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Q06210

- GFPT1_HUMAN

UniProt

Q06210 - GFPT1_HUMAN

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Protein

Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1

Gene

GFPT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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. Regulates the circadian expression of clock genes ARNTL/BMAL1 and CRY1.

Catalytic activityi

L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21For GATase activityBy similarity
Binding sitei444 – 4441Substrate
Binding sitei584 – 5841Substrate

GO - Molecular functioni

  1. amino acid binding Source: Ensembl
  2. carbohydrate binding Source: Ensembl
  3. glutamine-fructose-6-phosphate transaminase (isomerizing) activity Source: ProtInc

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  2. carbohydrate biosynthetic process Source: InterPro
  3. cellular protein metabolic process Source: Reactome
  4. cellular response to insulin stimulus Source: Ensembl
  5. circadian regulation of gene expression Source: UniProtKB
  6. dolichol-linked oligosaccharide biosynthetic process Source: Reactome
  7. endoplasmic reticulum unfolded protein response Source: Reactome
  8. energy reserve metabolic process Source: ProtInc
  9. fructose 6-phosphate metabolic process Source: ProtInc
  10. glucosamine biosynthetic process Source: Ensembl
  11. glutamine metabolic process Source: UniProtKB-KW
  12. negative regulation of glycogen biosynthetic process Source: Ensembl
  13. post-translational protein modification Source: Reactome
  14. protein homotetramerization Source: Ensembl
  15. protein N-linked glycosylation via asparagine Source: Reactome
  16. response to sucrose Source: Ensembl
  17. UDP-N-acetylglucosamine biosynthetic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Biological rhythms

Enzyme and pathway databases

BioCyciMetaCyc:HS09974-MONOMER.
ReactomeiREACT_18273. XBP1(S) activates chaperone genes.
REACT_22394. Synthesis of UDP-N-acetyl-glucosamine.
UniPathwayiUPA00113; UER00528.

Protein family/group databases

MEROPSiC44.970.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1 (EC:2.6.1.16)
Alternative name(s):
D-fructose-6-phosphate amidotransferase 1
Glutamine:fructose-6-phosphate amidotransferase 1
Short name:
GFAT 1
Short name:
GFAT1
Hexosephosphate aminotransferase 1
Gene namesi
Name:GFPT1
Synonyms:GFAT, GFPT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:4241. GFPT1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Myasthenic syndrome, congenital, with tubular aggregates, 1 (CMSTA1) [MIM:610542]: A congenital myasthenic syndrome characterized by onset of proximal muscle weakness in the first decade. Individuals with this condition have a recognizable pattern of weakness of shoulder and pelvic girdle muscles, and sparing of ocular or facial muscles. EMG classically shows a decremental response to repeated nerve stimulation, a sign of neuromuscular junction dysfunction. Affected individuals show a favorable response to acetylcholinesterase (AChE) inhibitors.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151T → A in CMSTA1. 1 Publication
VAR_065339
Natural varianti15 – 151T → M in CMSTA1. 1 Publication
VAR_065340
Natural varianti43 – 431D → V in CMSTA1. 1 Publication
VAR_065341
Natural varianti111 – 1111R → C in CMSTA1. 1 Publication
Corresponds to variant rs201322234 [ dbSNP | Ensembl ].
VAR_065342
Natural varianti121 – 1211I → T in CMSTA1. 1 Publication
VAR_065343
Natural varianti199 – 1991V → F in CMSTA1. 1 Publication
VAR_065344
Natural varianti366 – 3661D → Y in CMSTA1. 1 Publication
VAR_065345
Natural varianti403 – 4031R → H in CMSTA1. 1 Publication
VAR_065346
Natural varianti452 – 4521R → H in CMSTA1. 1 Publication
VAR_065347
Natural varianti509 – 5091M → T in CMSTA1. 1 Publication
VAR_065348
Natural varianti510 – 5101M → T in CMSTA1. 1 Publication
VAR_065349
Natural varianti514 – 5141R → W in CMSTA1. 1 Publication
VAR_065350
Natural varianti530 – 5301R → W in CMSTA1. 1 Publication
VAR_065351

Keywords - Diseasei

Congenital myasthenic syndrome, Disease mutation

Organism-specific databases

MIMi610542. phenotype.
Orphaneti353327. Congenital myasthenic syndromes with glycosylation defect.
PharmGKBiPA28651.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 699698Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1PRO_0000135280Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei261 – 2611Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ06210.
PaxDbiQ06210.
PRIDEiQ06210.

PTM databases

PhosphoSiteiQ06210.

Expressioni

Tissue specificityi

Isoform 1 is predominantly expressed in skeletal muscle. Not expressed in brain. Seems to be selectively expressed in striated muscle.1 Publication

Gene expression databases

BgeeiQ06210.
CleanExiHS_GFPT1.
GenevestigatoriQ06210.

Organism-specific databases

HPAiHPA047240.

Interactioni

Subunit structurei

Homotetramer Probable, may also exist as homodimers.1 Publication

Protein-protein interaction databases

BioGridi108941. 27 interactions.
IntActiQ06210. 4 interactions.
MINTiMINT-5001216.
STRINGi9606.ENSP00000354347.

Structurei

Secondary structure

1
699
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi339 – 3413
Helixi342 – 3487
Helixi350 – 3589
Turni359 – 3613
Turni364 – 3674
Helixi372 – 3743
Turni375 – 3773
Helixi378 – 3836
Beta strandi385 – 3917
Helixi393 – 41018
Beta strandi414 – 4185
Helixi419 – 4246
Beta strandi433 – 44210
Helixi445 – 45612
Beta strandi460 – 4667
Helixi471 – 4755
Beta strandi476 – 4816
Beta strandi489 – 4913
Helixi494 – 51017
Turni511 – 5133
Helixi515 – 5173
Helixi518 – 53922
Helixi542 – 55211
Beta strandi556 – 5627
Helixi564 – 5663
Helixi567 – 58115
Beta strandi584 – 5896
Helixi590 – 5956
Helixi597 – 6004
Beta strandi602 – 6054
Beta strandi607 – 6115
Helixi617 – 62913
Beta strandi635 – 6395
Helixi643 – 6486
Beta strandi650 – 6556
Turni660 – 6623
Helixi663 – 6675
Helixi669 – 68113
Beta strandi686 – 6883

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V4MX-ray2.29A/B/C/D332-699[»]
2ZJ3X-ray1.90A332-699[»]
2ZJ4X-ray2.20A332-699[»]
ProteinModelPortaliQ06210.
SMRiQ06210. Positions 16-230, 274-699.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06210.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 305304Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
BLAST
Domaini377 – 516140SIS 1PROSITE-ProRule annotationAdd
BLAST
Domaini548 – 689142SIS 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni313 – 680368IsomeraseAdd
BLAST
Regioni394 – 3952Substrate-binding
Regioni439 – 4413Substrate-binding

Sequence similaritiesi

Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation
Contains 2 SIS domains.PROSITE-ProRule annotation

Keywords - Domaini

Glutamine amidotransferase, Repeat

Phylogenomic databases

eggNOGiCOG0449.
GeneTreeiENSGT00390000010049.
HOGENOMiHOG000258898.
HOVERGENiHBG051724.
InParanoidiQ06210.
KOiK00820.
OMAiPVTRRFM.
OrthoDBiEOG73NG2S.
PhylomeDBiQ06210.
TreeFamiTF300864.

Family and domain databases

Gene3Di3.60.20.10. 2 hits.
InterProiIPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR005855. GlmS_trans.
IPR029055. Ntn_hydrolases_N.
IPR001347. SIS.
[Graphical view]
PfamiPF00310. GATase_2. 2 hits.
PF01380. SIS. 2 hits.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 2 hits.
TIGRFAMsiTIGR01135. glmS. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
PS51464. SIS. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q06210-1) [UniParc]FASTAAdd to Basket

Also known as: GFAT1m

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MCGIFAYLNY HVPRTRREIL ETLIKGLQRL EYRGYDSAGV GFDGGNDKDW
60 70 80 90 100
EANACKIQLI KKKGKVKALD EEVHKQQDMD LDIEFDVHLG IAHTRWATHG
110 120 130 140 150
EPSPVNSHPQ RSDKNNEFIV IHNGIITNYK DLKKFLESKG YDFESETDTE
160 170 180 190 200
TIAKLVKYMY DNRESQDTSF TTLVERVIQQ LEGAFALVFK SVHFPGQAVG
210 220 230 240 250
TRRGSPLLIG VRSEHKLSTD HIPILYRTAR TQIGSKFTRW GSQGERGKDK
260 270 280 290 300
KGSCNLSRVD STTCLFPVEE KAVEYYFASD ASAVIEHTNR VIFLEDDDVA
310 320 330 340 350
AVVDGRLSIH RIKRTAGDHP GRAVQTLQME LQQIMKGNFS SFMQKEIFEQ
360 370 380 390 400
PESVVNTMRG RVNFDDYTVN LGGLKDHIKE IQRCRRLILI ACGTSYHAGV
410 420 430 440 450
ATRQVLEELT ELPVMVELAS DFLDRNTPVF RDDVCFFLSQ SGETADTLMG
460 470 480 490 500
LRYCKERGAL TVGITNTVGS SISRETDCGV HINAGPEIGV ASTKAYTSQF
510 520 530 540 550
VSLVMFALMM CDDRISMQER RKEIMLGLKR LPDLIKEVLS MDDEIQKLAT
560 570 580 590 600
ELYHQKSVLI MGRGYHYATC LEGALKIKEI TYMHSEGILA GELKHGPLAL
610 620 630 640 650
VDKLMPVIMI IMRDHTYAKC QNALQQVVAR QGRPVVICDK EDTETIKNTK
660 670 680 690
RTIKVPHSVD CLQGILSVIP LQLLAFHLAV LRGYDVDFPR NLAKSVTVE
Length:699
Mass (Da):78,806
Last modified:January 23, 2007 - v3
Checksum:iF0533A7B762C7B98
GO
Isoform 2 (identifier: Q06210-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     229-246: Missing.

Show »
Length:681
Mass (Da):76,759
Checksum:i5CB56FDB5E4F76FA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151T → A in CMSTA1. 1 Publication
VAR_065339
Natural varianti15 – 151T → M in CMSTA1. 1 Publication
VAR_065340
Natural varianti43 – 431D → V in CMSTA1. 1 Publication
VAR_065341
Natural varianti111 – 1111R → C in CMSTA1. 1 Publication
Corresponds to variant rs201322234 [ dbSNP | Ensembl ].
VAR_065342
Natural varianti121 – 1211I → T in CMSTA1. 1 Publication
VAR_065343
Natural varianti199 – 1991V → F in CMSTA1. 1 Publication
VAR_065344
Natural varianti366 – 3661D → Y in CMSTA1. 1 Publication
VAR_065345
Natural varianti403 – 4031R → H in CMSTA1. 1 Publication
VAR_065346
Natural varianti452 – 4521R → H in CMSTA1. 1 Publication
VAR_065347
Natural varianti509 – 5091M → T in CMSTA1. 1 Publication
VAR_065348
Natural varianti510 – 5101M → T in CMSTA1. 1 Publication
VAR_065349
Natural varianti514 – 5141R → W in CMSTA1. 1 Publication
VAR_065350
Natural varianti530 – 5301R → W in CMSTA1. 1 Publication
VAR_065351

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei229 – 24618Missing in isoform 2. 2 PublicationsVSP_007497Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M90516 mRNA. Translation: AAA58502.1.
AC114772 Genomic DNA. Translation: AAY14827.1.
BC045641 mRNA. Translation: AAH45641.1.
AF334737 mRNA. Translation: AAK15342.1.
CCDSiCCDS33216.1. [Q06210-2]
CCDS58713.1. [Q06210-1]
PIRiA45055.
RefSeqiNP_001231639.1. NM_001244710.1. [Q06210-1]
NP_002047.2. NM_002056.3. [Q06210-2]
UniGeneiHs.580300.

Genome annotation databases

EnsembliENST00000357308; ENSP00000349860; ENSG00000198380. [Q06210-1]
ENST00000361060; ENSP00000354347; ENSG00000198380. [Q06210-2]
GeneIDi2673.
KEGGihsa:2673.
UCSCiuc002sfh.3. human. [Q06210-2]
uc002sfi.2. human. [Q06210-1]

Polymorphism databases

DMDMi30923274.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M90516 mRNA. Translation: AAA58502.1 .
AC114772 Genomic DNA. Translation: AAY14827.1 .
BC045641 mRNA. Translation: AAH45641.1 .
AF334737 mRNA. Translation: AAK15342.1 .
CCDSi CCDS33216.1. [Q06210-2 ]
CCDS58713.1. [Q06210-1 ]
PIRi A45055.
RefSeqi NP_001231639.1. NM_001244710.1. [Q06210-1 ]
NP_002047.2. NM_002056.3. [Q06210-2 ]
UniGenei Hs.580300.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2V4M X-ray 2.29 A/B/C/D 332-699 [» ]
2ZJ3 X-ray 1.90 A 332-699 [» ]
2ZJ4 X-ray 2.20 A 332-699 [» ]
ProteinModelPortali Q06210.
SMRi Q06210. Positions 16-230, 274-699.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108941. 27 interactions.
IntActi Q06210. 4 interactions.
MINTi MINT-5001216.
STRINGi 9606.ENSP00000354347.

Chemistry

BindingDBi Q06210.
ChEMBLi CHEMBL1909481.

Protein family/group databases

MEROPSi C44.970.

PTM databases

PhosphoSitei Q06210.

Polymorphism databases

DMDMi 30923274.

Proteomic databases

MaxQBi Q06210.
PaxDbi Q06210.
PRIDEi Q06210.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000357308 ; ENSP00000349860 ; ENSG00000198380 . [Q06210-1 ]
ENST00000361060 ; ENSP00000354347 ; ENSG00000198380 . [Q06210-2 ]
GeneIDi 2673.
KEGGi hsa:2673.
UCSCi uc002sfh.3. human. [Q06210-2 ]
uc002sfi.2. human. [Q06210-1 ]

Organism-specific databases

CTDi 2673.
GeneCardsi GC02M069546.
GeneReviewsi GFPT1.
HGNCi HGNC:4241. GFPT1.
HPAi HPA047240.
MIMi 138292. gene.
610542. phenotype.
neXtProti NX_Q06210.
Orphaneti 353327. Congenital myasthenic syndromes with glycosylation defect.
PharmGKBi PA28651.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0449.
GeneTreei ENSGT00390000010049.
HOGENOMi HOG000258898.
HOVERGENi HBG051724.
InParanoidi Q06210.
KOi K00820.
OMAi PVTRRFM.
OrthoDBi EOG73NG2S.
PhylomeDBi Q06210.
TreeFami TF300864.

Enzyme and pathway databases

UniPathwayi UPA00113 ; UER00528 .
BioCyci MetaCyc:HS09974-MONOMER.
Reactomei REACT_18273. XBP1(S) activates chaperone genes.
REACT_22394. Synthesis of UDP-N-acetyl-glucosamine.

Miscellaneous databases

ChiTaRSi GFPT1. human.
EvolutionaryTracei Q06210.
GeneWikii GFPT1.
GenomeRNAii 2673.
NextBioi 10550.
PROi Q06210.
SOURCEi Search...

Gene expression databases

Bgeei Q06210.
CleanExi HS_GFPT1.
Genevestigatori Q06210.

Family and domain databases

Gene3Di 3.60.20.10. 2 hits.
InterProi IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR005855. GlmS_trans.
IPR029055. Ntn_hydrolases_N.
IPR001347. SIS.
[Graphical view ]
Pfami PF00310. GATase_2. 2 hits.
PF01380. SIS. 2 hits.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 2 hits.
TIGRFAMsi TIGR01135. glmS. 1 hit.
PROSITEi PS51278. GATASE_TYPE_2. 1 hit.
PS51464. SIS. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, cDNA sequence, and bacterial expression of human glutamine:fructose-6-phosphate amidotransferase."
    McKnight G.L., Mudri S.L., Mathewes S.L., Traxinger R.R., Marshall S., Sheppard P.O., O'Hara P.J.
    J. Biol. Chem. 267:25208-25212(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  4. "A novel variant of glutamine:fructose-6-phosphate amidotransferase-1 (GFAT1) mRNA is selectively expressed in striated muscle."
    DeHaven J.E., Robinson K.A., Nelson B.A., Buse M.G.
    Diabetes 50:2419-2424(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 124-275 (ISOFORM 1), TISSUE SPECIFICITY.
  5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Structural analysis of human glutamine:fructose-6-phosphate amidotransferase, a key regulator in type 2 diabetes."
    Nakaishi Y., Bando M., Shimizu H., Watanabe K., Goto F., Tsuge H., Kondo K., Komatsu M.
    FEBS Lett. 583:163-167(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 332-699, SUBUNIT, SUBSTRATE-BINDING SITES.
  16. Cited for: VARIANTS CMSTA1 ALA-15; MET-15; VAL-43; CYS-111; THR-121; PHE-199; TYR-366; HIS-403; HIS-452; THR-509; THR-510; TRP-514 AND TRP-530.

Entry informationi

Entry nameiGFPT1_HUMAN
AccessioniPrimary (citable) accession number: Q06210
Secondary accession number(s): Q53QE6, Q9BXF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3