GUAA_MOUSE - dbPTM
GUAA_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GUAA_MOUSE
UniProt AC Q3THK7
Protein Name GMP synthase [glutamine-hydrolyzing]
Gene Name Gmps
Organism Mus musculus (Mouse).
Sequence Length 693
Subcellular Localization Cytoplasm.
Protein Description Involved in the de novo synthesis of guanine nucleotides which are not only essential for DNA and RNA synthesis, but also provide GTP, which is involved in a number of cellular processes important for cell division..
Protein Sequence MALCNGDSKPENAGGDLKDGSHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETPAFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPILGICYGMQMMNKVFGGTVHKKSVREDGVFNISMDNTCSLFRGLQKEEIVLLTHGDSVDKVADGFKVVARSGNIVAGIANESKKLYGVQFHPEVGLTENGKVILKNFLYDIAGCSGNFTVQNRELECIREIKEKVGTSKVLVLLSGGVDSTVCTALLNRALNQDQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAAHSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMSLKPEEVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVRILGRELDLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPHTLLQRVKACTTEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDWESLIFLARLIPRMCHNINRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILRESGFAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGVPATPGNEIPVEVVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE
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
2Acetylation------MALCNGDSK
------CCCCCCCCC		22.33-
8PhosphorylationMALCNGDSKPENAGG
CCCCCCCCCCCCCCC		52.05-
9AcetylationALCNGDSKPENAGGD
CCCCCCCCCCCCCCC		62.18-
65UbiquitinationETPAFAIKEQGFRAI
CCCCEEEHHCCCEEE		40.32-
145UbiquitinationSLFRGLQKEEIVLLT
HHHCCCCCCCEEEEE		63.46-
145AcetylationSLFRGLQKEEIVLLT
HHHCCCCCCCEEEEE		63.4622826441
165UbiquitinationDKVADGFKVVARSGN
HHHCCCEEEEEECCC		41.13-
165AcetylationDKVADGFKVVARSGN
HHHCCCEEEEEECCC		41.1322826441
182UbiquitinationAGIANESKKLYGVQF
EEEECCCCCCEEEEC		40.39-
183UbiquitinationGIANESKKLYGVQFH
EEECCCCCCEEEECC		57.11-
185PhosphorylationANESKKLYGVQFHPE
ECCCCCCEEEECCCC		24.9122802335
204AcetylationENGKVILKNFLYDIA
CCCEEEEEECCHHHC		34.2322826441
208PhosphorylationVILKNFLYDIAGCSG
EEEEECCHHHCCCCC		10.9322802335
214PhosphorylationLYDIAGCSGNFTVQN
CHHHCCCCCCEEECC		35.5322802335
218PhosphorylationAGCSGNFTVQNRELE
CCCCCCEEECCHHHH		25.7822802335
277UbiquitinationIDNGFMRKRESQSVE
ECCCCCCHHCCCCHH		49.05-
280PhosphorylationGFMRKRESQSVEEAL
CCCCHHCCCCHHHHH		31.6123737553
282PhosphorylationMRKRESQSVEEALKK
CCHHCCCCHHHHHHH		40.5523737553
288UbiquitinationQSVEEALKKLGIQVK
CCHHHHHHHCCCCEE		53.66-
302PhosphorylationKVINAAHSFYNGTTT
EEEECCCCCCCCCCC		25.3818846507
304PhosphorylationINAAHSFYNGTTTLP
EECCCCCCCCCCCCC		18.7218846507
307PhosphorylationAHSFYNGTTTLPISD
CCCCCCCCCCCCCCC		16.9926745281
308PhosphorylationHSFYNGTTTLPISDE
CCCCCCCCCCCCCCC		27.9526745281
309PhosphorylationSFYNGTTTLPISDED
CCCCCCCCCCCCCCC		30.3026745281
313PhosphorylationGTTTLPISDEDRTPR
CCCCCCCCCCCCCCC		32.7621082442
318PhosphorylationPISDEDRTPRKRISK
CCCCCCCCCCHHHHH		39.5026824392
326PhosphorylationPRKRISKTLNMTTSP
CCHHHHHHCCCCCCH		19.3028833060
329OxidationRISKTLNMTTSPEEK
HHHHHCCCCCCHHHH		4.9417242355
330PhosphorylationISKTLNMTTSPEEKR
HHHHCCCCCCHHHHH		24.0524925903
331PhosphorylationSKTLNMTTSPEEKRK
HHHCCCCCCHHHHHH		31.3625521595
332PhosphorylationKTLNMTTSPEEKRKI
HHCCCCCCHHHHHHH		22.5824925903
412UbiquitinationGKVIEPLKDFHKDEV
CCCCCCCCCCCHHHH		69.89-
456GlutathionylationCAEEPYICKDFPETN
ECCCCEECCCCCCCC		2.6024333276
457UbiquitinationAEEPYICKDFPETNN
CCCCEECCCCCCCCC		53.50-
477UbiquitinationADFSASVKKPHTLLQ
HHHHHCCCCHHHHHH		59.08-
478UbiquitinationDFSASVKKPHTLLQR
HHHHCCCCHHHHHHH		39.62-
487UbiquitinationHTLLQRVKACTTEED
HHHHHHHHCCCCHHH		39.68-
489GlutathionylationLLQRVKACTTEEDQE
HHHHHHCCCCHHHHH		3.9224333276
535UbiquitinationYVCGISSKDEPDWES
EECCCCCCCCCCHHH		60.36-
627UbiquitinationFDRDPLQKQPSCQRS
CCCCHHHCCCCCCCE		72.38-
631GlutathionylationPLQKQPSCQRSVVIR
HHHCCCCCCCEEEEE		5.0524333276
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 GUAA_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GUAA_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 GUAA_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of GUAA_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GUAA_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-332, AND MASSSPECTROMETRY.

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