P15291 (B4GT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-1,4-galactosyltransferase 1
Short name=Beta-1,4-GalTase 1
Short name=Beta4Gal-T1
Short name=b4Gal-T1
EC=2.4.1.-

Alternative name(s):
UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1
UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1

Cleaved into the following chain:

1. Processed beta-1,4-galactosyltransferase 1

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:	B4GALT1
Synonyms:	GGTB2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	398 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix.
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.
Subunit structure	Homodimer; and heterodimer with alpha-lactabulmin to form lactose synthase. Ref.14
Subcellular location	Isoform Long: Golgi apparatus › Golgi stack membrane; Single-pass type II membrane protein. Cell membrane; Single-pass type II membrane protein. Cell surface. Note: Found in trans cisternae of Golgi. Ref.13 Isoform Short: Golgi apparatus › Golgi stack membrane; Single-pass type II membrane protein. Note: Found in trans cisternae of Golgi. Ref.13 Processed beta-1,4-galactosyltransferase 1: Secreted. Note: Soluble form found in body fluids. Ref.13
Tissue specificity	Ubiquitously expressed, but at very low levels in fetal and adult brain.
Post-translational modification	The soluble form derives from the membrane forms by proteolytic processing.
Involvement in disease	Congenital disorder of glycosylation 2D (CDG2D) [MIM:607091]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions. Note: The disease is caused by mutations affecting the gene represented in this entry.
Sequence similarities	Belongs to the glycosyltransferase 7 family.

Ontologies

Keywords
Cellular component	Cell membrane Golgi apparatus Membrane Secreted
Coding sequence diversity	Alternative initiation Polymorphism
Disease	Congenital disorder of glycosylation
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Manganese Metal-binding
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Notch signaling pathway Traceable author statement. Source: Reactome acute inflammatory response Inferred from electronic annotation. Source: Compara angiogenesis involved in wound healing Inferred from electronic annotation. Source: Compara binding of sperm to zona pellucida Inferred from electronic annotation. Source: Compara branching morphogenesis of an epithelial tube Inferred from electronic annotation. Source: Compara cell adhesion Inferred from electronic annotation. Source: Compara development of secondary sexual characteristics Inferred from electronic annotation. Source: Compara epithelial cell development Inferred from electronic annotation. Source: Compara extracellular matrix organization Inferred from electronic annotation. Source: Compara galactose metabolic process Inferred from electronic annotation. Source: Compara keratan sulfate biosynthetic process Traceable author statement. Source: Reactome lactose biosynthetic process Inferred from electronic annotation. Source: Compara leukocyte migration Inferred from electronic annotation. Source: Compara mammary gland development Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara oligosaccharide biosynthetic process Inferred from direct assay Ref.12. Source: UniProtKB penetration of zona pellucida Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process involved in mammary gland involution Inferred from electronic annotation. Source: Compara positive regulation of epithelial cell proliferation involved in wound healing Inferred from electronic annotation. Source: Compara post-translational protein modification Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine Traceable author statement. Source: Reactome regulation of acrosome reaction Inferred from electronic annotation. Source: Compara regulation of cellular component movement Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi cisterna membrane Inferred from electronic annotation. Source: UniProtKB-SubCell Golgi membrane Traceable author statement. Source: Reactome Golgi trans cisterna Inferred from direct assay PubMed 6121819. Source: UniProtKB basolateral plasma membrane Inferred from direct assay PubMed 3917437. Source: UniProtKB brush border membrane Inferred from direct assay PubMed 3917437. Source: UniProtKB desmosome Inferred from direct assay PubMed 3917437. Source: UniProtKB external side of plasma membrane Inferred from direct assay PubMed 3917437. Source: UniProtKB extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell glycocalyx Inferred from direct assay PubMed 3917437. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	N-acetyllactosamine synthase activity Inferred from direct assay Ref.12PubMed 33805. Source: UniProtKB alpha-tubulin binding Inferred from direct assay Ref.14. Source: UniProtKB beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity Inferred from direct assay PubMed 33805. Source: UniProtKB lactose synthase activity Inferred from direct assay PubMed 33805. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein homodimerization activity Inferred from direct assay Ref.14. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform Long (identifier: P15291-1)

Also known as: Cell surface;

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 Short (identifier: P15291-2)

Also known as: Golgi complex;

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 398

398

Beta-1,4-galactosyltransferase 1

PRO_0000012278

Chain

? – 398

Processed beta-1,4-galactosyltransferase 1

PRO_0000296229

Regions

Topological domain

1 – 24

24

Cytoplasmic Potential

Transmembrane

25 – 44

20

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

45 – 398

354

Lumenal Potential

Sites

Metal binding

250

1

Manganese By similarity

Metal binding

343

1

Manganese By similarity

Site

77 – 78

2

Cleavage; to produce soluble form

Amino acid modifications

Glycosylation

113

1

N-linked (GlcNAc...) Potential

Disulfide bond

130 ↔ 172

By similarity

Disulfide bond

243 ↔ 262

By similarity

Natural variations

Alternative sequence

1 – 13

13

Missing in isoform Short.

VSP_018802

Natural variant

21

1

R → W.
Corresponds to variant rs1065764 [ dbSNP | Ensembl ].

VAR_054019

Natural variant

257

1

H → R.
Corresponds to variant rs9169 [ dbSNP | Ensembl ].

VAR_054020

Experimental info

Mutagenesis

282

1

Y → G: Reduction In N-acetylglucosamine binding. Ref.12

Mutagenesis

285

1

Y → F: No change in enzymatic activity. Ref.12

Mutagenesis

307

1

Y → G: Reduction In N-acetylglucosamine and UDP-galactose binding. Ref.12

Mutagenesis

308

1

W → G: Reduction In N-acetylglucosamine binding. Ref.12

Mutagenesis

310

1

W → G: Reduction In N-acetylglucosamine binding. Ref.12

Sequence conflict

10

1

G → R Ref.4

Sequence conflict

10

1

G → R Ref.5

Sequence conflict

11

1

Missing Ref.1

Sequence conflict

11

1

Missing Ref.3

Sequence conflict

11

1

Missing Ref.6

Sequence conflict

31 – 32

2

AL → VW in AAA35936. Ref.1

Sequence conflict

31 – 32

2

AL → VW in AAA35937. Ref.1

Sequence conflict

31 – 32

2

AL → VW in AAA68220. Ref.6

Sequence conflict

35

1

G → R in CAA31611. Ref.4

Sequence conflict

76

1

E → D in BAA06188. Ref.5

Sequence conflict

91 – 115

25

SSQPR…ASNLT → GKHAKSSFKQFLLQIKELSN PIDLD in AAA68219. Ref.6

Sequence conflict

212

1

Y → YGIY in CAA32247. Ref.1

Sequence conflict

212

1

Y → YGIY Ref.3

Sequence conflict

260

1

Y → D in AAA68218. Ref.6

Sequence conflict

292

1

L → S in BAA06188. Ref.5

Sequence conflict

337

1

R → T in BAA06188. Ref.5

Sequence conflict

340 – 341

2

MI → PA in AAA68220. Ref.6

Secondary structure

1

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398

Helix Strand Turn

Details...

Helix

151 – 157

7

Turn

163 – 165

3

Beta strand

170 – 173

4

Beta strand

177 – 186

10

Helix

188 – 204

17

Beta strand

208 – 216

9

Beta strand

218 – 220

3

Helix

224 – 238

15

Beta strand

243 – 247

5

Beta strand

251 – 255

5

Helix

274 – 276

3

Beta strand

288 – 293

6

Helix

294 – 299

6

Beta strand

309 – 312

4

Helix

313 – 323

11

Turn

333 – 335

3

Beta strand

337 – 340

4

Helix

359 – 365

7

Turn

366 – 368

3

Helix

371 – 373

3

Beta strand

377 – 384

8

Beta strand

387 – 393

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long (Cell surface) [UniParc]. Last modified October 17, 2006. Version 5. Checksum: 29B224C83C61E165	FASTA	398	43,920
	10 20 30 40 50 60 MRLREPLLSG SAAMPGASLQ RACRLLVAVC ALHLGVTLVY YLAGRDLSRL PQLVGVSTPL 70 80 90 100 110 120 QGGSNSAAAI GQSSGELRTG GARPPPPLGA SSQPRPGGDS SPVVDSGPGP ASNLTSVPVP 130 140 150 160 170 180 HTTALSLPAC PEESPLLVGP MLIEFNMPVD LELVAKQNPN VKMGGRYAPR DCVSPHKVAI 190 200 210 220 230 240 IIPFRNRQEH LKYWLYYLHP VLQRQQLDYG IYVINQAGDT IFNRAKLLNV GFQEALKDYD 250 260 270 280 290 300 YTCFVFSDVD LIPMNDHNAY RCFSQPRHIS VAMDKFGFSL PYVQYFGGVS ALSKQQFLTI 310 320 330 340 350 360 NGFPNNYWGW GGEDDDIFNR LVFRGMSISR PNAVVGRCRM IRHSRDKKNE PNPQRFDRIA 370 380 390 HTKETMLSDG LNSLTYQVLD VQRYPLYTQI TVDIGTPS
	Isoform Short (Golgi complex) [UniParc]. Checksum: A28CB67033107C83	FASTA	385	42,538
	10 20 30 40 50 60 MPGASLQRAC RLLVAVCALH LGVTLVYYLA GRDLSRLPQL VGVSTPLQGG SNSAAAIGQS 70 80 90 100 110 120 SGELRTGGAR PPPPLGASSQ PRPGGDSSPV VDSGPGPASN LTSVPVPHTT ALSLPACPEE 130 140 150 160 170 180 SPLLVGPMLI EFNMPVDLEL VAKQNPNVKM GGRYAPRDCV SPHKVAIIIP FRNRQEHLKY 190 200 210 220 230 240 WLYYLHPVLQ RQQLDYGIYV INQAGDTIFN RAKLLNVGFQ EALKDYDYTC FVFSDVDLIP 250 260 270 280 290 300 MNDHNAYRCF SQPRHISVAM DKFGFSLPYV QYFGGVSALS KQQFLTINGF PNNYWGWGGE 310 320 330 340 350 360 DDDIFNRLVF RGMSISRPNA VVGRCRMIRH SRDKKNEPNP QRFDRIAHTK ETMLSDGLNS 370 380 LTYQVLDVQR YPLYTQITVD IGTPS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of the full-length coding sequence for human galactosyltransferase (beta-N-acetylglucosaminide: beta 1,4-galactosyltransferase)." Masri K.A., Appert H.E., Fukuda M.N. Biochem. Biophys. Res. Commun. 157:657-663(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Near identity of HeLa cell galactosyltransferase with the human placental enzyme." Watzele G., Berger E.G. Nucleic Acids Res. 18:7174-7174(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Genomic structure and expression of human beta-1,4-galactosyltransferase." Mengle-Gaw L., McCoy-Haman M.F., Tiemeier D.C. Biochem. Biophys. Res. Commun. 176:1269-1276(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Complementary DNA cloning for galactosyltransferase associated with tumor and determination of antigenic epitopes recognized by specific monoclonal antibodies." Uejima T., Uemura M., Nozawa S., Narimatsu H. Cancer Res. 52:6158-6163(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[5]	"The beta 1, 4-galactosyltransferase gene is post-transcriptionally regulated during differentiation of mouse F9 teratocarcinoma cells." Kudo T., Narimatsu H. Glycobiology 5:397-403(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[6]	"Analysis of the sequences of human beta-1,4-galactosyltransferase cDNA clones." Chatterjee S.K., Mukerjee S., Tripathi P.K. Int. J. Biochem. Cell Biol. 27:329-336(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal liver.
[7]	"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] (ISOFORM LONG). Tissue: Testis.
[8]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	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. , 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].
[10]	"Isolation of a cDNA coding for human galactosyltransferase." Appert H.E., Rutherford T.J., Tarr G.E., Wiest J.S., Thomford N.R., McCorquodale D.J. Biochem. Biophys. Res. Commun. 139:163-168(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 138-398, PARTIAL PROTEIN SEQUENCE.
[11]	"Isolation of galactosyltransferase from human milk and the determination of its N-terminal amino acid sequence." Appert H.E., Rutherford T.J., Tarr G.E., Thomford N.R., McCorquodale D.J. Biochem. Biophys. Res. Commun. 138:224-229(1986) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 78-94.
[12]	"Analysis of the substrate binding sites of human galactosyltransferase by protein engineering." Aoki D., Appert H.E., Johnson D., Wong S.S., Fukuda M.N. EMBO J. 9:3171-3178(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 274-326, MUTAGENESIS OF TYR-282; TYR-285; TYR-307; TRP-308 AND TRP-310.
[13]	"Evidence for a molecular distinction between Golgi and cell surface forms of beta 1,4-galactosyltransferase." Lopez L.C., Youakim A., Evans S.C., Shur B.D. J. Biol. Chem. 266:15984-15991(1991) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE INITIATION, SUBCELLULAR LOCATION.
[14]	"Golgi retention mechanism of beta-1,4-galactosyltransferase. Membrane-spanning domain-dependent homodimerization and association with alpha- and beta-tubulins." Yamaguchi N., Fukuda M.N. J. Biol. Chem. 270:12170-12176(1995) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT.
[15]	"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.
[16]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Web resources

GeneReviews

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Beta-1,4-galactosyltransferase 1

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X14085 mRNA. Translation: CAA32247.1.
M22921 mRNA. Translation: AAA35936.1.
M22921 mRNA. Translation: AAA35937.1.
X55415 mRNA. Translation: CAA39073.1.
X55415 mRNA. Translation: CAA39074.1.
M70432 , M70427, M70428, M70429, M70430, M70431 Genomic DNA. Translation: AAB00776.1.
X13223 mRNA. Translation: CAA31611.1.
D29805 mRNA. Translation: BAA06188.1.
U10472 mRNA. Translation: AAA68218.1.
U10473 mRNA. Translation: AAA68219.1.
U10474 mRNA. Translation: AAA68220.1.
CH471071 Genomic DNA. Translation: EAW58520.1.
CH471071 Genomic DNA. Translation: EAW58521.1.
AK312797 mRNA. Translation: BAG35657.1.
AL161445 Genomic DNA. Translation: CAD13306.1.
M13701 mRNA. Translation: AAA35935.1.

IPI

IPI00215767.
IPI00759755.

PIR

JQ1030.

RefSeq

NP_001488.2. NM_001497.3.

UniGene

Hs.272011.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AE7	X-ray	2.00	A/B/C	126-397	[»]
2AEC	X-ray	2.00	A/B/C	126-397	[»]
2AES	X-ray	2.00	A/B/C	126-397	[»]
2AGD	X-ray	1.90	A/B/C	126-397	[»]
2AH9	X-ray	2.00	A/B/C	126-397	[»]
2FY7	X-ray	1.70	A	126-397	[»]
2FYA	X-ray	1.90	A	126-397	[»]
2FYB	X-ray	1.90	A	126-397	[»]
3EE5	X-ray	2.20	A/B/C	126-398	[»]
4EE3	X-ray	2.30	A/B/C	126-398	[»]
4EE4	X-ray	1.95	A/B/C	126-398	[»]
4EE5	X-ray	2.20	A/B/C	126-398	[»]
4EEA	X-ray	2.00	A/B/C	126-398	[»]
4EEG	X-ray	2.20	A/B/C	126-398	[»]
4EEM	X-ray	2.20	A/B/C	126-398	[»]
4EEO	X-ray	2.30	A/B/C	126-398	[»]

ProteinModelPortal

P15291.

ModBase

Search...

Protein-protein interaction databases

IntAct

P15291. 1 interaction.

STRING

9606.ENSP00000369055.

Protein family/group databases

CAZy

GT7. Glycosyltransferase Family 7.

PTM databases

PhosphoSite

P15291.

Polymorphism databases

DMDM

116241264.

Proteomic databases

PaxDb

P15291.

PRIDE

P15291.

Protocols and materials databases

DNASU

2683.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000379731; ENSP00000369055; ENSG00000086062.

GeneID

2683.

KEGG

hsa:2683.

UCSC

uc003zsg.2. human.

Organism-specific databases

CTD

2683.

GeneCards

GC09M033100.

HGNC

HGNC:924. B4GALT1.

HPA

HPA010806.
HPA010807.

MIM

137060. gene.
607091. phenotype.

neXtProt

NX_P15291.

Orphanet

79332. CDG syndrome type IId.

PharmGKB

PA25223.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG327897.

HOVERGEN

HBG058334.

InParanoid

P15291.

KO

K07966.

OMA

FNRLVFK.

OrthoDB

EOG4WWRK2.

Enzyme and pathway databases

BRENDA

2.4.1.38. 2681.

Reactome

REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_17015. Metabolism of proteins.

UniPathway

UPA00378.

Gene expression databases

ArrayExpress

P15291.

Bgee

P15291.

CleanEx

HS_B4GALT1.

Genevestigator

P15291.

GermOnline

ENSG00000086062. Homo sapiens.

Family and domain databases

InterPro

IPR003859. Galactosyl_T_2_met.
[Graphical view]

PANTHER

PTHR19300. PTHR19300. 1 hit.

Pfam

PF02709. Glyco_transf_7C. 1 hit.
[Graphical view]

PRINTS

PR02050. B14GALTRFASE.

ProtoNet

Search...

Other

BindingDB

P15291.

ChEMBL

CHEMBL4384.

ChiTaRS

B4GALT1. human.

DrugBank

DB00141. N-Acetyl-D-glucosamine.

EvolutionaryTrace

P15291.

GenomeRNAi

2683.

NextBio

10594.

SOURCE

Search...

Entry information

Entry name

B4GT1_HUMAN

Accession

Primary (citable) accession number: P15291
Secondary accession number(s): B2R710 , D3DRL2, Q12909, Q12910, Q12911, Q14456, Q14509, Q14523

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 152 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.