GFPT2_HUMAN - dbPTM
GFPT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GFPT2_HUMAN
UniProt AC O94808
Protein Name Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2
Gene Name GFPT2
Organism Homo sapiens (Human).
Sequence Length 682
Subcellular Localization
Protein Description Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins..
Protein Sequence MCGIFAYMNYRVPRTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNNHEVKERHIQLVKKRGKVKALDEELYKQDSMDLKVEFETHFGIAHTRWATHGVPSAVNSHPQRSDKGNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDNRETEDITFSTLVERVIQQLEGAFALVFKSVHYPGEAVATRRGSPLLIGVRSKYKLSTEQIPILYRTCTLENVKNICKTRMKRLDSSACLHAVGDKAVEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHRVKRSASDDPSRAIQTLQMELQQIMKGNFSAFMQKEIFEQPESVFNTMRGRVNFETNTVLLGGLKDHLKEIRRCRRLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLLALRYCKDRGALTVGVTNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFISLVMFGLMMSEDRISLQNRRQEIIRGLRSLPELIKEVLSLEEKIHDLALELYTQRSLLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFAKCQNALQQVTARQGRPIILCSKDDTESSKFAYKTIELPHTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE
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
50UbiquitinationDGNNHEVKERHIQLV
CCCCHHHHHHHHHHH
46.15-
64UbiquitinationVKKRGKVKALDEELY
HHHCCCCHHCCHHHH
46.87-
75PhosphorylationEELYKQDSMDLKVEF
HHHHHCCCCCEEEEE
16.2323828894
100PhosphorylationWATHGVPSAVNSHPQ
HHHCCCCCHHHCCCC
42.30-
136UbiquitinationLRKFLESKGYEFESE
HHHHHHHCCCCCCCC
57.02-
144PhosphorylationGYEFESETDTETIAK
CCCCCCCCCHHHHHH
58.46-
202PhosphorylationAVATRRGSPLLIGVR
HHHHCCCCCEEEEEE
15.5730266825
210PhosphorylationPLLIGVRSKYKLSTE
CEEEEEEECCCCCCC
37.6220049867
212PhosphorylationLIGVRSKYKLSTEQI
EEEEEECCCCCCCCC
20.5720049867
215PhosphorylationVRSKYKLSTEQIPIL
EEECCCCCCCCCCCE
26.2528348404
216PhosphorylationRSKYKLSTEQIPILY
EECCCCCCCCCCCEE
42.2028348404
227PhosphorylationPILYRTCTLENVKNI
CCEEEECCHHHHHHH
36.1728857561
244PhosphorylationTRMKRLDSSACLHAV
HHHHHCCCCHHHHHH
25.1529255136
245PhosphorylationRMKRLDSSACLHAVG
HHHHCCCCHHHHHHC
23.7530266825
254AcetylationCLHAVGDKAVEFFFA
HHHHHCHHHHHHHCC
48.6918586559
328UbiquitinationNFSAFMQKEIFEQPE
CHHHHHHHHHHHCCH
40.7821906983
349PhosphorylationRGRVNFETNTVLLGG
CCCCCCCCCEEEECC
31.8624043423
351PhosphorylationRVNFETNTVLLGGLK
CCCCCCCEEEECCHH
21.6824043423
393PhosphorylationRQVLEELTELPVMVE
HHHHHHHHCCCHHHH
38.4620639409
403PhosphorylationPVMVELASDFLDRNT
CHHHHHHHHHHCCCC
41.3320639409
444PhosphorylationCKDRGALTVGVTNTV
HCCCCCEEEEEECCC
18.06-
450PhosphorylationLTVGVTNTVGSSISR
EEEEEECCCCCCCCC
19.51-
453PhosphorylationGVTNTVGSSISRETD
EEECCCCCCCCCCCC
21.84-
456PhosphorylationNTVGSSISRETDCGV
CCCCCCCCCCCCCEE
26.47-
602UbiquitinationMKDPCFAKCQNALQQ
ECCHHHHHHHHHHHH
18.99-
622PhosphorylationGRPIILCSKDDTESS
CCCEEEEECCCCCCC
35.3625159151
630UbiquitinationKDDTESSKFAYKTIE
CCCCCCCCCCHHHCC
43.20-
677UbiquitinationDFPRNLAKSVTVE--
CCCCCHHCCCCCC--
48.9321906983
677AcetylationDFPRNLAKSVTVE--
CCCCCHHCCCCCC--
48.9321339330
678PhosphorylationFPRNLAKSVTVE---
CCCCHHCCCCCC---
19.8823911959
680PhosphorylationRNLAKSVTVE-----
CCHHCCCCCC-----
26.4727134283

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
202SPhosphorylationKinasePKA-FAMILY-GPS
202SPhosphorylationKinasePKA_GROUP-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GFPT2_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 GFPT2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TCPQ_HUMANCCT8physical
26344197
SYTC2_HUMANTARSL2physical
26344197
GFPT1_HUMANGFPT1physical
28514442
ACOT9_HUMANACOT9physical
28514442
FIGL1_HUMANFIGNL1physical
28514442

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 GFPT2_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-245, AND MASSSPECTROMETRY.

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