Full text data of WDR26
WDR26
(CDW2, MIP2)
[Confidence: low (only semi-automatic identification from reviews)]
WD repeat-containing protein 26 (CUL4- and DDB1-associated WDR protein 2; Myocardial ischemic preconditioning up-regulated protein 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
WD repeat-containing protein 26 (CUL4- and DDB1-associated WDR protein 2; Myocardial ischemic preconditioning up-regulated protein 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9H7D7
ID WDR26_HUMAN Reviewed; 661 AA.
AC Q9H7D7; A0MNN3; Q4G100; Q59EC4; Q5GLZ9; Q86UY4; Q9H3C2;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 20-MAR-2007, sequence version 3.
DT 22-JAN-2014, entry version 109.
DE RecName: Full=WD repeat-containing protein 26;
DE AltName: Full=CUL4- and DDB1-associated WDR protein 2;
DE AltName: Full=Myocardial ischemic preconditioning up-regulated protein 2;
GN Name=WDR26; Synonyms=CDW2, MIP2; ORFNames=PRO0852;
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] (ISOFORM 1).
RC TISSUE=Endothelial cell;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-661 (ISOFORM 3), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 138-661 (ISOFORM 1).
RC TISSUE=Lung, Testis, and Uterus;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 25-661 (ISOFORM 2).
RA Yuan C., Xiao X., Zhang H.;
RT "Human myocardial ischemic preconditioning upregulated gene 2.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 84-661 (ISOFORM 1), TISSUE SPECIFICITY,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Heart;
RX PubMed=15378603; DOI=10.1002/jcb.20175;
RA Zhu Y., Wang Y., Xia C., Li D., Li Y., Zeng W., Yuan W., Liu H.,
RA Zhu C., Wu X., Liu M.;
RT "WDR26: a novel Gbeta-like protein, suppresses MAPK signaling
RT pathway.";
RL J. Cell. Biochem. 93:579-587(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 86-661 (ISOFORM 4).
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y.,
RA Xu W., Gao F., Liu M., He F.;
RT "Functional prediction of the coding sequences of 75 new genes deduced
RT by analysis of cDNA clones from human fetal liver.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 138-661 (ISOFORM 1), INTERACTION WITH
RP CUL4, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17041588; DOI=10.1038/ncb1490;
RA Higa L.A., Wu M., Ye T., Kobayashi R., Sun H., Zhang H.;
RT "CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat
RT proteins and regulates histone methylation.";
RL Nat. Cell Biol. 8:1277-1283(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 265-661 (ISOFORM 1).
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND MASS
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND MASS
RP SPECTROMETRY.
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: May be involved in MAPK pathways.
CC -!- SUBUNIT: Interacts with DDB1-CUL4A/B E3 ligase complexes.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9H7D7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H7D7-2; Sequence=VSP_023895;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9H7D7-3; Sequence=VSP_023896, VSP_023898;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q9H7D7-4; Sequence=VSP_023897, VSP_023899;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in
CC heart and skeletal muscle.
CC -!- SIMILARITY: Contains 1 CTLH domain.
CC -!- SIMILARITY: Contains 1 LisH domain.
CC -!- SIMILARITY: Contains 6 WD repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG35477.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH52301.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH63817.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAO67709.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAQ74770.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=ABK41102.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB14955.1; Type=Erroneous termination; Positions=274; Note=Translated as Lys;
CC Sequence=BAD93124.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; AB209887; BAD93124.1; ALT_INIT; mRNA.
DR EMBL; AC099790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031471; AAH31471.2; -; mRNA.
DR EMBL; BC034498; AAH34498.1; -; mRNA.
DR EMBL; BC052301; AAH52301.2; ALT_INIT; mRNA.
DR EMBL; BC063817; AAH63817.2; ALT_INIT; mRNA.
DR EMBL; AY221751; AAO67709.1; ALT_INIT; mRNA.
DR EMBL; AY304473; AAQ74770.1; ALT_INIT; mRNA.
DR EMBL; AF130049; AAG35477.1; ALT_INIT; mRNA.
DR EMBL; EF011612; ABK41102.1; ALT_INIT; mRNA.
DR EMBL; AK024669; BAB14955.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001108585.2; NM_001115113.2.
DR RefSeq; NP_079436.4; NM_025160.6.
DR UniGene; Hs.497873; -.
DR UniGene; Hs.729289; -.
DR ProteinModelPortal; Q9H7D7; -.
DR SMR; Q9H7D7; 351-641.
DR IntAct; Q9H7D7; 11.
DR MINT; MINT-4830971; -.
DR STRING; 9606.ENSP00000295024; -.
DR PhosphoSite; Q9H7D7; -.
DR DMDM; 134047967; -.
DR PaxDb; Q9H7D7; -.
DR PRIDE; Q9H7D7; -.
DR Ensembl; ENST00000295024; ENSP00000295024; ENSG00000162923.
DR Ensembl; ENST00000366852; ENSP00000355817; ENSG00000162923.
DR Ensembl; ENST00000414423; ENSP00000408108; ENSG00000162923.
DR GeneID; 80232; -.
DR KEGG; hsa:80232; -.
DR UCSC; uc001hop.4; human.
DR CTD; 80232; -.
DR GeneCards; GC01M224573; -.
DR HGNC; HGNC:21208; WDR26.
DR HPA; HPA028539; -.
DR neXtProt; NX_Q9H7D7; -.
DR PharmGKB; PA134907873; -.
DR eggNOG; COG2319; -.
DR HOVERGEN; HBG083958; -.
DR InParanoid; Q9H7D7; -.
DR OMA; LLMCPPE; -.
DR OrthoDB; EOG73FQMM; -.
DR SignaLink; Q9H7D7; -.
DR ChiTaRS; WDR26; human.
DR GeneWiki; WDR26; -.
DR GenomeRNAi; 80232; -.
DR NextBio; 70673; -.
DR PRO; PR:Q9H7D7; -.
DR ArrayExpress; Q9H7D7; -.
DR Bgee; Q9H7D7; -.
DR CleanEx; HS_WDR26; -.
DR Genevestigator; Q9H7D7; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR006594; LisH_dimerisation.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00668; CTLH; 1.
DR SMART; SM00667; LisH; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm; Phosphoprotein;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1 661 WD repeat-containing protein 26.
FT /FTId=PRO_0000051373.
FT DOMAIN 123 155 LisH.
FT DOMAIN 156 231 CTLH.
FT REPEAT 353 392 WD 1.
FT REPEAT 399 438 WD 2.
FT REPEAT 444 484 WD 3.
FT REPEAT 524 563 WD 4.
FT REPEAT 566 608 WD 5.
FT REPEAT 611 651 WD 6.
FT MOD_RES 121 121 Phosphoserine.
FT VAR_SEQ 192 207 Missing (in isoform 2).
FT /FTId=VSP_023895.
FT VAR_SEQ 194 216 VRGALEISQTLLGIIVRMKFLLL -> AQTFSETSINFFPL
FT TAAFCHVRG (in isoform 3).
FT /FTId=VSP_023896.
FT VAR_SEQ 210 223 RMKFLLLQQKYLEY -> VNTLLFLVSHLCLF (in
FT isoform 4).
FT /FTId=VSP_023897.
FT VAR_SEQ 217 661 Missing (in isoform 3).
FT /FTId=VSP_023898.
FT VAR_SEQ 224 661 Missing (in isoform 4).
FT /FTId=VSP_023899.
FT CONFLICT 8 8 G -> A (in Ref. 3; AAH34498).
SQ SEQUENCE 661 AA; 72124 MW; E0B8AAFF44CB7DF7 CRC64;
MQANGAGGGG GGGGGGGGGG GGGGGQGQTP ELACLSAQNG ESSPSSSSSA GDLAHANGLL
PSAPSAASNN SNSLNVNNGV PGGAAAASSA TVAAASATTA ASSSLATPEL GSSLKKKKRL
SQSDEDVIRL IGQHLNGLGL NQTVDLLMQE SGCRLEHPSA TKFRNHVMEG DWDKAENDLN
ELKPLVHSPH AIVVRGALEI SQTLLGIIVR MKFLLLQQKY LEYLEDGKVL EALQVLRCEL
TPLKYNTERI HVLSGYLMCS HAEDLRAKAE WEGKGTASRS KLLDKLQTYL PPSVMLPPRR
LQTLLRQAVE LQRDRCLYHN TKLDNNLDSV SLLIDHVCSR RQFPCYTQQI LTEHCNEVWF
CKFSNDGTKL ATGSKDTTVI IWQVDPDTHL LKLLKTLEGH AYGVSYIAWS PDDNYLVACG
PDDCSELWLW NVQTGELRTK MSQSHEDSLT SVAWNPDGKR FVTGGQRGQF YQCDLDGNLL
DSWEGVRVQC LWCLSDGKTV LASDTHQRIR GYNFEDLTDR NIVQEDHPIM SFTISKNGRL
ALLNVATQGV HLWDLQDRVL VRKYQGVTQG FYTIHSCFGG HNEDFIASGS EDHKVYIWHK
RSELPIAELT GHTRTVNCVS WNPQIPSMMA SASDDGTVRI WGPAPFIDHQ NIEEECSSMD
S
//
ID WDR26_HUMAN Reviewed; 661 AA.
AC Q9H7D7; A0MNN3; Q4G100; Q59EC4; Q5GLZ9; Q86UY4; Q9H3C2;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 20-MAR-2007, sequence version 3.
DT 22-JAN-2014, entry version 109.
DE RecName: Full=WD repeat-containing protein 26;
DE AltName: Full=CUL4- and DDB1-associated WDR protein 2;
DE AltName: Full=Myocardial ischemic preconditioning up-regulated protein 2;
GN Name=WDR26; Synonyms=CDW2, MIP2; ORFNames=PRO0852;
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] (ISOFORM 1).
RC TISSUE=Endothelial cell;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-661 (ISOFORM 3), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 138-661 (ISOFORM 1).
RC TISSUE=Lung, Testis, and Uterus;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 25-661 (ISOFORM 2).
RA Yuan C., Xiao X., Zhang H.;
RT "Human myocardial ischemic preconditioning upregulated gene 2.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 84-661 (ISOFORM 1), TISSUE SPECIFICITY,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Heart;
RX PubMed=15378603; DOI=10.1002/jcb.20175;
RA Zhu Y., Wang Y., Xia C., Li D., Li Y., Zeng W., Yuan W., Liu H.,
RA Zhu C., Wu X., Liu M.;
RT "WDR26: a novel Gbeta-like protein, suppresses MAPK signaling
RT pathway.";
RL J. Cell. Biochem. 93:579-587(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 86-661 (ISOFORM 4).
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Bi J., Zhou G., Dong C., Zai Y.,
RA Xu W., Gao F., Liu M., He F.;
RT "Functional prediction of the coding sequences of 75 new genes deduced
RT by analysis of cDNA clones from human fetal liver.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 138-661 (ISOFORM 1), INTERACTION WITH
RP CUL4, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17041588; DOI=10.1038/ncb1490;
RA Higa L.A., Wu M., Ye T., Kobayashi R., Sun H., Zhang H.;
RT "CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat
RT proteins and regulates histone methylation.";
RL Nat. Cell Biol. 8:1277-1283(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 265-661 (ISOFORM 1).
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND MASS
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND MASS
RP SPECTROMETRY.
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: May be involved in MAPK pathways.
CC -!- SUBUNIT: Interacts with DDB1-CUL4A/B E3 ligase complexes.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9H7D7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H7D7-2; Sequence=VSP_023895;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9H7D7-3; Sequence=VSP_023896, VSP_023898;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q9H7D7-4; Sequence=VSP_023897, VSP_023899;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in
CC heart and skeletal muscle.
CC -!- SIMILARITY: Contains 1 CTLH domain.
CC -!- SIMILARITY: Contains 1 LisH domain.
CC -!- SIMILARITY: Contains 6 WD repeats.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG35477.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH52301.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH63817.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAO67709.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAQ74770.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=ABK41102.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=BAB14955.1; Type=Erroneous termination; Positions=274; Note=Translated as Lys;
CC Sequence=BAD93124.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; AB209887; BAD93124.1; ALT_INIT; mRNA.
DR EMBL; AC099790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031471; AAH31471.2; -; mRNA.
DR EMBL; BC034498; AAH34498.1; -; mRNA.
DR EMBL; BC052301; AAH52301.2; ALT_INIT; mRNA.
DR EMBL; BC063817; AAH63817.2; ALT_INIT; mRNA.
DR EMBL; AY221751; AAO67709.1; ALT_INIT; mRNA.
DR EMBL; AY304473; AAQ74770.1; ALT_INIT; mRNA.
DR EMBL; AF130049; AAG35477.1; ALT_INIT; mRNA.
DR EMBL; EF011612; ABK41102.1; ALT_INIT; mRNA.
DR EMBL; AK024669; BAB14955.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001108585.2; NM_001115113.2.
DR RefSeq; NP_079436.4; NM_025160.6.
DR UniGene; Hs.497873; -.
DR UniGene; Hs.729289; -.
DR ProteinModelPortal; Q9H7D7; -.
DR SMR; Q9H7D7; 351-641.
DR IntAct; Q9H7D7; 11.
DR MINT; MINT-4830971; -.
DR STRING; 9606.ENSP00000295024; -.
DR PhosphoSite; Q9H7D7; -.
DR DMDM; 134047967; -.
DR PaxDb; Q9H7D7; -.
DR PRIDE; Q9H7D7; -.
DR Ensembl; ENST00000295024; ENSP00000295024; ENSG00000162923.
DR Ensembl; ENST00000366852; ENSP00000355817; ENSG00000162923.
DR Ensembl; ENST00000414423; ENSP00000408108; ENSG00000162923.
DR GeneID; 80232; -.
DR KEGG; hsa:80232; -.
DR UCSC; uc001hop.4; human.
DR CTD; 80232; -.
DR GeneCards; GC01M224573; -.
DR HGNC; HGNC:21208; WDR26.
DR HPA; HPA028539; -.
DR neXtProt; NX_Q9H7D7; -.
DR PharmGKB; PA134907873; -.
DR eggNOG; COG2319; -.
DR HOVERGEN; HBG083958; -.
DR InParanoid; Q9H7D7; -.
DR OMA; LLMCPPE; -.
DR OrthoDB; EOG73FQMM; -.
DR SignaLink; Q9H7D7; -.
DR ChiTaRS; WDR26; human.
DR GeneWiki; WDR26; -.
DR GenomeRNAi; 80232; -.
DR NextBio; 70673; -.
DR PRO; PR:Q9H7D7; -.
DR ArrayExpress; Q9H7D7; -.
DR Bgee; Q9H7D7; -.
DR CleanEx; HS_WDR26; -.
DR Genevestigator; Q9H7D7; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR006594; LisH_dimerisation.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00668; CTLH; 1.
DR SMART; SM00667; LisH; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm; Phosphoprotein;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1 661 WD repeat-containing protein 26.
FT /FTId=PRO_0000051373.
FT DOMAIN 123 155 LisH.
FT DOMAIN 156 231 CTLH.
FT REPEAT 353 392 WD 1.
FT REPEAT 399 438 WD 2.
FT REPEAT 444 484 WD 3.
FT REPEAT 524 563 WD 4.
FT REPEAT 566 608 WD 5.
FT REPEAT 611 651 WD 6.
FT MOD_RES 121 121 Phosphoserine.
FT VAR_SEQ 192 207 Missing (in isoform 2).
FT /FTId=VSP_023895.
FT VAR_SEQ 194 216 VRGALEISQTLLGIIVRMKFLLL -> AQTFSETSINFFPL
FT TAAFCHVRG (in isoform 3).
FT /FTId=VSP_023896.
FT VAR_SEQ 210 223 RMKFLLLQQKYLEY -> VNTLLFLVSHLCLF (in
FT isoform 4).
FT /FTId=VSP_023897.
FT VAR_SEQ 217 661 Missing (in isoform 3).
FT /FTId=VSP_023898.
FT VAR_SEQ 224 661 Missing (in isoform 4).
FT /FTId=VSP_023899.
FT CONFLICT 8 8 G -> A (in Ref. 3; AAH34498).
SQ SEQUENCE 661 AA; 72124 MW; E0B8AAFF44CB7DF7 CRC64;
MQANGAGGGG GGGGGGGGGG GGGGGQGQTP ELACLSAQNG ESSPSSSSSA GDLAHANGLL
PSAPSAASNN SNSLNVNNGV PGGAAAASSA TVAAASATTA ASSSLATPEL GSSLKKKKRL
SQSDEDVIRL IGQHLNGLGL NQTVDLLMQE SGCRLEHPSA TKFRNHVMEG DWDKAENDLN
ELKPLVHSPH AIVVRGALEI SQTLLGIIVR MKFLLLQQKY LEYLEDGKVL EALQVLRCEL
TPLKYNTERI HVLSGYLMCS HAEDLRAKAE WEGKGTASRS KLLDKLQTYL PPSVMLPPRR
LQTLLRQAVE LQRDRCLYHN TKLDNNLDSV SLLIDHVCSR RQFPCYTQQI LTEHCNEVWF
CKFSNDGTKL ATGSKDTTVI IWQVDPDTHL LKLLKTLEGH AYGVSYIAWS PDDNYLVACG
PDDCSELWLW NVQTGELRTK MSQSHEDSLT SVAWNPDGKR FVTGGQRGQF YQCDLDGNLL
DSWEGVRVQC LWCLSDGKTV LASDTHQRIR GYNFEDLTDR NIVQEDHPIM SFTISKNGRL
ALLNVATQGV HLWDLQDRVL VRKYQGVTQG FYTIHSCFGG HNEDFIASGS EDHKVYIWHK
RSELPIAELT GHTRTVNCVS WNPQIPSMMA SASDDGTVRI WGPAPFIDHQ NIEEECSSMD
S
//