LRWD1_HUMAN - dbPTM
LRWD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRWD1_HUMAN
UniProt AC Q9UFC0
Protein Name Leucine-rich repeat and WD repeat-containing protein 1
Gene Name LRWD1
Organism Homo sapiens (Human).
Sequence Length 647
Subcellular Localization Nucleus. Chromosome, centromere. Chromosome, telomere. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Chromosome, centromere, kinetochore . Localizes to heterochromatin during G1 phase. Restricted to centromeres or telomeres as
Protein Description Required for G1/S transition. Recruits and stabilizes the origin recognition complex (ORC) onto chromatin during G1 to establish pre-replication complex (preRC) and to heterochromatic sites in post-replicated cells. Binds a combination of DNA and histone methylation repressive marks on heterochromatin. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3 in a cooperative manner with DNA methylation. Required for silencing of major satellite repeats. May be important ORC2, ORC3 and ORC4 stability..
Protein Sequence MGPLSARLLMQRGRPKSDRLGKIRSLDLSGLELLSEHLDPKLLCRLTQLQELDLSNNHLETLPDNLGLSHLRVLRCANNQLGDVTALCQFPKLEELSLEGNPFLTVNDNLKVSFLLPTLRKVNGKDASSTYSQVENLNRELTSRVTAHWEKFMATLGPEEEAEKAQADFVKSAVRDVRYGPESLSEFTQWRVRMISEELVAASRTQVQKANSPEKPPEAGAAHKPRARLAALKRPDDVPLSLSPSKRACASPSAQVEGSPVAGSDGSQPAVKLEPLHFLQCHSKNNSPQDLETQLWACAFEPAWEEGATSQTVATCGGEAVCVIDCQTGIVLHKYKAPGEEFFSVAWTALMVVTQAGHKKRWSVLAAAGLRGLVRLLHVRAGFCCGVIRAHKKAIATLCFSPAHETHLFTASYDKRIILWDIGVPNQDYEFQASQLLTLDTTSIPLRLCPVASCPDARLLAGCEGGCCCWDVRLDQPQKRRVCEVEFVFSEGSEASGRRVDGLAFVNEDIVASKGSGLGTICLWSWRQTWGGRGSQSTVAVVVLARLQWSSTELAYFSLSACPDKGIVLCGDEEGNVWLYDVSNILKQPPLLPAALQAPTQILKWPQPWALGQVVTKTMVNTVVANASFTYLTALTDSNIVAIWGRM
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
17PhosphorylationMQRGRPKSDRLGKIR
HHCCCCCCCCCCCCE		30.5522817900
25PhosphorylationDRLGKIRSLDLSGLE
CCCCCCEECCCCHHH		29.7027732954
29PhosphorylationKIRSLDLSGLELLSE
CCEECCCCHHHHHHH		40.7822115753
41UbiquitinationLSEHLDPKLLCRLTQ
HHHCCCHHHHHHHHH		54.48-
55PhosphorylationQLQELDLSNNHLETL
HHHCCCCCCCCHHCC		34.9427174698
61PhosphorylationLSNNHLETLPDNLGL
CCCCCHHCCCCCCCC		50.3727174698
69PhosphorylationLPDNLGLSHLRVLRC
CCCCCCCHHHHHHHC		20.7627174698
121UbiquitinationFLLPTLRKVNGKDAS
EEHHHHEECCCCCCC		43.07-
125UbiquitinationTLRKVNGKDASSTYS
HHEECCCCCCCCHHH		44.94-
130PhosphorylationNGKDASSTYSQVENL
CCCCCCCHHHHHHHH		25.3822210691
142PhosphorylationENLNRELTSRVTAHW
HHHCHHHHHHHHHHH		15.1022210691
146PhosphorylationRELTSRVTAHWEKFM
HHHHHHHHHHHHHHH		16.2222210691
151UbiquitinationRVTAHWEKFMATLGP
HHHHHHHHHHHHHCC		34.94-
171UbiquitinationKAQADFVKSAVRDVR
HHHHHHHHHHHHHHH		32.46-
183PhosphorylationDVRYGPESLSEFTQW
HHHCCCCCHHHHHHH		40.0927067055
196PhosphorylationQWRVRMISEELVAAS
HHHHHHHHHHHHHHH		18.7120860994
205PhosphorylationELVAASRTQVQKANS
HHHHHHHHHHHHCCC		30.5124732914
212PhosphorylationTQVQKANSPEKPPEA
HHHHHCCCCCCCCCC		39.0229255136
224UbiquitinationPEAGAAHKPRARLAA
CCCCCCCCHHHHHHH		31.32-
233AcetylationRARLAALKRPDDVPL
HHHHHHHCCCCCCCC		58.1025953088
241PhosphorylationRPDDVPLSLSPSKRA
CCCCCCCCCCCCCCC		22.2622167270
243PhosphorylationDDVPLSLSPSKRACA
CCCCCCCCCCCCCCC		24.6129255136
245PhosphorylationVPLSLSPSKRACASP
CCCCCCCCCCCCCCC		31.2522167270
246UbiquitinationPLSLSPSKRACASPS
CCCCCCCCCCCCCCC		47.61-
246AcetylationPLSLSPSKRACASPS
CCCCCCCCCCCCCCC		47.6125953088
251PhosphorylationPSKRACASPSAQVEG
CCCCCCCCCCCEECC		21.1919664994
253PhosphorylationKRACASPSAQVEGSP
CCCCCCCCCEECCCC		28.9229255136
259PhosphorylationPSAQVEGSPVAGSDG
CCCEECCCCCCCCCC		11.6029255136
264PhosphorylationEGSPVAGSDGSQPAV
CCCCCCCCCCCCCCE		29.1229255136
267PhosphorylationPVAGSDGSQPAVKLE
CCCCCCCCCCCEEEC		37.6717525332
283PhosphorylationLHFLQCHSKNNSPQD
CEEEECCCCCCCHHH		44.7126552605
328PhosphorylationVCVIDCQTGIVLHKY
EEEEECCCCEEEEEC		34.90-
335PhosphorylationTGIVLHKYKAPGEEF
CCEEEEECCCCCHHH		11.13-
443PhosphorylationLLTLDTTSIPLRLCP
CEEECCCCCCCCCCC		25.0524719451
628PhosphorylationNTVVANASFTYLTAL
HHHHHCCEEEEEEEC		20.2326853621
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of LRWD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRWD1_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of LRWD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ORC2_HUMANORC2physical
22935713
CUL4A_HUMANCUL4Aphysical
22935713
DDB1_HUMANDDB1physical
22935713
ORC2_HUMANORC2physical
22939629
ORC3_HUMANORC3physical
22939629
ORC5_HUMANORC5physical
22939629
ADDA_HUMANADD1physical
26496610
ORC1_HUMANORC1physical
26496610
ORC2_HUMANORC2physical
26496610
ORC4_HUMANORC4physical
26496610
ORC5_HUMANORC5physical
26496610
TBG1_HUMANTUBG1physical
26496610
GCP3_HUMANTUBGCP3physical
26496610
GCP2_HUMANTUBGCP2physical
26496610
ORC3_HUMANORC3physical
26496610
PRR3_HUMANPRR3physical
26496610
GCP6_HUMANTUBGCP6physical
26496610
MZT2A_HUMANMZT2Aphysical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LRWD1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-243 ANDSER-259, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251; SER-253 ANDSER-259, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-243; SER-251AND SER-259, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243; SER-245; SER-251AND SER-259, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251 AND SER-267, ANDMASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212 AND SER-243, ANDMASS SPECTROMETRY.

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