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Q9Y2G5

- OFUT2_HUMAN

UniProt

Q9Y2G5 - OFUT2_HUMAN

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Protein
GDP-fucose protein O-fucosyltransferase 2
Gene
POFUT2, C21orf80, FUT13, KIAA0958
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X(2,3)-S/T-C2-X(2)-G of thrombospondin type 1 repeats where C1 and C2 are the first and second cysteines, respectively. O-fucosylates members of several protein families including the ADAMTS family, the thrombosporin (TSP) and spondin families. The O-fucosylation of TSRs is also required for restricting epithelial to mesenchymal transition (EMT), maintaining the correct patterning of mesoderm and localization of the definite endoderm By similarity. Required for the proper secretion of ADAMTS family members such as ADAMSL1 and ADAMST13.5 Publications

Catalytic activityi

Transfers an alpha-L-fucosyl residue from GDP-beta-L-fucose to the serine hydroxy group of a protein acceptor.1 Publication

Enzyme regulationi

Inhibited by EDTA and by Zn2+.1 Publication

Kineticsi

  1. KM=9.8 µM for GDP-fucose1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei54 – 541Proton donor/acceptor Inferred
Binding sitei294 – 2941Substrate
Sitei396 – 3961Essential for catalytic activity

GO - Molecular functioni

  1. peptide-O-fucosyltransferase activity Source: UniProtKB

GO - Biological processi

  1. fucose metabolic process Source: UniProtKB-KW
  2. mesoderm formation Source: Ensembl
  3. protein O-linked fucosylation Source: UniProtKB
  4. regulation of epithelial to mesenchymal transition Source: Ensembl
  5. regulation of gene expression Source: Ensembl
  6. regulation of secretion Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Fucose metabolism

Enzyme and pathway databases

ReactomeiREACT_200626. O-glycosylation of TSR domain-containing proteins.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT68. Glycosyltransferase Family 68.

Names & Taxonomyi

Protein namesi
Recommended name:
GDP-fucose protein O-fucosyltransferase 2 (EC:2.4.1.221)
Alternative name(s):
Peptide-O-fucosyltransferase 2
Short name:
O-FucT-2
Gene namesi
Name:POFUT2
Synonyms:C21orf80, FUT13, KIAA0958
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 21

Organism-specific databases

HGNCiHGNC:14683. POFUT2.

Subcellular locationi

Endoplasmic reticulum. Golgi apparatus
Note: Mainly located in the endoplasmic reticulum.1 Publication

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB
  2. endoplasmic reticulum Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi54 – 541E → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi92 – 921W → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi152 – 1521W → A: Reduces enzyme activity. 1 Publication
Mutagenesisi273 – 2731W → A: Reduces enzyme activity. 1 Publication
Mutagenesisi294 – 2941R → A: Abolishes enzyme activity. 1 Publication
Mutagenesisi297 – 2971D → A: Reduces enzyme activity. 1 Publication
Mutagenesisi395 – 3951E → A: No enhanced secretion of ADASMTS13; when associated with A-396. 1 Publication
Mutagenesisi396 – 3961E → A: Reduces enzyme activity. No enhanced secretion of ADASMTS13; when associated with A-396. 2 Publications

Organism-specific databases

PharmGKBiPA25867.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121 Reviewed prediction
Add
BLAST
Chaini22 – 429408GDP-fucose protein O-fucosyltransferase 2
PRO_0000012154Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi161 ↔ 1921 Publication
Glycosylationi189 – 1891N-linked (GlcNAc...)1 Publication
Glycosylationi209 – 2091N-linked (GlcNAc...) Reviewed prediction
Glycosylationi259 – 2591N-linked (GlcNAc...)1 Publication
Disulfide bondi412 ↔ 4191 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9Y2G5.
PaxDbiQ9Y2G5.
PRIDEiQ9Y2G5.

PTM databases

PhosphoSiteiQ9Y2G5.

Expressioni

Tissue specificityi

Isoform A is expressed in fetal liver and peripheral blood lymphocytes. Isoform B is expressed in spleen, lung, testis, bone marrow, thymus, pancreas, prostate, fetal brain, fetal liver and fetal kidney. Isoform C is expressed in brain, heart, spleen, liver, lung, stomach, testis, placenta, skin, thymus, pancreas, mammary gland, prostate, fetal brain, fetal liver and fetal heart.1 Publication

Gene expression databases

ArrayExpressiQ9Y2G5.
BgeeiQ9Y2G5.
CleanExiHS_POFUT2.
GenevestigatoriQ9Y2G5.

Organism-specific databases

HPAiHPA044297.

Interactioni

Protein-protein interaction databases

BioGridi116876. 2 interactions.
IntActiQ9Y2G5. 3 interactions.
STRINGi9606.ENSP00000339613.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 485
Helixi56 – 7419
Beta strandi79 – 835
Helixi91 – 933
Helixi104 – 1063
Helixi110 – 1145
Beta strandi119 – 1213
Helixi122 – 1287
Beta strandi129 – 14113
Beta strandi156 – 1594
Helixi179 – 1813
Beta strandi186 – 19510
Helixi199 – 2024
Helixi203 – 2086
Beta strandi213 – 2197
Helixi220 – 2223
Helixi231 – 2388
Helixi244 – 25815
Turni262 – 2665
Helixi273 – 2753
Beta strandi286 – 2938
Turni296 – 3027
Beta strandi304 – 3063
Helixi309 – 32315
Beta strandi328 – 3325
Helixi336 – 34510
Beta strandi349 – 3513
Helixi356 – 37621
Beta strandi378 – 3836
Helixi388 – 40013
Helixi404 – 4063

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AP5X-ray3.00A/B22-429[»]
4AP6X-ray3.40A/B/C/D37-429[»]
ProteinModelPortaliQ9Y2G5.
SMRiQ9Y2G5. Positions 41-429.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 564Substrate binding
Regioni388 – 3892Substrate binding

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG77810.
HOVERGENiHBG053367.
InParanoidiQ9Y2G5.
KOiK03691.
OMAiICAHARC.
OrthoDBiEOG76T9S1.
PhylomeDBiQ9Y2G5.
TreeFamiTF314337.

Family and domain databases

InterProiIPR019378. GDP-Fuc_O-FucTrfase.
[Graphical view]
PfamiPF10250. O-FucT. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform C (identifier: Q9Y2G5-3) [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

MATLSFVFLL LGAVSWPPAS ASGQEFWPGQ SAADILSGAA SRRRYLLYDV    50
NPPEGFNLRR DVYIRIASLL KTLLKTEEWV LVLPPWGRLY HWQSPDIHQV 100
RIPWSEFFDL PSLNKNIPVI EYEQFIAESG GPFIDQVYVL QSYAEGWKEG 150
TWEEKVDERP CIDQLLYSQD KHEYYRGWFW GYEETRGLNV SCLSVQGSAS 200
IVAPLLLRNT SARSVMLDRA ENLLHDHYGG KEYWDTRRSM VFARHLREVG 250
DEFRSRHLNS TDDADRIPFQ EDWMKMKVKL GSALGGPYLG VHLRRKDFIW 300
GHRQDVPSLE GAVRKIRSLM KTHRLDKVFV ATDAVRKEYE ELKKLLPEMV 350
RFEPTWEELE LYKDGGVAII DQWICAHARF FIGTSVSTFS FRIHEEREIL 400
GLDPKTTYNR FCGDQEKACE QPTHWKITY 429
Length:429
Mass (Da):49,976
Last modified:February 15, 2005 - v3
Checksum:i36A4213D905AFFD1
GO
Isoform A (identifier: Q9Y2G5-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     380-429: FFIGTSVSTF...EQPTHWKITY → CLPTSLSAES...GHFHTVCLLV

Show »
Length:424
Mass (Da):48,896
Checksum:i60BA687F0DFB8875
GO
Isoform B (identifier: Q9Y2G5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     379-380: RF → SS
     381-429: Missing.

Show »
Length:380
Mass (Da):44,083
Checksum:i7D640225C9A977C0
GO

Sequence cautioni

The sequence BAA76802.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence CAB90496.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei379 – 3802RF → SS in isoform B.
VSP_003833
Alternative sequencei380 – 42950FFIGT…WKITY → CLPTSLSAESGSGGFQRFFC PKYSVSEQMVACVHSGHFHT VCLLV in isoform A.
VSP_003832Add
BLAST
Alternative sequencei381 – 42949Missing in isoform B.
VSP_003834Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ302080 mRNA. Translation: CAC24557.1.
AJ302079 mRNA. Translation: CAC24556.1.
AY066015 mRNA. Translation: AAL47681.2.
AJ575591 mRNA. Translation: CAE01472.1.
AB023175 mRNA. Translation: BAA76802.1. Different initiation.
AL110285 mRNA. Translation: CAB53715.2.
AL163301 Genomic DNA. Translation: CAB90496.1. Different initiation.
BC011044 mRNA. Translation: AAH11044.1.
BC064623 mRNA. Translation: AAH64623.1.
CCDSiCCDS13719.1. [Q9Y2G5-3]
CCDS13721.1. [Q9Y2G5-1]
RefSeqiNP_056042.1. NM_015227.4. [Q9Y2G5-1]
NP_598368.2. NM_133635.4. [Q9Y2G5-3]
UniGeneiHs.592164.

Genome annotation databases

EnsembliENST00000331343; ENSP00000329682; ENSG00000186866. [Q9Y2G5-1]
ENST00000334538; ENSP00000335427; ENSG00000186866. [Q9Y2G5-2]
ENST00000349485; ENSP00000339613; ENSG00000186866. [Q9Y2G5-3]
GeneIDi23275.
KEGGihsa:23275.
UCSCiuc002zhc.3. human. [Q9Y2G5-3]
uc002zhd.3. human. [Q9Y2G5-1]

Polymorphism databases

DMDMi59803123.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Peptide-O-fucosyltransferase 2

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ302080 mRNA. Translation: CAC24557.1 .
AJ302079 mRNA. Translation: CAC24556.1 .
AY066015 mRNA. Translation: AAL47681.2 .
AJ575591 mRNA. Translation: CAE01472.1 .
AB023175 mRNA. Translation: BAA76802.1 . Different initiation.
AL110285 mRNA. Translation: CAB53715.2 .
AL163301 Genomic DNA. Translation: CAB90496.1 . Different initiation.
BC011044 mRNA. Translation: AAH11044.1 .
BC064623 mRNA. Translation: AAH64623.1 .
CCDSi CCDS13719.1. [Q9Y2G5-3 ]
CCDS13721.1. [Q9Y2G5-1 ]
RefSeqi NP_056042.1. NM_015227.4. [Q9Y2G5-1 ]
NP_598368.2. NM_133635.4. [Q9Y2G5-3 ]
UniGenei Hs.592164.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4AP5 X-ray 3.00 A/B 22-429 [» ]
4AP6 X-ray 3.40 A/B/C/D 37-429 [» ]
ProteinModelPortali Q9Y2G5.
SMRi Q9Y2G5. Positions 41-429.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116876. 2 interactions.
IntActi Q9Y2G5. 3 interactions.
STRINGi 9606.ENSP00000339613.

Protein family/group databases

CAZyi GT68. Glycosyltransferase Family 68.

PTM databases

PhosphoSitei Q9Y2G5.

Polymorphism databases

DMDMi 59803123.

Proteomic databases

MaxQBi Q9Y2G5.
PaxDbi Q9Y2G5.
PRIDEi Q9Y2G5.

Protocols and materials databases

DNASUi 23275.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000331343 ; ENSP00000329682 ; ENSG00000186866 . [Q9Y2G5-1 ]
ENST00000334538 ; ENSP00000335427 ; ENSG00000186866 . [Q9Y2G5-2 ]
ENST00000349485 ; ENSP00000339613 ; ENSG00000186866 . [Q9Y2G5-3 ]
GeneIDi 23275.
KEGGi hsa:23275.
UCSCi uc002zhc.3. human. [Q9Y2G5-3 ]
uc002zhd.3. human. [Q9Y2G5-1 ]

Organism-specific databases

CTDi 23275.
GeneCardsi GC21M046683.
HGNCi HGNC:14683. POFUT2.
HPAi HPA044297.
MIMi 610249. gene.
neXtProti NX_Q9Y2G5.
PharmGKBi PA25867.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG77810.
HOVERGENi HBG053367.
InParanoidi Q9Y2G5.
KOi K03691.
OMAi ICAHARC.
OrthoDBi EOG76T9S1.
PhylomeDBi Q9Y2G5.
TreeFami TF314337.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_200626. O-glycosylation of TSR domain-containing proteins.

Miscellaneous databases

GenomeRNAii 23275.
NextBioi 45054.
PROi Q9Y2G5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y2G5.
Bgeei Q9Y2G5.
CleanExi HS_POFUT2.
Genevestigatori Q9Y2G5.

Family and domain databases

InterProi IPR019378. GDP-Fuc_O-FucTrfase.
[Graphical view ]
Pfami PF10250. O-FucT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The Caenorhabditis elegans ortholog of C21orf80, a potential new protein O-fucosyltransferase, is required for normal development."
    Menzel O., Vellai T., Takacs-Vellai K., Reymond A., Mueller F., Antonarakis S.E., Guipponi M.
    Genomics 84:320-330(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "A new superfamily of protein-O-fucosyltransferases, alpha2-fucosyltransferases, and alpha6-fucosyltransferases: phylogeny and identification of conserved peptide motifs."
    Martinez-Duncker I., Mollicone R., Candelier J.-J., Breton C., Oriol R.
    Glycobiology 13:1C-5C(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
  3. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
    Tissue: Testis.
  5. "The DNA sequence of human chromosome 21."
    Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
    , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
    Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS B AND C).
    Tissue: Brain.
  7. "C-mannosylation and O-fucosylation of the thrombospondin type 1 module."
    Hofsteenge J., Huwiler K.G., Macek B., Hess D., Lawler J., Mosher D.F., Peter-Katalinic J.
    J. Biol. Chem. 276:6485-6498(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Two distinct pathways for O-fucosylation of epidermal growth factor-like or thrombospondin type 1 repeats."
    Luo Y., Nita-Lazar A., Haltiwanger R.S.
    J. Biol. Chem. 281:9385-9392(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. Cited for: FUNCTION, MUTAGENESIS OF GLU-395 AND GLU-396.
  10. "O-fucosylation of thrombospondin type 1 repeats in ADAMTS-like-1/punctin-1 regulates secretion: implications for the ADAMTS superfamily."
    Wang L.W., Dlugosz M., Somerville R.P., Raed M., Haltiwanger R.S., Apte S.S.
    J. Biol. Chem. 282:17024-17031(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Structure of human POFUT2: insights into thrombospondin type 1 repeat fold and O-fucosylation."
    Chen C.I., Keusch J.J., Klein D., Hess D., Hofsteenge J., Gut H.
    EMBO J. 31:3183-3197(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 22-429 IN COMPLEX WITH GDP-FUCOSE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLU-54; TRP-92; TRP-152; TRP-273; ARG-294; ASP-297 AND GLU-396, GLYCOSYLATION AT ASN-189 AND ASN-259, DISULFIDE BONDS.

Entry informationi

Entry nameiOFUT2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2G5
Secondary accession number(s): Q6PJV1
, Q7Z4N0, Q8WWU6, Q9BQS4, Q9BQS5, Q9UFY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 15, 2005
Last modified: September 3, 2014
This is version 106 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 21
    Human chromosome 21: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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