332 WD 7.
FT MOD_RES 14 14 Phosphoserine.
FT MOD_RES 378 378 Phosphothreonine.
FT MOD_RES 382 382 Phosphoserine.
FT VAR_SEQ 1 218 Missing (in isoform 2).
FT /FTId=VSP_037275.
FT VARIANT 50 50 R -> C (in dbSNP:rs34342435).
FT /FTId=VAR_037056.
FT VARIANT 151 151 C -> R (in dbSNP:rs2530245).
FT /FTId=VAR_037057.
FT VARIANT 210 210 S -> F (in dbSNP:rs2286394).
FT /FTId=VAR_037058.
FT VARIANT 235 235 Y -> C (in dbSNP:rs35983033).
FT /FTId=VAR_037059.
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
//
ID WDR55_HUMAN Reviewed; 383 AA.
AC Q9H6Y2; Q9NXK4;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 2.
DT 22-JAN-2014, entry version 100.
DE RecName: Full=WD repeat-containing protein 55;
GN Name=WDR55;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA 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
RP 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
RT project: 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,
RP AND MASS SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Nucleolar protein that acts as a modulator of rRNA
CC synthesis. Plays a central role during organogenesis (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity).
CC Cytoplasm (By similarity).
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 Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the WD repeat WDR55 family.
CC -!- SIMILARITY: Contains 7 WD repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_060176.2; NM_017706.4.
DR RefSeq; XP_005268526.1; XM_005268469.1.
DR UniGene; Hs.286261; -.
DR ProteinModelPortal; Q9H6Y2; -.
DR SMR; Q9H6Y2; 43-323.
DR IntAct; Q9H6Y2; 2.
DR MINT; MINT-3068722; -.
DR STRING; 9606.ENSP00000351100; -.
DR PhosphoSite; Q9H6Y2; -.
DR DMDM; 296453035; -.
DR PaxDb; Q9H6Y2; -.
DR PRIDE; Q9H6Y2; -.
DR Ensembl; ENST00000358337; ENSP00000351100; ENSG00000120314.
DR GeneID; 54853; -.
DR KEGG; hsa:54853; -.
DR UCSC; uc003lgr.4; human.
DR CTD; 54853; -.
DR GeneCards; GC05P140044; -.
DR HGNC; HGNC:25971; WDR55.
DR HPA; HPA043470; -.
DR HPA; HPA048143; -.
DR neXtProt; NX_Q9H6Y2; -.
DR PharmGKB; PA142670590; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000242496; -.
DR HOVERGEN; HBG054778; -.
DR InParanoid; Q9H6Y2; -.
DR OMA; IFNWNGF; -.
DR PhylomeDB; Q9H6Y2; -.
DR SignaLink; Q9H6Y2; -.
DR ChiTaRS; WDR55; human.
DR GenomeRNAi; 54853; -.
DR NextBio; 57710; -.
DR PRO; PR:Q9H6Y2; -.
DR ArrayExpress; Q9H6Y2; -.
DR Bgee; Q9H6Y2; -.
DR CleanEx; HS_WDR55; -.
DR Genevestigator; Q9H6Y2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR InterPro; IPR017422; WD_repeat_p55.
DR Pfam; PF00400; WD40; 4.
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 Alternative splicing; Complete proteome; Cytoplasm; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat;
KW rRNA processing; WD repeat.
FT CHAIN 1 383 WD repeat-containing protein 55.
FT /FTId=PRO_0000237598.
FT REPEAT 36 75 WD 1.
FT REPEAT 82 121 WD 2.
FT REPEAT 125 163 WD 3.
FT REPEAT 166 205 WD 4.
FT REPEAT 208 247 WD 5.
FT REPEAT 250 289 WD 6.
FT REPEAT 293 332 WD 7.
FT MOD_RES 14 14 Phosphoserine.
FT MOD_RES 378 378 Phosphothreonine.
FT MOD_RES 382 382 Phosphoserine.
FT VAR_SEQ 1 218 Missing (in isoform 2).
FT /FTId=VSP_037275.
FT VARIANT 50 50 R -> C (in dbSNP:rs34342435).
FT /FTId=VAR_037056.
FT VARIANT 151 151 C -> R (in dbSNP:rs2530245).
FT /FTId=VAR_037057.
FT VARIANT 210 210 S -> F (in dbSNP:rs2286394).
FT /FTId=VAR_037058.
FT VARIANT 235 235 Y -> C (in dbSNP:rs35983033).
FT /FTId=VAR_037059.
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
//