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UniProtKB - Q12001 (ALG6_YEAST)

>sp|Q12001|ALG6_YEAST Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=ALG6 PE=1 SV=1
MAIGKRLLVNKPAEESFYASPMYDFLYPFRPVGNQWLPEYIIFVCAVILRCTIGLGPYSG
KGSPPLYGDFEAQRHWMEITQHLPLSKWYWYDLQYWGLDYPPLTAFHSYLLGLIGSFFNP
SWFALEKSRGFESPDNGLKTYMRSTVIISDILFYFPAVIYFTKWLGRYRNQSPIGQSIAA
SAILFQPSLMLIDHGHFQYNSVMLGLTAYAINNLLDEYYAMAAVCFVLSICFKQMALYYA
PIFFAYLLSRSLLFPKFNIARLTVIAFATLATFAIIFAPLYFLGGGLKNIHQCIHRIFPF
ARGIFEDKVANFWCVTNVFVKYKERFTIQQLQLYSLIATVIGFLPAMIMTLLHPKKHLLP
YVLIACSMSFFLFSFQVHEKTILIPLLPITLLYSSTDWNVLSLVSWINNVALFTLWPLLK
KDGLHLQYAVSFLLSNWLIGNFSFITPRFLPKSLTPGPSISSINSDYRRRSLLPYNVVWK
SFIIGTYIAMGFYHFLDQFVAPPSKYPDLWVLLNCAVGFICFSIFWLWSYYKIFTSGSKS
MKDL

Entry version 156 (25 May 2022)
Sequence version 1 (01 Nov 1997)
Previous versions | rss

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Protein

Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase

Gene

ALG6

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Adds the first glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Man₉GlcNAc₂-PP-Dol.

1 Publication

Catalytic activityⁱ

α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
dolichyl β-D-glucosyl phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
=
α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
dolichyl phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.5
  "Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway."
  Reiss G., te Heesen S., Zimmerman J., Robbins P.W., Aebi M.
  Glycobiology 6:493-498(1996) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, CHARACTERIZATION.
EC:
2.4.1.267
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.5
  "Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway."
  Reiss G., te Heesen S., Zimmerman J., Robbins P.W., Aebi M.
  Glycobiology 6:493-498(1996) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, CHARACTERIZATION.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol
zoom
+
dolichyl β-D-glucosyl phosphate
zoom
=
α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol
zoom
+
dolichyl phosphate
zoom
+
H⁺

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.

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Glycosyltransferase, Transferase

Molecular function

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAⁱ	2.4.1.267, 984
Reactomeⁱ	R-SCE-446193, Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein
UniPathwayⁱ	UPA00378

Protein family/group databases

Carbohydrate-Active enZymes More...CAZyⁱ	GT57, Glycosyltransferase Family 57

CAZyⁱ

GT57, Glycosyltransferase Family 57

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase (EC:2.4.1.2671 Publication) Alternative name(s): Asparagine-linked glycosylation protein 6 Dol-P-Glc:Man(9)GlcNAc(2)-PP-Dol alpha-1,3-glucosyltransferase Dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase
Gene namesⁱ	Name:ALG6 Ordered Locus Names:YOR002W ORF Names:UNA544
Organismⁱ	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifierⁱ	559292 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae
Proteomesⁱ	UP000002311 Componentⁱ: Chromosome XV

Organism-specific databases

Saccharomyces Genome Database More...SGDⁱ	S000005528, ALG6
VEuPathDBⁱ	FungiDB:YOR002W

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 35	CytoplasmicSequence analysisAdd BLAST	35
Transmembraneⁱ	36 – 56	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	57 – 104	LumenalSequence analysisAdd BLAST	48
Transmembraneⁱ	105 – 125	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	126 – 145	CytoplasmicSequence analysisAdd BLAST	20
Transmembraneⁱ	146 – 166	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	167 – 171	LumenalSequence analysis	5
Transmembraneⁱ	172 – 192	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	193 – 223	CytoplasmicSequence analysisAdd BLAST	31
Transmembraneⁱ	224 – 244	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	245 – 263	LumenalSequence analysisAdd BLAST	19
Transmembraneⁱ	264 – 284	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	285 – 332	CytoplasmicSequence analysisAdd BLAST	48
Transmembraneⁱ	333 – 353	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	354 – 356	LumenalSequence analysis	3
Transmembraneⁱ	357 – 377	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	378 – 398	CytoplasmicSequence analysisAdd BLAST	21
Transmembraneⁱ	399 – 419	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	420 – 425	LumenalSequence analysis	6
Transmembraneⁱ	426 – 446	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	447 – 481	CytoplasmicSequence analysisAdd BLAST	35
Transmembraneⁱ	482 – 502	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	503 – 508	LumenalSequence analysis	6
Transmembraneⁱ	509 – 529	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	530 – 544	CytoplasmicSequence analysisAdd BLAST	15

Keywords - Cellular componentⁱ

Endoplasmic reticulum, Membrane

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000174161	1 – 544	Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferaseAdd BLAST		544

Proteomic databases

PaxDbⁱ	Q12001
PRIDEⁱ	Q12001

PTM databases

iPTMnetⁱ	Q12001

iPTMnetⁱ

Q12001

Interactionⁱ

Protein-protein interaction databases

BioGRIDⁱ	34405, 342 interactors
STRINGⁱ	4932.YOR002W

Miscellaneous databases

RNActⁱ	Q12001, protein

RNActⁱ

Q12001, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	42 – 52	Combined sources	11
Helixⁱ	53 – 55	Combined sources	3
Beta strandⁱ	64 – 66	Combined sources	3
Helixⁱ	69 – 80	Combined sources	12
Turnⁱ	88 – 90	Combined sources	3
Turnⁱ	94 – 96	Combined sources	3
Helixⁱ	102 – 118	Combined sources	17
Turnⁱ	120 – 123	Combined sources	4
Beta strandⁱ	125 – 128	Combined sources	4
Beta strandⁱ	138 – 140	Combined sources	3
Helixⁱ	141 – 153	Combined sources	13
Helixⁱ	155 – 169	Combined sources	15
Helixⁱ	173 – 184	Combined sources	12
Helixⁱ	187 – 193	Combined sources	7
Turnⁱ	194 – 196	Combined sources	3
Helixⁱ	200 – 216	Combined sources	17
Helixⁱ	219 – 230	Combined sources	12
Helixⁱ	234 – 236	Combined sources	3
Helixⁱ	240 – 252	Combined sources	13
Helixⁱ	259 – 281	Combined sources	23
Turnⁱ	282 – 284	Combined sources	3
Helixⁱ	287 – 297	Combined sources	11
Beta strandⁱ	303 – 305	Combined sources	3
Beta strandⁱ	310 – 312	Combined sources	3
Helixⁱ	313 – 316	Combined sources	4
Turnⁱ	317 – 319	Combined sources	3
Helixⁱ	322 – 324	Combined sources	3
Helixⁱ	328 – 351	Combined sources	24
Beta strandⁱ	356 – 358	Combined sources	3
Helixⁱ	359 – 373	Combined sources	15
Helixⁱ	383 – 391	Combined sources	9
Helixⁱ	392 – 394	Combined sources	3
Helixⁱ	399 – 413	Combined sources	15
Helixⁱ	416 – 420	Combined sources	5
Beta strandⁱ	421 – 423	Combined sources	3
Helixⁱ	425 – 439	Combined sources	15
Turnⁱ	440 – 442	Combined sources	3
Helixⁱ	477 – 490	Combined sources	14
Helixⁱ	493 – 496	Combined sources	4
Turnⁱ	497 – 499	Combined sources	3
Beta strandⁱ	504 – 509	Combined sources	6
Helixⁱ	510 – 535	Combined sources	26

Show more details

3D structure databases

AlphaFoldDBⁱ	Q12001
SMRⁱ	Q12001
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the ALG6/ALG8 glucosyltransferase family.Curated

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG2575, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000153733
HOGENOMⁱ	CLU_008110_2_1_1
InParanoidⁱ	Q12001
OMAⁱ	RQWYFNT

Family and domain databases

InterProⁱ	View protein in InterPro IPR039488, ALG6 IPR004856, Glyco_trans_ALG6/ALG8
PANTHERⁱ	PTHR12413, PTHR12413, 1 hit PTHR12413:SF1, PTHR12413:SF1, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF03155, Alg6_Alg8, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Q12001-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MAIGKRLLVN KPAEESFYAS PMYDFLYPFR PVGNQWLPEY IIFVCAVILR 
        60         70         80         90        100
CTIGLGPYSG KGSPPLYGDF EAQRHWMEIT QHLPLSKWYW YDLQYWGLDY 
       110        120        130        140        150
PPLTAFHSYL LGLIGSFFNP SWFALEKSRG FESPDNGLKT YMRSTVIISD 
       160        170        180        190        200
ILFYFPAVIY FTKWLGRYRN QSPIGQSIAA SAILFQPSLM LIDHGHFQYN 
       210        220        230        240        250
SVMLGLTAYA INNLLDEYYA MAAVCFVLSI CFKQMALYYA PIFFAYLLSR 
       260        270        280        290        300
SLLFPKFNIA RLTVIAFATL ATFAIIFAPL YFLGGGLKNI HQCIHRIFPF 
       310        320        330        340        350
ARGIFEDKVA NFWCVTNVFV KYKERFTIQQ LQLYSLIATV IGFLPAMIMT 
       360        370        380        390        400
LLHPKKHLLP YVLIACSMSF FLFSFQVHEK TILIPLLPIT LLYSSTDWNV 
       410        420        430        440        450
LSLVSWINNV ALFTLWPLLK KDGLHLQYAV SFLLSNWLIG NFSFITPRFL 
       460        470        480        490        500
PKSLTPGPSI SSINSDYRRR SLLPYNVVWK SFIIGTYIAM GFYHFLDQFV 
       510        520        530        540 
APPSKYPDLW VLLNCAVGFI CFSIFWLWSY YKIFTSGSKS MKDL

Length:544

Mass (Da):62,783

Last modified:November 1, 1997 - v1

Checksum:ⁱ64BFA11A1F6D02B7

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	203	M → V in AAT92914 (PubMed:17322287).Curated		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U43491 Genomic DNA Translation: AAC49481.1 Z74910 Genomic DNA Translation: CAA99190.1 AY692895 Genomic DNA Translation: AAT92914.1 BK006948 Genomic DNA Translation: DAA10784.1
PIRⁱ	S61985
NCBI Reference Sequences More...RefSeqⁱ	NP_014644.1, NM_001183421.1

Genome annotation databases

EnsemblFungiⁱ	YOR002W_mRNA; YOR002W; YOR002W
GeneIDⁱ	854163
KEGGⁱ	sce:YOR002W

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q12001	Alpha-1,3-glucosyltransferase		SACAR		544	UniRef90_Q12001
Alpha-1,3-glucosyltransferase		SACK1		544
Alpha-1,3-glucosyltransferase		SACCK		544
Alpha-1,3-glucosyltransferase		YEASX		544
Alpha-1,3-glucosyltransferase		YEASK		544
+14

Protein	Similar proteins		Species	Score	Length	Source
Q12001	Alpha-1,3-glucosyltransferase		Saccharomyces boulardii (nom. inval.)		544	UniRef50_Q12001
Alpha-1,3-glucosyltransferase		YEAS2		544
Alpha-1,3-glucosyltransferase		Saccharomyces cerevisiae PE-2		544
Alpha-1,3-glucosyltransferase		YEAS7		544
Alpha-1,3-glucosyltransferase		SACK1		544
+77

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U43491 Genomic DNA Translation: AAC49481.1 Z74910 Genomic DNA Translation: CAA99190.1 AY692895 Genomic DNA Translation: AAT92914.1 BK006948 Genomic DNA Translation: DAA10784.1
PIRⁱ	S61985
RefSeqⁱ	NP_014644.1, NM_001183421.1

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 entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	6SNH	electron microscopy	3.90	X	1-544	[»]
	6SNI	electron microscopy	3.00	X	1-544	[»]
AlphaFoldDBⁱ	Q12001
SMRⁱ	Q12001
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	34405, 342 interactors
STRINGⁱ	4932.YOR002W

Protein family/group databases

CAZyⁱ	GT57, Glycosyltransferase Family 57

CAZyⁱ

GT57, Glycosyltransferase Family 57

PTM databases

iPTMnetⁱ	Q12001

iPTMnetⁱ

Q12001

Proteomic databases

PaxDbⁱ	Q12001
PRIDEⁱ	Q12001

Protocols and materials databases

ABCDⁱ	Q12001, 1 sequenced antibody

ABCDⁱ

Q12001, 1 sequenced antibody

Genome annotation databases

EnsemblFungiⁱ	YOR002W_mRNA; YOR002W; YOR002W
GeneIDⁱ	854163
KEGGⁱ	sce:YOR002W

Organism-specific databases

SGDⁱ	S000005528, ALG6
VEuPathDBⁱ	FungiDB:YOR002W

Phylogenomic databases

eggNOGⁱ	KOG2575, Eukaryota
GeneTreeⁱ	ENSGT00940000153733
HOGENOMⁱ	CLU_008110_2_1_1
InParanoidⁱ	Q12001
OMAⁱ	RQWYFNT

Enzyme and pathway databases

UniPathwayⁱ	UPA00378
BRENDAⁱ	2.4.1.267, 984
Reactomeⁱ	R-SCE-446193, Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:Q12001
RNActⁱ	Q12001, protein

Family and domain databases

InterProⁱ	View protein in InterPro IPR039488, ALG6 IPR004856, Glyco_trans_ALG6/ALG8
PANTHERⁱ	PTHR12413, PTHR12413, 1 hit PTHR12413:SF1, PTHR12413:SF1, 1 hit
Pfamⁱ	View protein in Pfam PF03155, Alg6_Alg8, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ALG6_YEAST
Accessionⁱ	Q12001Primary (citable) accession number: Q12001 Secondary accession number(s): D6W268, E9P8Y7
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
	Last sequence update:	November 1, 1997
	Last modified:	May 25, 2022
	This is version 156 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Fungal Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Reference proteome

Documents

Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
Yeast chromosome XV
Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q12001 (ALG6_YEAST)

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Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase

ALG6

Select a section on the left to see content.

<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

<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 <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

<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

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<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

Organism-specific databases

<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

Endoplasmic reticulum

Endoplasmic reticulum

Other locations

Topology

Keywords - Cellular componenti

<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

Proteomic databases

PTM databases

<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

Protein-protein interaction databases

Miscellaneous databases

<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

3D structure databases

<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

<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

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<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

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<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 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

Documents

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Functionⁱ

Catalytic activityⁱ

Pathwayⁱ: protein glycosylation

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ