Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
We will be switching to the new UniProt website soon. Please explore and share your feedback. Take me to the new website.

UniProtKB - P08037 (B4GT1_BOVIN)

Entry version 206 (23 Feb 2022)
Sequence version 3 (17 Oct 2006)
Previous versions | rss
Add a publicationFeedback
Protein

Beta-1,4-galactosyltransferase 1

Gene

B4GALT1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

1 Publication

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. The secreted form is responsible for the synthesis of complex-type to N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids (PubMed:9405390).

1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mn2+By similarity

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.034 mM for UDP-galactose1 Publication
  2. KM=0.53 mM for benzyl-beta-D-GlcNAc1 Publication
  3. KM=9.6 mM for D-GlcNAc1 Publication
  1. Vmax=73 pmol/min/mg enzyme towards UDP-galactose1 Publication
  2. Vmax=44.1 pmol/min/mg enzyme towards for benzyl-beta-D-GlcNAc1 Publication
  3. Vmax=56.8 pmol/min/mg enzyme towards D-GlcNAc1 Publication
  4. Vmax=297 nmol/h/mg enzyme towards lactotriaosylceramide (d18:1(4E))1 Publication
  5. Vmax=333 nmol/h/mg enzyme towards lactopentaosylceramide (d18:1(4E))1 Publication
  6. Vmax=40.3 nmol/h/mg enzyme towards GlcCer1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.1 Publication
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi254Manganese1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei314UDP-alpha-D-galactose1
Metal bindingi347Manganese; via tele nitrogen1
Binding sitei359N-acetyl-D-glucosamine1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGlycosyltransferase, Transferase
Biological processLipid metabolism
LigandManganese, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.4.1.133, 908
2.4.1.38, 908
2.4.1.90, 908

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-BTA-2022854, Keratan sulfate biosynthesis
R-BTA-5653890, Lactose synthesis
R-BTA-6798695, Neutrophil degranulation
R-BTA-975577, N-Glycan antennae elongation

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P08037

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00378

Protein family/group databases

Carbohydrate-Active enZymes

More...CAZyi		GT7, Glycosyltransferase Family 7

MoonProt database of moonlighting proteins

More...MoonProti		P08037

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Beta-1,4-galactosyltransferase 1Curated (EC:2.4.1.-1 Publication)
Short name:
Beta-1,4-GalTase 1
Short name:
Beta4Gal-T1
Short name:
b4Gal-T1
Alternative name(s):
Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase
Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase1 Publication (EC:2.4.1.381 Publication)
Lactose synthase A protein (EC:2.4.1.22)
N-acetyllactosamine synthase1 Publication (EC:2.4.1.901 Publication)
Nal synthase
Neolactotriaosylceramide beta-1,4-galactosyltransferase1 Publication (EC:2.4.1.2751 Publication)
UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1
UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1
Cleaved into the following chain:
Processed beta-1,4-galactosyltransferase 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:B4GALT1
Synonyms:GALT, GGTB2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 8

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSBTAG00000015249

Vertebrate Gene Nomenclature Database

More...VGNCi		VGNC:26388, B4GALT1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 24CytoplasmicSequence analysisAdd BLAST24
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei25 – 44Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST20
Topological domaini45 – 402LumenalSequence analysisAdd BLAST358

Keywords - Cellular componenti

Cell membrane, Cell projection, Golgi apparatus, Membrane, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi314W → A: Reduces galactosyltransferase activity, lactose synthase activity and substrate binding by 99%. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3214

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000122761 – 402Beta-1,4-galactosyltransferase 1Add BLAST402
ChainiPRO_0000296228? – 402Processed beta-1,4-galactosyltransferase 1

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi90N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi117N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi134 ↔ 176
Disulfide bondi247 ↔ 266

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P08037

PeptideAtlas

More...PeptideAtlasi		P08037

PRoteomics IDEntifications database

More...PRIDEi		P08037

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P08037

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in milk (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSBTAG00000015249, Expressed in mammary gland and 96 other tissues

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; and heterodimer with alpha-lactalbumin to form lactose synthase (PubMed:10393171, PubMed:11419947, PubMed:12051854, PubMed:12927542).

Interacts (via N-terminal cytoplasmic domain) with UBE2Q1 (via N-terminus); the interaction is direct (By similarity).

By similarity4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

Protein interaction database and analysis system

More...IntActi		P08037, 1 interactor

STRING: functional protein association networks

More...STRINGi		9913.ENSBTAP00000020286

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P08037

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1402
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P08037

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P08037

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni77 – 130DisorderedSequence analysisAdd BLAST54
Regioni187 – 191UDP-alpha-D-galactose binding5
Regioni226 – 228UDP-alpha-D-galactose binding3
Regioni253 – 254UDP-alpha-D-galactose binding2
Regioni316 – 319N-acetyl-D-glucosamine binding4
Regioni347 – 349UDP-alpha-D-galactose binding3

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glycosyltransferase 7 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3916, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155244

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_044391_0_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P08037

Identification of Orthologs from Complete Genome Data

More...OMAi		CRYKIMG

Database of Orthologous Groups

More...OrthoDBi		1201618at2759

TreeFam database of animal gene trees

More...TreeFami		TF312834

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.90.550.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003859, Galactosyl_T
IPR027791, Galactosyl_T_C
IPR027995, Galactosyl_T_N
IPR029044, Nucleotide-diphossugar_trans

The PANTHER Classification System

More...PANTHERi		PTHR19300, PTHR19300, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02709, Glyco_transf_7C, 1 hit
PF13733, Glyco_transf_7N, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR02050, B14GALTRFASE

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53448, SSF53448, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket
Isoform Long (identifier: P08037-1) [UniParc]FASTAAdd to basket
Also known as: Cell surface

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti65 – 66HG → QA (PubMed:2105947).Curated2
Sequence conflicti158V → I in CAA32695 (PubMed:2502398).Curated1
Sequence conflicti187P → L in CAA32695 (PubMed:2502398).Curated1
Sequence conflicti205 – 206IL → MV in CAA32695 (PubMed:2502398).Curated2
Sequence conflicti282F → L in AAA30534 (PubMed:2419911).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0188011 – 13Missing in isoform Short. CuratedAdd BLAST13

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

Protein sequence database of the Protein Information Resource

More...PIRi		I45897
S05018

NCBI Reference Sequences

More...RefSeqi		NP_803478.1, NM_177512.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSBTAT00000020286; ENSBTAP00000020286; ENSBTAG00000015249 [P08037-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		281781

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		bta:281781

Keywords - Coding sequence diversityi

Alternative initiation

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
PIRiI45897
S05018
RefSeqiNP_803478.1, NM_177512.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB 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[»]
SMRiP08037
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP08037, 1 interactor
STRINGi9913.ENSBTAP00000020286

Chemistry databases

BindingDBiP08037
ChEMBLiCHEMBL3214

Protein family/group databases

CAZyiGT7, Glycosyltransferase Family 7
MoonProtiP08037

PTM databases

iPTMnetiP08037

Proteomic databases

PaxDbiP08037
PeptideAtlasiP08037
PRIDEiP08037

Genome annotation databases

EnsembliENSBTAT00000020286; ENSBTAP00000020286; ENSBTAG00000015249 [P08037-1]
GeneIDi281781
KEGGibta:281781

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2683
VEuPathDBiHostDB:ENSBTAG00000015249
VGNCiVGNC:26388, B4GALT1

Phylogenomic databases

eggNOGiKOG3916, Eukaryota
GeneTreeiENSGT00940000155244
HOGENOMiCLU_044391_0_1_1
InParanoidiP08037
OMAiCRYKIMG
OrthoDBi1201618at2759
TreeFamiTF312834

Enzyme and pathway databases

UniPathwayiUPA00378
BRENDAi2.4.1.133, 908
2.4.1.38, 908
2.4.1.90, 908
ReactomeiR-BTA-2022854, Keratan sulfate biosynthesis
R-BTA-5653890, Lactose synthesis
R-BTA-6798695, Neutrophil degranulation
R-BTA-975577, N-Glycan antennae elongation
SABIO-RKiP08037

Miscellaneous databases

EvolutionaryTraceiP08037

Gene expression databases

BgeeiENSBTAG00000015249, Expressed in mammary gland and 96 other tissues

Family and domain databases

Gene3Di3.90.550.10, 1 hit
InterProiView protein in InterPro
IPR003859, Galactosyl_T
IPR027791, Galactosyl_T_C
IPR027995, Galactosyl_T_N
IPR029044, Nucleotide-diphossugar_trans
PANTHERiPTHR19300, PTHR19300, 1 hit
PfamiView protein in Pfam
PF02709, Glyco_transf_7C, 1 hit
PF13733, Glyco_transf_7N, 1 hit
PRINTSiPR02050, B14GALTRFASE
SUPFAMiSSF53448, SSF53448, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiB4GT1_BOVIN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P08037
Secondary accession number(s): Q0VC05, Q8MIG0
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: October 17, 2006
Last modified: February 23, 2022
This is version 206 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again