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O14772

- FPGT_HUMAN

UniProt

O14772 - FPGT_HUMAN

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Protein

Fucose-1-phosphate guanylyltransferase

Gene

FPGT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the formation of GDP-L-fucose from GTP and L-fucose-1-phosphate. Functions as a salvage pathway to reutilize L-fucose arising from the turnover of glycoproteins and glycolipids.

Catalytic activityi

GTP + beta-L-fucose 1-phosphate = diphosphate + GDP-L-fucose.

GO - Molecular functioni

  1. catalytic activity Source: ProtInc
  2. fucose-1-phosphate guanylyltransferase activity Source: UniProtKB-EC
  3. GTP binding Source: UniProtKB-KW

GO - Biological processi

  1. fucose metabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fucose-1-phosphate guanylyltransferase (EC:2.7.7.30)
Alternative name(s):
GDP-L-fucose diphosphorylase
GDP-L-fucose pyrophosphorylase
Gene namesi
Name:FPGT
Synonyms:GFPP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3825. FPGT.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28243.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 594594Fucose-1-phosphate guanylyltransferasePRO_0000087327Add
BLAST

Proteomic databases

MaxQBiO14772.
PaxDbiO14772.
PRIDEiO14772.

Expressioni

Tissue specificityi

Expressed in many tissues.

Gene expression databases

BgeeiO14772.
CleanExiHS_FPGT.
ExpressionAtlasiO14772. baseline and differential.
GenevestigatoriO14772.

Interactioni

Protein-protein interaction databases

BioGridi114318. 2 interactions.
STRINGi9606.ENSP00000359928.

Structurei

3D structure databases

ProteinModelPortaliO14772.
SMRiO14772. Positions 109-168.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00570000079453.
HOGENOMiHOG000067964.
HOVERGENiHBG025123.
InParanoidiO14772.
KOiK00976.
OMAiKLAMYVD.
OrthoDBiEOG7SFHW9.
PhylomeDBiO14772.
TreeFamiTF328750.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR012887. Fucokinase.
IPR012120. Fucose-1-phosphate_GuaTrfase.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view]
PfamiPF07959. Fucokinase. 1 hit.
[Graphical view]
PIRSFiPIRSF036640. FPGT. 1 hit.
SUPFAMiSSF51161. SSF51161. 1 hit.

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 2 (identifier: O14772-1) [UniParc]FASTAAdd to Basket

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
MAAARDPPEV SLREATQRKL RRFSELRGKL VARGEFWDIV AITAADEKQE
60 70 80 90 100
LAYNQQLSEK LKRKELPLGV QYHVFVDPAG AKIGNGGSTL CALQCLEKLY
110 120 130 140 150
GDKWNSFTIL LIHSGGYSQR LPNASALGKI FTALPLGNPI YQMLELKLAM
160 170 180 190 200
YIDFPLNMNP GILVTCADDI ELYSIGEFEF IRFDKPGFTA LAHPSSLTIG
210 220 230 240 250
TTHGVFVLDP FDDLKHRDLE YRSCHRFLHK PSIEKMYQFN AVCRPGNFCQ
260 270 280 290 300
QDFAGGDIAD LKLDSDYVYT DSLFYMDHKS AKMLLAFYEK IGTLSCEIDA
310 320 330 340 350
YGDFLQALGP GATVEYTRNT SNVIKEESEL VEMRQRIFHL LKGTSLNVVV
360 370 380 390 400
LNNSKFYHIG TTEEYLFYFT SDNSLKSELG LQSITFSIFP DIPECSGKTS
410 420 430 440 450
CIIQSILDSR CSVAPGSVVE YSRLGPDVSV GENCIISGSY ILTKAALPAH
460 470 480 490 500
SFVCSLSLKM NRCLKYATMA FGVQDNLKKS VKTLSDIKLL QFFGVCFLSC
510 520 530 540 550
LDVWNLKVTE ELFSGNKTCL SLWTARIFPV CSSLSDSVIT SLKMLNAVKN
560 570 580 590
KSAFSLNSYK LLSIEEMLIY KDVEDMITYR EQIFLEISLK SSLM
Length:594
Mass (Da):66,599
Last modified:February 20, 2007 - v2
Checksum:i15BA9CB906C70CC7
GO
Isoform 1 (identifier: Q59H18-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform can be found in the external entry Q59H18.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Based on a naturally occurring readthrough transcript which produces a FPGT-TNNI3K fusion protein.

Length:936
Mass (Da):104,179
GO
Isoform 3 (identifier: Q59H18-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform can be found in the external entry Q59H18.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Based on a naturally occurring readthrough transcript which produces a FPGT-TNNI3K fusion protein.

Length:697
Mass (Da):77,957
GO
Isoform 4 (identifier: Q59H18-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform can be found in the external entry Q59H18.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Based on a naturally occurring readthrough transcript which produces a FPGT-TNNI3K fusion protein.

Length:843
Mass (Da):94,517
GO
Isoform 5 (identifier: O14772-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     137-390: Missing.

Note: No experimental confirmation available.

Show »
Length:340
Mass (Da):37,631
Checksum:i804504F161653FD2
GO
Isoform 6 (identifier: O14772-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     115-594: GGYSQRLPNA...LEISLKSSLM → VSFQIYQNAL...KTALLVVLTS

Note: No experimental confirmation available.

Show »
Length:169
Mass (Da):19,170
Checksum:iE8D68424A3C4D277
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441A → T in BAG61434. (PubMed:14702039)Curated
Sequence conflicti322 – 3221N → H in AAC73005. (PubMed:9804772)Curated
Sequence conflicti549 – 5491K → R in BAG61434. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti448 – 4481P → L.
Corresponds to variant rs55882158 [ dbSNP | Ensembl ].
VAR_061650

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei115 – 594480GGYSQ…KSSLM → VSFQIYQNALAKHPVSFKAY WIQDVLWHLAQLWSIPDWGL MFQLGKTALLVVLTS in isoform 6. 1 PublicationVSP_046460Add
BLAST
Alternative sequencei137 – 390254Missing in isoform 5. 1 PublicationVSP_045076Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF017445 mRNA. Translation: AAC73005.1.
AF017446 Genomic DNA. Translation: AAC82511.1.
AK299468 mRNA. Translation: BAG61434.1.
AK304490 mRNA. Translation: BAG65299.1. Sequence problems.
AC098692 Genomic DNA. No translation available.
BC032308 mRNA. Translation: AAH32308.1.
RefSeqiNP_001186257.2. NM_001199328.2.
NP_001186258.2. NM_001199329.2.
NP_003829.3. NM_003838.4.
UniGeneiHs.480085.

Genome annotation databases

EnsembliENST00000370894; ENSP00000359931; ENSG00000254685. [O14772-3]
ENST00000534056; ENSP00000432819; ENSG00000254685. [O14772-2]
GeneIDi8790.
KEGGihsa:8790.
UCSCiuc001dgb.2. human. [O14772-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF017445 mRNA. Translation: AAC73005.1 .
AF017446 Genomic DNA. Translation: AAC82511.1 .
AK299468 mRNA. Translation: BAG61434.1 .
AK304490 mRNA. Translation: BAG65299.1 . Sequence problems.
AC098692 Genomic DNA. No translation available.
BC032308 mRNA. Translation: AAH32308.1 .
RefSeqi NP_001186257.2. NM_001199328.2.
NP_001186258.2. NM_001199329.2.
NP_003829.3. NM_003838.4.
UniGenei Hs.480085.

3D structure databases

ProteinModelPortali O14772.
SMRi O14772. Positions 109-168.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114318. 2 interactions.
STRINGi 9606.ENSP00000359928.

Proteomic databases

MaxQBi O14772.
PaxDbi O14772.
PRIDEi O14772.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000370894 ; ENSP00000359931 ; ENSG00000254685 . [O14772-3 ]
ENST00000534056 ; ENSP00000432819 ; ENSG00000254685 . [O14772-2 ]
GeneIDi 8790.
KEGGi hsa:8790.
UCSCi uc001dgb.2. human. [O14772-1 ]

Organism-specific databases

CTDi 8790.
GeneCardsi GC01P074663.
HGNCi HGNC:3825. FPGT.
MIMi 603609. gene.
neXtProti NX_O14772.
PharmGKBi PA28243.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0666.
GeneTreei ENSGT00570000079453.
HOGENOMi HOG000067964.
HOVERGENi HBG025123.
InParanoidi O14772.
KOi K00976.
OMAi KLAMYVD.
OrthoDBi EOG7SFHW9.
PhylomeDBi O14772.
TreeFami TF328750.

Miscellaneous databases

GeneWikii FPGT.
GenomeRNAii 8790.
NextBioi 32968.
PROi O14772.
SOURCEi Search...

Gene expression databases

Bgeei O14772.
CleanExi HS_FPGT.
ExpressionAtlasi O14772. baseline and differential.
Genevestigatori O14772.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR012887. Fucokinase.
IPR012120. Fucose-1-phosphate_GuaTrfase.
IPR029044. Nucleotide-diphossugar_trans.
IPR011004. Trimer_LpxA-like.
[Graphical view ]
Pfami PF07959. Fucokinase. 1 hit.
[Graphical view ]
PIRSFi PIRSF036640. FPGT. 1 hit.
SUPFAMi SSF51161. SSF51161. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "GDP-L-fucose pyrophosphorylase: purification, cDNA cloning, and properties of the enzyme."
    Pastuszak I., Ketchum C., Hermanson G., Sjoberg E.J., Drake R., Elbein A.D.
    J. Biol. Chem. 273:30165-30174(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), CHARACTERIZATION.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6).
    Tissue: Tongue and Uterus.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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).
    Tissue: Colon and Kidney.

Entry informationi

Entry nameiFPGT_HUMAN
AccessioniPrimary (citable) accession number: O14772
Secondary accession number(s): A6NMH3
, B4DRX2, B4E2Y7, E9PNQ2, Q8N5J7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: February 20, 2007
Last modified: October 29, 2014
This is version 110 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

External Data

Dasty 3