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Q9H488 (OFUT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GDP-fucose protein O-fucosyltransferase 1

EC=2.4.1.221
Alternative name(s):
Peptide-O-fucosyltransferase 1
Short name=O-FucT-1
Gene names
Name:POFUT1
Synonyms:FUT12, KIAA0180
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. Specifically uses GDP-fucose as donor substrate and proper disulfide pairing of the substrate EGF domains is required for fucose transfer. Plays a crucial role in NOTCH signaling. Initial fucosylation of NOTCH by POFUT1 generates a substrate for FRINGE/RFNG, an acetylglucosaminyltransferase that can then extend the fucosylation on the NOTCH EGF repeats. This extended fucosylation is required for optimal ligand binding and canonical NOTCH signaling induced by DLL1 or JAGGED1. Fucosylates AGRN and determines its ability to cluster acetylcholine receptors (AChRs). Ref.1 Ref.8

Catalytic activity

Transfers an alpha-L-fucosyl residue from GDP-beta-L-fucose to the serine hydroxy group of a protein acceptor.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum By similarity.

Tissue specificity

Highly expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Ref.1

Post-translational modification

N-glycosylated.

Involvement in disease

Dowling-Degos disease 2 (DDD2) [MIM:615327]: An autosomal dominant genodermatosis. Affected individuals develop a postpubertal reticulate hyperpigmentation that is progressive and disfiguring, and small hyperkeratotic dark brown papules that affect mainly the flexures and great skin folds. Patients usually show no abnormalities of the hair or nails.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11

Sequence similarities

Belongs to the glycosyltransferase 68 family.

Biophysicochemical properties

Kinetic parameters:

KM=6 µM for F7 EGF domain Ref.1

KM=4 µM for GDP-fucose

Vmax=3 µmol/min/mg enzyme

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Fucose metabolism
Notch signaling pathway
   Cellular componentEndoplasmic reticulum
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
   LigandManganese
   Molecular functionGlycosyltransferase
Transferase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNotch signaling pathway

Non-traceable author statement PubMed 15653671. Source: UniProtKB

O-glycan processing

Traceable author statement PubMed 11698403. Source: UniProtKB

angiogenesis

Inferred from electronic annotation. Source: Ensembl

embryo development

Non-traceable author statement PubMed 11698403. Source: UniProtKB

fucose metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

heart development

Inferred from electronic annotation. Source: Ensembl

nervous system development

Inferred from electronic annotation. Source: Ensembl

protein O-linked fucosylation

Inferred from direct assay PubMed 15653671. Source: UniProtKB

protein O-linked glycosylation

Inferred from direct assay Ref.1PubMed 9023546. Source: UniProtKB

regulation of transcription, DNA-templated

Non-traceable author statement PubMed 11698403. Source: UniProtKB

somitogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentendoplasmic reticulum

Inferred from direct assay PubMed 15653671. Source: UniProtKB

membrane

Inferred from direct assay Ref.1PubMed 9023546. Source: UniProtKB

   Molecular_functionfucosyltransferase activity

Inferred from direct assay Ref.1PubMed 9023546. Source: UniProtKB

peptide-O-fucosyltransferase activity

Inferred from direct assay PubMed 15653671. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H488-1)

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.
Isoform 2 (identifier: Q9H488-2)

The sequence of this isoform differs from the canonical sequence as follows:
     182-388: FSPKEHPVLA...DRPPKLRDEF → RENHSCVTLLFPR
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 388362GDP-fucose protein O-fucosyltransferase 1
PRO_0000012148

Regions

Region44 – 463Substrate binding By similarity
Region238 – 2403Substrate binding By similarity
Region356 – 3572Substrate binding By similarity
Motif385 – 3884Prevents secretion from ER Potential

Sites

Binding site3351Substrate By similarity

Amino acid modifications

Glycosylation621N-linked (GlcNAc...) Potential
Glycosylation1601N-linked (GlcNAc...) Ref.9
Disulfide bond38 ↔ 40 By similarity
Disulfide bond126 ↔ 140 By similarity
Disulfide bond249 ↔ 283 By similarity
Disulfide bond267 ↔ 354 By similarity

Natural variations

Alternative sequence182 – 388207FSPKE…LRDEF → RENHSCVTLLFPR in isoform 2.
VSP_001809
Natural variant3221L → F.
Corresponds to variant rs17268666 [ dbSNP | Ensembl ].
VAR_049231
Natural variant3481D → N.
Corresponds to variant rs35259534 [ dbSNP | Ensembl ].
VAR_049232

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 3FACCCA434D02415

FASTA38843,956
        10         20         30         40         50         60 
MGAAAWARPL SVSFLLLLLP LPGMPAGSWD PAGYLLYCPC MGRFGNQADH FLGSLAFAKL 

        70         80         90        100        110        120 
LNRTLAVPPW IEYQHHKPPF TNLHVSYQKY FKLEPLQAYH RVISLEDFME KLAPTHWPPE 

       130        140        150        160        170        180 
KRVAYCFEVA AQRSPDKKTC PMKEGNPFGP FWDQFHVSFN KSELFTGISF SASYREQWSQ 

       190        200        210        220        230        240 
RFSPKEHPVL ALPGAPAQFP VLEEHRPLQK YMVWSDEMVK TGEAQIHAHL VRPYVGIHLR 

       250        260        270        280        290        300 
IGSDWKNACA MLKDGTAGSH FMASPQCVGY SRSTAAPLTM TMCLPDLKEI QRAVKLWVRS 

       310        320        330        340        350        360 
LDAQSVYVAT DSESYVPELQ QLFKGKVKVV SLKPEVAQVD LYILGQADHF IGNCVSSFTA 

       370        380 
FVKRERDLQG RPSSFFGMDR PPKLRDEF 

« Hide

Isoform 2 [UniParc].

Checksum: 5ADE77CE45147644
Show »

FASTA19422,338

References

« Hide 'large scale' references
[1]"Modification of epidermal growth factor-like repeats with O-fucose: molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase."
Wang Y., Shao L., Shi S., Harris R.J., Spellman M.W., Stanley P., Haltiwanger R.S.
J. Biol. Chem. 276:40338-40345(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
Tissue: Heart.
[2]"Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Bone marrow.
[3]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[4]"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. expand/collapse author list , 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] (ISOFORM 1).
[5]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: Brain.
[8]"O-linked fucose and other post-translational modifications unique to EGF modules."
Harris R.J., Spellman M.W.
Glycobiology 3:219-224(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-160.
Tissue: Liver.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Mutations in POFUT1, encoding protein O-fucosyltransferase 1, cause generalized Dowling-Degos disease."
Li M., Cheng R., Liang J., Yan H., Zhang H., Yang L., Li C., Jiao Q., Lu Z., He J., Ji J., Shen Z., Li C., Hao F., Yu H., Yao Z.
Am. J. Hum. Genet. 92:895-903(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN DDD2.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Peptide-O-fucosyltransferase 1

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF375884 mRNA. Translation: AAL09576.1.
D80002 mRNA. Translation: BAA11497.2.
AL121897 Genomic DNA. Translation: CAC16424.1.
AL121897 Genomic DNA. Translation: CAH73300.1.
AK291033 mRNA. Translation: BAF83722.1.
CH471077 Genomic DNA. Translation: EAW76383.1.
CH471077 Genomic DNA. Translation: EAW76384.1.
CH471077 Genomic DNA. Translation: EAW76385.1.
BC000582 mRNA. Translation: AAH00582.1.
CCDSCCDS13198.1. [Q9H488-1]
CCDS13199.1. [Q9H488-2]
RefSeqNP_056167.1. NM_015352.1. [Q9H488-1]
NP_758436.1. NM_172236.1. [Q9H488-2]
UniGeneHs.472409.

3D structure databases

ProteinModelPortalQ9H488.
SMRQ9H488. Positions 30-378.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117056. 5 interactions.
IntActQ9H488. 2 interactions.
STRING9606.ENSP00000364902.

Protein family/group databases

CAZyGT65. Glycosyltransferase Family 65.

PTM databases

PhosphoSiteQ9H488.

Polymorphism databases

DMDM23396787.

Proteomic databases

MaxQBQ9H488.
PaxDbQ9H488.
PeptideAtlasQ9H488.
PRIDEQ9H488.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375730; ENSP00000364882; ENSG00000101346. [Q9H488-2]
ENST00000375749; ENSP00000364902; ENSG00000101346. [Q9H488-1]
GeneID23509.
KEGGhsa:23509.
UCSCuc002wxo.3. human. [Q9H488-2]
uc002wxp.3. human. [Q9H488-1]

Organism-specific databases

CTD23509.
GeneCardsGC20P030795.
HGNCHGNC:14988. POFUT1.
HPAHPA054519.
MIM607491. gene.
615327. phenotype.
neXtProtNX_Q9H488.
Orphanet79145. Dowling-Degos disease.
PharmGKBPA33495.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG250895.
HOGENOMHOG000231651.
HOVERGENHBG059976.
InParanoidQ9H488.
KOK03691.
OMASEHPVLA.
PhylomeDBQ9H488.
TreeFamTF314805.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ9H488.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ9H488.
BgeeQ9H488.
CleanExHS_POFUT1.
GenevestigatorQ9H488.

Family and domain databases

InterProIPR019378. GDP-Fuc_O-FucTrfase.
[Graphical view]
PfamPF10250. O-FucT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPOFUT1. human.
GenomeRNAi23509.
NextBio45915.
PROQ9H488.
SOURCESearch...

Entry information

Entry nameOFUT1_HUMAN
AccessionPrimary (citable) accession number: Q9H488
Secondary accession number(s): A8K4R8 expand/collapse secondary AC list , E1P5M4, Q14685, Q5W185, Q9BW76
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM