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 | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
50 | Ubiquitination | DGNNHEVKERHIQLV CCCCHHHHHHHHHHH | 46.15 | - | |
64 | Ubiquitination | VKKRGKVKALDEELY HHHCCCCHHCCHHHH | 46.87 | - | |
75 | Phosphorylation | EELYKQDSMDLKVEF HHHHHCCCCCEEEEE | 16.23 | 23828894 | |
100 | Phosphorylation | WATHGVPSAVNSHPQ HHHCCCCCHHHCCCC | 42.30 | - | |
136 | Ubiquitination | LRKFLESKGYEFESE HHHHHHHCCCCCCCC | 57.02 | - | |
144 | Phosphorylation | GYEFESETDTETIAK CCCCCCCCCHHHHHH | 58.46 | - | |
202 | Phosphorylation | AVATRRGSPLLIGVR HHHHCCCCCEEEEEE | 15.57 | 30266825 | |
210 | Phosphorylation | PLLIGVRSKYKLSTE CEEEEEEECCCCCCC | 37.62 | 20049867 | |
212 | Phosphorylation | LIGVRSKYKLSTEQI EEEEEECCCCCCCCC | 20.57 | 20049867 | |
215 | Phosphorylation | VRSKYKLSTEQIPIL EEECCCCCCCCCCCE | 26.25 | 28348404 | |
216 | Phosphorylation | RSKYKLSTEQIPILY EECCCCCCCCCCCEE | 42.20 | 28348404 | |
227 | Phosphorylation | PILYRTCTLENVKNI CCEEEECCHHHHHHH | 36.17 | 28857561 | |
244 | Phosphorylation | TRMKRLDSSACLHAV HHHHHCCCCHHHHHH | 25.15 | 29255136 | |
245 | Phosphorylation | RMKRLDSSACLHAVG HHHHCCCCHHHHHHC | 23.75 | 30266825 | |
254 | Acetylation | CLHAVGDKAVEFFFA HHHHHCHHHHHHHCC | 48.69 | 18586559 | |
328 | Ubiquitination | NFSAFMQKEIFEQPE CHHHHHHHHHHHCCH | 40.78 | 21906983 | |
349 | Phosphorylation | RGRVNFETNTVLLGG CCCCCCCCCEEEECC | 31.86 | 24043423 | |
351 | Phosphorylation | RVNFETNTVLLGGLK CCCCCCCEEEECCHH | 21.68 | 24043423 | |
393 | Phosphorylation | RQVLEELTELPVMVE HHHHHHHHCCCHHHH | 38.46 | 20639409 | |
403 | Phosphorylation | PVMVELASDFLDRNT CHHHHHHHHHHCCCC | 41.33 | 20639409 | |
444 | Phosphorylation | CKDRGALTVGVTNTV HCCCCCEEEEEECCC | 18.06 | - | |
450 | Phosphorylation | LTVGVTNTVGSSISR EEEEEECCCCCCCCC | 19.51 | - | |
453 | Phosphorylation | GVTNTVGSSISRETD EEECCCCCCCCCCCC | 21.84 | - | |
456 | Phosphorylation | NTVGSSISRETDCGV CCCCCCCCCCCCCEE | 26.47 | - | |
602 | Ubiquitination | MKDPCFAKCQNALQQ ECCHHHHHHHHHHHH | 18.99 | - | |
622 | Phosphorylation | GRPIILCSKDDTESS CCCEEEEECCCCCCC | 35.36 | 25159151 | |
630 | Ubiquitination | KDDTESSKFAYKTIE CCCCCCCCCCHHHCC | 43.20 | - | |
677 | Ubiquitination | DFPRNLAKSVTVE-- CCCCCHHCCCCCC-- | 48.93 | 21906983 | |
677 | Acetylation | DFPRNLAKSVTVE-- CCCCCHHCCCCCC-- | 48.93 | 21339330 | |
678 | Phosphorylation | FPRNLAKSVTVE--- CCCCHHCCCCCC--- | 19.88 | 23911959 | |
680 | Phosphorylation | RNLAKSVTVE----- CCHHCCCCCC----- | 26.47 | 27134283 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
202 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
202 | S | Phosphorylation | Kinase | PKA_GROUP | - | PhosphoELM |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GFPT2_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
TCPQ_HUMAN | CCT8 | physical | 26344197 | |
SYTC2_HUMAN | TARSL2 | physical | 26344197 | |
GFPT1_HUMAN | GFPT1 | physical | 28514442 | |
ACOT9_HUMAN | ACOT9 | physical | 28514442 | |
FIGL1_HUMAN | FIGNL1 | physical | 28514442 |
Kegg Disease | |
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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 | |
DB00130 | L-Glutamine |
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Phosphorylation | |
Reference | PubMed |
"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. |