WDR70_HUMAN
ID WDR70_HUMAN Reviewed; 654 AA.
AC Q9NW82; Q9H053;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=WD repeat-containing protein 70;
GN Name=WDR70;
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].
RC TISSUE=Embryo;
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].
RC TISSUE=Brain;
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 MRNA].
RC TISSUE=Brain, and 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-638, AND IDENTIFICATION BY
RP 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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-638, 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-452, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-638, 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 [10]
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., Buerckstuemmer T.,
RA 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-638, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-579; SER-621 AND SER-638, 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).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-296, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-590 AND LYS-596, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- SIMILARITY: Belongs to the WD repeat GAD-1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC21644.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK001095; BAA91502.1; -; mRNA.
DR EMBL; AL512685; CAC21644.1; ALT_INIT; mRNA.
DR EMBL; BC009648; AAH09648.1; -; mRNA.
DR EMBL; BC025315; AAH25315.1; -; mRNA.
DR CCDS; CCDS34147.1; -.
DR RefSeq; NP_060504.1; NM_018034.3.
DR PDB; 6ZYM; EM; 3.40 A; p=1-654.
DR PDB; 7A5P; EM; 5.00 A; p=1-654.
DR PDBsum; 6ZYM; -.
DR PDBsum; 7A5P; -.
DR AlphaFoldDB; Q9NW82; -.
DR SMR; Q9NW82; -.
DR BioGRID; 120410; 63.
DR IntAct; Q9NW82; 14.
DR MINT; Q9NW82; -.
DR STRING; 9606.ENSP00000265107; -.
DR GlyGen; Q9NW82; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NW82; -.
DR PhosphoSitePlus; Q9NW82; -.
DR BioMuta; WDR70; -.
DR DMDM; 74761752; -.
DR EPD; Q9NW82; -.
DR jPOST; Q9NW82; -.
DR MassIVE; Q9NW82; -.
DR MaxQB; Q9NW82; -.
DR PaxDb; Q9NW82; -.
DR PeptideAtlas; Q9NW82; -.
DR PRIDE; Q9NW82; -.
DR ProteomicsDB; 82913; -.
DR Antibodypedia; 23003; 33 antibodies from 13 providers.
DR DNASU; 55100; -.
DR Ensembl; ENST00000265107.9; ENSP00000265107.4; ENSG00000082068.9.
DR GeneID; 55100; -.
DR KEGG; hsa:55100; -.
DR MANE-Select; ENST00000265107.9; ENSP00000265107.4; NM_018034.4; NP_060504.1.
DR UCSC; uc003jkv.4; human.
DR CTD; 55100; -.
DR DisGeNET; 55100; -.
DR GeneCards; WDR70; -.
DR HGNC; HGNC:25495; WDR70.
DR HPA; ENSG00000082068; Low tissue specificity.
DR neXtProt; NX_Q9NW82; -.
DR OpenTargets; ENSG00000082068; -.
DR PharmGKB; PA142670603; -.
DR VEuPathDB; HostDB:ENSG00000082068; -.
DR eggNOG; KOG0772; Eukaryota.
DR GeneTree; ENSGT00390000015433; -.
DR HOGENOM; CLU_014033_1_2_1; -.
DR InParanoid; Q9NW82; -.
DR OMA; QGGLRTN; -.
DR OrthoDB; 729650at2759; -.
DR PhylomeDB; Q9NW82; -.
DR TreeFam; TF105809; -.
DR PathwayCommons; Q9NW82; -.
DR SignaLink; Q9NW82; -.
DR BioGRID-ORCS; 55100; 750 hits in 1085 CRISPR screens.
DR ChiTaRS; WDR70; human.
DR GenomeRNAi; 55100; -.
DR Pharos; Q9NW82; Tdark.
DR PRO; PR:Q9NW82; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9NW82; protein.
DR Bgee; ENSG00000082068; Expressed in sural nerve and 187 other tissues.
DR ExpressionAtlas; Q9NW82; baseline and differential.
DR Genevisible; Q9NW82; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:1903775; P:regulation of DNA double-strand break processing; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation; WD repeat.
FT CHAIN 1..654
FT /note="WD repeat-containing protein 70"
FT /id="PRO_0000305144"
FT REPEAT 180..219
FT /note="WD 1"
FT REPEAT 227..268
FT /note="WD 2"
FT REPEAT 281..321
FT /note="WD 3"
FT REPEAT 330..369
FT /note="WD 4"
FT REPEAT 376..415
FT /note="WD 5"
FT REPEAT 421..466
FT /note="WD 6"
FT REPEAT 469..508
FT /note="WD 7"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..165
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 452
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 579
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 296
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 590
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 596
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:6ZYM"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 347..353
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 374..379
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 388..395
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 453..460
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 476..479
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 486..489
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 493..497
FT /evidence="ECO:0007829|PDB:6ZYM"
SQ SEQUENCE 654 AA; 73201 MW; 5AE0E1B43A5B8E18 CRC64;
MERSGPSEVT GSDASGPDPQ LAVTMGFTGF GKKARTFDLE AMFEQTRRTA VERSRKTLEA
REKEEEMNRE KELRRQNEDI EPTSSRSNVV RDCSKSSSRD TSSSESEQSS DSSDDELIGP
PLPPKMVGKP VNFMEEDILG PLPPPLNEEE EEAEEEEEEE EEEENPVHKI PDSHEITLKH
GTKTVSALGL DPSGARLVTG GYDYDVKFWD FAGMDASFKA FRSLQPCECH QIKSLQYSNT
GDMILVVSGS SQAKVIDRDG FEVMECIKGD QYIVDMANTK GHTAMLHTGS WHPKIKGEFM
TCSNDATVRT WEVENPKKQK SVFKPRTMQG KKVIPTTCTY SRDGNLIAAA CQNGSIQIWD
RNLTVHPKFH YKQAHDSGTD TSCVTFSYDG NVLASRGGDD SLKLWDIRQF NKPLFSASGL
PTMFPMTDCC FSPDDKLIVT GTSIQRGCGS GKLVFFERRT FQRVYEIDIT DASVVRCLWH
PKLNQIMVGT GNGLAKVYYD PNKSQRGAKL CVVKTQRKAK QAETLTQDYI ITPHALPMFR
EPRQRSTRKQ LEKDRLDPLK SHKPEPPVAG PGRGGRVGTH GGTLSSYIVK NIALDKTDDS
NPREAILRHA KAAEDSPYWV SPAYSKTQPK TMFAQVESDD EEAKNEPEWK KRKI
