GEPH_HUMAN - dbPTM
GEPH_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GEPH_HUMAN
UniProt AC Q9NQX3
Protein Name Gephyrin {ECO:0000303|PubMed:10839351}
Gene Name GPHN {ECO:0000312|HGNC:HGNC:15465}
Organism Homo sapiens (Human).
Sequence Length 736
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. 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 MATEGMILTNHDHQIRVGVLTVSDSCFRNLAEDRSGINLKDLVQDPSLLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTTGGTGFAPRDVTPEATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPHAIDLLRDAIVKVKEVHDELEDLPSPPPPLSPPPTTSPHKQTEDKGVQCEEEEEEKKDSGVASTEDSSSSHITAAAIAAKIPDSIISRGVQVLPRDTASLSTTPSESPRAQATSRLSTASCPTPKVQSRCSSKENILRASHSAVDITKVARRHRMSPFPLTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTQTVMPGQVMRVTTGAPIPCGADAVVQVEDTELIRESDDGTEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGEKDYLKQVLDIDLHAQIHFGRVFMKPGLPTTFATLDIDGVRKIIFALPGNPVSAVVTCNLFVVPALRKMQGILDPRPTIIKARLSCDVKLDPRPEYHRCILTWHHQEPLPWAQSTGNQMSSRLMSMRSANGLLMLPPKTEQYVELHKGEVVDVMVIGRL
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
3Phosphorylation-----MATEGMILTN
-----CCCCCEEEEC		31.6020068231
9PhosphorylationATEGMILTNHDHQIR
CCCCEEEECCCCEEE		21.4120068231
26GlutathionylationVLTVSDSCFRNLAED
EEEECHHHHHHHCCC		4.4522555962
34MethylationFRNLAEDRSGINLKD
HHHHCCCCCCCCHHH		28.43-
35PhosphorylationRNLAEDRSGINLKDL
HHHCCCCCCCCHHHH		57.2429083192
47PhosphorylationKDLVQDPSLLGGTIS
HHHCCCHHHCCCEEE		44.5129083192
52PhosphorylationDPSLLGGTISAYKIV
CHHHCCCEEEEEEEC		15.2329083192
54PhosphorylationSLLGGTISAYKIVPD
HHCCCEEEEEEECHH		25.9429083192
56PhosphorylationLGGTISAYKIVPDEI
CCCEEEEEEECHHHH		8.4129083192
57UbiquitinationGGTISAYKIVPDEIE
CCEEEEEEECHHHHH		36.6229967540
96PhosphorylationGFAPRDVTPEATKEV
CCCCCCCCHHHHHHH		21.50-
100PhosphorylationRDVTPEATKEVIERE
CCCCHHHHHHHHHHH		26.52-
1382-HydroxyisobutyrylationPVCGIRGKTLIINLP
CCCEECCCEEEEECC		30.24-
139PhosphorylationVCGIRGKTLIINLPG
CCEECCCEEEEECCC		26.4718491316
147PhosphorylationLIINLPGSKKGSQEC
EEEECCCCCCCHHHH		29.2920068231
188PhosphorylationDELEDLPSPPPPLSP
HHHHCCCCCCCCCCC		58.2929255136
191UbiquitinationEDLPSPPPPLSPPPT
HCCCCCCCCCCCCCC		45.9424816145
194PhosphorylationPSPPPPLSPPPTTSP
CCCCCCCCCCCCCCC		40.9329255136
198PhosphorylationPPLSPPPTTSPHKQT
CCCCCCCCCCCCCCC		45.7629255136
199PhosphorylationPLSPPPTTSPHKQTE
CCCCCCCCCCCCCCC		46.1429255136
200PhosphorylationLSPPPTTSPHKQTED
CCCCCCCCCCCCCCC		27.7329255136
205PhosphorylationTTSPHKQTEDKGVQC
CCCCCCCCCCCCCCC		51.4530266825
211UbiquitinationQTEDKGVQCEEEEEE
CCCCCCCCCCHHHHH		37.2624816145
212S-palmitoylationTEDKGVQCEEEEEEK
CCCCCCCCCHHHHHH		7.0725025157
215UbiquitinationKGVQCEEEEEEKKDS
CCCCCCHHHHHHHCC		48.7124816145
222 (in isoform 2)Phosphorylation-44.0129083192
226 (in isoform 2)Phosphorylation-29.8929083192
227 (in isoform 2)Phosphorylation-33.7929083192
230PhosphorylationGVASTEDSSSSHITA
CCCCCCCCCCCHHHH		26.3628555341
230 (in isoform 2)Phosphorylation-26.3629083192
231 (in isoform 2)Phosphorylation-48.4529083192
232 (in isoform 2)Phosphorylation-29.8629083192
233 (in isoform 2)Phosphorylation-22.3629083192
236 (in isoform 2)Phosphorylation-12.5729083192
247PhosphorylationIAAKIPDSIISRGVQ
HHHHCCHHHHHCCCE		19.2324719451
248 (in isoform 2)Phosphorylation-4.29-
249 (in isoform 2)Phosphorylation-2.38-
250PhosphorylationKIPDSIISRGVQVLP
HCCHHHHHCCCEECC		22.7020068231
250 (in isoform 2)Phosphorylation-22.70-
260O-linked_GlycosylationVQVLPRDTASLSTTP
CEECCCCCCCCCCCC		21.3028657654
260PhosphorylationVQVLPRDTASLSTTP
CEECCCCCCCCCCCC		21.3021815630
262PhosphorylationVLPRDTASLSTTPSE
ECCCCCCCCCCCCCC		25.5822167270
264PhosphorylationPRDTASLSTTPSESP
CCCCCCCCCCCCCCC		27.9530266825
265O-linked_GlycosylationRDTASLSTTPSESPR
CCCCCCCCCCCCCCC		48.2828657654
265PhosphorylationRDTASLSTTPSESPR
CCCCCCCCCCCCCCC		48.2830266825
266PhosphorylationDTASLSTTPSESPRA
CCCCCCCCCCCCCCC		22.8030266825
268PhosphorylationASLSTTPSESPRAQA
CCCCCCCCCCCCCHH		48.9230266825
270PhosphorylationLSTTPSESPRAQATS
CCCCCCCCCCCHHCC		24.8329255136
274UbiquitinationPSESPRAQATSRLST
CCCCCCCHHCCCCCC		46.5924816145
276PhosphorylationESPRAQATSRLSTAS
CCCCCHHCCCCCCCC		11.4223403867
277PhosphorylationSPRAQATSRLSTASC
CCCCHHCCCCCCCCC		33.9525159151
280PhosphorylationAQATSRLSTASCPTP
CHHCCCCCCCCCCCH		22.3330266825
281PhosphorylationQATSRLSTASCPTPK
HHCCCCCCCCCCCHH		27.4730266825
283PhosphorylationTSRLSTASCPTPKVQ
CCCCCCCCCCCHHHH		22.2530266825
283 (in isoform 2)Phosphorylation-22.2520068231
284S-palmitoylationSRLSTASCPTPKVQS
CCCCCCCCCCHHHHH		3.9525025157
286PhosphorylationLSTASCPTPKVQSRC
CCCCCCCCHHHHHHC		39.8230266825
288UbiquitinationTASCPTPKVQSRCSS
CCCCCCHHHHHHCCC		56.2224816145
291PhosphorylationCPTPKVQSRCSSKEN
CCCHHHHHHCCCHHH		37.9422617229
294PhosphorylationPKVQSRCSSKENILR
HHHHHHCCCHHHHHH		43.2530278072
295PhosphorylationKVQSRCSSKENILRA
HHHHHCCCHHHHHHH		47.8423401153
296UbiquitinationVQSRCSSKENILRAS
HHHHCCCHHHHHHHH		38.1929967540
301UbiquitinationSSKENILRASHSAVD
CCHHHHHHHHHHHHH		30.1924816145
303PhosphorylationKENILRASHSAVDIT
HHHHHHHHHHHHHHH		16.1330266825
305PhosphorylationNILRASHSAVDITKV
HHHHHHHHHHHHHHH		27.7423401153
310PhosphorylationSHSAVDITKVARRHR
HHHHHHHHHHHHHHC		18.2723403867
311UbiquitinationHSAVDITKVARRHRM
HHHHHHHHHHHHHCC		33.9433845483
319PhosphorylationVARRHRMSPFPLTSM
HHHHHCCCCCCCCCC		24.2818669648
321UbiquitinationRRHRMSPFPLTSMDK
HHHCCCCCCCCCCCH		6.4124816145
329UbiquitinationPLTSMDKAFITVLEM
CCCCCCHHHEEEEEC		9.2329967540
334UbiquitinationDKAFITVLEMTPVLG
CHHHEEEEECCCCCC		2.5224816145
344UbiquitinationTPVLGTEIINYRDGM
CCCCCCEEEECCCCC		2.1933845483
371PhosphorylationNLPPFPASVKDGYAV
CCCCCCCCCCCCEEE		29.9121406692
388UbiquitinationADGPGDRFIIGESQA
CCCCCCEEEEECCCC		5.9324816145
393PhosphorylationDRFIIGESQAGEQPT
CEEEEECCCCCCCCC		21.8124719451
400PhosphorylationSQAGEQPTQTVMPGQ
CCCCCCCCCCCCCCC		36.2424719451
402PhosphorylationAGEQPTQTVMPGQVM
CCCCCCCCCCCCCEE		22.65-
431UbiquitinationVVQVEDTELIRESDD
EEEECCCEEEEECCC		55.3024816145
451UbiquitinationEVRILVQARPGQDIR
EEEEEEECCCCCCCC		16.5024816145
465AcetylationRPIGHDIKRGECVLA
CCCCCCCCCCCEEEE		61.4819413330
465UbiquitinationRPIGHDIKRGECVLA
CCCCCCCCCCCEEEE		61.4824816145
478UbiquitinationLAKGTHMGPSEIGLL
EECCCCCCHHHHEEE		18.2524816145
480PhosphorylationKGTHMGPSEIGLLAT
CCCCCCHHHHEEEEE		35.80-
484UbiquitinationMGPSEIGLLATVGVT
CCHHHHEEEEEECCC		3.4524816145
489UbiquitinationIGLLATVGVTEVEVN
HEEEEEECCCEEECC		19.1024816145
497UbiquitinationVTEVEVNKFPVVAVM
CCEEECCCCCEEEEE		57.1124816145
498AcetylationTEVEVNKFPVVAVMS
CEEECCCCCEEEEEE		4.7219413330
498UbiquitinationTEVEVNKFPVVAVMS
CEEECCCCCEEEEEE		4.7224816145
502UbiquitinationVNKFPVVAVMSTGNE
CCCCCEEEEEECCCC		7.4824816145
505UbiquitinationFPVVAVMSTGNELLN
CCEEEEEECCCCCCC		26.9424816145
508UbiquitinationVAVMSTGNELLNPED
EEEEECCCCCCCCCC		36.5124816145
511UbiquitinationMSTGNELLNPEDDLL
EECCCCCCCCCCCCC		9.0724816145
518UbiquitinationLNPEDDLLPGKIRDS
CCCCCCCCCCCCCCC		7.2724816145
521UbiquitinationEDDLLPGKIRDSNRS
CCCCCCCCCCCCCCC		32.4024816145
530UbiquitinationRDSNRSTLLATIQEH
CCCCCCCEEHHHHHH		3.0224816145
535UbiquitinationSTLLATIQEHGYPTI
CCEEHHHHHHCCCEE		32.0724816145
541UbiquitinationIQEHGYPTINLGIVG
HHHHCCCEEEEEEEC		17.6424816145
551UbiquitinationLGIVGDNPDDLLNAL
EEEECCCHHHHHHHH		41.0324816145
554UbiquitinationVGDNPDDLLNALNEG
ECCCHHHHHHHHHHC		5.3224816145
570PhosphorylationSRADVIITSGGVSMG
CCCCEEEECCCCCCC		15.36-
571PhosphorylationRADVIITSGGVSMGE
CCCEEEECCCCCCCC		24.12-
575PhosphorylationIITSGGVSMGEKDYL
EEECCCCCCCCHHHH		25.09-
607PhosphorylationFMKPGLPTTFATLDI
ECCCCCCCEEEEECC		39.3220068231
608PhosphorylationMKPGLPTTFATLDID
CCCCCCCEEEEECCC		14.8820068231
611PhosphorylationGLPTTFATLDIDGVR
CCCCEEEEECCCCCE		22.2920068231
655PhosphorylationGILDPRPTIIKARLS
CCCCCCCCEEEEEEE		36.29-
666AcetylationARLSCDVKLDPRPEY
EEEECCEECCCCCCC		33.6425953088
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 GEPH_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GEPH_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 GEPH_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARHG9_HUMANARHGEF9physical
10607391
MTOR_HUMANMTORphysical
10325225
SPAS1_HUMANSPATS1physical
21988832
GEPH_HUMANGPHNphysical
21988832
KHDR1_HUMANKHDRBS1physical
21988832
BRCC3_HUMANBRCC3physical
22863883
PAAF1_HUMANPAAF1physical
22863883
PP4R1_HUMANPPP4R1physical
22863883
ROCK2_HUMANROCK2physical
22863883
SPTN1_HUMANSPTAN1physical
22863883
VASP_HUMANVASPphysical
16376568
ENAH_HUMANENAHphysical
16376568
Drug and Disease Associations
Kegg Disease
H00192 Xanthinuria
H00769 Hyperekplexia
OMIM Disease
615501Molybdenum cofactor deficiency, complementation group C (MOCODC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GEPH_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-188 AND SER-194, ANDMASS 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-270 AND THR-286, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-266 AND THR-286, ANDMASS SPECTROMETRY.

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