PUR4_HUMAN - dbPTM
PUR4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PUR4_HUMAN
UniProt AC O15067
Protein Name Phosphoribosylformylglycinamidine synthase
Gene Name PFAS
Organism Homo sapiens (Human).
Sequence Length 1338
Subcellular Localization Cytoplasm.
Protein Description Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate (By similarity)..
Protein Sequence MSPVLHFYVRPSGHEGAAPGHTRRKLQGKLPELQGVETELCYNVNWTAEALPSAEETKKLMWLFGCPLLLDDVARESWLLPGSNDLLLEVGPRLNFSTPTSTNIVSVCRATGLGPVDRVETTRRYRLSFAHPPSAEVEAIALATLHDRMTEQHFPHPIQSFSPESMPEPLNGPINILGEGRLALEKANQELGLALDSWDLDFYTKRFQELQRNPSTVEAFDLAQSNSEHSRHWFFKGQLHVDGQKLVHSLFESIMSTQESSNPNNVLKFCDNSSAIQGKEVRFLRPEDPTRPSRFQQQQGLRHVVFTAETHNFPTGVCPFSGATTGTGGRIRDVQCTGRGAHVVAGTAGYCFGNLHIPGYNLPWEDPSFQYPGNFARPLEVAIEASNGASDYGNKFGEPVLAGFARSLGLQLPDGQRREWIKPIMFSGGIGSMEADHISKEAPEPGMEVVKVGGPVYRIGVGGGAASSVQVQGDNTSDLDFGAVQRGDPEMEQKMNRVIRACVEAPKGNPICSLHDQGAGGNGNVLKELSDPAGAIIYTSRFQLGDPTLNALEIWGAEYQESNALLLRSPNRDFLTHVSARERCPACFVGTITGDRRIVLVDDRECPVRRNGQGDAPPTPLPTPVDLELEWVLGKMPRKEFFLQRKPPMLQPLALPPGLSVHQALERVLRLPAVASKRYLTNKVDRSVGGLVAQQQCVGPLQTPLADVAVVALSHEELIGAATALGEQPVKSLLDPKVAARLAVAEALTNLVFALVTDLRDVKCSGNWMWAAKLPGEGAALADACEAMVAVMAALGVAVDGGKDSLSMAARVGTETVRAPGSLVISAYAVCPDITATVTPDLKHPEGRGHLLYVALSPGQHRLGGTALAQCFSQLGEHPPDLDLPENLVRAFSITQGLLKDRLLCSGHDVSDGGLVTCLLEMAFAGNCGLQVDVPVPRVDVLSVLFAEEPGLVLEVQEPDLAQVLKRYRDAGLHCLELGHTGEAGPHAMVRVSVNGAVVLEEPVGELRALWEETSFQLDRLQAEPRCVAEEERGLRERMGPSYCLPPTFPKASVPREPGGPSPRVAILREEGSNGDREMADAFHLAGFEVWDVTMQDLCSGAIGLDTFRGVAFVGGFSYADVLGSAKGWAAAVTFHPRAGAELRRFRKRPDTFSLGVCNGCQLLALLGWVGGDPNEDAAEMGPDSQPARPGLLLRHNLSGRYESRWASVRVGPGPALMLRGMEGAVLPVWSAHGEGYVAFSSPELQAQIEARGLAPLHWADDDGNPTEQYPLNPNGSPGGVAGICSCDGRHLAVMPHPERAVRPWQWAWRPPPFDTLTTSPWLQLFINARNWTLEGSC
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
2Phosphorylation------MSPVLHFYV
------CCCEEEEEE		34.7120873877
12PhosphorylationLHFYVRPSGHEGAAP
EEEEECCCCCCCCCC		42.0724719451
59UbiquitinationPSAEETKKLMWLFGC
CCHHHHHHHHHHHCC		51.50-
83PhosphorylationESWLLPGSNDLLLEV
HHCCCCCCCCEEEEE		25.8228464451
108GlutathionylationSTNIVSVCRATGLGP
CCCHHHHHHHCCCCC		1.5822555962
118MethylationTGLGPVDRVETTRRY
CCCCCCCCCEECCEE		28.53115487047
125PhosphorylationRVETTRRYRLSFAHP
CCEECCEEEEECCCC		16.7730108239
128PhosphorylationTTRRYRLSFAHPPSA
ECCEEEEECCCCCCH		16.0530108239
134PhosphorylationLSFAHPPSAEVEAIA
EECCCCCCHHHHHHH		41.3230108239
186UbiquitinationEGRLALEKANQELGL
CHHHHHHHHHHHHCC		54.19-
205UbiquitinationWDLDFYTKRFQELQR
CCHHHHHHHHHHHHH		39.5821906983
215PhosphorylationQELQRNPSTVEAFDL
HHHHHCCCHHHHHHH		48.9427273156
216PhosphorylationELQRNPSTVEAFDLA
HHHHCCCHHHHHHHH		24.5030576142
225PhosphorylationEAFDLAQSNSEHSRH
HHHHHHHCCCCCCCE		36.3921406692
227PhosphorylationFDLAQSNSEHSRHWF
HHHHHCCCCCCCEEE		41.7721406692
230PhosphorylationAQSNSEHSRHWFFKG
HHCCCCCCCEEEEEE		23.0721406692
231MethylationQSNSEHSRHWFFKGQ
HCCCCCCCEEEEEEE		32.72115487059
236UbiquitinationHSRHWFFKGQLHVDG
CCCEEEEEEEEEECH		35.95-
245UbiquitinationQLHVDGQKLVHSLFE
EEEECHHHHHHHHHH		58.99-
255SulfoxidationHSLFESIMSTQESSN
HHHHHHHHCCCCCCC		5.0328183972
268UbiquitinationSNPNNVLKFCDNSSA
CCCCCCEEECCCCHH		39.40-
279AcetylationNSSAIQGKEVRFLRP
CCHHHCCEEEEECCC		36.3425953088
279UbiquitinationNSSAIQGKEVRFLRP
CCHHHCCEEEEECCC		36.3421890473
282MethylationAIQGKEVRFLRPEDP
HHCCEEEEECCCCCC		26.44115383455
302MethylationFQQQQGLRHVVFTAE
HHHHCCCCEEEEEEE		27.6497816521
307PhosphorylationGLRHVVFTAETHNFP
CCCEEEEEEECCCCC		16.3924043423
310PhosphorylationHVVFTAETHNFPTGV
EEEEEEECCCCCCCC		21.4724043423
315PhosphorylationAETHNFPTGVCPFSG
EECCCCCCCCCCCCC		37.8024043423
321O-linked_GlycosylationPTGVCPFSGATTGTG
CCCCCCCCCCCCCCC		16.8030059200
321PhosphorylationPTGVCPFSGATTGTG
CCCCCCCCCCCCCCC		16.8024043423
324PhosphorylationVCPFSGATTGTGGRI
CCCCCCCCCCCCCCE		29.3224043423
325PhosphorylationCPFSGATTGTGGRIR
CCCCCCCCCCCCCEE		32.0124043423
327PhosphorylationFSGATTGTGGRIRDV
CCCCCCCCCCCEEEE		34.0824043423
395SumoylationGASDYGNKFGEPVLA
CCCCCCCCCCCCHHH		50.84-
422UbiquitinationGQRREWIKPIMFSGG
CCCCCCCCCEEECCC		29.5721906983
440UbiquitinationMEADHISKEAPEPGM
CCHHHHCCCCCCCCC		58.24-
447SulfoxidationKEAPEPGMEVVKVGG
CCCCCCCCEEEEECC		5.3121406390
451UbiquitinationEPGMEVVKVGGPVYR
CCCCEEEEECCEEEE		40.1021906983
457PhosphorylationVKVGGPVYRIGVGGG
EEECCEEEEEEECCC		10.31-
477PhosphorylationQVQGDNTSDLDFGAV
EECCCCCCCCCCCCH		42.2930175587
491SulfoxidationVQRGDPEMEQKMNRV
HHCCCHHHHHHHHHH		8.8830846556
494UbiquitinationGDPEMEQKMNRVIRA
CCHHHHHHHHHHHHH		25.4921906983
507UbiquitinationRACVEAPKGNPICSL
HHHHHCCCCCCCCCC		77.65-
507AcetylationRACVEAPKGNPICSL
HHHHHCCCCCCCCCC		77.6526051181
527UbiquitinationGGNGNVLKELSDPAG
CCCCCHHHHHCCCCC		52.94-
530PhosphorylationGNVLKELSDPAGAII
CCHHHHHCCCCCEEE		42.5121945579
538PhosphorylationDPAGAIIYTSRFQLG
CCCCEEEEEECCCCC		7.7921945579
539PhosphorylationPAGAIIYTSRFQLGD
CCCEEEEEECCCCCC		11.7421945579
540PhosphorylationAGAIIYTSRFQLGDP
CCEEEEEECCCCCCC		17.7121945579
548PhosphorylationRFQLGDPTLNALEIW
CCCCCCCCCCHHHHH		37.0726434776
559PhosphorylationLEIWGAEYQESNALL
HHHHCCCHHHCCCEE		19.6226434776
562PhosphorylationWGAEYQESNALLLRS
HCCCHHHCCCEEECC		16.3326074081
569PhosphorylationSNALLLRSPNRDFLT
CCCEEECCCCCCHHH		26.8822167270
576PhosphorylationSPNRDFLTHVSARER
CCCCCHHHHCCHHHH		21.8930266825
579PhosphorylationRDFLTHVSARERCPA
CCHHHHCCHHHHCCC		17.6328985074
593PhosphorylationACFVGTITGDRRIVL
CEEEEEEECCCEEEE		32.63-
606GlutathionylationVLVDDRECPVRRNGQ
EEECCCCCCCCCCCC		3.8322555962
619PhosphorylationGQGDAPPTPLPTPVD
CCCCCCCCCCCCCCC		36.0828464451
623PhosphorylationAPPTPLPTPVDLELE
CCCCCCCCCCCEEEH		43.5628464451
639UbiquitinationVLGKMPRKEFFLQRK
HHCCCCCHHHHHCCC		53.67-
646UbiquitinationKEFFLQRKPPMLQPL
HHHHHCCCCCCCCCC		40.28-
677UbiquitinationRLPAVASKRYLTNKV
CCHHHHCHHHHCCCC		35.01-
6772-HydroxyisobutyrylationRLPAVASKRYLTNKV
CCHHHHCHHHHCCCC		35.01-
679PhosphorylationPAVASKRYLTNKVDR
HHHHCHHHHCCCCCC		22.9328152594
681PhosphorylationVASKRYLTNKVDRSV
HHCHHHHCCCCCCCC		24.86-
6832-HydroxyisobutyrylationSKRYLTNKVDRSVGG
CHHHHCCCCCCCCCH		40.03-
683UbiquitinationSKRYLTNKVDRSVGG
CHHHHCCCCCCCCCH		40.0321906983
737UbiquitinationVKSLLDPKVAARLAV
CHHHCCHHHHHHHHH		44.1421906983
7372-HydroxyisobutyrylationVKSLLDPKVAARLAV
CHHHCCHHHHHHHHH		44.14-
803UbiquitinationGVAVDGGKDSLSMAA
CCCCCCCCCHHHHHH		50.07-
814PhosphorylationSMAARVGTETVRAPG
HHHHHHCCCEECCCC		26.1430576142
816PhosphorylationAARVGTETVRAPGSL
HHHHCCCEECCCCCE		18.3530576142
828PhosphorylationGSLVISAYAVCPDIT
CCEEEEEEEECCCCE		7.8730576142
831GlutathionylationVISAYAVCPDITATV
EEEEEEECCCCEEEE		1.5822555962
835PhosphorylationYAVCPDITATVTPDL
EEECCCCEEEECCCC		24.5330576142
843UbiquitinationATVTPDLKHPEGRGH
EEECCCCCCCCCCCE		65.57-
871GlutathionylationGGTALAQCFSQLGEH
HHHHHHHHHHHHCCC		2.7022555962
873PhosphorylationTALAQCFSQLGEHPP
HHHHHHHHHHCCCCC		31.93-
893PhosphorylationENLVRAFSITQGLLK
HHHHHHHHHHHCHHC		24.6021712546
900UbiquitinationSITQGLLKDRLLCSG
HHHHCHHCCCEEECC		45.9321906983
900AcetylationSITQGLLKDRLLCSG
HHHHCHHCCCEEECC		45.9326051181
9002-HydroxyisobutyrylationSITQGLLKDRLLCSG
HHHHCHHCCCEEECC		45.93-
989SulfoxidationGEAGPHAMVRVSVNG
CCCCCCCEEEEEECC		1.4730846556
1014PhosphorylationLRALWEETSFQLDRL
HHHHHHHHCHHHHHH		24.2724719451
1033MethylationRCVAEEERGLRERMG
CHHHHHHHCHHHHHC		53.37115487053
1051UbiquitinationCLPPTFPKASVPREP
CCCCCCCCCCCCCCC		49.45-
1053PhosphorylationPPTFPKASVPREPGG
CCCCCCCCCCCCCCC		38.4924719451
1062PhosphorylationPREPGGPSPRVAILR
CCCCCCCCCCEEEEE		28.7220068231
1119PhosphorylationAFVGGFSYADVLGSA
EEECCCCHHHHHCCC		12.45-
1218SulfoxidationVGPGPALMLRGMEGA
ECCCCHHHCCCCCCC		2.3221406390
1337PhosphorylationRNWTLEGSC------
CCCEEECCC------		13.7922617229
1338GlutathionylationNWTLEGSC-------
CCEEECCC-------		10.7222555962
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 PUR4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PUR4_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 PUR4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPS1_HUMANSEPHS1physical
22939629
UBR1_HUMANUBR1physical
22939629
ZN593_HUMANZNF593physical
22939629
UBP14_HUMANUSP14physical
22939629
XIAP_HUMANXIAPphysical
22939629
PP6R3_HUMANPPP6R3physical
22939629
SGTA_HUMANSGTAphysical
22939629
UBP28_HUMANUSP28physical
22939629
ABHEA_HUMANABHD14Aphysical
22863883
BZW2_HUMANBZW2physical
22863883
CAN1_HUMANCAPN1physical
22863883
CNBP_HUMANCNBPphysical
22863883
ECHM_HUMANECHS1physical
22863883
IF5_HUMANEIF5physical
22863883
FERM2_HUMANFERMT2physical
22863883
PSF3_HUMANGINS3physical
22863883
GRP75_HUMANHSPA9physical
22863883
MAT2B_HUMANMAT2Bphysical
22863883
MOES_HUMANMSNphysical
22863883
PDC10_HUMANPDCD10physical
22863883
GDS1_HUMANRAP1GDS1physical
22863883
VINC_HUMANVCLphysical
22863883
PUR8_HUMANADSLphysical
26344197
IF4H_HUMANEIF4Hphysical
26344197
PABP1_HUMANPABPC1physical
26344197
PUR1_HUMANPPATphysical
26344197
MSS4_HUMANRABIFphysical
26344197
VAC14_HUMANVAC14physical
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
DB00130L-Glutamine
Regulatory Network of PUR4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, AND MASSSPECTROMETRY.
"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 THR-619 AND THR-623, ANDMASS SPECTROMETRY.

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