GRWD1_HUMAN - dbPTM
GRWD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GRWD1_HUMAN
UniProt AC Q9BQ67
Protein Name Glutamate-rich WD repeat-containing protein 1
Gene Name GRWD1
Organism Homo sapiens (Human).
Sequence Length 446
Subcellular Localization Nucleus, nucleolus . Nucleus . Chromosome . Present in the nucleus throughout interphase and is detached from chromatin at the onset of mitosis and rebinds at telophase when the pre-replication complexes (pre-RC) is formed (PubMed:25990725).
Protein Description Histone binding-protein that regulates chromatin dynamics and minichromosome maintenance (MCM) loading at replication origins, possibly by promoting chromatin openness. [PubMed: 25990725]
Protein Sequence MAARKGRRRTCETGEPMEAESGDTSSEGPAQVYLPGRGPPLREGEELVMDEEAYVLYHRAQTGAPCLSFDIVRDHLGDNRTELPLTLYLCAGTQAESAQSNRLMMLRMHNLHGTKPPPSEGSDEEEEEEDEEDEEERKPQLELAMVPHYGGINRVRVSWLGEEPVAGVWSEKGQVEVFALRRLLQVVEEPQALAAFLRDEQAQMKPIFSFAGHMGEGFALDWSPRVTGRLLTGDCQKNIHLWTPTDGGSWHVDQRPFVGHTRSVEDLQWSPTENTVFASCSADASIRIWDIRAAPSKACMLTTATAHDGDVNVISWSRREPFLLSGGDDGALKIWDLRQFKSGSPVATFKQHVAPVTSVEWHPQDSGVFAASGADHQITQWDLAVERDPEAGDVEADPGLADLPQQLLFVHQGETELKELHWHPQCPGLLVSTALSGFTIFRTISV
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
10PhosphorylationARKGRRRTCETGEPM
CCCCCCCCCCCCCCC		16.9429255136
13PhosphorylationGRRRTCETGEPMEAE
CCCCCCCCCCCCCCC		49.3329255136
21PhosphorylationGEPMEAESGDTSSEG
CCCCCCCCCCCCCCC		49.3623927012
24PhosphorylationMEAESGDTSSEGPAQ
CCCCCCCCCCCCCCE		37.3625159151
25PhosphorylationEAESGDTSSEGPAQV
CCCCCCCCCCCCCEE		31.0025159151
26PhosphorylationAESGDTSSEGPAQVY
CCCCCCCCCCCCEEE		48.9823927012
33PhosphorylationSEGPAQVYLPGRGPP
CCCCCEEECCCCCCC		8.6318669648
49SulfoxidationREGEELVMDEEAYVL
CCCCEEEECCCHHHH		9.3130846556
66GlutathionylationRAQTGAPCLSFDIVR
HHCCCCCEEEEEEEE		5.0122555962
114PhosphorylationRMHNLHGTKPPPSEG
EHHHCCCCCCCCCCC		29.6323927012
119PhosphorylationHGTKPPPSEGSDEEE
CCCCCCCCCCCCHHH		61.4323927012
122PhosphorylationKPPPSEGSDEEEEEE
CCCCCCCCCHHHHHC		37.4823927012
149PhosphorylationELAMVPHYGGINRVR
HHEECCCCCCCCEEE		15.8130576142
158PhosphorylationGINRVRVSWLGEEPV
CCCEEEEEECCCCCC		13.1527067055
172UbiquitinationVAGVWSEKGQVEVFA
CEEEECCCCCEEHHH		49.4821987572
181MethylationQVEVFALRRLLQVVE
CEEHHHHHHHHHHHH		24.62-
223PhosphorylationEGFALDWSPRVTGRL
CCCCCCCCCCCCCEE		11.5124719451
237AcetylationLLTGDCQKNIHLWTP
EEECCCCCCEEEECC		65.2926051181
237UbiquitinationLLTGDCQKNIHLWTP
EEECCCCCCEEEECC		65.29-
249PhosphorylationWTPTDGGSWHVDQRP
ECCCCCCCCEECCCC		21.3820873877
263PhosphorylationPFVGHTRSVEDLQWS
CCCCCCCCHHHCCCC		30.8927251275
280GlutathionylationENTVFASCSADASIR
CCEEEEEECCCCEEE		3.3122555962
297UbiquitinationDIRAAPSKACMLTTA
EECCCCCCEEEEEEE		44.54-
333UbiquitinationGGDDGALKIWDLRQF
CCCCCCEEEEEHHHC		41.0121906983
341SumoylationIWDLRQFKSGSPVAT
EEEHHHCCCCCCCEE		45.64-
341UbiquitinationIWDLRQFKSGSPVAT
EEEHHHCCCCCCCEE		45.6432015554
341SumoylationIWDLRQFKSGSPVAT
EEEHHHCCCCCCCEE		45.64-
341AcetylationIWDLRQFKSGSPVAT
EEEHHHCCCCCCCEE		45.6425953088
342PhosphorylationWDLRQFKSGSPVATF
EEHHHCCCCCCCEEE		45.8827794612
344PhosphorylationLRQFKSGSPVATFKQ
HHHCCCCCCCEEEEE		24.2425159151
348PhosphorylationKSGSPVATFKQHVAP
CCCCCCEEEEECCCC		31.4423403867
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 GRWD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GRWD1_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 GRWD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDT1_HUMANCDT1physical
18162579
WDR5_HUMANWDR5physical
17041588
NOC2L_HUMANNOC2Lphysical
26344197
RPA49_HUMANPOLR1Ephysical
26344197
RBM19_HUMANRBM19physical
26344197
RL11_HUMANRPL11physical
27856536
CDT1_HUMANCDT1physical
25990725
CDC6_HUMANCDC6physical
25990725
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 GRWD1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-344, 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-119 AND SER-122, ANDMASS 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 THR-10, AND MASSSPECTROMETRY.

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