LRWD1_HUMAN
ID LRWD1_HUMAN Reviewed; 647 AA.
AC Q9UFC0; A8K4K2; B2R9G2; Q8N0T9; Q8WV43; Q96GJ2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Leucine-rich repeat and WD repeat-containing protein 1;
DE AltName: Full=Centromere protein 33;
DE Short=CENP-33;
DE AltName: Full=Origin recognition complex-associated protein;
DE Short=ORC-associated protein;
DE Short=ORCA;
GN Name=LRWD1; Synonyms=CENP-33 {ECO:0000303|PubMed:20813266}, ORCA;
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=Testis;
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=Testis;
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 GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
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 [LARGE SCALE MRNA].
RC TISSUE=Brain, and Eye;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, 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 [7]
RP TISSUE SPECIFICITY.
RX PubMed=17074343; DOI=10.1016/j.fertnstert.2006.04.039;
RA Lin Y.H., Lin Y.M., Teng Y.N., Hsieh T.Y., Lin Y.S., Kuo P.L.;
RT "Identification of ten novel genes involved in human spermatogenesis by
RT microarray analysis of testicular tissue.";
RL Fertil. Steril. 86:1650-1658(2006).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=18445686; DOI=10.1242/jcs.019174;
RA Tegha-Dunghu J., Neumann B., Reber S., Krause R., Erfle H., Walter T.,
RA Held M., Rogers P., Hupfeld K., Ruppert T., Ellenberg J., Gruss O.J.;
RT "EML3 is a nuclear microtubule-binding protein required for the correct
RT alignment of chromosomes in metaphase.";
RL J. Cell Sci. 121:1718-1726(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243; SER-251 AND SER-259, AND
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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-243 AND SER-259, AND
RP IDENTIFICATION BY 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 [13]
RP SUBCELLULAR LOCATION.
RX PubMed=20813266; DOI=10.1016/j.cell.2010.07.047;
RA Ohta S., Bukowski-Wills J.C., Sanchez-Pulido L., Alves Fde L., Wood L.,
RA Chen Z.A., Platani M., Fischer L., Hudson D.F., Ponting C.P., Fukagawa T.,
RA Earnshaw W.C., Rappsilber J.;
RT "The protein composition of mitotic chromosomes determined using
RT multiclassifier combinatorial proteomics.";
RL Cell 142:810-821(2010).
RN [14]
RP IDENTIFICATION IN THE ORC COMPLEX, AND FUNCTION.
RX PubMed=20850016; DOI=10.1016/j.cell.2010.08.020;
RA Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S., Butter F.,
RA Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G., Mann M.;
RT "Quantitative interaction proteomics and genome-wide profiling of
RT epigenetic histone marks and their readers.";
RL Cell 142:967-980(2010).
RN [15]
RP SUBCELLULAR LOCATION, IDENTIFICATION IN THE ORC COMPLEX, AND FUNCTION.
RX PubMed=21029866; DOI=10.1016/j.cell.2010.10.012;
RA Bartke T., Vermeulen M., Xhemalce B., Robson S.C., Mann M., Kouzarides T.;
RT "Nucleosome-interacting proteins regulated by DNA and histone
RT methylation.";
RL Cell 143:470-484(2010).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN WD REPEATS, IDENTIFICATION BY MASS
RP SPECTROMETRY, IDENTIFICATION IN THE ORC COMPLEX, AND DEVELOPMENTAL STAGE.
RX PubMed=20932478; DOI=10.1016/j.molcel.2010.09.021;
RA Shen Z., Sathyan K.M., Geng Y., Zheng R., Chakraborty A., Freeman B.,
RA Wang F., Prasanth K.V., Prasanth S.G.;
RT "A WD-repeat protein stabilizes ORC binding to chromatin.";
RL Mol. Cell 40:99-111(2010).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212 AND SER-243, AND
RP IDENTIFICATION BY 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212 AND SER-243, AND
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., 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 [19]
RP INTERACTION WITH ORC2; CUL4A AND DDB1, SUBCELLULAR LOCATION,
RP UBIQUITINATION, AND DEVELOPMENTAL STAGE.
RX PubMed=22935713; DOI=10.4161/cc.21870;
RA Shen Z., Prasanth S.G.;
RT "Orc2 protects ORCA from ubiquitin-mediated degradation.";
RL Cell Cycle 11:3578-3589(2012).
RN [20]
RP FUNCTION, BINDING TO HISTONE H3 AND H4 TRIMETHYLATION MARKS, SUBCELLULAR
RP LOCATION, AND DOMAIN.
RX PubMed=22427655; DOI=10.1074/jbc.m111.337980;
RA Chan K.M., Zhang Z.;
RT "Leucine-rich repeat and WD repeat-containing protein 1 is recruited to
RT pericentric heterochromatin by trimethylated lysine 9 of histone H3 and
RT maintains heterochromatin silencing.";
RL J. Biol. Chem. 287:15024-15033(2012).
RN [21]
RP FUNCTION, INTERACTION WITH CDT1; GMNN; ORC1 AND ORC2, STOICHIOMETRY OF THE
RP COMPLEX, AND DOMAIN.
RX PubMed=22645314; DOI=10.1128/mcb.00362-12;
RA Shen Z., Chakraborty A., Jain A., Giri S., Ha T., Prasanth K.V.,
RA Prasanth S.G.;
RT "Dynamic association of ORCA with prereplicative complex components
RT regulates DNA replication initiation.";
RL Mol. Cell. Biol. 32:3107-3120(2012).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-243; SER-251 AND
RP SER-259, AND 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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-259 AND SER-264, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Required for G1/S transition. Recruits and stabilizes the
CC origin recognition complex (ORC) onto chromatin during G1 to establish
CC pre-replication complex (preRC) and to heterochromatic sites in post-
CC replicated cells. Binds a combination of DNA and histone methylation
CC repressive marks on heterochromatin. Binds histone H3 and H4
CC trimethylation marks H3K9me3, H3K27me3 and H4K20me3 in a cooperative
CC manner with DNA methylation. Required for silencing of major satellite
CC repeats. May be important ORC2, ORC3 and ORC4 stability.
CC {ECO:0000269|PubMed:20850016, ECO:0000269|PubMed:20932478,
CC ECO:0000269|PubMed:21029866, ECO:0000269|PubMed:22427655,
CC ECO:0000269|PubMed:22645314}.
CC -!- SUBUNIT: Integral component of the ORC complex. Directly interacts with
CC CDT1, GMNN and ORC2. Interacts with ORC2 only when non-ubiquitinated;
CC this interaction prevents LRWD1 ubiquitination and degradation. Some of
CC these interactions are regulated in a cell-cycle dependent manner.
CC Interaction with ORC1 occurs predominantly during G1. Association with
CC phosphorylated ORC1 during mitosis is not efficient. Interaction with
CC CDT1 occurs during G1 phase, as well as during mitosis with
CC phosphorylated CDT1. Interaction with GMNN occurs from G1/S to mitosis.
CC Interaction with ORC2 is observed throughout the cell cycle. The
CC stoichiometry of the ORCA/ORC/CDT1/GMNN complex is 1:1:1:2. Interacts
CC with CUL4A and DDB1; this interaction may lead to ubiquitination.
CC {ECO:0000269|PubMed:20850016, ECO:0000269|PubMed:20932478,
CC ECO:0000269|PubMed:21029866, ECO:0000269|PubMed:22645314,
CC ECO:0000269|PubMed:22935713}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18445686}.
CC Chromosome, centromere. Chromosome, telomere. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q8BUI3}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:20813266}. Note=Localizes to heterochromatin during
CC G1 phase. Restricted to centromeres or telomeres as cells progress
CC though S phase. When cells enter mitosis, relocalizes to centromeres.
CC Recruitment to pericentric heterochromatin largely depends on the
CC presence of H3K9me3.
CC -!- TISSUE SPECIFICITY: Testis-specific. Drastically down-regulated in
CC testis from patients with Sertoli cell-only syndrome (SCOS).
CC {ECO:0000269|PubMed:17074343}.
CC -!- DEVELOPMENTAL STAGE: Regulated in a cell-cycle dependent manner.
CC Highest expression in G1 phase. Expression decreases during S phase,
CC rises again during G2 and drops during mitosis (at protein level). In
CC contrast to protein levels, transcript levels do not show any
CC significant variation during different stages of the cell cycle
CC (PubMed:22935713). {ECO:0000269|PubMed:20932478,
CC ECO:0000269|PubMed:22935713}.
CC -!- DOMAIN: The entire WD repeat region is required for the interaction
CC with ORC, CDT1 and GMNN, as well as for association with chromatin and
CC for binding to histone H3 and H4 trimethylation marks H3K9me3 and
CC H4K20me3. {ECO:0000269|PubMed:20932478, ECO:0000269|PubMed:22427655,
CC ECO:0000269|PubMed:22645314}.
CC -!- PTM: Ubiquitinated; undergoes 'Lys-48'-linked polyubiquitination
CC leading to proteasomal degradation. Ubiquitination occurs within the WD
CC repeats at the end of the G1 phase. Ubiquitination may be catalyzed by
CC the CUL4-DDB1 E3 ubiquitin-protein ligase complex and other E3 ligases.
CC {ECO:0000269|PubMed:22935713}.
CC -!- SIMILARITY: Belongs to the LRWD1 family. {ECO:0000305}.
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DR EMBL; AK290967; BAF83656.1; -; mRNA.
DR EMBL; AK313771; BAG36509.1; -; mRNA.
DR EMBL; AL133057; CAB61382.2; -; mRNA.
DR EMBL; AC093668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471197; EAW50250.1; -; Genomic_DNA.
DR EMBL; BC009436; AAH09436.1; -; mRNA.
DR EMBL; BC018769; AAH18769.1; -; mRNA.
DR EMBL; BC030547; AAH30547.1; -; mRNA.
DR CCDS; CCDS34715.1; -.
DR PIR; T42659; T42659.
DR RefSeq; NP_001304650.1; NM_001317721.1.
DR RefSeq; NP_690852.1; NM_152892.2.
DR AlphaFoldDB; Q9UFC0; -.
DR BioGRID; 128790; 108.
DR IntAct; Q9UFC0; 37.
DR MINT; Q9UFC0; -.
DR STRING; 9606.ENSP00000292616; -.
DR GlyGen; Q9UFC0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UFC0; -.
DR PhosphoSitePlus; Q9UFC0; -.
DR BioMuta; LRWD1; -.
DR DMDM; 74761931; -.
DR EPD; Q9UFC0; -.
DR jPOST; Q9UFC0; -.
DR MassIVE; Q9UFC0; -.
DR MaxQB; Q9UFC0; -.
DR PaxDb; Q9UFC0; -.
DR PeptideAtlas; Q9UFC0; -.
DR PRIDE; Q9UFC0; -.
DR ProteomicsDB; 84177; -.
DR Antibodypedia; 16796; 113 antibodies from 22 providers.
DR DNASU; 222229; -.
DR Ensembl; ENST00000292616.10; ENSP00000292616.5; ENSG00000161036.13.
DR GeneID; 222229; -.
DR KEGG; hsa:222229; -.
DR MANE-Select; ENST00000292616.10; ENSP00000292616.5; NM_152892.3; NP_690852.1.
DR UCSC; uc003uzn.4; human.
DR CTD; 222229; -.
DR DisGeNET; 222229; -.
DR GeneCards; LRWD1; -.
DR HGNC; HGNC:21769; LRWD1.
DR HPA; ENSG00000161036; Tissue enriched (testis).
DR MIM; 615167; gene.
DR neXtProt; NX_Q9UFC0; -.
DR OpenTargets; ENSG00000161036; -.
DR PharmGKB; PA162394694; -.
DR VEuPathDB; HostDB:ENSG00000161036; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000154248; -.
DR HOGENOM; CLU_022994_0_0_1; -.
DR InParanoid; Q9UFC0; -.
DR OMA; CPEQYLL; -.
DR OrthoDB; 810613at2759; -.
DR PhylomeDB; Q9UFC0; -.
DR TreeFam; TF329554; -.
DR PathwayCommons; Q9UFC0; -.
DR SignaLink; Q9UFC0; -.
DR BioGRID-ORCS; 222229; 51 hits in 1088 CRISPR screens.
DR ChiTaRS; LRWD1; human.
DR GenomeRNAi; 222229; -.
DR Pharos; Q9UFC0; Tbio.
DR PRO; PR:Q9UFC0; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UFC0; protein.
DR Bgee; ENSG00000161036; Expressed in left testis and 173 other tissues.
DR ExpressionAtlas; Q9UFC0; baseline and differential.
DR Genevisible; Q9UFC0; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005664; C:nuclear origin of replication recognition complex; IDA:UniProtKB.
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:0005721; C:pericentric heterochromatin; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0008327; F:methyl-CpG binding; IDA:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IMP:UniProtKB.
DR GO; GO:0006270; P:DNA replication initiation; TAS:UniProtKB.
DR GO; GO:0071169; P:establishment of protein localization to chromatin; IDA:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
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; PF12799; LRR_4; 1.
DR SMART; SM00369; LRR_TYP; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS51450; LRR; 3.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Centromere; Chromatin regulator; Chromosome; Cytoplasm; Cytoskeleton;
KW DNA replication; Kinetochore; Leucine-rich repeat; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Telomere; Ubl conjugation; WD repeat.
FT CHAIN 1..647
FT /note="Leucine-rich repeat and WD repeat-containing protein
FT 1"
FT /id="PRO_0000310994"
FT REPEAT 22..43
FT /note="LRR 1"
FT REPEAT 48..69
FT /note="LRR 2"
FT REPEAT 70..91
FT /note="LRR 3"
FT REPEAT 92..113
FT /note="LRR 4"
FT REPEAT 282..335
FT /note="WD 1"
FT REPEAT 341..379
FT /note="WD 2"
FT REPEAT 383..422
FT /note="WD 3"
FT REPEAT 426..472
FT /note="WD 4"
FT REPEAT 484..526
FT /note="WD 5"
FT REPEAT 542..582
FT /note="WD 6"
FT REPEAT 598..646
FT /note="WD 7"
FT REGION 204..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 212
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 ECO:0007744|PubMed:24275569"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CONFLICT 629
FT /note="F -> S (in Ref. 1; BAF83656)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 647 AA; 70861 MW; 59C6ABF57A957D9F CRC64;
MGPLSARLLM QRGRPKSDRL GKIRSLDLSG LELLSEHLDP KLLCRLTQLQ ELDLSNNHLE
TLPDNLGLSH LRVLRCANNQ LGDVTALCQF PKLEELSLEG NPFLTVNDNL KVSFLLPTLR
KVNGKDASST YSQVENLNRE LTSRVTAHWE KFMATLGPEE EAEKAQADFV KSAVRDVRYG
PESLSEFTQW RVRMISEELV AASRTQVQKA NSPEKPPEAG AAHKPRARLA ALKRPDDVPL
SLSPSKRACA SPSAQVEGSP VAGSDGSQPA VKLEPLHFLQ CHSKNNSPQD LETQLWACAF
EPAWEEGATS QTVATCGGEA VCVIDCQTGI VLHKYKAPGE EFFSVAWTAL MVVTQAGHKK
RWSVLAAAGL RGLVRLLHVR AGFCCGVIRA HKKAIATLCF SPAHETHLFT ASYDKRIILW
DIGVPNQDYE FQASQLLTLD TTSIPLRLCP VASCPDARLL AGCEGGCCCW DVRLDQPQKR
RVCEVEFVFS EGSEASGRRV DGLAFVNEDI VASKGSGLGT ICLWSWRQTW GGRGSQSTVA
VVVLARLQWS STELAYFSLS ACPDKGIVLC GDEEGNVWLY DVSNILKQPP LLPAALQAPT
QILKWPQPWA LGQVVTKTMV NTVVANASFT YLTALTDSNI VAIWGRM
