SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q6Y288

- B3GLT_HUMAN

UniProt

Q6Y288 - B3GLT_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Beta-1,3-glucosyltransferase

Gene
B3GALTL, B3GTL
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

O-fucosyltransferase that transfers glucose toward fucose with a beta-1,3 linkage. Specifically glucosylates O-linked fucosylglycan on TSP type-1 domains of proteins, thereby contributing to elongation of O-fucosylglycan.1 Publication

Pathwayi

GO - Molecular functioni

  1. transferase activity, transferring glycosyl groups Source: UniProtKB-KW

GO - Biological processi

  1. fucose metabolic process Source: UniProtKB-KW
  2. protein glycosylation Source: UniProtKB-UniPathway
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

CAZyiGT31. Glycosyltransferase Family 31.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-1,3-glucosyltransferase (EC:2.4.1.-)
Short name:
Beta3Glc-T
Alternative name(s):
Beta-3-glycosyltransferase-like
Gene namesi
Name:B3GALTL
Synonyms:B3GTL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:20207. B3GALTL.

Subcellular locationi

Endoplasmic reticulum membrane; Single-pass type II membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66Cytoplasmic Reviewed prediction
Transmembranei7 – 2721Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini28 – 498471Lumenal Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Peters-plus syndrome (PpS) [MIM:261540]: Autosomal recessive disorder characterized by anterior eye-chamber abnormalities, disproportionate short stature, developmental delay, characteristic craniofacial features, cleft lip and/or palate.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi495 – 4984Missing: Abolishes endoplasmic reticulum localization. 1 Publication

Keywords - Diseasei

Congenital disorder of glycosylation

Organism-specific databases

MIMi261540. phenotype.
Orphaneti709. Peters-plus syndrome.
PharmGKBiPA144596515.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 498498Beta-1,3-glucosyltransferasePRO_0000252399Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi336 – 3361N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ6Y288.
PaxDbiQ6Y288.
PRIDEiQ6Y288.

PTM databases

PhosphoSiteiQ6Y288.

Expressioni

Tissue specificityi

Widely expressed, with highest levels in testis and uterus.2 Publications

Gene expression databases

BgeeiQ6Y288.
CleanExiHS_B3GALTL.
GenevestigatoriQ6Y288.

Organism-specific databases

HPAiHPA017664.

Interactioni

Protein-protein interaction databases

BioGridi126890. 1 interaction.
STRINGi9606.ENSP00000343002.

Structurei

3D structure databases

ProteinModelPortaliQ6Y288.
SMRiQ6Y288. Positions 268-442.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi495 – 4984Prevents secretion from ER

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG150034.
HOGENOMiHOG000007375.
HOVERGENiHBG059386.
InParanoidiQ6Y288.
KOiK13675.
OMAiTGGYSYV.
OrthoDBiEOG75XGMG.
PhylomeDBiQ6Y288.
TreeFamiTF313496.

Family and domain databases

InterProiIPR003378. Fringe-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF02434. Fringe. 2 hits.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6Y288-1 [UniParc]FASTAAdd to Basket

« Hide

MRPPACWWLL APPALLALLT CSLAFGLASE DTKKEVKQSQ DLEKSGISRK    50
NDIDLKGIVF VIQSQSNSFH AKRAEQLKKS ILKQAADLTQ ELPSVLLLHQ 100
LAKQEGAWTI LPLLPHFSVT YSRNSSWIFF CEEETRIQIP KLLETLRRYD 150
PSKEWFLGKA LHDEEATIIH HYAFSENPTV FKYPDFAAGW ALSIPLVNKL 200
TKRLKSESLK SDFTIDLKHE IALYIWDKGG GPPLTPVPEF CTNDVDFYCA 250
TTFHSFLPLC RKPVKKKDIF VAVKTCKKFH GDRIPIVKQT WESQASLIEY 300
YSDYTENSIP TVDLGIPNTD RGHCGKTFAI LERFLNRSQD KTAWLVIVDD 350
DTLISISRLQ HLLSCYDSGE PVFLGERYGY GLGTGGYSYI TGGGGMVFSR 400
EAVRRLLASK CRCYSNDAPD DMVLGMCFSG LGIPVTHSPL FHQARPVDYP 450
KDYLSHQVPI SFHKHWNIDP VKVYFTWLAP SDEDKARQET QKGFREEL 498
Length:498
Mass (Da):56,564
Last modified:October 17, 2006 - v2
Checksum:iCDC6A479A1564D48
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti370 – 3701E → K.4 Publications
Corresponds to variant rs1041073 [ dbSNP | Ensembl ].
VAR_027849

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti284 – 2841I → M in AAH68595. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY190526 mRNA. Translation: AAO37647.1.
AB101481 mRNA. Translation: BAD13528.1.
AK291273 mRNA. Translation: BAF83962.1.
AL137142, AL138965 Genomic DNA. Translation: CAI12432.2.
AL138965, AL137142 Genomic DNA. Translation: CAH73049.2.
CH471075 Genomic DNA. Translation: EAX08483.1.
BC068595 mRNA. Translation: AAH68595.1.
CCDSiCCDS9341.1.
RefSeqiNP_919299.3. NM_194318.3.
UniGeneiHs.13205.

Genome annotation databases

EnsembliENST00000343307; ENSP00000343002; ENSG00000187676.
GeneIDi145173.
KEGGihsa:145173.
UCSCiuc010aaz.3. human.

Polymorphism databases

DMDMi116243011.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY190526 mRNA. Translation: AAO37647.1 .
AB101481 mRNA. Translation: BAD13528.1 .
AK291273 mRNA. Translation: BAF83962.1 .
AL137142 , AL138965 Genomic DNA. Translation: CAI12432.2 .
AL138965 , AL137142 Genomic DNA. Translation: CAH73049.2 .
CH471075 Genomic DNA. Translation: EAX08483.1 .
BC068595 mRNA. Translation: AAH68595.1 .
CCDSi CCDS9341.1.
RefSeqi NP_919299.3. NM_194318.3.
UniGenei Hs.13205.

3D structure databases

ProteinModelPortali Q6Y288.
SMRi Q6Y288. Positions 268-442.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 126890. 1 interaction.
STRINGi 9606.ENSP00000343002.

Protein family/group databases

CAZyi GT31. Glycosyltransferase Family 31.

PTM databases

PhosphoSitei Q6Y288.

Polymorphism databases

DMDMi 116243011.

Proteomic databases

MaxQBi Q6Y288.
PaxDbi Q6Y288.
PRIDEi Q6Y288.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000343307 ; ENSP00000343002 ; ENSG00000187676 .
GeneIDi 145173.
KEGGi hsa:145173.
UCSCi uc010aaz.3. human.

Organism-specific databases

CTDi 145173.
GeneCardsi GC13P031774.
GeneReviewsi B3GALTL.
H-InvDB HIX0011217.
HGNCi HGNC:20207. B3GALTL.
HPAi HPA017664.
MIMi 261540. phenotype.
610308. gene.
neXtProti NX_Q6Y288.
Orphaneti 709. Peters-plus syndrome.
PharmGKBi PA144596515.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG150034.
HOGENOMi HOG000007375.
HOVERGENi HBG059386.
InParanoidi Q6Y288.
KOi K13675.
OMAi TGGYSYV.
OrthoDBi EOG75XGMG.
PhylomeDBi Q6Y288.
TreeFami TF313496.

Enzyme and pathway databases

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

Miscellaneous databases

GeneWikii B3GALTL.
GenomeRNAii 145173.
NextBioi 85032.
PROi Q6Y288.
SOURCEi Search...

Gene expression databases

Bgeei Q6Y288.
CleanExi HS_B3GALTL.
Genevestigatori Q6Y288.

Family and domain databases

InterProi IPR003378. Fringe-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view ]
Pfami PF02434. Fringe. 2 hits.
[Graphical view ]
SUPFAMi SSF53448. SSF53448. 1 hit.
PROSITEi PS00014. ER_TARGET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel human glycosyltransferase: primary structure and characterization of the gene and transcripts."
    Heinonen T.Y.K., Pasternack L., Lindfors K., Breton C., Gastinel L.N., Maeki M., Kainulainen H.
    Biochem. Biophys. Res. Commun. 309:166-174(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT LYS-370.
  2. "Molecular cloning and characterization of a novel human beta1,3-glucosyltransferase, which is localized at the endoplasmic reticulum and glucosylates O-linked fucosylglycan on thrombospondin type 1 repeat domain."
    Sato T., Sato M., Kiyohara K., Sogabe M., Shikanai T., Kikuchi N., Togayachi A., Ishida H., Ito H., Kameyama A., Gotoh M., Narimatsu H.
    Glycobiology 16:1194-1206(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF 495-ARG--LEU-498, VARIANT LYS-370.
  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], VARIANT LYS-370.
  4. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LYS-370.
  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].
    Tissue: Testis.
  7. "Peters plus syndrome is caused by mutations in B3GALTL, a putative glycosyltransferase."
    Lesnik Oberstein S.A., Kriek M., White S.J., Kalf M.E., Szuhai K., den Dunnen J.T., Breuning M.H., Hennekam R.C.M.
    Am. J. Hum. Genet. 79:562-566(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN PPS.

Entry informationi

Entry nameiB3GLT_HUMAN
AccessioniPrimary (citable) accession number: Q6Y288
Secondary accession number(s): A8K5F8, Q5W0H2, Q6NUI3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 17, 2006
Last modified: September 3, 2014
This is version 87 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 13
    Human chromosome 13: 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