GEPH_MOUSE - dbPTM
GEPH_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GEPH_MOUSE
UniProt AC Q8BUV3
Protein Name Gephyrin
Gene Name Gphn
Organism Mus musculus (Mouse).
Sequence Length 769
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 MATEGMILTNHDHQIRVGVLTVSDSCFRNLAEDRSGINLKDLVQDPSLLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTTGGTGFAPRDVTPEATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPHAIDLLRDAIVKVKEVHDELEDLPSPPPPLSPPPTTSPHKQTEDKGVQCEEEEEEKKDSGVASTEDSSSSHITAAALAAKIPDSIISRGVQVLPRDTASLSTTPSESPRAQATSRLSTASCPTPKQIRRPDESKGVASRVGSLKARLPSCSSTYSVSEVQSRCSSKENILRASHSAVDITKVARRHRMSPFPLTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTQTVMPGQVMRVTTGAPIPCGADAVVQVEDTELIRESDDGTEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGEKDYLKQVLDIDLHAQIHFGRVFMKPGLPTTFATLDIDGVRKIIFALPGNPVSAVVTCNLFVVPALRKMQGILDPRPTIIKARLSCDVKLDPRPEYHRCILTWHHQEPLPWAQSTGNQMSSRLMSMRSANGLLMLPPKTEQYVELHKGEVVDVMVIGRL
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
23PhosphorylationRVGVLTVSDSCFRNL
EEEEEEECHHHHHHH
20.6929472430
25PhosphorylationGVLTVSDSCFRNLAE
EEEEECHHHHHHHCC
13.9829472430
26S-palmitoylationVLTVSDSCFRNLAED
EEEECHHHHHHHCCC
4.4528526873
26GlutathionylationVLTVSDSCFRNLAED
EEEECHHHHHHHCCC
4.4524333276
35PhosphorylationRNLAEDRSGINLKDL
HHHCCCCCCCCHHHH
57.2429550500
101UbiquitinationDVTPEATKEVIEREA
CCCHHHHHHHHHHHC
57.96-
147PhosphorylationLIINLPGSKKGSQEC
EEEECCCCCCCHHHH
29.2929472430
148UbiquitinationIINLPGSKKGSQECF
EEECCCCCCCHHHHH
68.05-
148MalonylationIINLPGSKKGSQECF
EEECCCCCCCHHHHH
68.0526320211
148AcetylationIINLPGSKKGSQECF
EEECCCCCCCHHHHH
68.052390343
188PhosphorylationDELEDLPSPPPPLSP
HHHHCCCCCCCCCCC
58.2925521595
194PhosphorylationPSPPPPLSPPPTTSP
CCCCCCCCCCCCCCC
40.9325521595
198PhosphorylationPPLSPPPTTSPHKQT
CCCCCCCCCCCCCCC
45.7625521595
199PhosphorylationPLSPPPTTSPHKQTE
CCCCCCCCCCCCCCC
46.1425521595
200PhosphorylationLSPPPTTSPHKQTED
CCCCCCCCCCCCCCC
27.7325521595
205PhosphorylationTTSPHKQTEDKGVQC
CCCCCCCCCCCCCCC
51.4519060867
212S-palmitoylationTEDKGVQCEEEEEEK
CCCCCCCCCHHHHHH
7.07-
222PhosphorylationEEEEKKDSGVASTED
HHHHHHCCCCCCCCC
44.0129899451
226PhosphorylationKKDSGVASTEDSSSS
HHCCCCCCCCCCCCH
29.8929899451
227PhosphorylationKDSGVASTEDSSSSH
HCCCCCCCCCCCCHH
33.7930352176
231PhosphorylationVASTEDSSSSHITAA
CCCCCCCCCHHHHHH
48.4529899451
232PhosphorylationASTEDSSSSHITAAA
CCCCCCCCHHHHHHH
29.8629899451
233PhosphorylationSTEDSSSSHITAAAL
CCCCCCCHHHHHHHH
22.3629899451
236O-linked_GlycosylationDSSSSHITAAALAAK
CCCCHHHHHHHHHCC
12.5755412099
236PhosphorylationDSSSSHITAAALAAK
CCCCHHHHHHHHHCC
12.5729899451
243UbiquitinationTAAALAAKIPDSIIS
HHHHHHCCCCHHHHH
49.5222790023
260PhosphorylationVQVLPRDTASLSTTP
CEECCCCCCCCCCCC
21.3025619855
260O-linked_GlycosylationVQVLPRDTASLSTTP
CEECCCCCCCCCCCC
21.3034802821
262PhosphorylationVLPRDTASLSTTPSE
ECCCCCCCCCCCCCC
25.5825521595
264PhosphorylationPRDTASLSTTPSESP
CCCCCCCCCCCCCCC
27.9525521595
265PhosphorylationRDTASLSTTPSESPR
CCCCCCCCCCCCCCC
48.2825521595
266PhosphorylationDTASLSTTPSESPRA
CCCCCCCCCCCCCCC
22.8025521595
268PhosphorylationASLSTTPSESPRAQA
CCCCCCCCCCCCCHH
48.9225521595
270PhosphorylationLSTTPSESPRAQATS
CCCCCCCCCCCHHCC
24.8325521595
276PhosphorylationESPRAQATSRLSTAS
CCCCCHHCCCCCCCC
11.4222324799
277PhosphorylationSPRAQATSRLSTASC
CCCCHHCCCCCCCCC
33.9522324799
280PhosphorylationAQATSRLSTASCPTP
CHHCCCCCCCCCCCH
22.3325521595
281PhosphorylationQATSRLSTASCPTPK
HHCCCCCCCCCCCHH
27.4719060867
283PhosphorylationTSRLSTASCPTPKQI
CCCCCCCCCCCHHHC
22.2525521595
284GlutathionylationSRLSTASCPTPKQIR
CCCCCCCCCCHHHCC
3.9524333276
284S-nitrosylationSRLSTASCPTPKQIR
CCCCCCCCCCHHHCC
3.9522178444
284S-palmitoylationSRLSTASCPTPKQIR
CCCCCCCCCCHHHCC
3.95-
284S-nitrosocysteineSRLSTASCPTPKQIR
CCCCCCCCCCHHHCC
3.95-
286PhosphorylationLSTASCPTPKQIRRP
CCCCCCCCHHHCCCC
47.6625521595
301PhosphorylationDESKGVASRVGSLKA
CCCCCHHHHHHCCEE
25.7022324799
305PhosphorylationGVASRVGSLKARLPS
CHHHHHHCCEEECCC
24.6829899451
312PhosphorylationSLKARLPSCSSTYSV
CCEEECCCCCCCCCH
31.0929899451
324PhosphorylationYSVSEVQSRCSSKEN
CCHHHHHHHHCCHHH
40.1924759943
327PhosphorylationSEVQSRCSSKENILR
HHHHHHHCCHHHHHH
43.2525159016
328PhosphorylationEVQSRCSSKENILRA
HHHHHHCCHHHHHHH
47.8425159016
329MalonylationVQSRCSSKENILRAS
HHHHHCCHHHHHHHH
38.1926320211
336PhosphorylationKENILRASHSAVDIT
HHHHHHHHHHHHHHH
16.1325521595
338PhosphorylationNILRASHSAVDITKV
HHHHHHHHHHHHHHH
27.7425521595
343PhosphorylationSHSAVDITKVARRHR
HHHHHHHHHHHHHHC
18.2725777480
344UbiquitinationHSAVDITKVARRHRM
HHHHHHHHHHHHHCC
33.94-
352PhosphorylationVARRHRMSPFPLTSM
HHHHHCCCCCCCCCC
24.2825521595
357PhosphorylationRMSPFPLTSMDKAFI
CCCCCCCCCCCHHHE
23.42-
406AcetylationPPFPASVKDGYAVRA
CCCCCCCCCCEEEEE
42.8323954790
498AcetylationRPIGHDIKRGECVLA
CCCCCCCCCCCEEEE
61.4815618151
635AcetylationHFGRVFMKPGLPTTF
EECCEECCCCCCCEE
25.1923954790
678UbiquitinationFVVPALRKMQGILDP
EHHHHHHHHCCCCCC
36.10-
699AcetylationARLSCDVKLDPRPEY
EEEECCEECCCCCCC
33.647622373
748AcetylationGLLMLPPKTEQYVEL
CCEECCCCCHHHEEE
63.8623954790

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
270SPhosphorylationKinaseGSK3BP49841
PSP
270SPhosphorylationKinaseGSK3BQ9WV60
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GEPH_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of GEPH_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GEPH_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-194, ANDMASS SPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-194, ANDMASS SPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, AND MASSSPECTROMETRY.

TOP