GEPH_RAT - dbPTM
GEPH_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GEPH_RAT
UniProt AC Q03555
Protein Name Gephyrin
Gene Name Gphn
Organism Rattus norvegicus (Rat).
Sequence Length 768
Subcellular Localization Cell junction, synapse . Cell junction, synapse, postsynaptic cell membrane
Peripheral membrane protein
Cytoplasmic side . Cytoplasm, cytoskeleton . Cell membrane
Peripheral membrane protein
Cytoplasmic side . Cell projection, dendrite . Cyto
Protein Description Microtubule-associated protein involved in membrane protein-cytoskeleton interactions. It is thought to anchor the inhibitory glycine receptor (GLYR) to subsynaptic microtubules. [PubMed: 8264797 Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released]
Protein Sequence MATEGMILTNHDHQIRVGVLTVSDSCFRNLAEDRSGINLKDLVQDPSLLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTTGGTGFAPRDVTPEKFPTFPFCGLQKGATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPHAIDLLRDAIVKVKEVHDELEDLPSPPPPLSPPPTTSPHKQTEDKGVQCEEEEEEKKDSGVASTEDSSSSHITAAALAAKIPDSIISRGVQVLPRDTASLSTTPSESPRAQATSRLSTASCPTPKQIRRPDESKGVASRVGSLKVQSRCSSKENILRASHSAVDITKVARRHRMSPFPLTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTQTVMPGQVMRVTTGAPIPCGADAVVQVEDTELIRESDDGTEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGEKDYLKQVLDIDLHAQIHFGRVFMKPGLPTTFATLDIDGVRKIIFALPGNPVSAVVTCNLFVVPALRKMQGILDPRPTIIKARLSCDVKLDPRPEYHRCILTWHHQEPLPWAQSTGNQMSSRLMSMRSANGLLMLPPKTEQYVELHKGEVVDVMVIGRL
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
151AcetylationPVCGIRGKTLIINLP
CCCEECCCEEEEECC		30.2455874043
160AcetylationLIINLPGSKKGSQEC
EEEECCCCCCCHHHH		29.2936747285
161AcetylationIINLPGSKKGSQECF
EEECCCCCCCHHHHH		68.0522902405
201PhosphorylationDELEDLPSPPPPLSP
HHHHCCCCCCCCCCC		58.2928825834
207PhosphorylationPSPPPPLSPPPTTSP
CCCCCCCCCCCCCCC		40.9328825834
211PhosphorylationPPLSPPPTTSPHKQT
CCCCCCCCCCCCCCC		45.7627097102
212PhosphorylationPLSPPPTTSPHKQTE
CCCCCCCCCCCCCCC		46.1427097102
212S-palmitoylationPLSPPPTTSPHKQTE
CCCCCCCCCCCCCCC		46.1425025157
213PhosphorylationLSPPPTTSPHKQTED
CCCCCCCCCCCCCCC		27.7330411139
218PhosphorylationTTSPHKQTEDKGVQC
CCCCCCCCCCCCCCC		51.4522351777
225S-palmitoylationTEDKGVQCEEEEEEK
CCCCCCCCCHHHHHH		7.07-
235PhosphorylationEEEEKKDSGVASTED
HHHHHHCCCCCCCCC		44.0122351777
239PhosphorylationKKDSGVASTEDSSSS
HHCCCCCCCCCCCCH		29.8922351777
240PhosphorylationKDSGVASTEDSSSSH
HCCCCCCCCCCCCHH		33.7922351777
243PhosphorylationGVASTEDSSSSHITA
CCCCCCCCCCHHHHH		26.3630181290
244PhosphorylationVASTEDSSSSHITAA
CCCCCCCCCHHHHHH		48.4530181290
260AcetylationLAAKIPDSIISRGVQ
HHCCCCHHHHHCCCE		19.2355874037
263AcetylationKIPDSIISRGVQVLP
CCCHHHHHCCCEECC		22.7036747287
273PhosphorylationVQVLPRDTASLSTTP
CEECCCCCCCCCCCC		21.3027097102
275PhosphorylationVLPRDTASLSTTPSE
ECCCCCCCCCCCCCC		25.5827097102
275AcetylationVLPRDTASLSTTPSE
ECCCCCCCCCCCCCC		25.584042801
277PhosphorylationPRDTASLSTTPSESP
CCCCCCCCCCCCCCC		27.9527097102
278AcetylationRDTASLSTTPSESPR
CCCCCCCCCCCCCCC		48.284042809
278PhosphorylationRDTASLSTTPSESPR
CCCCCCCCCCCCCCC		48.2827097102
279AcetylationDTASLSTTPSESPRA
CCCCCCCCCCCCCCC		22.801919159
279PhosphorylationDTASLSTTPSESPRA
CCCCCCCCCCCCCCC		22.8027097102
281AcetylationASLSTTPSESPRAQA
CCCCCCCCCCCCCHH		48.921919161
281PhosphorylationASLSTTPSESPRAQA
CCCCCCCCCCCCCHH		48.9227097102
283PhosphorylationLSTTPSESPRAQATS
CCCCCCCCCCCHHCC		24.8328689409
284S-palmitoylationSTTPSESPRAQATSR
CCCCCCCCCCHHCCC		31.4125025157
289PhosphorylationESPRAQATSRLSTAS
CCCCCHHCCCCCCCC		11.4225575281
290PhosphorylationSPRAQATSRLSTASC
CCCCHHCCCCCCCCC		33.9522351777
293PhosphorylationAQATSRLSTASCPTP
CHHCCCCCCCCCCCH		22.3325403869
294PhosphorylationQATSRLSTASCPTPK
HHCCCCCCCCCCCHH		27.4725403869
296PhosphorylationTSRLSTASCPTPKQI
CCCCCCCCCCCHHHC		22.2525403869
297S-palmitoylationSRLSTASCPTPKQIR
CCCCCCCCCCHHHCC		3.95-
299PhosphorylationLSTASCPTPKQIRRP
CCCCCCCCHHHCCCC		47.6625403869
318PhosphorylationGVASRVGSLKVQSRC
CCHHHHCCCEEECCC		23.3516452087
323PhosphorylationVGSLKVQSRCSSKEN
HCCCEEECCCCCHHH		37.9416452087
326PhosphorylationLKVQSRCSSKENILR
CEEECCCCCHHHHHH		43.2525575281
327PhosphorylationKVQSRCSSKENILRA
EEECCCCCHHHHHHH		47.8427097102
335PhosphorylationKENILRASHSAVDIT
HHHHHHHHHHHHHHH		16.1325403869
337PhosphorylationNILRASHSAVDITKV
HHHHHHHHHHHHHHH		27.7428689409
351PhosphorylationVARRHRMSPFPLTSM
HHHHHCCCCCCCCCC		24.28-
356PhosphorylationRMSPFPLTSMDKAFI
CCCCCCCCCCCHHHE		23.4222351777
405AcetylationPPFPASVKDGYAVRA
CCCCCCCCCCEEEEE		42.8322902405
468AcetylationDTELIRESDDGTEEL
CCEEEEECCCCCCEE		31.0255874051
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
281SPhosphorylationKinaseMAPK1P28482
GPS
281SPhosphorylationKinaseMAPK3P27361
GPS
283SPhosphorylationKinaseCDK1P06493
PSP
283SPhosphorylationKinaseCDK2P24941
PSP
283SPhosphorylationKinaseCDK5Q00535
PSP
283SPhosphorylationKinaseCDK5Q03114
PSP
335SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
337SPhosphorylationKinasePKACAP17612
PSP
337SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GEPH_RAT !!
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 GEPH_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PROF1_RATPfn1physical
12967995
PROF2_RATPfn2physical
12967995
GLRB_RATGlrbphysical
16449194
DC1I1_RATDync1i1physical
16449194
DYHC1_RATDync1h1physical
16449194
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GEPH_RAT

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Related Literatures of Post-Translational Modification

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