Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O60909 (B4GT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. 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:
Beta-1,4-galactosyltransferase 2

Short name=Beta-1,4-GalTase 2
Short name=Beta4Gal-T2
Short name=b4Gal-T2
EC=2.4.1.-
Alternative name(s):
UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 2
UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 2

Including the following 4 domains:

  1. Lactose synthase A protein
    EC=2.4.1.22
  2. N-acetyllactosamine synthase
    EC=2.4.1.90
    Alternative name(s):
    Nal synthase
  3. Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase
    EC=2.4.1.38
  4. Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase
    EC=2.4.1.-
Gene names
Name:B4GALT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. Can produce lactose.

Catalytic activity

UDP-alpha-D-galactose + D-glucose = UDP + lactose.

UDP-alpha-D-galactose + N-acetyl-beta-D-glucosaminylglycopeptide = UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminylglycopeptide.

UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine.

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatusGolgi stack membrane; Single-pass type II membrane protein. Note: Trans cisternae of Golgi stack.

Tissue specificity

Weakly expressed in various tissues. Highest expression in prostate, testis, ovary, intestine, muscle, and in fetal brain.

Sequence similarities

Belongs to the glycosyltransferase 7 family.

Biophysicochemical properties

Kinetic parameters:

KM=71 µM for GlcNAc-B-S-pNP Ref.3

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandManganese
Metal-binding
   Molecular functionGlycosyltransferase
Transferase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

keratan sulfate biosynthetic process

Traceable author statement. Source: Reactome

keratan sulfate metabolic process

Traceable author statement. Source: Reactome

post-translational protein modification

Traceable author statement. Source: Reactome

protein N-linked glycosylation via asparagine

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi cisterna membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Golgi membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionN-acetyllactosamine synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

galactosyltransferase activity

Traceable author statement Ref.1. Source: ProtInc

lactose synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60909-1)

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: O60909-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-118: Missing.
     119-119: E → MPSTQLLAAAAAAATAPGPTPPPLAPGSLRSPVPCPVPRLPRCHPVLTRHLVL
Note: No experimental confirmation available.
Isoform 3 (identifier: O60909-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAVEVQEQWPCLPAAGCPGPLGGPVAACGM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 372372Beta-1,4-galactosyltransferase 2
PRO_0000080533

Regions

Topological domain1 – 1515Cytoplasmic Potential
Transmembrane16 – 3621Helical; Signal-anchor for type II membrane protein; Potential
Topological domain37 – 372336Lumenal Potential
Region150 – 1545UDP-alpha-D-galactose binding By similarity
Region189 – 1913UDP-alpha-D-galactose binding By similarity
Region217 – 2182UDP-alpha-D-galactose binding By similarity
Region280 – 2834N-acetyl-D-glucosamine binding By similarity
Region311 – 3133UDP-alpha-D-galactose binding By similarity

Sites

Metal binding2181Manganese By similarity
Metal binding3111Manganese; via tele nitrogen By similarity
Binding site2781UDP-alpha-D-galactose By similarity
Binding site3231N-acetyl-D-glucosamine By similarity

Amino acid modifications

Glycosylation661N-linked (GlcNAc...) Potential
Glycosylation711N-linked (GlcNAc...) Potential
Glycosylation3571N-linked (GlcNAc...) Potential
Disulfide bond97 ↔ 139 By similarity
Disulfide bond211 ↔ 230 By similarity

Natural variations

Alternative sequence1 – 118118Missing in isoform 2.
VSP_014103
Alternative sequence11M → MAVEVQEQWPCLPAAGCPGP LGGPVAACGM in isoform 3.
VSP_043010
Alternative sequence1191E → MPSTQLLAAAAAAATAPGPT PPPLAPGSLRSPVPCPVPRL PRCHPVLTRHLVL in isoform 2.
VSP_014104
Natural variant1221Q → H. Ref.7
Corresponds to variant rs1859728 [ dbSNP | Ensembl ].
VAR_020487
Natural variant3381G → R.
Corresponds to variant rs35904809 [ dbSNP | Ensembl ].
VAR_054021

Experimental info

Sequence conflict1001S → TS Ref.2
Sequence conflict1361P → S in AAC39733. Ref.2
Sequence conflict1771G → C in AAC39733. Ref.2
Sequence conflict315 – 3162KH → ND in AAC39733. Ref.2

Sequences

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

Last modified August 1, 1998. Version 1.
Checksum: A6F7800251AA1E4F

FASTA37241,972
        10         20         30         40         50         60 
MSRLLGGTLE RVCKAVLLLC LLHFLVAVIL YFDVYAQHLA FFSRFSARGP AHALHPAASS 

        70         80         90        100        110        120 
SSSSSNCSRP NATASSSGLP EVPSALPGPT APTLPPCPDS PPGLVGRLLI EFTSPMPLER 

       130        140        150        160        170        180 
VQRENPGVLM GGRYTPPDCT PAQTVAVIIP FRHREHHLRY WLHYLHPILR RQRLRYGVYV 

       190        200        210        220        230        240 
INQHGEDTFN RAKLLNVGFL EALKEDAAYD CFIFSDVDLV PMDDRNLYRC GDQPRHFAIA 

       250        260        270        280        290        300 
MDKFGFRLPY AGYFGGVSGL SKAQFLRING FPNEYWGWGG EDDDIFNRIS LTGMKISRPD 

       310        320        330        340        350        360 
IRIGRYRMIK HDRDKHNEPN PQRFTKIQNT KLTMKRDGIG SVRYQVLEVS RQPLFTNITV 

       370 
DIGRPPSWPP RG 

« Hide

Isoform 2 [UniParc].

Checksum: A483868104528A2B
Show »

FASTA30634,883
Isoform 3 [UniParc].

Checksum: 70B4877C779850C1
Show »

FASTA40144,764

References

« Hide 'large scale' references
[1]"A family of human beta4-galactosyltransferases. Cloning and expression of two novel UDP-galactose:beta-n-acetylglucosamine beta1, 4-galactosyltransferases, beta4Gal-T2 and beta4Gal-T3."
Almeida R., Amado M., David L., Levery S.B., Holmes E.H., Merkx G., van Kessel A.G., Rygaard E., Hassan H., Bennett E., Clausen H.
J. Biol. Chem. 272:31979-31991(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The expanding beta 4-galactosyltransferase gene family: messages from the databanks."
Lo N.-W., Shaper J.H., Pevsner J., Shaper N.L.
Glycobiology 8:517-526(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells."
Guo S., Sato T., Shirane K., Furukawa K.
Glycobiology 11:813-820(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), BIOPHYSICOCHEMICAL PROPERTIES.
Tissue: Erythroleukemia.
[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] (ISOFORMS 1 AND 3).
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [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 1), VARIANT HIS-122.
Tissue: Chondrosarcoma.
[8]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 149-372 (ISOFORMS 1/2).
Tissue: Uterus.
[9]"Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions."
Amado M., Almeida R., Schwientek T., Clausen H.
Biochim. Biophys. Acta 1473:35-53(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Beta-1,4-galactosyltransferase 2

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y12510 mRNA. Translation: CAA73112.1.
AF038660 mRNA. Translation: AAC39733.1.
AB024434 mRNA. Translation: BAA75819.1.
AK095873 mRNA. Translation: BAG53152.1.
AK293418 mRNA. Translation: BAG56925.1.
AL139220, AL357079 Genomic DNA. Translation: CAI19431.1.
AL139220, AL357079 Genomic DNA. Translation: CAI19432.1.
AL357079, AL139220 Genomic DNA. Translation: CAI16802.1.
AL357079, AL139220 Genomic DNA. Translation: CAI16803.1.
CH471059 Genomic DNA. Translation: EAX07062.1.
CH471059 Genomic DNA. Translation: EAX07063.1.
CH471059 Genomic DNA. Translation: EAX07064.1.
CH471059 Genomic DNA. Translation: EAX07065.1.
BC096821 mRNA. Translation: AAH96821.1.
AL137647 mRNA. Translation: CAB70857.1.
PIRT46511.
RefSeqNP_001005417.1. NM_001005417.2.
NP_003771.1. NM_003780.4.
NP_085076.2. NM_030587.2.
XP_005271361.1. XM_005271304.2.
UniGeneHs.632403.
Hs.736507.

3D structure databases

ProteinModelPortalO60909.
SMRO60909. Positions 97-365.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114247. 1 interaction.
IntActO60909. 1 interaction.
STRING9606.ENSP00000349293.

Chemistry

DrugBankDB00141. N-Acetyl-D-glucosamine.

Protein family/group databases

CAZyGT7. Glycosyltransferase Family 7.

PTM databases

PhosphoSiteO60909.

Proteomic databases

PaxDbO60909.
PRIDEO60909.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309519; ENSP00000310696; ENSG00000117411. [O60909-3]
ENST00000356836; ENSP00000349293; ENSG00000117411. [O60909-1]
ENST00000372324; ENSP00000361399; ENSG00000117411. [O60909-1]
ENST00000434555; ENSP00000407468; ENSG00000117411. [O60909-2]
GeneID8704.
KEGGhsa:8704.
UCSCuc001clg.3. human. [O60909-1]
uc001clh.3. human. [O60909-2]
uc010okl.2. human. [O60909-3]

Organism-specific databases

CTD8704.
GeneCardsGC01P044444.
HGNCHGNC:925. B4GALT2.
HPAHPA047739.
MIM604013. gene.
neXtProtNX_O60909.
PharmGKBPA25224.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG327897.
HOGENOMHOG000231027.
HOVERGENHBG058334.
InParanoidO60909.
KOK07967.
OMATNCSRPN.
OrthoDBEOG7060R0.
PhylomeDBO60909.
TreeFamTF312834.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
REACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressO60909.
BgeeO60909.
CleanExHS_B4GALT2.
GenevestigatorO60909.

Family and domain databases

InterProIPR003859. Galactosyl_T.
IPR027791. Galactosyl_T_C.
IPR027995. Galactosyl_T_N.
[Graphical view]
PANTHERPTHR19300. PTHR19300. 1 hit.
PfamPF02709. Glyco_transf_7C. 1 hit.
PF13733. Glyco_transf_7N. 1 hit.
[Graphical view]
PRINTSPR02050. B14GALTRFASE.
ProtoNetSearch...

Other

GeneWikiB4GALT2.
GenomeRNAi8704.
NextBio32635.
PROO60909.
SOURCESearch...

Entry information

Entry nameB4GT2_HUMAN
AccessionPrimary (citable) accession number: O60909
Secondary accession number(s): B3KTP0 expand/collapse secondary AC list , B4DE14, D3DPY6, D3DPY7, O60511, Q4V9L9, Q5T4X5, Q5T4Y5, Q9BUP6, Q9NSY7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 131 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 1

Human chromosome 1: entries, gene names and cross-references to MIM