FCSK

Protein identityUniProt · HPA

UniProt accession

Q8N0W3

Gene

FCSK

Ensembl

ENSG00000157353

Chromosome

16

Canonical length

1084 aa

Protein class

Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Potential drug targets, Predicted intracellular proteins

Subcellular location

Vesicles

OverviewNCBI Gene

The protein encoded by this gene belongs to the GHMP (galacto-, homoserine, mevalonate and phosphomevalonate) kinase family and catalyzes the phosphorylation of L-fucose to form beta-L-fucose 1-phosphate. This enzyme catalyzes the first step in the utilization of free L-fucose in glycoprotein and glycolipid synthesis. L-fucose may be important in mediating a number of cell-cell interactions such as blood group antigen recognition, inflammation, and metastatis. While several transcript variants may exist for this gene, the full-length nature of only one has been described to date. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

1084 residues, UniProt reviewed canonical sequence.

>Q8N0W3|FCSK
     1  MEQPKGVDWT VIILTCQYKD SVQVFQRELE VRQKREQIPA GTLLLAVEDP EKRVGSGGAT
    61  LNALLVAAEH LSARAGFTVV TSDVLHSAWI LILHMGRDFP FDDCGRAFTC LPVENPEAPV
   121  EALVCNLDCL LDIMTYRLGP GSPPGVWVCS TDMLLSVPAN PGISWDSFRG ARVIALPGSP
   181  AYAQNHGVYL TDPQGLVLDI YYQGTEAEIQ RCVRPDGRVP LVSGVVFFSV ETAERLLATH
   241  VSPPLDACTY LGLDSGARPV QLSLFFDILH CMAENVTRED FLVGRPPELG QGDADVAGYL
   301  QSARAQLWRE LRDQPLTMAY VSSGSYSYMT SSASEFLLSL TLPGAPGAQI VHSQVEEQQL
   361  LAAGSSVVSC LLEGPVQLGP GSVLQHCHLQ GPIHIGAGCL VTGLDTAHSK ALHGRELRDL
   421  VLQGHHTRLH GSPGHAFTLV GRLDSWERQG AGTYLNVPWS EFFKRTGVRA WDLWDPETLP
   481  AEYCLPSARL FPVLHPSREL GPQDLLWMLD HQEDGGEALR AWRASWRLSW EQLQPCLDRA
   541  ATLASRRDLF FRQALHKARH VLEARQDLSL RPLIWAAVRE GCPGPLLATL DQVAAGAGDP
   601  GVAARALACV ADVLGCMAEG RGGLRSGPAA NPEWMRPFSY LECGDLAAGV EALAQERDKW
   661  LSRPALLVRA ARHYEGAGQI LIRQAVMSAQ HFVSTEQVEL PGPGQWVVAE CPARVDFSGG
   721  WSDTPPLAYE LGGAVLGLAV RVDGRRPIGA RARRIPEPEL WLAVGPRQDE MTVKIVCRCL
   781  ADLRDYCQPH APGALLKAAF ICAGIVHVHS ELQLSEQLLR TFGGGFELHT WSELPHGSGL
   841  GTSSILAGTA LAALQRAAGR VVGTEALIHA VLHLEQVLTT GGGWQDQVGG LMPGIKVGRS
   901  RAQLPLKVEV EEVTVPEGFV QKLNDHLLLV YTGKTRLARN LLQDVLRSWY ARLPAVVQNA
   961  HSLVRQTEEC AEGFRQGSLP LLGQCLTSYW EQKKLMAPGC EPLTVRRMMD VLAPHVHGQS
  1021  LAGAGGGGFL YLLTKEPQQK EALEAVLAKT EGLGNYSIHL VEVDTQGLSL KLLGTEASTC
  1081  CPFP

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against FCSK can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.22

Highest tissue expression

10 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about FCSK.

Disease | AllUniProt

Conditions FCSK is implicated in, by any mechanism.

• Congenital disorder of glycosylation with defective fucosylation 2 (CDGF2) MIM:618324

Disease | GeneticClinVar

7 pathogenic / likely-pathogenic of 688 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Congenital disorder of glycosylation with defective fucosylation 2

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

1.13

gnomAD pLI

0

DepMap mean gene effect

0.02

DepMap dependency class

none

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• carbohydrate phosphorylation
• GDP-L-fucose biosynthetic process
• GDP-L-fucose salvage

Molecular functions

• ATP binding
• fucokinase activity

Cellular components

• cytosol

Protein domainsUniProt · Pfam · InterPro

• GHMP kinase N-terminal domain
• GDP-fucose pyrophosphorylase domain
• GHMP kinase, C-terminal domain
• Ribosomal protein uS5 domain 2-type superfamily
• GHMP kinase, C-terminal domain superfamily
• GHMP kinases N terminal domain
• Fucose pyrophosphorylase domain
• GHMP kinases C terminal
• GHMP Kinase-Related Enzymes

KeywordsUniProt

• ATP-binding
• Congenital disorder of glycosylation
• Kinase
• Nucleotide-binding
• Transferase