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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
23 | Phosphorylation | RVGVLTVSDSCFRNL EEEEEEECHHHHHHH | 20.69 | 29472430 | |
25 | Phosphorylation | GVLTVSDSCFRNLAE EEEEECHHHHHHHCC | 13.98 | 29472430 | |
26 | S-palmitoylation | VLTVSDSCFRNLAED EEEECHHHHHHHCCC | 4.45 | 28526873 | |
26 | Glutathionylation | VLTVSDSCFRNLAED EEEECHHHHHHHCCC | 4.45 | 24333276 | |
35 | Phosphorylation | RNLAEDRSGINLKDL HHHCCCCCCCCHHHH | 57.24 | 29550500 | |
101 | Ubiquitination | DVTPEATKEVIEREA CCCHHHHHHHHHHHC | 57.96 | - | |
147 | Phosphorylation | LIINLPGSKKGSQEC EEEECCCCCCCHHHH | 29.29 | 29472430 | |
148 | Ubiquitination | IINLPGSKKGSQECF EEECCCCCCCHHHHH | 68.05 | - | |
148 | Malonylation | IINLPGSKKGSQECF EEECCCCCCCHHHHH | 68.05 | 26320211 | |
148 | Acetylation | IINLPGSKKGSQECF EEECCCCCCCHHHHH | 68.05 | 2390343 | |
188 | Phosphorylation | DELEDLPSPPPPLSP HHHHCCCCCCCCCCC | 58.29 | 25521595 | |
194 | Phosphorylation | PSPPPPLSPPPTTSP CCCCCCCCCCCCCCC | 40.93 | 25521595 | |
198 | Phosphorylation | PPLSPPPTTSPHKQT CCCCCCCCCCCCCCC | 45.76 | 25521595 | |
199 | Phosphorylation | PLSPPPTTSPHKQTE CCCCCCCCCCCCCCC | 46.14 | 25521595 | |
200 | Phosphorylation | LSPPPTTSPHKQTED CCCCCCCCCCCCCCC | 27.73 | 25521595 | |
205 | Phosphorylation | TTSPHKQTEDKGVQC CCCCCCCCCCCCCCC | 51.45 | 19060867 | |
212 | S-palmitoylation | TEDKGVQCEEEEEEK CCCCCCCCCHHHHHH | 7.07 | - | |
222 | Phosphorylation | EEEEKKDSGVASTED HHHHHHCCCCCCCCC | 44.01 | 29899451 | |
226 | Phosphorylation | KKDSGVASTEDSSSS HHCCCCCCCCCCCCH | 29.89 | 29899451 | |
227 | Phosphorylation | KDSGVASTEDSSSSH HCCCCCCCCCCCCHH | 33.79 | 30352176 | |
231 | Phosphorylation | VASTEDSSSSHITAA CCCCCCCCCHHHHHH | 48.45 | 29899451 | |
232 | Phosphorylation | ASTEDSSSSHITAAA CCCCCCCCHHHHHHH | 29.86 | 29899451 | |
233 | Phosphorylation | STEDSSSSHITAAAL CCCCCCCHHHHHHHH | 22.36 | 29899451 | |
236 | O-linked_Glycosylation | DSSSSHITAAALAAK CCCCHHHHHHHHHCC | 12.57 | 55412099 | |
236 | Phosphorylation | DSSSSHITAAALAAK CCCCHHHHHHHHHCC | 12.57 | 29899451 | |
243 | Ubiquitination | TAAALAAKIPDSIIS HHHHHHCCCCHHHHH | 49.52 | 22790023 | |
260 | Phosphorylation | VQVLPRDTASLSTTP CEECCCCCCCCCCCC | 21.30 | 25619855 | |
260 | O-linked_Glycosylation | VQVLPRDTASLSTTP CEECCCCCCCCCCCC | 21.30 | 34802821 | |
262 | Phosphorylation | VLPRDTASLSTTPSE ECCCCCCCCCCCCCC | 25.58 | 25521595 | |
264 | Phosphorylation | PRDTASLSTTPSESP CCCCCCCCCCCCCCC | 27.95 | 25521595 | |
265 | Phosphorylation | RDTASLSTTPSESPR CCCCCCCCCCCCCCC | 48.28 | 25521595 | |
266 | Phosphorylation | DTASLSTTPSESPRA CCCCCCCCCCCCCCC | 22.80 | 25521595 | |
268 | Phosphorylation | ASLSTTPSESPRAQA CCCCCCCCCCCCCHH | 48.92 | 25521595 | |
270 | Phosphorylation | LSTTPSESPRAQATS CCCCCCCCCCCHHCC | 24.83 | 25521595 | |
276 | Phosphorylation | ESPRAQATSRLSTAS CCCCCHHCCCCCCCC | 11.42 | 22324799 | |
277 | Phosphorylation | SPRAQATSRLSTASC CCCCHHCCCCCCCCC | 33.95 | 22324799 | |
280 | Phosphorylation | AQATSRLSTASCPTP CHHCCCCCCCCCCCH | 22.33 | 25521595 | |
281 | Phosphorylation | QATSRLSTASCPTPK HHCCCCCCCCCCCHH | 27.47 | 19060867 | |
283 | Phosphorylation | TSRLSTASCPTPKQI CCCCCCCCCCCHHHC | 22.25 | 25521595 | |
284 | Glutathionylation | SRLSTASCPTPKQIR CCCCCCCCCCHHHCC | 3.95 | 24333276 | |
284 | S-nitrosylation | SRLSTASCPTPKQIR CCCCCCCCCCHHHCC | 3.95 | 22178444 | |
284 | S-palmitoylation | SRLSTASCPTPKQIR CCCCCCCCCCHHHCC | 3.95 | - | |
284 | S-nitrosocysteine | SRLSTASCPTPKQIR CCCCCCCCCCHHHCC | 3.95 | - | |
286 | Phosphorylation | LSTASCPTPKQIRRP CCCCCCCCHHHCCCC | 47.66 | 25521595 | |
301 | Phosphorylation | DESKGVASRVGSLKA CCCCCHHHHHHCCEE | 25.70 | 22324799 | |
305 | Phosphorylation | GVASRVGSLKARLPS CHHHHHHCCEEECCC | 24.68 | 29899451 | |
312 | Phosphorylation | SLKARLPSCSSTYSV CCEEECCCCCCCCCH | 31.09 | 29899451 | |
324 | Phosphorylation | YSVSEVQSRCSSKEN CCHHHHHHHHCCHHH | 40.19 | 24759943 | |
327 | Phosphorylation | SEVQSRCSSKENILR HHHHHHHCCHHHHHH | 43.25 | 25159016 | |
328 | Phosphorylation | EVQSRCSSKENILRA HHHHHHCCHHHHHHH | 47.84 | 25159016 | |
329 | Malonylation | VQSRCSSKENILRAS HHHHHCCHHHHHHHH | 38.19 | 26320211 | |
336 | Phosphorylation | KENILRASHSAVDIT HHHHHHHHHHHHHHH | 16.13 | 25521595 | |
338 | Phosphorylation | NILRASHSAVDITKV HHHHHHHHHHHHHHH | 27.74 | 25521595 | |
343 | Phosphorylation | SHSAVDITKVARRHR HHHHHHHHHHHHHHC | 18.27 | 25777480 | |
344 | Ubiquitination | HSAVDITKVARRHRM HHHHHHHHHHHHHCC | 33.94 | - | |
352 | Phosphorylation | VARRHRMSPFPLTSM HHHHHCCCCCCCCCC | 24.28 | 25521595 | |
357 | Phosphorylation | RMSPFPLTSMDKAFI CCCCCCCCCCCHHHE | 23.42 | - | |
406 | Acetylation | PPFPASVKDGYAVRA CCCCCCCCCCEEEEE | 42.83 | 23954790 | |
498 | Acetylation | RPIGHDIKRGECVLA CCCCCCCCCCCEEEE | 61.48 | 15618151 | |
635 | Acetylation | HFGRVFMKPGLPTTF EECCEECCCCCCCEE | 25.19 | 23954790 | |
678 | Ubiquitination | FVVPALRKMQGILDP EHHHHHHHHCCCCCC | 36.10 | - | |
699 | Acetylation | ARLSCDVKLDPRPEY EEEECCEECCCCCCC | 33.64 | 7622373 | |
748 | Acetylation | GLLMLPPKTEQYVEL CCEECCCCCHHHEEE | 63.86 | 23954790 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GEPH_MOUSE !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of GEPH_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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. |