GUAD_HUMAN - dbPTM
GUAD_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GUAD_HUMAN
UniProt AC Q9Y2T3
Protein Name Guanine deaminase
Gene Name GDA
Organism Homo sapiens (Human).
Sequence Length 454
Subcellular Localization
Protein Description Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia..
Protein Sequence MCAAQMPPLAHIFRGTFVHSTWTCPMEVLRDHLLGVSDSGKIVFLEEASQQEKLAKEWCFKPCEIRELSHHEFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVRRTLKNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNDTFPEYKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILLINKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDSPIDLFYGDFFGDISEAVIQKFLYLGDDRNIEEVYVGGKQVVPFSSSV
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
37PhosphorylationRDHLLGVSDSGKIVF
HHHHCCCCCCCCEEE		25.0224275569
39PhosphorylationHLLGVSDSGKIVFLE
HHCCCCCCCCEEEEE		34.1824719451
41UbiquitinationLGVSDSGKIVFLEEA
CCCCCCCCEEEEECH		39.38-
49PhosphorylationIVFLEEASQQEKLAK
EEEEECHHHHHHHHH		35.3621601212
53UbiquitinationEEASQQEKLAKEWCF
ECHHHHHHHHHHHCC		49.7821906983
56AcetylationSQQEKLAKEWCFKPC
HHHHHHHHHHCCCCC		63.2826051181
61AcetylationLAKEWCFKPCEIREL
HHHHHCCCCCHHHHC		45.6926051181
81PhosphorylationFMPGLVDTHIHASQY
CCCCCCCCEECCHHC		18.4324043423
86PhosphorylationVDTHIHASQYSFAGS
CCCEECCHHCCCCCC		18.5824043423
88PhosphorylationTHIHASQYSFAGSSI
CEECCHHCCCCCCCC		11.8524043423
89PhosphorylationHIHASQYSFAGSSID
EECCHHCCCCCCCCC		10.8624043423
93PhosphorylationSQYSFAGSSIDLPLL
HHCCCCCCCCCHHHH		22.2324043423
94PhosphorylationQYSFAGSSIDLPLLE
HCCCCCCCCCHHHHH		21.1424043423
104PhosphorylationLPLLEWLTKYTFPAE
HHHHHHHHHCCCCHH		24.0724043423
106PhosphorylationLLEWLTKYTFPAEHR
HHHHHHHCCCCHHHC		14.3728152594
107PhosphorylationLEWLTKYTFPAEHRF
HHHHHHCCCCHHHCC		25.3828152594
124PhosphorylationIDFAEEVYTRVVRRT
CCHHHHHHHHHHHHH		7.66-
133UbiquitinationRVVRRTLKNGTTTAC
HHHHHHCCCCCEEEE		53.36-
181UbiquitinationNDTFPEYKETTEESI
CCCCHHHHHCHHHHH		47.09-
189UbiquitinationETTEESIKETERFVS
HCHHHHHHHHHHHHH		68.7921906983
201UbiquitinationFVSEMLQKNYSRVKP
HHHHHHHHHHCCCCC		54.62-
207UbiquitinationQKNYSRVKPIVTPRF
HHHHCCCCCCCCCCC		28.10-
231UbiquitinationGELGNIAKTRDLHIQ
HHHHHHHHHHHHHHH		40.05-
252UbiquitinationRDEVEAVKNLYPSYK
HHHHHHHHHHCHHHC		48.56-
255PhosphorylationVEAVKNLYPSYKNYT
HHHHHHHCHHHCCCC		10.26-
259UbiquitinationKNLYPSYKNYTSVYD
HHHCHHHCCCCCEEC		48.0621906983
261PhosphorylationLYPSYKNYTSVYDKN
HCHHHCCCCCEECCC		9.02-
267AcetylationNYTSVYDKNNLLTNK
CCCCEECCCCCCCCC		30.0126051181
267UbiquitinationNYTSVYDKNNLLTNK
CCCCEECCCCCCCCC		30.012190698
284PhosphorylationMAHGCYLSAEELNVF
EECCCEECHHHHCCH		13.7328857561
361UbiquitinationLINKVNEKSLTLKEV
EEECCCCCCCCHHHH		45.63-
362PhosphorylationINKVNEKSLTLKEVF
EECCCCCCCCHHHHH		22.0224719451
366UbiquitinationNEKSLTLKEVFRLAT
CCCCCCHHHHHHHHH		46.74-
366AcetylationNEKSLTLKEVFRLAT
CCCCCCHHHHHHHHH		46.7427452117
407PhosphorylationINPKASDSPIDLFYG
ECCCCCCCCCCEECC		22.6628857561
441PhosphorylationDRNIEEVYVGGKQVV
CCCEEEEEECCEEEE		9.17-
445UbiquitinationEEVYVGGKQVVPFSS
EEEEECCEEEEECCC		33.71-
451PhosphorylationGKQVVPFSSSV----
CEEEEECCCCC----		18.6828857561
452PhosphorylationKQVVPFSSSV-----
EEEEECCCCC-----		35.1828857561
453PhosphorylationQVVPFSSSV------
EEEECCCCC------		30.5525159151
457 (in isoform 3)Phosphorylation-29083192
463 (in isoform 3)Phosphorylation-23663014
464 (in isoform 3)Phosphorylation-23663014
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 GUAD_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GUAD_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 GUAD_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BCCIP_HUMANBCCIPphysical
22863883
IF5A1_HUMANEIF5Aphysical
22863883
GLSK_HUMANGLSphysical
22863883
CH60_HUMANHSPD1physical
22863883
KYNU_HUMANKYNUphysical
22863883
LDH6B_HUMANLDHAL6Bphysical
22863883
MVD1_HUMANMVDphysical
22863883
NAGK_HUMANNAGKphysical
22863883
KS6A3_HUMANRPS6KA3physical
22863883
NHRF1_HUMANSLC9A3R1physical
22863883
SMAP_HUMANC11orf58physical
22863883
SPSY_HUMANSMSphysical
22863883
GABT_HUMANABATphysical
26344197
HUTI_HUMANAMDHD1physical
26344197
AP1G1_HUMANAP1G1physical
26344197
ATRIP_HUMANATRIPphysical
26344197
FAHD1_HUMANFAHD1physical
26344197
SYLC_HUMANLARSphysical
26344197
TYW4_HUMANLCMT2physical
26344197
PEPL1_HUMANNPEPL1physical
26344197
TIPRL_HUMANTIPRLphysical
26344197
UBA1_HUMANUBA1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GUAD_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory