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P08037

- B4GT1_BOVIN

UniProt

P08037 - B4GT1_BOVIN

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Protein

Beta-1,4-galactosyltransferase 1

Gene

B4GALT1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

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.

Cofactori

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi254 – 2541Manganese
Binding sitei314 – 3141UDP-alpha-D-galactose
Metal bindingi347 – 3471Manganese; via tele nitrogen
Binding sitei359 – 3591N-acetyl-D-glucosamine

GO - Molecular functioni

  1. alpha-tubulin binding Source: UniProtKB
  2. beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity Source: UniProtKB
  3. beta-tubulin binding Source: UniProtKB
  4. lactose synthase activity Source: UniProtKB
  5. manganese ion binding Source: UniProtKB
  6. N-acetyllactosamine synthase activity Source: UniProtKB
  7. protein homodimerization activity Source: UniProtKB
  8. UDP-galactosyltransferase activity Source: UniProtKB

GO - Biological processi

  1. acute inflammatory response Source: Ensembl
  2. angiogenesis involved in wound healing Source: Ensembl
  3. binding of sperm to zona pellucida Source: Ensembl
  4. branching morphogenesis of an epithelial tube Source: Ensembl
  5. cell adhesion Source: Ensembl
  6. development of secondary sexual characteristics Source: Ensembl
  7. epithelial cell development Source: Ensembl
  8. extracellular matrix organization Source: Ensembl
  9. galactose metabolic process Source: Ensembl
  10. lactose biosynthetic process Source: Ensembl
  11. leukocyte migration Source: Ensembl
  12. mammary gland development Source: Ensembl
  13. negative regulation of cell proliferation Source: Ensembl
  14. oligosaccharide biosynthetic process Source: UniProtKB
  15. penetration of zona pellucida Source: Ensembl
  16. positive regulation of apoptotic process involved in mammary gland involution Source: Ensembl
  17. positive regulation of epithelial cell proliferation involved in wound healing Source: Ensembl
  18. protein N-linked glycosylation Source: UniProtKB
  19. regulation of acrosome reaction Source: Ensembl
  20. regulation of cellular component movement Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_205470. Pre-NOTCH Processing in Golgi.
REACT_210187. Interaction With The Zona Pellucida.
REACT_211440. Keratan sulfate biosynthesis.
REACT_225710. N-Glycan antennae elongation.
SABIO-RKP08037.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT7. Glycosyltransferase Family 7.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-1,4-galactosyltransferase 1 (EC:2.4.1.-)
Short name:
Beta-1,4-GalTase 1
Short name:
Beta4Gal-T1
Short name:
b4Gal-T1
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:
Including the following 4 domains:
Lactose synthase A protein (EC:2.4.1.22)
N-acetyllactosamine synthase (EC:2.4.1.90)
Alternative name(s):
Nal synthase
Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase (EC:2.4.1.38)
Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase (EC:2.4.1.-)
Gene namesi
Name:B4GALT1
Synonyms:GALT, GGTB2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 8

Subcellular locationi

Chain Processed beta-1,4-galactosyltransferase 1 : Secreted
Note: Soluble form found in body fluids.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2424CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei25 – 4420Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini45 – 402358LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. basolateral plasma membrane Source: UniProtKB
  2. brush border membrane Source: UniProtKB
  3. desmosome Source: UniProtKB
  4. external side of plasma membrane Source: UniProtKB
  5. extracellular space Source: Ensembl
  6. extracellular vesicular exosome Source: Ensembl
  7. glycocalyx Source: UniProtKB
  8. Golgi apparatus Source: UniProtKB
  9. Golgi trans cisterna Source: UniProtKB
  10. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Golgi apparatus, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi314 – 3141W → A: Reduces galactosyltransferase activity, lactose synthase activity and substrate binding by 99%. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 402Processed beta-1,4-galactosyltransferase 1PRO_0000296228
Chaini1 – 402402Beta-1,4-galactosyltransferase 1PRO_0000012276Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi90 – 901N-linked (GlcNAc...)1 Publication
Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi134 ↔ 176
Disulfide bondi247 ↔ 266

Post-translational modificationi

The soluble form derives from the membrane forms by proteolytic processing.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP08037.
PRIDEiP08037.

Interactioni

Subunit structurei

Homodimer; and heterodimer with alpha-lactalbumin to form lactose synthase.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LalbaP2975210EBI-1031436,EBI-1031454From a different organism.

Protein-protein interaction databases

IntActiP08037. 1 interaction.

Structurei

Secondary structure

1
402
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi149 – 1513Combined sources
Helixi155 – 1617Combined sources
Turni167 – 1693Combined sources
Beta strandi174 – 1774Combined sources
Beta strandi181 – 19010Combined sources
Helixi192 – 20817Combined sources
Beta strandi212 – 2209Combined sources
Beta strandi222 – 2243Combined sources
Helixi228 – 24215Combined sources
Beta strandi247 – 2515Combined sources
Beta strandi255 – 2595Combined sources
Helixi278 – 2803Combined sources
Beta strandi292 – 2976Combined sources
Helixi298 – 3036Combined sources
Beta strandi313 – 3164Combined sources
Helixi317 – 32711Combined sources
Turni337 – 3404Combined sources
Beta strandi341 – 3444Combined sources
Turni347 – 3493Combined sources
Helixi351 – 3533Combined sources
Helixi359 – 3646Combined sources
Helixi366 – 3694Combined sources
Turni370 – 3723Combined sources
Helixi375 – 3773Combined sources
Beta strandi381 – 3877Combined sources
Beta strandi392 – 3976Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FGXX-ray2.40A/B115-402[»]
1FR8X-ray2.40A/B115-402[»]
1NF5X-ray2.00B/D130-402[»]
1NHEX-ray2.50B/D130-402[»]
1NKHX-ray2.00B/D130-402[»]
1NMMX-ray2.00B/D130-402[»]
1NQIX-ray2.00B/D130-402[»]
1NWGX-ray2.32B/D130-402[»]
1O0RX-ray2.30A/B130-402[»]
1O23X-ray2.32B/D130-402[»]
1OQMX-ray2.10B/D130-402[»]
1PZTX-ray1.92A130-402[»]
1PZYX-ray2.30B/D130-402[»]
1TVYX-ray2.30A/B130-402[»]
1TW1X-ray2.30A/B130-402[»]
1TW5X-ray2.30A/B130-402[»]
1YROX-ray1.90B/D130-402[»]
2FYCX-ray2.00B/D130-402[»]
2FYDX-ray2.00B/D130-400[»]
4KRVX-ray2.40A/B130-402[»]
ProteinModelPortaliP08037.
SMRiP08037. Positions 131-402.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08037.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni187 – 1915UDP-alpha-D-galactose binding
Regioni226 – 2283UDP-alpha-D-galactose binding
Regioni253 – 2542UDP-alpha-D-galactose binding
Regioni316 – 3194N-acetyl-D-glucosamine binding
Regioni347 – 3493UDP-alpha-D-galactose binding

Sequence similaritiesi

Belongs to the glycosyltransferase 7 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG327897.
GeneTreeiENSGT00760000119140.
HOGENOMiHOG000231027.
HOVERGENiHBG058334.
InParanoidiP08037.
KOiK07966.
OMAiVGGRYTP.
OrthoDBiEOG7060R0.
TreeFamiTF312834.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR003859. Galactosyl_T.
IPR027791. Galactosyl_T_C.
IPR027995. Galactosyl_T_N.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR19300. PTHR19300. 1 hit.
PfamiPF02709. Glyco_transf_7C. 1 hit.
PF13733. Glyco_transf_7N. 1 hit.
[Graphical view]
PRINTSiPR02050. B14GALTRFASE.
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. Align

Isoform Long (identifier: P08037-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MKFREPLLGG SAAMPGASLQ RACRLLVAVC ALHLGVTLVY YLAGRDLRRL
60 70 80 90 100
PQLVGVHPPL QGSSHGAAAI GQPSGELRLR GVAPPPPLQN SSKPRSRAPS
110 120 130 140 150
NLDAYSHPGP GPGPGSNLTS APVPSTTTRS LTACPEESPL LVGPMLIEFN
160 170 180 190 200
IPVDLKLVEQ QNPKVKLGGR YTPMDCISPH KVAIIIPFRN RQEHLKYWLY
210 220 230 240 250
YLHPILQRQQ LDYGIYVINQ AGESMFNRAK LLNVGFKEAL KDYDYNCFVF
260 270 280 290 300
SDVDLIPMND HNTYRCFSQP RHISVAMDKF GFSLPYVQYF GGVSALSKQQ
310 320 330 340 350
FLSINGFPNN YWGWGGEDDD IYNRLAFRGM SVSRPNAVIG KCRMIRHSRD
360 370 380 390 400
KKNEPNPQRF DRIAHTKETM LSDGLNSLTY MVLEVQRYPL YTKITVDIGT

PS
Length:402
Mass (Da):44,843
Last modified:October 17, 2006 - v3
Checksum:iFABF94E74E0C6F81
GO
Isoform Short (identifier: P08037-2) [UniParc]FASTAAdd to Basket

Also known as: Golgi complex

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

Show »
Length:389
Mass (Da):43,484
Checksum:i6C016BFC25872CCA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 662HG → QA(PubMed:2105947)Curated
Sequence conflicti158 – 1581V → I in CAA32695. (PubMed:2502398)Curated
Sequence conflicti187 – 1871P → L in CAA32695. (PubMed:2502398)Curated
Sequence conflicti205 – 2062IL → MV in CAA32695. (PubMed:2502398)Curated
Sequence conflicti282 – 2821F → L in AAA30534. (PubMed:2419911)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1313Missing in isoform Short. CuratedVSP_018801Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14558 mRNA. Translation: CAA32695.1.
BC120415 mRNA. Translation: AAI20416.1.
M13214 mRNA. Translation: AAA30534.1.
AF515786 mRNA. Translation: AAM54035.2.
M25398 Genomic DNA. Translation: AAA30533.1.
J05217 mRNA. Translation: AAA30559.1.
PIRiI45897.
S05018.
RefSeqiNP_803478.1. NM_177512.2.
UniGeneiBt.5141.

Genome annotation databases

EnsembliENSBTAT00000020286; ENSBTAP00000020286; ENSBTAG00000015249. [P08037-2]
GeneIDi281781.
KEGGibta:281781.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14558 mRNA. Translation: CAA32695.1 .
BC120415 mRNA. Translation: AAI20416.1 .
M13214 mRNA. Translation: AAA30534.1 .
AF515786 mRNA. Translation: AAM54035.2 .
M25398 Genomic DNA. Translation: AAA30533.1 .
J05217 mRNA. Translation: AAA30559.1 .
PIRi I45897.
S05018.
RefSeqi NP_803478.1. NM_177512.2.
UniGenei Bt.5141.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FGX X-ray 2.40 A/B 115-402 [» ]
1FR8 X-ray 2.40 A/B 115-402 [» ]
1NF5 X-ray 2.00 B/D 130-402 [» ]
1NHE X-ray 2.50 B/D 130-402 [» ]
1NKH X-ray 2.00 B/D 130-402 [» ]
1NMM X-ray 2.00 B/D 130-402 [» ]
1NQI X-ray 2.00 B/D 130-402 [» ]
1NWG X-ray 2.32 B/D 130-402 [» ]
1O0R X-ray 2.30 A/B 130-402 [» ]
1O23 X-ray 2.32 B/D 130-402 [» ]
1OQM X-ray 2.10 B/D 130-402 [» ]
1PZT X-ray 1.92 A 130-402 [» ]
1PZY X-ray 2.30 B/D 130-402 [» ]
1TVY X-ray 2.30 A/B 130-402 [» ]
1TW1 X-ray 2.30 A/B 130-402 [» ]
1TW5 X-ray 2.30 A/B 130-402 [» ]
1YRO X-ray 1.90 B/D 130-402 [» ]
2FYC X-ray 2.00 B/D 130-402 [» ]
2FYD X-ray 2.00 B/D 130-400 [» ]
4KRV X-ray 2.40 A/B 130-402 [» ]
ProteinModelPortali P08037.
SMRi P08037. Positions 131-402.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P08037. 1 interaction.

Chemistry

BindingDBi P08037.
ChEMBLi CHEMBL3214.

Protein family/group databases

CAZyi GT7. Glycosyltransferase Family 7.

Proteomic databases

PaxDbi P08037.
PRIDEi P08037.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000020286 ; ENSBTAP00000020286 ; ENSBTAG00000015249 . [P08037-2 ]
GeneIDi 281781.
KEGGi bta:281781.

Organism-specific databases

CTDi 2683.

Phylogenomic databases

eggNOGi NOG327897.
GeneTreei ENSGT00760000119140.
HOGENOMi HOG000231027.
HOVERGENi HBG058334.
InParanoidi P08037.
KOi K07966.
OMAi VGGRYTP.
OrthoDBi EOG7060R0.
TreeFami TF312834.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_205470. Pre-NOTCH Processing in Golgi.
REACT_210187. Interaction With The Zona Pellucida.
REACT_211440. Keratan sulfate biosynthesis.
REACT_225710. N-Glycan antennae elongation.
SABIO-RK P08037.

Miscellaneous databases

EvolutionaryTracei P08037.
NextBioi 20805694.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR003859. Galactosyl_T.
IPR027791. Galactosyl_T_C.
IPR027995. Galactosyl_T_N.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view ]
PANTHERi PTHR19300. PTHR19300. 1 hit.
Pfami PF02709. Glyco_transf_7C. 1 hit.
PF13733. Glyco_transf_7N. 1 hit.
[Graphical view ]
PRINTSi PR02050. B14GALTRFASE.
SUPFAMi SSF53448. SSF53448. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of cDNA encoding the membrane-bound form of bovine beta 1,4-galactosyltransferase."
    D'Agostaro G., Bendiak B., Tropak M.
    Eur. J. Biochem. 183:211-217(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal skin.
  3. "Bovine galactosyltransferase: identification of a clone by direct immunological screening of a cDNA expression library."
    Shaper N.L., Shaper J.H., Meuth J.L., Fox J.L., Chang H., Kirsch I.R., Hollis G.F.
    Proc. Natl. Acad. Sci. U.S.A. 83:1573-1577(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 69-402.
  4. "Cloning and sequencing of cDNA of bovine N-acetylglucosamine (beta 1-4)galactosyltransferase."
    Narimatsu H., Sinha S., Brew K., Okayama H., Qasba P.K.
    Proc. Natl. Acad. Sci. U.S.A. 83:4720-4724(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 74-402.
  5. Qasba P.K., Narimatsu H., Masibay A.S.
    Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 164; 256 AND 265.
  6. "Expression of bovine beta-1,4-galactosyltransferase cDNA in COS-7 cells."
    Masibay A.S., Qasba P.K.
    Proc. Natl. Acad. Sci. U.S.A. 86:5733-5737(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-77.
  7. "Bovine beta 1-->4-galactosyltransferase: two sets of mRNA transcripts encode two forms of the protein with different amino-terminal domains. In vitro translation experiments demonstrate that both the short and the long forms of the enzyme are type II membrane-bound glycoproteins."
    Russo R.N., Shaper N.L., Shaper J.H.
    J. Biol. Chem. 265:3324-3331(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-165.
  8. "Identification of a region of UDP-galactose:N-acetylglucosamine beta 4-galactosyltransferase involved in UDP-galactose binding by differential labeling."
    Yadav S.P., Brew K.
    J. Biol. Chem. 265:14163-14169(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-90.
  9. "Structure and function in galactosyltransferase. Sequence locations of alpha-lactalbumin binding site, thiol groups, and disulfide bond."
    Yadav S.P., Brew K.
    J. Biol. Chem. 266:698-703(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BOND.
  10. "Crystal structures of the bovine beta4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose."
    Gastinel L.N., Cambillau C., Bourne Y.
    EMBO J. 18:3546-3557(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 115-402 IN COMPLEX WITH SUBSTRATE, DISULFIDE BONDS.
  11. "Crystal structure of lactose synthase reveals a large conformational change in its catalytic component, the beta1,4-galactosyltransferase-I."
    Ramakrishnan B., Qasba P.K.
    J. Mol. Biol. 310:205-218(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 117-402 IN COMPLEX WITH SUBSTRATE AND MANGANESE IONS.
  12. "Crystal structure of beta1,4-galactosyltransferase complex with UDP-Gal reveals an oligosaccharide acceptor binding site."
    Ramakrishnan B., Balaji P.V., Qasba P.K.
    J. Mol. Biol. 318:491-502(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 117-402 IN COMPLEX WITH SUBSTRATE AND MANGANESE IONS.
  13. "The role of tryptophan 314 in the conformational changes of beta1,4-galactosyltransferase-I."
    Ramasamy V., Ramakrishnan B., Boeggeman E., Qasba P.K.
    J. Mol. Biol. 331:1065-1076(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 117-402 OF MUTANT THR-342 IN COMPLEX WITH SUBSTRATE AND MANGANESE IONS, MUTAGENESIS OF TRP-314.

Entry informationi

Entry nameiB4GT1_BOVIN
AccessioniPrimary (citable) accession number: P08037
Secondary accession number(s): Q0VC05, Q8MIG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: October 17, 2006
Last modified: November 26, 2014
This is version 162 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3