MNS2

Functionⁱ

Class I alpha-mannosidase essential for early N-glycan processing. Progressively trims alpha-1,2-linked mannose residues. Produces Man₅GlcNAc₂ from Man₈GlcNAc₂, but only Man₆GlcNAc₂ from Man₉GlcNAc₂. Has difficulty acting on the terminal mannose of the b-branch. Involved in root development and cell wall biosynthesis.

2 Publications

Catalytic activityⁱ

4
H₂O
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
N⁴-(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)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A_1,2,3B_1,2,3)
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
= 4
β-D-mannose
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
N⁴-(α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A_1,2)
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.6
  "Two Arabidopsis thaliana Golgi alpha-mannosidase I enzymes are responsible for plant N-glycan maturation."
  Kajiura H., Koiwa H., Nakazawa Y., Okazawa A., Kobayashi A., Seki T., Fujiyama K.
  Glycobiology 20:235-247(2010) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
EC:
3.2.1.113
- 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.6
  "Two Arabidopsis thaliana Golgi alpha-mannosidase I enzymes are responsible for plant N-glycan maturation."
  Kajiura H., Koiwa H., Nakazawa Y., Okazawa A., Kobayashi A., Seki T., Fujiyama K.
  Glycobiology 20:235-247(2010) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
4
H₂O
+
N⁴-(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)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A_1,2,3B_1,2,3)
N⁴-[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)-β-D-GlcNAc]-L-Asn residue
zoom
=
4
β-D-mannose
zoom
+
N⁴-(α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A_1,2)
N⁴-(α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc)-L-Asn residue
zoom
3
H₂O
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
N⁴-(α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[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)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A_1,2,3B_1,3)
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
= 3
β-D-mannose
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
N⁴-(α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A_1,2)
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.6
  "Two Arabidopsis thaliana Golgi alpha-mannosidase I enzymes are responsible for plant N-glycan maturation."
  Kajiura H., Koiwa H., Nakazawa Y., Okazawa A., Kobayashi A., Seki T., Fujiyama K.
  Glycobiology 20:235-247(2010) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
EC:
3.2.1.113
- 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.6
  "Two Arabidopsis thaliana Golgi alpha-mannosidase I enzymes are responsible for plant N-glycan maturation."
  Kajiura H., Koiwa H., Nakazawa Y., Okazawa A., Kobayashi A., Seki T., Fujiyama K.
  Glycobiology 20:235-247(2010) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
3
H₂O
+
N⁴-(α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[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)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A_1,2,3B_1,3)
N⁴-{α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[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)-β-D-GlcNAc}-L-Asn residue
zoom
=
3
β-D-mannose
zoom
+
N⁴-(α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A_1,2)
N⁴-(α-D-Man-(1→3)-[α-D-Man-(1→3)-[α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-β-D-GlcNAc)-L-Asn residue
zoom

Cofactorⁱ

Ca²⁺1 Publication, Mn²⁺1 Publication, Mg²⁺1 PublicationNote: Ca²⁺ or Mn²⁺. Mg²⁺ can be used to a lesser extent.1 Publication

Activity regulationⁱ

Inhibited by kifunensine and 1-deoxymannojirimycin, but not by swainsonine.2 Publications

pH dependenceⁱ

Optimum pH is 7.0. Stable from pH 5.0 to 10.0.1 Publication

Temperature dependenceⁱ

Optimum temperature is 25 degrees Celsius.1 Publication

Pathwayⁱ: protein glycosylation

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

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	180	Proton donorBy similarity	1
Active siteⁱ	312	By similarity	1
Active siteⁱ	424	Proton donorBy similarity	1
Active siteⁱ	446	By similarity	1
Metal bindingⁱ	530	CalciumBy similarity	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase
Ligand	Calcium, Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

BioCycⁱ	ARA:AT3G21160-MONOMER
BRENDAⁱ	3.2.1.113, 399
UniPathwayⁱ	UPA00378

Protein family/group databases

Carbohydrate-Active enZymes More...CAZyⁱ	GH47, Glycoside Hydrolase Family 47

CAZyⁱ

GH47, Glycoside Hydrolase Family 47

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS2 (EC:3.2.1.1131 Publication) Short name: AtMANIa Alternative name(s): Alpha-mannosidase IA
Gene namesⁱ	Name:MNS2 Synonyms:MANIA Ordered Locus Names:At3g21160 ORF Names:MSA6.31
Organismⁱ	Arabidopsis thaliana (Mouse-ear cress)
Taxonomic identifierⁱ	3702 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliopsida › Mesangiospermae › eudicotyledons › Gunneridae › Pentapetalae › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis
Proteomesⁱ	UP000006548 Componentⁱ: Chromosome 3

Organism-specific databases

Arabidopsis Information Portal More...Araportⁱ	AT3G21160
TAIRⁱ	locus:2092965, AT3G21160

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 27	CytoplasmicSequence analysisAdd BLAST	27
Transmembraneⁱ	28 – 45	Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST	18
Topological domainⁱ	46 – 572	LumenalSequence analysisAdd BLAST	527

Keywords - Cellular componentⁱ

Golgi apparatus, Membrane

Pathology & Biotechⁱ

Disruption phenotypeⁱ

No visible phenotype; due the redundancy with MNS1. Lack of complex N-glycans, shorter roots and increased lateral root formation in mns1 and mns2 double mutants.2 Publications

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000397934	1 – 572	Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS2Add BLAST		572

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Glycosylationⁱ	326	N-linked (GlcNAc...) asparagineSequence analysis	1
Disulfide bondⁱ	377 ↔ 410	By similarity
Glycosylationⁱ	460	N-linked (GlcNAc...) asparagineSequence analysis	1

Keywords - PTMⁱ

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbⁱ	Q8H116
PRIDEⁱ	Q8H116
ProteomicsDBⁱ	239061

Expressionⁱ

Tissue specificityⁱ

Expressed in flowers, siliques, stems, leaves, roots, pollen grains and shoot apical meristems.2 Publications

Gene expression databases

ExpressionAtlasⁱ	Q8H116, baseline and differential
Genevisibleⁱ	Q8H116, AT

Interactionⁱ

Protein-protein interaction databases

BioGRIDⁱ	7000, 1 interactor
IntActⁱ	Q8H116, 1 interactor
STRINGⁱ	3702.AT3G21160.1

Structureⁱ

3D structure databases

SMRⁱ	Q8H116
ModBaseⁱ	Search...

Family & Domainsⁱ

Coiled coil

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Coiled coilⁱ	51 – 81	Sequence analysisAdd BLAST		31

Sequence similaritiesⁱ

Belongs to the glycosyl hydrolase 47 family.Curated

Keywords - Domainⁱ

Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG2204, Eukaryota
HOGENOMⁱ	CLU_003818_3_2_1
InParanoidⁱ	Q8H116
Database of Orthologous Groups More...OrthoDBⁱ	693882at2759
PhylomeDBⁱ	Q8H116

Family and domain databases

Gene3Dⁱ	1.50.10.10, 1 hit
InterProⁱ	View protein in InterPro IPR012341, 6hp_glycosidase-like_sf IPR001382, Glyco_hydro_47 IPR036026, Seven-hairpin_glycosidases
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01532, Glyco_hydro_47, 1 hit
PRINTSⁱ	PR00747, GLYHDRLASE47
SUPFAMⁱ	SSF48225, SSF48225, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show all Align All

Q8H116-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MARNKLVSGS HGIWKYFNPA FYLRRPRRLA LLIILFVSVS MVVWDRQSLS 
        60         70         80         90        100
RDYQFEVSKL NEEVLRLQQM LEEIKSVTED VSVNSLKDVQ EDPVDAQRMQ 
       110        120        130        140        150
RVKEAMVHAW SSYEKYAWGQ DELQPQTKDG VDSFGGLGAT MIDALDTLYI 
       160        170        180        190        200
MGLDEQFQKA REWVASSLDF DKDYAASMFE TTIRVVGGLL SAYDLSGDKI 
       210        220        230        240        250
FLEKAMDIAD RLLPAWDTQS GIPYNIINLK HGNAHNPTWA GGDSILADSG 
       260        270        280        290        300
TEQLEFIALS QRTGDPKYQQ KVEKVISVLN KNFPADGLLP IYINPDTANP 
       310        320        330        340        350
SQSTITFGAM GDSFYEYLLK VWVFGNKTSA VKHYRDMWEK SMNGLLSLVK 
       360        370        380        390        400
KSTPLSFTYI CEKSGNSLID KMDELACFAP GMLALGASGY SDPAEGKKFL 
       410        420        430        440        450
TLAEELAWTC YNFYQSTPTK LAGENYFFNS GSDMSVGTSW NILRPETVES 
       460        470        480        490        500
LFYLWRLTGN KTYQEWGWNI FEAFEKNSRI ESGYVGLKDV NTGVKDNKMQ 
       510        520        530        540        550
SFFLAETLKY LYLLFSPTTV IPLDEWVFNT EAHPLKIKSR NDQVNLKQSN 
       560        570 
KVLLRKPAFR IRQRHYGRIT KK

Length:572

Mass (Da):65,136

Last modified:March 1, 2003 - v1

Checksum:ⁱ14614DD4525F9499

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	A0A1I9LRE8	A0A1I9LRE8_ARATH		alpha-1,2-Mannosidase alpha-1,2-Mannosidase, EC 3.2.1.-	MNS2 alpha-mannosidase 2, ALPHA-MANNOSIDASE IA, MANIA, MSA6.31, At3g21160	408	Annotation score:

Sequence cautionⁱ

The sequence BAB01459 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	113	Y → H in AAK92711 (PubMed:14593172).Curated		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AP000604, AB023045 Genomic DNA Translation: BAB01459.1 Sequence problems. CP002686 Genomic DNA Translation: AEE76468.1 AY050776 mRNA Translation: AAK92711.1 BT000893 mRNA Translation: AAN41293.1
NCBI Reference Sequences More...RefSeqⁱ	NP_566675.1, NM_113010.3

Genome annotation databases

EnsemblPlantsⁱ	AT3G21160.1; AT3G21160.1; AT3G21160
GeneIDⁱ	821668
Grameneⁱ	AT3G21160.1; AT3G21160.1; AT3G21160
KEGGⁱ	ath:AT3G21160

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q8H116	Putative alpha 1,2-mannosidase (Fragment)		ARATH		108	UniRef100_Q8H116

Protein	Similar proteins		Species	Score	Length	Source
Q8H116	Putative alpha 1,2-mannosidase (Fragment)		ARATH		108	UniRef90_Q8H116
alpha-1,2-Mannosidase		Capsella rubella		574
alpha-1,2-Mannosidase		ARAAL		573
alpha-1,2-Mannosidase		ARALL		571
alpha-1,2-Mannosidase		ARATH		572
+5

Protein	Similar proteins		Species	Score	Length	Source
Q8H116	Putative alpha 1,2-mannosidase (Fragment)		ARATH		108	UniRef50_Q8H116
alpha-1,2-Mannosidase		Capsella rubella		574
alpha-1,2-Mannosidase		ARAAL		573
alpha-1,2-Mannosidase		ARALL		571
alpha-1,2-Mannosidase		ANACO		576
+201

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AP000604, AB023045 Genomic DNA Translation: BAB01459.1 Sequence problems. CP002686 Genomic DNA Translation: AEE76468.1 AY050776 mRNA Translation: AAK92711.1 BT000893 mRNA Translation: AAN41293.1
RefSeqⁱ	NP_566675.1, NM_113010.3

3D structure databases

SMRⁱ	Q8H116
ModBaseⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	7000, 1 interactor
IntActⁱ	Q8H116, 1 interactor
STRINGⁱ	3702.AT3G21160.1

Protein family/group databases

CAZyⁱ	GH47, Glycoside Hydrolase Family 47

CAZyⁱ

GH47, Glycoside Hydrolase Family 47

Proteomic databases

PaxDbⁱ	Q8H116
PRIDEⁱ	Q8H116
ProteomicsDBⁱ	239061

Genome annotation databases

EnsemblPlantsⁱ	AT3G21160.1; AT3G21160.1; AT3G21160
GeneIDⁱ	821668
Grameneⁱ	AT3G21160.1; AT3G21160.1; AT3G21160
KEGGⁱ	ath:AT3G21160

Organism-specific databases

Araportⁱ	AT3G21160
TAIRⁱ	locus:2092965, AT3G21160

Phylogenomic databases

eggNOGⁱ	KOG2204, Eukaryota
HOGENOMⁱ	CLU_003818_3_2_1
InParanoidⁱ	Q8H116
OrthoDBⁱ	693882at2759
PhylomeDBⁱ	Q8H116

Enzyme and pathway databases

UniPathwayⁱ	UPA00378
BioCycⁱ	ARA:AT3G21160-MONOMER
BRENDAⁱ	3.2.1.113, 399

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:Q8H116

PROⁱ

PR:Q8H116

Gene expression databases

ExpressionAtlasⁱ	Q8H116, baseline and differential
Genevisibleⁱ	Q8H116, AT

Family and domain databases

Gene3Dⁱ	1.50.10.10, 1 hit
InterProⁱ	View protein in InterPro IPR012341, 6hp_glycosidase-like_sf IPR001382, Glyco_hydro_47 IPR036026, Seven-hairpin_glycosidases
Pfamⁱ	View protein in Pfam PF01532, Glyco_hydro_47, 1 hit
PRINTSⁱ	PR00747, GLYHDRLASE47
SUPFAMⁱ	SSF48225, SSF48225, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	MNS2_ARATH
Accessionⁱ	Q8H116Primary (citable) accession number: Q8H116 Secondary accession number(s): Q94A04, Q9LJB6
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
	Last sequence update:	March 1, 2003
	Last modified:	February 23, 2022
	This is version 110 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Plant Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Reference proteome

Documents

Glycosyl hydrolases
Classification of glycosyl hydrolase families and list of entries
Arabidopsis thaliana
Arabidopsis thaliana: entries and gene names
PATHWAY comments
Index of metabolic and biosynthesis pathways
SIMILARITY comments
Index of protein domains and families

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q8H116 (MNS2_ARATH)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the 'basket' to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS2

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 '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>pH dependencei

Temperature dependencei

<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

Sites

<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

Golgi apparatus

Endoplasmic reticulum

Endosome

Golgi apparatus

Other locations

Topology

Keywords - Cellular componenti

<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

<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

Amino acid modifications

Keywords - PTMi

Proteomic databases

<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

Gene expression 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

<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

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

Coiled coil

<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

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression 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

pH dependenceⁱ

Temperature dependenceⁱ

Pathwayⁱ: protein glycosylation

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ