IMDH1_HUMAN - dbPTM
IMDH1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IMDH1_HUMAN
UniProt AC P20839
Protein Name Inosine-5'-monophosphate dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_03156}
Gene Name IMPDH1 {ECO:0000255|HAMAP-Rule:MF_03156}
Organism Homo sapiens (Human).
Sequence Length 514
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors..
Protein Sequence MADYLISGGTGYVPEDGLTAQQLFASADGLTYNDFLILPGFIDFIADEVDLTSALTRKITLKTPLISSPMDTVTEADMAIAMALMGGIGFIHHNCTPEFQANEVRKVKKFEQGFITDPVVLSPSHTVGDVLEAKMRHGFSGIPITETGTMGSKLVGIVTSRDIDFLAEKDHTTLLSEVMTPRIELVVAPAGVTLKEANEILQRSKKGKLPIVNDCDELVAIIARTDLKKNRDYPLASKDSQKQLLCGAAVGTREDDKYRLDLLTQAGVDVIVLDSSQGNSVYQIAMVHYIKQKYPHLQVIGGNVVTAAQAKNLIDAGVDGLRVGMGCGSICITQEVMACGRPQGTAVYKVAEYARRFGVPIIADGGIQTVGHVVKALALGASTVMMGSLLAATTEAPGEYFFSDGVRLKKYRGMGSLDAMEKSSSSQKRYFSEGDKVKIAQGVSGSIQDKGSIQKFVPYLIAGIQHGCQDIGARSLSVLRSMMYSGELKFEKRTMSAQIEGGVHGLHSYEKRLY
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
6Phosphorylation--MADYLISGGTGYV
--CCCEEECCCCCCC		2.68-
6 (in isoform 3)Phosphorylation-2.6825159151
6 (in isoform 5)Phosphorylation-2.6825159151
6 (in isoform 6)Phosphorylation-2.6825159151
6 (in isoform 7)Phosphorylation-2.6825159151
31 (in isoform 3)Phosphorylation-26.3027251275
31 (in isoform 5)Phosphorylation-26.3027251275
31 (in isoform 6)Phosphorylation-26.3027251275
31 (in isoform 7)Phosphorylation-26.3027251275
36 (in isoform 3)Phosphorylation-4.36-
36 (in isoform 5)Phosphorylation-4.36-
36 (in isoform 6)Phosphorylation-4.36-
36 (in isoform 7)Phosphorylation-4.36-
37 (in isoform 3)Phosphorylation-4.3827251275
37 (in isoform 5)Phosphorylation-4.3827251275
37 (in isoform 6)Phosphorylation-4.3827251275
37 (in isoform 7)Phosphorylation-4.3827251275
45 (in isoform 6)Phosphorylation-4.13-
45 (in isoform 7)Phosphorylation-4.13-
56PhosphorylationVDLTSALTRKITLKT
CCHHHHHHCEEECCC		29.63-
56 (in isoform 6)Phosphorylation-29.6322210691
56 (in isoform 7)Phosphorylation-29.6322210691
59 (in isoform 6)Phosphorylation-5.0022210691
59 (in isoform 7)Phosphorylation-5.0022210691
60PhosphorylationSALTRKITLKTPLIS
HHHHCEEECCCCCCC		25.8218491316
60 (in isoform 6)Phosphorylation-25.8218491316
60 (in isoform 7)Phosphorylation-25.8218491316
63PhosphorylationTRKITLKTPLISSPM
HCEEECCCCCCCCCC		26.8324043423
63 (in isoform 6)Phosphorylation-26.8318491316
63 (in isoform 7)Phosphorylation-26.8318491316
66 (in isoform 6)Phosphorylation-3.9518491316
66 (in isoform 7)Phosphorylation-3.9518491316
67PhosphorylationTLKTPLISSPMDTVT
ECCCCCCCCCCCCCC		35.7524043423
68PhosphorylationLKTPLISSPMDTVTE
CCCCCCCCCCCCCCH		19.7624043423
68 (in isoform 2)Phosphorylation-19.7620860994
72PhosphorylationLISSPMDTVTEADMA
CCCCCCCCCCHHHHH		24.0724043423
72 (in isoform 2)Phosphorylation-24.0720860994
74PhosphorylationSSPMDTVTEADMAIA
CCCCCCCCHHHHHHH		27.7824043423
75 (in isoform 5)Phosphorylation-38.03-
85PhosphorylationMAIAMALMGGIGFIH
HHHHHHHHCCCCCCC		3.16-
85 (in isoform 6)Phosphorylation-3.16-
85 (in isoform 7)Phosphorylation-3.16-
96PhosphorylationGFIHHNCTPEFQANE
CCCCCCCCHHHCHHH		31.0424043423
108PhosphorylationANEVRKVKKFEQGFI
HHHHHHHHHCCCCCC		55.57-
109UbiquitinationNEVRKVKKFEQGFIT
HHHHHHHHCCCCCCC		58.06-
109 (in isoform 2)Ubiquitination-58.0621890473
122PhosphorylationITDPVVLSPSHTVGD
CCCCEEECCCCCHHH		16.8525159151
124PhosphorylationDPVVLSPSHTVGDVL
CCEEECCCCCHHHHH		28.5426074081
126PhosphorylationVVLSPSHTVGDVLEA
EEECCCCCHHHHHHH		30.4426074081
128 (in isoform 2)Ubiquitination-22.0621890473
129UbiquitinationSPSHTVGDVLEAKMR
CCCCCHHHHHHHHHH		37.1821890473
134UbiquitinationVGDVLEAKMRHGFSG
HHHHHHHHHHHCCCC		27.3921890473
140PhosphorylationAKMRHGFSGIPITET
HHHHHCCCCCEEECC		40.1726074081
142UbiquitinationMRHGFSGIPITETGT
HHHCCCCCEEECCCC		1.8521890473
142 (in isoform 1)Ubiquitination-1.8521890473
145PhosphorylationGFSGIPITETGTMGS
CCCCCEEECCCCCCC		23.3420068231
147PhosphorylationSGIPITETGTMGSKL
CCCEEECCCCCCCEE		29.3329759185
149PhosphorylationIPITETGTMGSKLVG
CEEECCCCCCCEEEE		26.2729759185
152PhosphorylationTETGTMGSKLVGIVT
ECCCCCCCEEEEEEE		16.4020068231
153UbiquitinationETGTMGSKLVGIVTS
CCCCCCCEEEEEEEC		41.2721906983
159PhosphorylationSKLVGIVTSRDIDFL
CEEEEEEECCCCHHH		19.0028450419
160PhosphorylationKLVGIVTSRDIDFLA
EEEEEEECCCCHHHH		19.6428450419
161 (in isoform 1)Ubiquitination-35.2221890473
169UbiquitinationDIDFLAEKDHTTLLS
CCHHHHCCCHHHHHH		49.56-
172PhosphorylationFLAEKDHTTLLSEVM
HHHCCCHHHHHHHHC		29.3120068231
173PhosphorylationLAEKDHTTLLSEVMT
HHCCCHHHHHHHHCC		23.4520068231
176PhosphorylationKDHTTLLSEVMTPRI
CCHHHHHHHHCCCCE		31.1220068231
180PhosphorylationTLLSEVMTPRIELVV
HHHHHHCCCCEEEEE		18.0020068231
183 (in isoform 3)Ubiquitination-5.1721890473
186UbiquitinationMTPRIELVVAPAGVT
CCCCEEEEEECCCCC		1.9321890473
195UbiquitinationAPAGVTLKEANEILQ
ECCCCCHHHHHHHHH		45.47-
202 (in isoform 3)Ubiquitination-53.9421890473
203MethylationEANEILQRSKKGKLP
HHHHHHHHHHCCCCC		47.18-
205UbiquitinationNEILQRSKKGKLPIV
HHHHHHHHCCCCCCC		68.67-
206UbiquitinationEILQRSKKGKLPIVN
HHHHHHHCCCCCCCC		63.63-
208UbiquitinationLQRSKKGKLPIVNDC
HHHHHCCCCCCCCCH		61.03-
215GlutathionylationKLPIVNDCDELVAII
CCCCCCCHHHHHHHH		3.5522555962
217 (in isoform 2)Ubiquitination-52.0221890473
219UbiquitinationVNDCDELVAIIARTD
CCCHHHHHHHHHHCC		3.1921890473
231MethylationRTDLKKNRDYPLASK
HCCHHHCCCCCCCCH		54.44-
233PhosphorylationDLKKNRDYPLASKDS
CHHHCCCCCCCCHHH		9.2628152594
237PhosphorylationNRDYPLASKDSQKQL
CCCCCCCCHHHHHHH		44.6820068231
237UbiquitinationNRDYPLASKDSQKQL
CCCCCCCCHHHHHHH		44.6821890473
238UbiquitinationRDYPLASKDSQKQLL
CCCCCCCHHHHHHHH		56.65-
242AcetylationLASKDSQKQLLCGAA
CCCHHHHHHHHCCEE		47.03163915
242UbiquitinationLASKDSQKQLLCGAA
CCCHHHHHHHHCCEE		47.0321890473
250UbiquitinationQLLCGAAVGTREDDK
HHHCCEEECCCCCCH		8.7921890473
250 (in isoform 1)Ubiquitination-8.7921890473
252PhosphorylationLCGAAVGTREDDKYR
HCCEEECCCCCCHHH		25.04-
286 (in isoform 2)Ubiquitination-1.7221890473
291 (in isoform 3)Ubiquitination-33.3021890473
293UbiquitinationMVHYIKQKYPHLQVI
HHHHHHHHCCCEEEE		56.60-
293AcetylationMVHYIKQKYPHLQVI
HHHHHHHHCCCEEEE		56.6026051181
294UbiquitinationVHYIKQKYPHLQVIG
HHHHHHHCCCEEEEC		8.0621890473
306PhosphorylationVIGGNVVTAAQAKNL
EECCEEECHHHHHCH		16.40-
311UbiquitinationVVTAAQAKNLIDAGV
EECHHHHHCHHHCCC		39.9621906983
319 (in isoform 1)Ubiquitination-49.8721890473
322MethylationDAGVDGLRVGMGCGS
HCCCCCEEECCCCCC		28.59115367821
327UbiquitinationGLRVGMGCGSICITQ
CEEECCCCCCEEEEH		2.6121890473
341MethylationQEVMACGRPQGTAVY
HHHHHCCCCCCCHHH		21.91-
355MethylationYKVAEYARRFGVPII
HHHHHHHHHHCCCEE		33.29-
360 (in isoform 3)Ubiquitination-16.7921890473
385 (in isoform 2)Ubiquitination-2.2621890473
400PhosphorylationTTEAPGEYFFSDGVR
CCCCCCCEECCCCCE		18.81-
410UbiquitinationSDGVRLKKYRGMGSL
CCCCEEEEECCCCCH		44.7821906983
416PhosphorylationKKYRGMGSLDAMEKS
EEECCCCCHHHHHHC		17.7423927012
418 (in isoform 1)Ubiquitination-45.6321890473
422UbiquitinationGSLDAMEKSSSSQKR
CCHHHHHHCCCCCCC		42.42-
425 (in isoform 2)Ubiquitination-43.8321890473
428UbiquitinationEKSSSSQKRYFSEGD
HHCCCCCCCCCCCCC		51.52-
430PhosphorylationSSSSQKRYFSEGDKV
CCCCCCCCCCCCCCE		20.6328152594
432PhosphorylationSSQKRYFSEGDKVKI
CCCCCCCCCCCCEEE		31.5623312004
436AcetylationRYFSEGDKVKIAQGV
CCCCCCCCEEEEECC		57.1723749302
436UbiquitinationRYFSEGDKVKIAQGV
CCCCCCCCEEEEECC		57.17-
438UbiquitinationFSEGDKVKIAQGVSG
CCCCCCEEEEECCCC		37.76-
450UbiquitinationVSGSIQDKGSIQKFV
CCCCCCCCCHHHHHH		37.882190698
458 (in isoform 1)Ubiquitination-22.7321890473
459PhosphorylationSIQKFVPYLIAGIQH
HHHHHHHHHHHHHHH		12.8720049867
459 (in isoform 3)Ubiquitination-12.8721890473
477PhosphorylationDIGARSLSVLRSMMY
HHHHHHHHHHHHHHH		21.9824719451
499 (in isoform 3)Ubiquitination-5.4821890473
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 IMDH1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IMDH1_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 IMDH1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IMDH2_HUMANIMPDH2physical
22939629
IMDH2_HUMANIMPDH2physical
22863883
PYRG1_HUMANCTPS1physical
26344197
DDX3X_HUMANDDX3Xphysical
26344197
DDX5_HUMANDDX5physical
26344197
EDF1_HUMANEDF1physical
26344197
IMDH2_HUMANIMPDH2physical
26344197
NH2L1_HUMANNHP2L1physical
26344197
NOP9_HUMANNOP9physical
26344197
SH3K1_HUMANSH3KBP1physical
26344197
UBL7_HUMANUBL7physical
26344197
SMCR8_HUMANSMCR8physical
28514442
WDR25_HUMANWDR25physical
28514442
C560_HUMANSDHCphysical
28514442
ARG39_HUMANARHGEF39physical
28514442
TRIM6_HUMANTRIM6physical
28514442
ANKR9_HUMANANKRD9physical
28514442
S2544_HUMANSLC25A44physical
28514442
MRM2_HUMANFTSJ2physical
28514442
B3GNL_HUMANB3GNTL1physical
28514442
MTMR8_HUMANMTMR8physical
28514442
PI51A_HUMANPIP5K1Aphysical
28514442
ABCBA_HUMANABCB10physical
28514442
DCAF4_HUMANDCAF4physical
28514442
PUSL1_HUMANPUSL1physical
28514442
ABD18_HUMANC4orf29physical
28514442
MOK_HUMANMOKphysical
28514442
SKP2_HUMANSKP2physical
28514442
ATG4D_HUMANATG4Dphysical
28514442
DCAKD_HUMANDCAKDphysical
28514442
STK19_HUMANSTK19physical
28514442
F120B_HUMANFAM120Bphysical
28514442
MTCH2_HUMANMTCH2physical
28514442
ZRAB3_HUMANZRANB3physical
28514442
GUCD1_HUMANGUCD1physical
28514442
WDR76_HUMANWDR76physical
28514442
DPH1_HUMANDPH1physical
28514442
GTPB8_HUMANGTPBP8physical
28514442
TMM11_HUMANTMEM11physical
28514442
BCS1_HUMANBCS1Lphysical
28514442
PEX6_HUMANPEX6physical
28514442
KLD8B_HUMANKLHDC8Bphysical
28514442
ACSF3_HUMANACSF3physical
28514442
TYW4_HUMANLCMT2physical
28514442
UCP5_HUMANSLC25A14physical
28514442
CAF17_HUMANIBA57physical
28514442
HSDL1_HUMANHSDL1physical
28514442
MTCH1_HUMANMTCH1physical
28514442
NDUC2_HUMANNDUFC2physical
28514442
CLPP_HUMANCLPPphysical
28514442
CHK1_HUMANCHEK1genetic
27453043
WEE1_HUMANWEE1genetic
27453043
RS11_HUMANRPS11genetic
27453043
CDC73_HUMANCDC73genetic
27453043
SH3G1_HUMANSH3GL1genetic
27453043
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
180105Retinitis pigmentosa 10 (RP10)
613837Leber congenital amaurosis 11 (LCA11)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB01033Mercaptopurine
DB00688Mycophenolate mofetil
DB01024Mycophenolic acid
DB00811Ribavirin
Regulatory Network of IMDH1_HUMAN

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