QRIC1_HUMAN - dbPTM
QRIC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID QRIC1_HUMAN
UniProt AC Q2TAL8
Protein Name Glutamine-rich protein 1
Gene Name QRICH1
Organism Homo sapiens (Human).
Sequence Length 776
Subcellular Localization
Protein Description
Protein Sequence MNNSLENTISFEEYIRVKARSVPQHRMKEFLDSLASKGPEALQEFQQTATTTMVYQQGGNCIYTDSTEVAGSLLELACPVTTSVQPQTQQEQQIQVQQPQQVQVQVQVQQSPQQVSAQLSPQLTVHQPTEQPIQVQVQIQGQAPQSAAPSIQTPSLQSPSPSQLQAAQIQVQHVQAAQQIQAAEIPEEHIPHQQIQAQLVAGQSLAGGQQIQIQTVGALSPPPSQQGSPREGERRVGTASVLQPVKKRKVDMPITVSYAISGQPVATVLAIPQGQQQSYVSLRPDLLTVDSAHLYSATGTITSPTGETWTIPVYSAQPRGDPQQQSITHIAIPQEAYNAVHVSGSPTALAAVKLEDDKEKMVGTTSVVKNSHEEVVQTLANSLFPAQFMNGNIHIPVAVQAVAGTYQNTAQTVHIWDPQQQPQQQTPQEQTPPPQQQQQQLQVTCSAQTVQVAEVEPQSQPQPSPELLLPNSLKPEEGLEVWKNWAQTKNAELEKDAQNRLAPIGRRQLLRFQEDLISSAVAELNYGLCLMTREARNGEGEPYDPDVLYYIFLCIQKYLFENGRVDDIFSDLYYVRFTEWLHEVLKDVQPRVTPLGYVLPSHVTEEMLWECKQLGAHSPSTLLTTLMFFNTKYFLLKTVDQHMKLAFSKVLRQTKKNPSNPKDKSTSIRYLKALGIHQTGQKVTDDMYAEQTENPENPLRCPIKLYDFYLFKCPQSVKGRNDTFYLTPEPVVAPNSPIWYSVQPISREQMGQMLTRILVIREIQEAIAVANASTMH
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
1Acetylation-------MNNSLENT
-------CCCCCCCC		10.9222814378
14PhosphorylationNTISFEEYIRVKARS
CCCCHHHHHHHHHCC		6.19-
28SumoylationSVPQHRMKEFLDSLA
CCCHHHHHHHHHHHH		45.32-
28UbiquitinationSVPQHRMKEFLDSLA
CCCHHHHHHHHHHHH		45.3221890473
28SumoylationSVPQHRMKEFLDSLA
CCCHHHHHHHHHHHH		45.32-
215PhosphorylationGQQIQIQTVGALSPP
CCEEEEEEEEECCCC		23.6526074081
220PhosphorylationIQTVGALSPPPSQQG
EEEEEECCCCHHHCC		34.5226074081
224PhosphorylationGALSPPPSQQGSPRE
EECCCCHHHCCCCCC		40.6926074081
228PhosphorylationPPPSQQGSPREGERR
CCHHHCCCCCCCCCC		19.2226074081
238PhosphorylationEGERRVGTASVLQPV
CCCCCCCCHHHCCCC		16.9526074081
240PhosphorylationERRVGTASVLQPVKK
CCCCCCHHHCCCCCC		24.1725159151
246SumoylationASVLQPVKKRKVDMP
HHHCCCCCCCCCCCC		54.25-
246UbiquitinationASVLQPVKKRKVDMP
HHHCCCCCCCCCCCC		54.25-
246SumoylationASVLQPVKKRKVDMP
HHHCCCCCCCCCCCC		54.25-
246AcetylationASVLQPVKKRKVDMP
HHHCCCCCCCCCCCC		54.2525953088
247MethylationSVLQPVKKRKVDMPI
HHCCCCCCCCCCCCE		58.65116252817
247UbiquitinationSVLQPVKKRKVDMPI
HHCCCCCCCCCCCCE		58.65-
255O-linked_GlycosylationRKVDMPITVSYAISG
CCCCCCEEEEEEECC		9.4930059200
257O-linked_GlycosylationVDMPITVSYAISGQP
CCCCEEEEEEECCCE		10.5330059200
302PhosphorylationYSATGTITSPTGETW
EEEECEEECCCCCCE		28.6126074081
303PhosphorylationSATGTITSPTGETWT
EEECEEECCCCCCEE		19.3326074081
305PhosphorylationTGTITSPTGETWTIP
ECEEECCCCCCEEEE		47.6326074081
308PhosphorylationITSPTGETWTIPVYS
EECCCCCCEEEEEEE		29.2926074081
326PhosphorylationRGDPQQQSITHIAIP
CCCCCCCCEEEEECC		25.7229978859
328PhosphorylationDPQQQSITHIAIPQE
CCCCCCEEEEECCHH		16.6929978859
337PhosphorylationIAIPQEAYNAVHVSG
EECCHHHHHCEEECC		11.6927794612
343PhosphorylationAYNAVHVSGSPTALA
HHHCEEECCCCCEEE		20.7625159151
345PhosphorylationNAVHVSGSPTALAAV
HCEEECCCCCEEEEE		16.1523401153
347PhosphorylationVHVSGSPTALAAVKL
EEECCCCCEEEEEEC		35.6825159151
353UbiquitinationPTALAAVKLEDDKEK
CCEEEEEECCCCCHH		41.24-
353SumoylationPTALAAVKLEDDKEK
CCEEEEEECCCCCHH		41.2428112733
358SumoylationAVKLEDDKEKMVGTT
EEECCCCCHHEECCE		72.1228112733
360SumoylationKLEDDKEKMVGTTSV
ECCCCCHHEECCEEH		44.63-
360SumoylationKLEDDKEKMVGTTSV
ECCCCCHHEECCEEH		44.63-
360UbiquitinationKLEDDKEKMVGTTSV
ECCCCCHHEECCEEH		44.63-
361SulfoxidationLEDDKEKMVGTTSVV
CCCCCHHEECCEEHH		3.3521406390
364PhosphorylationDKEKMVGTTSVVKNS
CCHHEECCEEHHCCC		12.42-
364O-linked_GlycosylationDKEKMVGTTSVVKNS
CCHHEECCEEHHCCC		12.4230059200
365O-linked_GlycosylationKEKMVGTTSVVKNSH
CHHEECCEEHHCCCH		17.3730059200
371PhosphorylationTTSVVKNSHEEVVQT
CEEHHCCCHHHHHHH		26.93-
459PhosphorylationVAEVEPQSQPQPSPE
EEEECCCCCCCCCCC		55.3226074081
464PhosphorylationPQSQPQPSPELLLPN
CCCCCCCCCCCCCCC		26.2626657352
472PhosphorylationPELLLPNSLKPEEGL
CCCCCCCCCCHHHHH		35.5126074081
474SumoylationLLLPNSLKPEEGLEV
CCCCCCCCHHHHHHH		50.64-
489SumoylationWKNWAQTKNAELEKD
HHHHHHHCCHHHHHH		41.92-
489SumoylationWKNWAQTKNAELEKD
HHHHHHHCCHHHHHH		41.92-
489UbiquitinationWKNWAQTKNAELEKD
HHHHHHHCCHHHHHH		41.9221890473
495UbiquitinationTKNAELEKDAQNRLA
HCCHHHHHHHHHCCC		71.6221890473
500MethylationLEKDAQNRLAPIGRR
HHHHHHHCCCCCCHH		21.83115489779
586UbiquitinationEWLHEVLKDVQPRVT
HHHHHHHHHCCCCCC		62.11-
618PhosphorylationCKQLGAHSPSTLLTT
HHHCCCCCHHHHHHH		21.7320068231
620PhosphorylationQLGAHSPSTLLTTLM
HCCCCCHHHHHHHHH		34.4028270605
621PhosphorylationLGAHSPSTLLTTLMF
CCCCCHHHHHHHHHH		29.2228270605
624PhosphorylationHSPSTLLTTLMFFNT
CCHHHHHHHHHHHCH		22.4628270605
625PhosphorylationSPSTLLTTLMFFNTK
CHHHHHHHHHHHCHH		19.0528270605
631PhosphorylationTTLMFFNTKYFLLKT
HHHHHHCHHCHHHHH		23.2028270605
637UbiquitinationNTKYFLLKTVDQHMK
CHHCHHHHHHHHHHH		48.96-
644UbiquitinationKTVDQHMKLAFSKVL
HHHHHHHHHHHHHHH		34.24-
649UbiquitinationHMKLAFSKVLRQTKK
HHHHHHHHHHHHHCC		38.54-
649AcetylationHMKLAFSKVLRQTKK
HHHHHHHHHHHHHCC		38.5425953088
655MalonylationSKVLRQTKKNPSNPK
HHHHHHHCCCCCCCC		42.0626320211
659PhosphorylationRQTKKNPSNPKDKST
HHHCCCCCCCCCHHH		75.1423403867
662UbiquitinationKKNPSNPKDKSTSIR
CCCCCCCCCHHHHHH		80.28-
664UbiquitinationNPSNPKDKSTSIRYL
CCCCCCCHHHHHHHH		62.86-
672SumoylationSTSIRYLKALGIHQT
HHHHHHHHHCCCCCC		32.41-
672UbiquitinationSTSIRYLKALGIHQT
HHHHHHHHHCCCCCC		32.41-
672SumoylationSTSIRYLKALGIHQT
HHHHHHHHHCCCCCC		32.41-
679PhosphorylationKALGIHQTGQKVTDD
HHCCCCCCCCCCCCC		27.6728555341
682UbiquitinationGIHQTGQKVTDDMYA
CCCCCCCCCCCCCHH		48.7421890473
682AcetylationGIHQTGQKVTDDMYA
CCCCCCCCCCCCCHH		48.7426051181
684PhosphorylationHQTGQKVTDDMYAEQ
CCCCCCCCCCCHHHC		33.0620860994
704UbiquitinationNPLRCPIKLYDFYLF
CCCCCCEEEEEEEEE		26.57-
712UbiquitinationLYDFYLFKCPQSVKG
EEEEEEEECCCCCCC		42.2721890473
775SulfoxidationAVANASTMH------
HHHCHHCCC------		3.0621406390
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 QRIC1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of QRIC1_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 QRIC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NUDC3_HUMANNUDCD3physical
22863883
GLU2B_HUMANPRKCSHphysical
22863883
RL11_HUMANRPL11physical
22863883
SP16H_HUMANSUPT16Hphysical
22863883
QRIC1_HUMANQRICH1physical
25416956
GMCL1_HUMANGMCL1physical
25416956
SPF45_HUMANRBM17physical
25416956
HSFY1_HUMANHSFY1physical
25416956
A4_HUMANAPPphysical
15923395
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 QRIC1_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-345, AND MASSSPECTROMETRY.

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