Reviewed, UniProtKB/Swiss-Prot O60512 (B4GT3_HUMAN)

Names and origin

Protein names

Recommended name:
    Beta-1,4-galactosyltransferase 3
      Short name=Beta-1,4-GalTase 3
      Short name=Beta4Gal-T3
      Short name=b4Gal-T3
    EC=2.4.1.-
Alternative name(s):
    UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 3
    UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 3
Including the following 3 domains:
    1- Recommended name:
            N-acetyllactosamine synthase
              EC=2.4.1.90
        Alternative name(s):
            Nal synthetase
    2- Recommended name:
            Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase
              EC=2.4.1.38
    3- Recommended name:
            Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase
              EC=2.4.1.-

Gene names

Name:

B4GALT3

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Catalytic activity	UDP-galactose + N-acetyl-beta-D-glucosaminylglycopeptide = UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminylglycopeptide. UDP-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine.
Cofactor	Manganese By similarity.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus › Golgi stack membrane; Single-pass type II membrane protein. Note: Trans cisternae of Golgi stack.
Tissue specificity	Found in various tissues. Highest expression in placenta, prostate, testis, ovary, intestine and muscle, and in fetal brain.
Sequence similarities	Belongs to the glycosyltransferase 7 family.
Biophysicochemical properties	Kinetic parameters: KM=63 µM for GlcNAc-B-S-pNP

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal-anchor Transmembrane
Ligand	Manganese Metal-binding
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi apparatus Inferred from direct assay. Source: HPA integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	N-acetyllactosamine synthase activity Inferred from electronic annotation. Source: EC beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity Inferred from electronic annotation. Source: EC manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O60512-1)

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: O60512-2)

The sequence of this isoform differs from the canonical sequence as follows:
     116-145: PAGCEPRSRTAIIVPHRAREHHLRLLLYHL → PAALPPAPLLAAPAACLWHLCHPPGWKWNI
     146-393: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 393	393	Beta-1,4-galactosyltransferase 3		PRO_0000080537
Regions
	Topological domain	1 – 10	10	Cytoplasmic Potential
	Transmembrane	11 – 31	21	Signal-anchor for type II membrane protein Potential
	Topological domain	32 – 393	362	Lumenal Potential
Sites
	Metal binding	197	1	Manganese By similarity
	Metal binding	291	1	Manganese By similarity
Amino acid modifications
	Glycosylation	57	1	N-linked (GlcNAc...) Potential
	Glycosylation	166	1	N-linked (GlcNAc...) Potential
	Glycosylation	337	1	N-linked (GlcNAc...) Potential
	Glycosylation	385	1	N-linked (GlcNAc...) Potential
	Disulfide bond	77 ↔ 119		By similarity
	Disulfide bond	190 ↔ 209		By similarity
Natural variations
	Alternative sequence	116 – 145	30	PAGCE…LLYHL → PAALPPAPLLAAPAACLWHL CHPPGWKWNI in isoform 2.		VSP_014106
	Alternative sequence	146 – 393	248	Missing in isoform 2.		VSP_014107
Experimental info
	Sequence conflict	64	1	A → R in AAC39734. Ref.2
	Sequence conflict	112	1	G → A in AAC39734. Ref.2
	Sequence conflict	223	1	K → S in AAC39734. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 21, 2005. Version 2. Checksum: CA0BF955F95ED1F4	FASTA	393	43,928
	10 20 30 40 50 60 MLRRLLERPC TLALLVGSQL AVMMYLSLGG FRSLSALFGR DQGPTFDYSH PRDVYSNLSH 70 80 90 100 110 120 LPGAPGGPPA PQGLPYCPER SPLLVGPVSV SFSPVPSLAE IVERNPRVEP GGRYRPAGCE 130 140 150 160 170 180 PRSRTAIIVP HRAREHHLRL LLYHLHPFLQ RQQLAYGIYV IHQAGNGTFN RAKLLNVGVR 190 200 210 220 230 240 EALRDEEWDC LFLHDVDLLP ENDHNLYVCD PRGPRHVAVA MNKFGYSLPY PQYFGGVSAL 250 260 270 280 290 300 TPDQYLKMNG FPNEYWGWGG EDDDIATRVR LAGMKISRPP TSVGHYKMVK HRGDKGNEEN 310 320 330 340 350 360 PHRFDLLVRT QNSWTQDGMN SLTYQLLARE LGPLYTNITA DIGTDPRGPR APSGPRYPPG 370 380 390 SSQAFRQEML QRRPPARPGP LSTANHTALR GSH
	Isoform 2. Checksum: 4231F9B50756A99C	FASTA	145	15,654
	10 20 30 40 50 60 MLRRLLERPC TLALLVGSQL AVMMYLSLGG FRSLSALFGR DQGPTFDYSH PRDVYSNLSH 70 80 90 100 110 120 LPGAPGGPPA PQGLPYCPER SPLLVGPVSV SFSPVPSLAE IVERNPRVEP GGRYRPAALP 130 140 PAPLLAAPAA CLWHLCHPPG WKWNI

References

	« Hide 'large scale' referencesShow '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: 9405390] [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: 9597550] [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: 11588157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), BIOPHYSICOCHEMICAL PROPERTIES.
[4]	"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. , 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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Ovary.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain, Eye and Lymph.
[7]	"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: 10580128] [Abstract] Cited for: REVIEW.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Beta-1,4-galactosyltransferase 3

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y12509 mRNA. Translation: CAA73111.1. AF038661 mRNA. Translation: AAC39734.1. AB024435 mRNA. Translation: BAA75820.1. AL590714 Genomic DNA. Translation: CAH72145.1. AK023311 mRNA. Translation: BAB14520.1. BC000276 mRNA. Translation: AAH00276.1. BC006099 mRNA. Translation: AAH06099.1. BC009985 mRNA. Translation: AAH09985.1.
IPI	IPI00654619. IPI00873139.
RefSeq	NP_003770.1.
UniGene	Hs.321231
3D structure databases
SMR	O60512. Positions 74-344.
ModBase	Search...
Protein-protein interaction databases
IntAct	O60512. 3 interactions.
STRING	O60512.
Protein family/group databases
CAZy	GT7. Glycosyltransferase Family 7.
Proteomic databases
PRIDE	O60512.
Genome annotation databases
Ensembl	ENST00000319769; ENSP00000320965; ENSG00000158850; Homo sapiens. [Genome view] ENST00000367998; ENSP00000356977; ENSG00000158850; Homo sapiens. [Genome view]
GeneID	8703.
KEGG	hsa:8703.
UCSC	uc001fyq.1. human.
Organism-specific databases
CTD	8703.
GeneCards	GC01M159407.
H-InvDB	HIX0001235.
HGNC	HGNC:926. B4GALT3.
HPA	HPA010793.
MIM	604014. gene.
PharmGKB	PA25225.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG05440.
HOGENOM	HBG717407.
HOVERGEN	O60512.
InParanoid	O60512.
OMA	DYSHPRD.
OrthoDB	EOG9W9MPD.
PhylomeDB	O60512.
Enzyme and pathway databases
BRENDA	2.4.1.38. 247. 2.4.1.90. 247.
Gene expression databases
ArrayExpress	O60512.
Bgee	O60512.
CleanEx	HS_B4GALT3.
Genevestigator	O60512.
GermOnline	ENSG00000158850. Homo sapiens.
Family and domain databases
InterPro	IPR003859. Galactosyl_T_2. [Graphical view]
PANTHER	PTHR19300. Galactosyl_T_2. 1 hit.
ProtoNet	Search...
Other Resources
DrugBank	DB00141. N-Acetyl-D-glucosamine.
NextBio	32631.
SOURCE	Search...

Entry information

Entry name

B4GT3_HUMAN

Accession

Primary (citable) accession number: O60512
Secondary accession number(s): O60910, Q9BPZ4, Q9H8T2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	June 21, 2005
Last modified:	February 9, 2010
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.