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Protein

Alpha-(1,3)-fucosyltransferase 5

Gene

FUT5

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

Functioni

May catalyze alpha-1,3 glycosidic linkages involved in the expression of VIM-2, Lewis X/SSEA-1 and sialyl Lewis X antigens.

Catalytic activityi

GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-D-glucosaminyl-R = GDP + beta-D-galactosyl-(1->3)-(alpha-L-fucosyl-(1->4))-N-acetyl-beta-D-glucosaminyl-R.

Pathway: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

  • 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity Source: UniProtKB-EC
  • alpha-(1->3)-fucosyltransferase activity Source: UniProtKB
  • fucosyltransferase activity Source: ProtInc

GO - Biological processi

  • carbohydrate metabolic process Source: ProtInc
  • fucosylation Source: GOC
  • L-fucose catabolic process Source: UniProtKB
  • protein glycosylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.1.152. 2681.
2.4.1.65. 2681.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT10. Glycosyltransferase Family 10.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-(1,3)-fucosyltransferase 5 (EC:2.4.1.65)
Alternative name(s):
Fucosyltransferase 5
Fucosyltransferase V
Short name:
Fuc-TV
Short name:
FucT-V
Galactoside 3-L-fucosyltransferase
Gene namesi
Name:FUT5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:4016. FUT5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1515CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei16 – 3419Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini35 – 374340LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • Golgi apparatus Source: UniProtKB
  • Golgi cisterna membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28432.

Polymorphism and mutation databases

BioMutaiFUT5.
DMDMi1730135.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 374374Alpha-(1,3)-fucosyltransferase 5PRO_0000221105Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi60 – 601N-linked (GlcNAc...)Sequence Analysis
Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence Analysis
Glycosylationi167 – 1671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ11128.
PaxDbiQ11128.
PRIDEiQ11128.

PTM databases

PhosphoSiteiQ11128.

Expressioni

Tissue specificityi

Liver, colon and testis and trace amounts in T-cells and brain.

Gene expression databases

BgeeiQ11128.
CleanExiHS_FUT5.
ExpressionAtlasiQ11128. baseline.
GenevisibleiQ11128. HS.

Organism-specific databases

HPAiHPA046966.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000252675.

Structurei

3D structure databases

ProteinModelPortaliQ11128.
SMRiQ11128. Positions 200-339.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 10 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG283180.
HOGENOMiHOG000045583.
HOVERGENiHBG000274.
InParanoidiQ11128.
KOiK07633.
PhylomeDBiQ11128.

Family and domain databases

InterProiIPR001503. Glyco_trans_10.
[Graphical view]
PANTHERiPTHR11929. PTHR11929. 1 hit.
PfamiPF00852. Glyco_transf_10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q11128-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPLGPAKPQ WLWRRCLAGL LFQLLVAVCF FSYLRVSRDD ATGSPRPGLM
60 70 80 90 100
AVEPVTGAPN GSRCQDSMAT PAHPTLLILL WTWPFNTPVA LPRCSEMVPG
110 120 130 140 150
AADCNITADS SVYPQADAVI VHHWDIMYNP SANLPPPTRP QGQRWIWFSM
160 170 180 190 200
ESPSNCRHLE ALDGYFNLTM SYRSDSDIFT PYGWLEPWSG QPAHPPLNLS
210 220 230 240 250
AKTELVAWAV SNWKPDSARV RYYQSLQAHL KVDVYGRSHK PLPKGTMMET
260 270 280 290 300
LSRYKFYLAF ENSLHPDYIT EKLWRNALEA WAVPVVLGPS RSNYERFLPP
310 320 330 340 350
DAFIHVDDFQ SPKDLARYLQ ELDKDHARYL SYFRWRETLR PRSFSWALAF
360 370
CKACWKLQQE SRYQTVRSIA AWFT
Length:374
Mass (Da):43,008
Last modified:October 1, 1996 - v1
Checksum:iB825281521B57939
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti187 – 1871P → L.
Corresponds to variant rs778970 [ dbSNP | Ensembl ].
VAR_022122
Natural varianti338 – 3381T → M.
Corresponds to variant rs4807054 [ dbSNP | Ensembl ].
VAR_055845

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81485 Genomic DNA. Translation: AAA98117.1.
U27329 mRNA. Translation: AAC50188.1.
U27330 mRNA. Translation: AAC50189.1.
AK291087 mRNA. Translation: BAF83776.1.
AC024592 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW69134.1.
BC140905 mRNA. Translation: AAI40906.1.
CCDSiCCDS12154.1.
PIRiA42270.
RefSeqiNP_002025.2. NM_002034.2.
UniGeneiHs.631843.

Genome annotation databases

EnsembliENST00000252675; ENSP00000252675; ENSG00000130383.
GeneIDi2527.
KEGGihsa:2527.
UCSCiuc002mdo.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Fucosyltransferase 5

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81485 Genomic DNA. Translation: AAA98117.1.
U27329 mRNA. Translation: AAC50188.1.
U27330 mRNA. Translation: AAC50189.1.
AK291087 mRNA. Translation: BAF83776.1.
AC024592 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW69134.1.
BC140905 mRNA. Translation: AAI40906.1.
CCDSiCCDS12154.1.
PIRiA42270.
RefSeqiNP_002025.2. NM_002034.2.
UniGeneiHs.631843.

3D structure databases

ProteinModelPortaliQ11128.
SMRiQ11128. Positions 200-339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000252675.

Chemistry

BindingDBiQ11128.
ChEMBLiCHEMBL3146.

Protein family/group databases

CAZyiGT10. Glycosyltransferase Family 10.

PTM databases

PhosphoSiteiQ11128.

Polymorphism and mutation databases

BioMutaiFUT5.
DMDMi1730135.

Proteomic databases

MaxQBiQ11128.
PaxDbiQ11128.
PRIDEiQ11128.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000252675; ENSP00000252675; ENSG00000130383.
GeneIDi2527.
KEGGihsa:2527.
UCSCiuc002mdo.4. human.

Organism-specific databases

CTDi2527.
GeneCardsiGC19M005865.
H-InvDBHIX0213024.
HGNCiHGNC:4016. FUT5.
HPAiHPA046966.
MIMi136835. gene.
neXtProtiNX_Q11128.
PharmGKBiPA28432.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG283180.
HOGENOMiHOG000045583.
HOVERGENiHBG000274.
InParanoidiQ11128.
KOiK07633.
PhylomeDBiQ11128.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.152. 2681.
2.4.1.65. 2681.

Miscellaneous databases

ChiTaRSiFUT5. human.
GeneWikiiFUT5.
GenomeRNAii2527.
NextBioi9957.
PROiQ11128.
SOURCEiSearch...

Gene expression databases

BgeeiQ11128.
CleanExiHS_FUT5.
ExpressionAtlasiQ11128. baseline.
GenevisibleiQ11128. HS.

Family and domain databases

InterProiIPR001503. Glyco_trans_10.
[Graphical view]
PANTHERiPTHR11929. PTHR11929. 1 hit.
PfamiPF00852. Glyco_transf_10. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of a novel human alpha (1,3)fucosyltransferase gene and molecular comparison to the human Lewis blood group alpha (1,3/1,4)fucosyltransferase gene. Syntenic, homologous, nonallelic genes encoding enzymes with distinct acceptor substrate specificities."
    Weston B.W., Nair R.P., Larsen R.D., Lowe J.B.
    J. Biol. Chem. 267:4152-4160(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Peripheral blood leukocyte.
  2. "Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms."
    Cameron H.S., Szczepaniak D., Weston B.W.
    J. Biol. Chem. 270:20112-20122(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Colon, Kidney and Liver.
  3. "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].
  4. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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].

Entry informationi

Entry nameiFUT5_HUMAN
AccessioniPrimary (citable) accession number: Q11128
Secondary accession number(s): A8K4X2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 134 of the entry and version 1 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 19
    Human chromosome 19: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.