GRWD1_HUMAN
ID GRWD1_HUMAN Reviewed; 446 AA.
AC Q9BQ67; A0MNN5; Q8TF59;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Glutamate-rich WD repeat-containing protein 1;
GN Name=GRWD1; Synonyms=GRWD, KIAA1942, WDR28;
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 [MRNA].
RA Fletcher B.S., Gratenstein K.B., Notterpek L.M.;
RT "Cloning and expression of a novel glutamate rich WD repeat (GRWD) protein
RT with roles in cell proliferation.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], 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 proteins
RT and regulates histone methylation.";
RL Nat. Cell Biol. 8:1277-1283(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-446, AND VARIANT GLN-319.
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII. The
RT complete sequences of 50 new cDNA clones which code for large proteins.";
RL DNA Res. 8:319-327(2001).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [8]
RP INDUCTION.
RX PubMed=14990995; DOI=10.1038/sj.onc.1207488;
RA Yoshida K., Inoue I.;
RT "Regulation of Geminin and Cdt1 expression by E2F transcription factors.";
RL Oncogene 23:3802-3812(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-122, AND
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
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 [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., 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10 AND SER-344, 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 [15]
RP INTERACTION WITH METTL18.
RX PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
RA Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
RT "A newly uncovered group of distantly related lysine methyltransferases
RT preferentially interact with molecular chaperones to regulate their
RT activity.";
RL PLoS Genet. 9:E1003210-E1003210(2013).
RN [16]
RP INTERACTION WITH CDT1 AND CDC6, FUNCTION, SUBCELLULAR LOCATION, AND
RP HISTONE-BINDING.
RX PubMed=25990725; DOI=10.1093/nar/gkv509;
RA Sugimoto N., Maehara K., Yoshida K., Yasukouchi S., Osano S., Watanabe S.,
RA Aizawa M., Yugawa T., Kiyono T., Kurumizaka H., Ohkawa Y., Fujita M.;
RT "Cdt1-binding protein GRWD1 is a novel histone-binding protein that
RT facilitates MCM loading through its influence on chromatin architecture.";
RL Nucleic Acids Res. 43:5898-5911(2015).
CC -!- FUNCTION: Histone binding-protein that regulates chromatin dynamics and
CC minichromosome maintenance (MCM) loading at replication origins,
CC possibly by promoting chromatin openness (PubMed:25990725).
CC {ECO:0000269|PubMed:25990725}.
CC -!- SUBUNIT: Interacts with METTL18 (PubMed:23349634). Interacts with CDT1;
CC origin binding of GRWD1 is dependent on CDT1 (PubMed:25990725).
CC Interacts with CDC6; origin binding of GRWD1 is dependent on CDC6
CC (PubMed:25990725). Binds to histone H2A-H2B and H3-H4 complexes
CC (PubMed:25990725). {ECO:0000269|PubMed:23349634,
CC ECO:0000269|PubMed:25990725}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}.
CC Nucleus {ECO:0000269|PubMed:25990725}. Chromosome
CC {ECO:0000269|PubMed:25990725}. Note=Present in the nucleus throughout
CC interphase and is detached from chromatin at the onset of mitosis and
CC rebinds at telophase when the pre-replication complexes (pre-RC) is
CC formed (PubMed:25990725). {ECO:0000269|PubMed:25990725}.
CC -!- INDUCTION: Induced by E2F transcription factors (PubMed:14990995).
CC {ECO:0000269|PubMed:14990995}.
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DR EMBL; AF337808; AAK17998.1; -; mRNA.
DR EMBL; EF011614; ABK41104.1; -; mRNA.
DR EMBL; AC008403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471177; EAW52347.1; -; Genomic_DNA.
DR EMBL; BC002440; AAH02440.1; -; mRNA.
DR EMBL; AB075822; BAB85528.1; -; mRNA.
DR CCDS; CCDS12720.1; -.
DR RefSeq; NP_113673.3; NM_031485.3.
DR AlphaFoldDB; Q9BQ67; -.
DR SMR; Q9BQ67; -.
DR BioGRID; 123751; 338.
DR CORUM; Q9BQ67; -.
DR IntAct; Q9BQ67; 35.
DR MINT; Q9BQ67; -.
DR STRING; 9606.ENSP00000253237; -.
DR GlyGen; Q9BQ67; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BQ67; -.
DR MetOSite; Q9BQ67; -.
DR PhosphoSitePlus; Q9BQ67; -.
DR SwissPalm; Q9BQ67; -.
DR BioMuta; GRWD1; -.
DR DMDM; 18202731; -.
DR SWISS-2DPAGE; Q9BQ67; -.
DR EPD; Q9BQ67; -.
DR jPOST; Q9BQ67; -.
DR MassIVE; Q9BQ67; -.
DR MaxQB; Q9BQ67; -.
DR PaxDb; Q9BQ67; -.
DR PeptideAtlas; Q9BQ67; -.
DR PRIDE; Q9BQ67; -.
DR ProteomicsDB; 78636; -.
DR Antibodypedia; 31711; 136 antibodies from 22 providers.
DR DNASU; 83743; -.
DR Ensembl; ENST00000253237.10; ENSP00000253237.4; ENSG00000105447.13.
DR GeneID; 83743; -.
DR KEGG; hsa:83743; -.
DR MANE-Select; ENST00000253237.10; ENSP00000253237.4; NM_031485.4; NP_113673.3.
DR UCSC; uc002pjd.3; human.
DR CTD; 83743; -.
DR DisGeNET; 83743; -.
DR GeneCards; GRWD1; -.
DR HGNC; HGNC:21270; GRWD1.
DR HPA; ENSG00000105447; Low tissue specificity.
DR MIM; 610597; gene.
DR neXtProt; NX_Q9BQ67; -.
DR OpenTargets; ENSG00000105447; -.
DR PharmGKB; PA134897548; -.
DR VEuPathDB; HostDB:ENSG00000105447; -.
DR eggNOG; KOG0302; Eukaryota.
DR GeneTree; ENSGT00550000075124; -.
DR HOGENOM; CLU_025272_1_1_1; -.
DR InParanoid; Q9BQ67; -.
DR OMA; DWSPLQP; -.
DR OrthoDB; 831322at2759; -.
DR PhylomeDB; Q9BQ67; -.
DR TreeFam; TF312982; -.
DR PathwayCommons; Q9BQ67; -.
DR SignaLink; Q9BQ67; -.
DR BioGRID-ORCS; 83743; 633 hits in 1083 CRISPR screens.
DR ChiTaRS; GRWD1; human.
DR GeneWiki; GRWD1; -.
DR GenomeRNAi; 83743; -.
DR Pharos; Q9BQ67; Tbio.
DR PRO; PR:Q9BQ67; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BQ67; protein.
DR Bgee; ENSG00000105447; Expressed in tongue squamous epithelium and 200 other tissues.
DR ExpressionAtlas; Q9BQ67; baseline and differential.
DR Genevisible; Q9BQ67; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IMP:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
DR GO; GO:0006337; P:nucleosome disassembly; IMP:UniProtKB.
DR GO; GO:0042254; P:ribosome biogenesis; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR022052; Histone-bd_RBBP4_N.
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 Pfam; PF12265; CAF1C_H4-bd; 1.
DR Pfam; PF00400; WD40; 3.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 4.
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 Chromosome; DNA replication; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1..446
FT /note="Glutamate-rich WD repeat-containing protein 1"
FT /id="PRO_0000051011"
FT REPEAT 54..110
FT /note="WD 1"
FT REPEAT 163..204
FT /note="WD 2"
FT REPEAT 205..250
FT /note="WD 3"
FT REPEAT 251..297
FT /note="WD 4"
FT REPEAT 298..343
FT /note="WD 5"
FT REPEAT 344..405
FT /note="WD 6"
FT REPEAT 406..442
FT /note="WD 7"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..137
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 319
FT /note="R -> Q (in dbSNP:rs2302951)"
FT /evidence="ECO:0000269|PubMed:11853319"
FT /id="VAR_046334"
SQ SEQUENCE 446 AA; 49419 MW; 748CA005313FF8A8 CRC64;
MAARKGRRRT CETGEPMEAE SGDTSSEGPA QVYLPGRGPP LREGEELVMD EEAYVLYHRA
QTGAPCLSFD IVRDHLGDNR TELPLTLYLC AGTQAESAQS NRLMMLRMHN LHGTKPPPSE
GSDEEEEEED EEDEEERKPQ LELAMVPHYG GINRVRVSWL GEEPVAGVWS EKGQVEVFAL
RRLLQVVEEP QALAAFLRDE QAQMKPIFSF AGHMGEGFAL DWSPRVTGRL LTGDCQKNIH
LWTPTDGGSW HVDQRPFVGH TRSVEDLQWS PTENTVFASC SADASIRIWD IRAAPSKACM
LTTATAHDGD VNVISWSRRE PFLLSGGDDG ALKIWDLRQF KSGSPVATFK QHVAPVTSVE
WHPQDSGVFA ASGADHQITQ WDLAVERDPE AGDVEADPGL ADLPQQLLFV HQGETELKEL
HWHPQCPGLL VSTALSGFTI FRTISV
