GLYR1_HUMAN - dbPTM
GLYR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLYR1_HUMAN
UniProt AC Q49A26
Protein Name Putative oxidoreductase GLYR1
Gene Name GLYR1
Organism Homo sapiens (Human).
Sequence Length 553
Subcellular Localization Nucleus .
Protein Description Putative oxidoreductase that is recruited on chromatin and promotes KDM1B demethylase activity. [PubMed: 23260659 Recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3)]
Protein Sequence MAAVSLRLGDLVWGKLGRYPPWPGKIVNPPKDLKKPRGKKCFFVKFFGTEDHAWIKVEQLKPYHAHKEEMIKINKGKRFQQAVDAVEEFLRRAKGKDQTSSHNSSDDKNRRNSSEERSRPNSGDEKRKLSLSEGKVKKNMGEGKKRVSSGSSERGSKSPLKRAQEQSPRKRGRPPKDEKDLTIPESSTVKGMMAGPMAAFKWQPTASEPVKDADPHFHHFLLSQTEKPAVCYQAITKKLKICEEETGSTSIQAADSTAVNGSITPTDKKIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEKCDLFIQEGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGVLQGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFLGEVGNAAKMMLIVNMVQGSFMATIAEGLTLAHVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYIQKDLRLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAYIH
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
25AcetylationRYPPWPGKIVNPPKD
CCCCCCCCCCCCCHH		39.1319608861
61UbiquitinationWIKVEQLKPYHAHKE
EEEHHHCCCCCCCHH		43.13-
63PhosphorylationKVEQLKPYHAHKEEM
EHHHCCCCCCCHHHH		15.2820860994
72AcetylationAHKEEMIKINKGKRF
CCHHHHHCCCCCHHH		38.6390479
77AcetylationMIKINKGKRFQQAVD
HHCCCCCHHHHHHHH		52.2090483
91MethylationDAVEEFLRRAKGKDQ
HHHHHHHHHHCCCCC		41.66115484343
96MethylationFLRRAKGKDQTSSHN
HHHHHCCCCCCCCCC		46.05-
99PhosphorylationRAKGKDQTSSHNSSD
HHCCCCCCCCCCCCC		42.1823312004
100PhosphorylationAKGKDQTSSHNSSDD
HCCCCCCCCCCCCCC		24.7823312004
101PhosphorylationKGKDQTSSHNSSDDK
CCCCCCCCCCCCCCC		30.0323312004
104PhosphorylationDQTSSHNSSDDKNRR
CCCCCCCCCCCCCCC		29.7123312004
105PhosphorylationQTSSHNSSDDKNRRN
CCCCCCCCCCCCCCC		55.9623312004
108MethylationSHNSSDDKNRRNSSE
CCCCCCCCCCCCCHH		58.29-
113PhosphorylationDDKNRRNSSEERSRP
CCCCCCCCHHHHHCC		37.0025884760
114PhosphorylationDKNRRNSSEERSRPN
CCCCCCCHHHHHCCC		47.2125159151
118PhosphorylationRNSSEERSRPNSGDE
CCCHHHHHCCCCHHH		56.2026074081
122PhosphorylationEERSRPNSGDEKRKL
HHHHCCCCHHHHHHC		50.7528176443
130 (in isoform 5)Ubiquitination-32.6521890473
130PhosphorylationGDEKRKLSLSEGKVK
HHHHHHCHHCCCCHH		32.6529255136
132PhosphorylationEKRKLSLSEGKVKKN
HHHHCHHCCCCHHCC		40.7130266825
135SumoylationKLSLSEGKVKKNMGE
HCHHCCCCHHCCCCC		46.9928112733
135AcetylationKLSLSEGKVKKNMGE
HCHHCCCCHHCCCCC		46.9923749302
142 (in isoform 4)Ubiquitination-58.0121890473
148PhosphorylationGEGKKRVSSGSSERG
CCCCCCCCCCCCCCC		32.7725849741
149PhosphorylationEGKKRVSSGSSERGS
CCCCCCCCCCCCCCC		39.5826074081
151PhosphorylationKKRVSSGSSERGSKS
CCCCCCCCCCCCCCC		30.8528176443
152PhosphorylationKRVSSGSSERGSKSP
CCCCCCCCCCCCCCH		34.5326074081
156PhosphorylationSGSSERGSKSPLKRA
CCCCCCCCCCHHHHH		35.8626074081
158PhosphorylationSSERGSKSPLKRAQE
CCCCCCCCHHHHHHH		36.8422167270
167PhosphorylationLKRAQEQSPRKRGRP
HHHHHHHCCCCCCCC		26.3926329039
176SumoylationRKRGRPPKDEKDLTI
CCCCCCCCCCCCCCC		79.7028112733
179SumoylationGRPPKDEKDLTIPES
CCCCCCCCCCCCCCC		69.0828112733
182PhosphorylationPKDEKDLTIPESSTV
CCCCCCCCCCCCCCC		44.6220068231
186PhosphorylationKDLTIPESSTVKGMM
CCCCCCCCCCCCCCE		26.4220068231
187PhosphorylationDLTIPESSTVKGMMA
CCCCCCCCCCCCCEE		35.2430576142
188PhosphorylationLTIPESSTVKGMMAG
CCCCCCCCCCCCEEC		35.2030576142
190UbiquitinationIPESSTVKGMMAGPM
CCCCCCCCCCEECCE		40.97-
201UbiquitinationAGPMAAFKWQPTASE
ECCEEECCCCCCCCC		39.94-
201SumoylationAGPMAAFKWQPTASE
ECCEEECCCCCCCCC		39.9428112733
205PhosphorylationAAFKWQPTASEPVKD
EECCCCCCCCCCCCC		27.9328555341
211 (in isoform 1)Ubiquitination-58.8921890473
211 (in isoform 2)Ubiquitination-58.8921890473
211SumoylationPTASEPVKDADPHFH
CCCCCCCCCCCCCHH		58.8928112733
211UbiquitinationPTASEPVKDADPHFH
CCCCCCCCCCCCCHH		58.8921890473
211 (in isoform 3)Ubiquitination-58.8921890473
227UbiquitinationFLLSQTEKPAVCYQA
HHCCCCCCCHHHHHH		41.48-
227AcetylationFLLSQTEKPAVCYQA
HHCCCCCCCHHHHHH		41.48164497443
227SumoylationFLLSQTEKPAVCYQA
HHCCCCCCCHHHHHH		41.4828112733
232PhosphorylationTEKPAVCYQAITKKL
CCCCHHHHHHHHHHH		8.3825159151
237UbiquitinationVCYQAITKKLKICEE
HHHHHHHHHHCCCHH		50.42-
237SumoylationVCYQAITKKLKICEE
HHHHHHHHHHCCCHH		50.4228112733
240SumoylationQAITKKLKICEEETG
HHHHHHHCCCHHHHC		54.9428112733
246PhosphorylationLKICEEETGSTSIQA
HCCCHHHHCCCEEEE		39.4524260401
256PhosphorylationTSIQAADSTAVNGSI
CEEEECCCCCCCCCC		17.3428348404
257 (in isoform 5)Ubiquitination-34.8621890473
257PhosphorylationSIQAADSTAVNGSIT
EEEECCCCCCCCCCC		34.8628348404
262PhosphorylationDSTAVNGSITPTDKK
CCCCCCCCCCCCCCC		20.3428674419
264PhosphorylationTAVNGSITPTDKKIG
CCCCCCCCCCCCCEE		23.1028348404
269SumoylationSITPTDKKIGFLGLG
CCCCCCCCEEEECCC		51.3628112733
269 (in isoform 4)Ubiquitination-51.3621890473
269SumoylationSITPTDKKIGFLGLG
CCCCCCCCEEEECCC		51.36-
280PhosphorylationLGLGLMGSGIVSNLL
ECCCCCCCCHHHHHH		16.04-
292PhosphorylationNLLKMGHTVTVWNRT
HHHHCCCEEEEEECC		16.49-
294PhosphorylationLKMGHTVTVWNRTAE
HHCCCEEEEEECCHH		22.43-
302UbiquitinationVWNRTAEKCDLFIQE
EEECCHHHCCEEEEC		30.50-
302SumoylationVWNRTAEKCDLFIQE
EEECCHHHCCEEEEC		30.5028112733
303GlutathionylationWNRTAEKCDLFIQEG
EECCHHHCCEEEECC		4.0722555962
321 (in isoform 2)Ubiquitination-2.7021890473
332 (in isoform 3)Ubiquitination-48.3421890473
335UbiquitinationFACVSDPKAAKDLVL
EEEECCHHHHHHCEE		67.00-
338UbiquitinationVSDPKAAKDLVLGPS
ECCHHHHHHCEECCC		57.3521890473
338 (in isoform 1)Ubiquitination-57.3521890473
345PhosphorylationKDLVLGPSGVLQGIR
HHCEECCCHHCCCCC		39.4721406692
414 (in isoform 5)Ubiquitination-42.3221890473
426 (in isoform 4)Ubiquitination-9.5621890473
454 (in isoform 5)Ubiquitination-18.2321890473
466 (in isoform 4)Ubiquitination-39.0921890473
478 (in isoform 2)Ubiquitination-7.8421890473
489 (in isoform 3)Ubiquitination-0.9421890473
495 (in isoform 1)Ubiquitination-47.9121890473
495UbiquitinationNILQGNFKPDFYLKY
HHHCCCCCCCHHHHH		47.9121890473
499PhosphorylationGNFKPDFYLKYIQKD
CCCCCCHHHHHHHHH		15.0623898821
502PhosphorylationKPDFYLKYIQKDLRL
CCCHHHHHHHHHHHH		13.1423898821
505UbiquitinationFYLKYIQKDLRLAIA
HHHHHHHHHHHHHHH		49.53-
518 (in isoform 2)Ubiquitination-36.8221890473
529 (in isoform 3)Ubiquitination-42.3621890473
532UbiquitinationAAANEVYKRAKALDQ
HHHHHHHHHHHHHCC		51.56-
535 (in isoform 1)Ubiquitination-54.2221890473
535UbiquitinationNEVYKRAKALDQSDN
HHHHHHHHHHCCCCC		54.2221890473
540PhosphorylationRAKALDQSDNDMSAV
HHHHHCCCCCHHHHH		37.7423401153
545PhosphorylationDQSDNDMSAVYRAYI
CCCCCHHHHHHHHHC		19.9030108239
548PhosphorylationDNDMSAVYRAYIH--
CCHHHHHHHHHCC--		6.8321406692
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
-KUbiquitinationE3 ubiquitin ligaseSPOPO43791
PMID:25278611
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLYR1_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 GLYR1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KDM1A_HUMANKDM1Aphysical
23455924
NSD3_HUMANWHSC1L1physical
23455924
CF206_HUMANC6orf165physical
25416956
NFH_HUMANNEFHphysical
26186194
BLK_HUMANBLKphysical
26186194
HUTH_HUMANHALphysical
26186194
KDM1B_HUMANKDM1Bphysical
26186194
PLSL_HUMANLCP1physical
26186194
SPA12_HUMANSERPINA12physical
26186194
CPNS2_HUMANCAPNS2physical
26186194
FNTB_HUMANFNTBphysical
26186194
LOXE3_HUMANALOXE3physical
26186194
NOC2L_HUMANNOC2Lphysical
26344197
KDM1B_HUMANKDM1Bphysical
28514442
SPA12_HUMANSERPINA12physical
28514442
FNTB_HUMANFNTBphysical
28514442
CPNS2_HUMANCAPNS2physical
28514442
ECM1_HUMANECM1physical
28514442
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 GLYR1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-25, AND MASS SPECTROMETRY.
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-540, AND MASSSPECTROMETRY.
"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-130 AND SER-132, ANDMASS SPECTROMETRY.
"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-130; SER-132 ANDSER-167, AND MASS SPECTROMETRY.

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