WDR70_RAT
ID WDR70_RAT Reviewed; 655 AA.
AC Q5EB92;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=WD repeat-containing protein 70;
GN Name=Wdr70;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- SIMILARITY: Belongs to the WD repeat GAD-1 family. {ECO:0000305}.
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DR EMBL; BC089903; AAH89903.1; -; mRNA.
DR RefSeq; NP_001013931.1; NM_001013909.1.
DR AlphaFoldDB; Q5EB92; -.
DR SMR; Q5EB92; -.
DR IntAct; Q5EB92; 1.
DR STRING; 10116.ENSRNOP00000056890; -.
DR iPTMnet; Q5EB92; -.
DR PhosphoSitePlus; Q5EB92; -.
DR jPOST; Q5EB92; -.
DR PaxDb; Q5EB92; -.
DR PRIDE; Q5EB92; -.
DR Ensembl; ENSRNOT00000060146; ENSRNOP00000056890; ENSRNOG00000013336.
DR GeneID; 294783; -.
DR KEGG; rno:294783; -.
DR CTD; 55100; -.
DR RGD; 1309487; Wdr70.
DR eggNOG; KOG0772; Eukaryota.
DR GeneTree; ENSGT00390000015433; -.
DR HOGENOM; CLU_014033_1_2_1; -.
DR InParanoid; Q5EB92; -.
DR OMA; QGGLRTN; -.
DR OrthoDB; 729650at2759; -.
DR PhylomeDB; Q5EB92; -.
DR TreeFam; TF105809; -.
DR PRO; PR:Q5EB92; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000013336; Expressed in testis and 20 other tissues.
DR Genevisible; Q5EB92; RN.
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; ISO:RGD.
DR GO; GO:1903775; P:regulation of DNA double-strand break processing; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
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 PRINTS; PR00320; GPROTEINBRPT.
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 Acetylation; Isopeptide bond; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation; WD repeat.
FT CHAIN 1..655
FT /note="WD repeat-containing protein 70"
FT /id="PRO_0000305146"
FT REPEAT 181..220
FT /note="WD 1"
FT REPEAT 228..269
FT /note="WD 2"
FT REPEAT 282..322
FT /note="WD 3"
FT REPEAT 331..370
FT /note="WD 4"
FT REPEAT 377..416
FT /note="WD 5"
FT REPEAT 422..467
FT /note="WD 6"
FT REPEAT 470..509
FT /note="WD 7"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..163
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 453
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NW82"
FT MOD_RES 580
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NW82"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NW82"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NW82"
FT CROSSLNK 591
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NW82"
FT CROSSLNK 597
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NW82"
SQ SEQUENCE 655 AA; 72836 MW; 861669E7B023E78D CRC64;
MEHSGPSEVT GADTAGPDPQ LAVTMGFTGF GKKARTFDLE AMFEQTRRTA VERSRKTLEA
REKEEEMNRE KELRKQLEDI EPTPSSSSAV RERSKSSSRD TSSSDSDHSS GSSDDELIGP
PLPPEMVGGP VNTVDEDILG PLPPPLCEEG EDDDDDDLED EGEEDNPIHR IPDSHEITLK
HGTKTVSALG LDPSGARLVT GGYDYDVKFW DFAGMDASFK AFRSLQPCEC HQIKSLQYSN
TGDMILVVSG SSQAKVIDRD GFEVMECIKG DQYIVDMANT KGHTAMLHTG SWHPKIKGEF
MTCSNDATVR LWEVENPKKQ KSVFKPRTMQ GKKVIPTTCT YSRDGNLVAA ACQNGSIQIW
DRNLTVHPKF HYKQAHAPGT DTSCVAFSYD GNVLASRGGD DTLKLWDVRQ FNKPLFSASD
LPTLFPMTDC CFSPDDKLIV TGTSVQRGCG SGKLVFFERR TFQRVYEIHI TDASVVRCLW
HPKLNQIMVG TGNGLAKVYY DPNKSQRGAK LCVVKTQRKA KQAETLTQDY IITPHALPMF
REPRQRSTRK QLEKDRLDPL KSHKPEPPVA GPGRGGRVGT HGGTLSSYIV KNIALDKTDD
SNPREAILRH AKAAEDNPYW VSPAYSKTQP KTMFAQVESD DEESKNEPEW KKRKI
