ALDOA

Functionⁱ

Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein.1 Publication

Miscellaneous

In vertebrates, three forms of this ubiquitous glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver and aldolase C in brain.

Alkylation of Arg-43 inactivates the enzyme.

Catalytic activityⁱ

β-D-fructose 1,6-bisphosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
D-glyceraldehyde 3-phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
dihydroxyacetone phosphate
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.18
  "Mechanism of aldolase control of sorting nexin 9 function in endocytosis."
  Rangarajan E.S., Park H., Fortin E., Sygusch J., Izard T.
  J. Biol. Chem. 285:11983-11990(2010) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SNX9, INTERACTION WITH SNX9, SUBUNIT, CATALYTIC ACTIVITY.
EC:4.1.2.13
1 Publication
Manual assertion based on experiment inⁱ
- Ref.18
  "Mechanism of aldolase control of sorting nexin 9 function in endocytosis."
  Rangarajan E.S., Park H., Fortin E., Sygusch J., Izard T.
  J. Biol. Chem. 285:11983-11990(2010) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SNX9, INTERACTION WITH SNX9, SUBUNIT, CATALYTIC ACTIVITY.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
β-D-fructose 1,6-bisphosphate
zoom
=
D-glyceraldehyde 3-phosphate
zoom
+
dihydroxyacetone phosphate
zoom

Pathwayⁱ: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:

no protein annotated in this organism
Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI)
ATP-dependent 6-phosphofructokinase (PFKM), ATP-dependent 6-phosphofructokinase (PFKP), ATP-dependent 6-phosphofructokinase (PFKP), ATP-dependent 6-phosphofructokinase, platelet type (PFKP), ATP-dependent 6-phosphofructokinase, muscle type (PFKM)
Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase A (ALDOA), Fructose-bisphosphate aldolase B (ALDOB)

This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	43	SubstrateCombined sources1 Publication	1
Siteⁱ	73	Essential for substrate cleavage	1
Siteⁱ	108	Essential for substrate cleavage	1
Siteⁱ	147	Alkylation inactivates the enzyme	1
Active siteⁱ	188	Proton acceptor1 Publication	1
Active siteⁱ	230	Schiff-base intermediate with dihydroxyacetone-P1 Publication	1
Binding siteⁱ	304	SubstrateCombined sources1 Publication	1
Siteⁱ	362	Alkylation inactivates the enzyme; essential for the subsequent hydrolysis of the dihydroxyacetone Schiff base	1
Siteⁱ	364	Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate	1

GO - Molecular functionⁱ

fructose-bisphosphate aldolase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 20129922

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

glycolytic process
Source: UniProtKB
Inferred from direct assayⁱ
- 20129922
negative regulation of Arp2/3 complex-mediated actin nucleation
Source: CAFA
Inferred from mutant phenotypeⁱ
- 23495010
positive regulation of cell migration
Source: CAFA
Inferred from direct assayⁱ
- 23495010
protein homotetramerization
Source: UniProtKB
Inferred from physical interactionⁱ
- 20129922

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Lyase
Biological process	Glycolysis
Ligand	Schiff base

Enzyme and pathway databases

BRENDAⁱ	4.1.2.13 1749
SABIO-RKⁱ	P00883
UniPathwayⁱ	UPA00109;UER00183

Protein family/group databases

MoonProtⁱ	P00883

MoonProtⁱ

P00883

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Fructose-bisphosphate aldolase A (EC:4.1.2.13) Alternative name(s): Muscle-type aldolase
Gene namesⁱ	Name:ALDOA
Organismⁱ	Oryctolagus cuniculus (Rabbit)
Taxonomic identifierⁱ	9986 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus
Proteomesⁱ	UP000001811 Componentⁱ: Chromosome 6

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	35	E → A: Reduces activity 14-fold. 1 Publication	1
Mutagenesisⁱ	43	R → A: Reduces activity 14-fold. 1 Publication	1
Mutagenesisⁱ	129	D → V: Alters protein-protein interactions, leading to a dimeric protein.	1
Mutagenesisⁱ	147	K → A: Loss of activity. 1 Publication	1
Mutagenesisⁱ	188	E → A: Reduces activity over 100-fold. 1 Publication	1
Mutagenesisⁱ	188	E → Q: Reduces activity over 1000-fold. 1 Publication	1
Mutagenesisⁱ	190	E → Q: Reduces activity 20-fold. 1 Publication	1
Mutagenesisⁱ	230	K → M: Loss of activity. 1 Publication	1
Mutagenesisⁱ	304	R → A: Reduces activity 400-fold. 1 Publication	1

Chemistry databases

ChEMBLⁱ	CHEMBL4695

ChEMBLⁱ

CHEMBL4695

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed2 Publications
ChainⁱPRO_0000216938	2 – 364	Fructose-bisphosphate aldolase AAdd BLAST		363

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	9	PhosphothreonineBy similarity	1
Modified residueⁱ	36	PhosphoserineBy similarity	1
Modified residueⁱ	39	PhosphoserineBy similarity	1
Modified residueⁱ	42	N6-acetyllysine; alternateBy similarity	1
Cross-linkⁱ	42	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linkⁱ	42	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residueⁱ	46	PhosphoserineBy similarity	1
Modified residueⁱ	108	N6-acetyllysineBy similarity	1
Modified residueⁱ	111	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	111	N6-malonyllysine; alternateBy similarity	1
Modified residueⁱ	132	PhosphoserineBy similarity	1
Modified residueⁱ	272	PhosphoserineBy similarity	1
Modified residueⁱ	312	N6-malonyllysineBy similarity	1
Modified residueⁱ	330	N6-acetyllysineBy similarity	1
Modified residueⁱ	361	Deamidated asparagine; in form beta1 Publication	1

Post-translational modificationⁱ

Asn-361 in form alpha is deaminated to Asp in form beta.

Keywords - PTMⁱ

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEⁱ	P00883

PRIDEⁱ

P00883

PTM databases

iPTMnetⁱ	P00883

iPTMnetⁱ

P00883

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSOCUG00000006329 Expressed in 3 organ(s), highest expression level in prefrontal cortex

Bgeeⁱ

ENSOCUG00000006329 Expressed in 3 organ(s), highest expression level in prefrontal cortex

Interactionⁱ

Subunit structureⁱ

Homotetramer. Interacts with SNX9 and WAS. Interacts with FBP2; the interaction blocks FBP2 inhibition by physiological concentrations of AMP and reduces inhibition by Ca²⁺.6 Publications

Protein-protein interaction databases

BioGridⁱ	1172078, 2 interactors
IntActⁱ	P00883, 1 interactor
Molecular INTeraction database More...MINTⁱ	P00883
STRINGⁱ	9986.ENSOCUP00000020204

Chemistry databases

BindingDBⁱ

P00883

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	10 – 23	Combined sources	14
Beta strandⁱ	29 – 33	Combined sources	5
Helixⁱ	37 – 45	Combined sources	9
Turnⁱ	46 – 48	Combined sources	3
Helixⁱ	53 – 64	Combined sources	12
Helixⁱ	68 – 70	Combined sources	3
Turnⁱ	71 – 73	Combined sources	3
Beta strandⁱ	74 – 79	Combined sources	6
Helixⁱ	81 – 84	Combined sources	4
Turnⁱ	89 – 91	Combined sources	3
Helixⁱ	94 – 100	Combined sources	7
Beta strandⁱ	104 – 108	Combined sources	5
Beta strandⁱ	113 – 115	Combined sources	3
Beta strandⁱ	119 – 121	Combined sources	3
Beta strandⁱ	123 – 125	Combined sources	3
Helixⁱ	131 – 140	Combined sources	10
Beta strandⁱ	145 – 152	Combined sources	8
Beta strandⁱ	155 – 157	Combined sources	3
Helixⁱ	161 – 180	Combined sources	20
Beta strandⁱ	184 – 191	Combined sources	8
Helixⁱ	199 – 219	Combined sources	21
Helixⁱ	224 – 226	Combined sources	3
Helixⁱ	246 – 258	Combined sources	13
Beta strandⁱ	267 – 270	Combined sources	4
Helixⁱ	277 – 289	Combined sources	13
Beta strandⁱ	290 – 292	Combined sources	3
Beta strandⁱ	296 – 303	Combined sources	8
Helixⁱ	304 – 314	Combined sources	11
Helixⁱ	318 – 320	Combined sources	3
Helixⁱ	321 – 338	Combined sources	18
Turnⁱ	339 – 341	Combined sources	3
Beta strandⁱ	345 – 347	Combined sources	3
Helixⁱ	351 – 354	Combined sources	4
Beta strandⁱ	358 – 360	Combined sources	3
Helixⁱ	361 – 363	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	P00883
SMRⁱ	P00883
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P00883

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	272 – 274	Substrate bindingCombined sources1 Publication		3

Sequence similaritiesⁱ

Belongs to the class I fructose-bisphosphate aldolase family.Curated

Phylogenomic databases

eggNOGⁱ	KOG1557 Eukaryota COG3588 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000010235
HOGENOMⁱ	HOG000220876
HOVERGENⁱ	HBG002386
InParanoidⁱ	P00883
KEGG Orthology (KO) More...KOⁱ	K01623
OMAⁱ	DYREMLF
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0A9T

Family and domain databases

Gene3Dⁱ	3.20.20.70, 1 hit
InterProⁱ	View protein in InterPro IPR029768 Aldolase_I_AS IPR013785 Aldolase_TIM IPR000741 FBA_I
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00274 Glycolytic, 1 hit
PROSITEⁱ	View protein in PROSITE PS00158 ALDOLASE_CLASS_I, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P00883-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MPHSHPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE 
        60         70         80         90        100
NTEENRRFYR QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS 
       110        120        130        140        150
KGGVVGIKVD KGVVPLAGTN GETTTQGLDG LSERCAQYKK DGADFAKWRC 
       160        170        180        190        200
VLKIGEHTPS ALAIMENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK 
       210        220        230        240        250
RCQYVTEKVL AAVYKALSDH HIYLEGTLLK PNMVTPGHAC TQKYSHEEIA 
       260        270        280        290        300
MATVTALRRT VPPAVTGVTF LSGGQSEEEA SINLNAINKC PLLKPWALTF 
       310        320        330        340        350
SYGRALQASA LKAWGGKKEN LKAAQEEYVK RALANSLACQ GKYTPSGQAG 
       360 
AAASESLFIS NHAY

Length:364

Mass (Da):39,343

Last modified:January 23, 2007 - v2

Checksum:ⁱE61BCBC60F668324

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	35	E → Q AA sequence (PubMed:1122141).Curated	1
Sequence conflictⁱ	274 – 276	GQS → SQE AA sequence (PubMed:1122142).Curated	3
Sequence conflictⁱ	276	S → E AA sequence (PubMed:1122142).Curated	1
Sequence conflictⁱ	294 – 296	KPW → WPK AA sequence (PubMed:1122142).Curated	3
Sequence conflictⁱ	354	S → R in CAA24246 (PubMed:6687628).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	K02300 mRNA Translation: AAA31156.1 V00876 mRNA Translation: CAA24245.1 V00877 mRNA Translation: CAA24246.1
PIRⁱ	A92444 ADRBA
NCBI Reference Sequences More...RefSeqⁱ	NP_001075707.1, NM_001082238.1 XP_008256151.1, XM_008257929.2 XP_008256152.1, XM_008257930.2 XP_017197924.1, XM_017342435.1
UniGeneⁱ	Ocu.864

Genome annotation databases

Ensemblⁱ	ENSOCUT00000009869; ENSOCUP00000008499; ENSOCUG00000006329
GeneIDⁱ	100009055
KEGGⁱ	ocu:100009055

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P00883	Fructose-bisphosphate aldolase A		MOUSE		364	UniRef90_P05064
Fructose-bisphosphate aldolase A		RAT		364
Fructose-bisphosphate aldolase A		PONAB		364
Fructose-bisphosphate aldolase A		PANTR		364
Fructose-bisphosphate aldolase		Daphnia magna		364
+190

Protein	Similar proteins		Species	Score	Length	Source
P00883	Fructose-bisphosphate aldolase A		MOUSE		364	UniRef50_P05064
Fructose-bisphosphate aldolase A		RAT		364
Fructose-bisphosphate aldolase A		PANTR		364
Fructose-bisphosphate aldolase A		PONAB		364
Fructose-bisphosphate aldolase C		MACFA		364
+418

Cross-referencesⁱ

Web resourcesⁱ

Worthington enzyme manual

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	K02300 mRNA Translation: AAA31156.1 V00876 mRNA Translation: CAA24245.1 V00877 mRNA Translation: CAA24246.1
PIRⁱ	A92444 ADRBA
RefSeqⁱ	NP_001075707.1, NM_001082238.1 XP_008256151.1, XM_008257929.2 XP_008256152.1, XM_008257930.2 XP_017197924.1, XM_017342435.1
UniGeneⁱ	Ocu.864

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
	1ADO	X-ray	1.90	A/B/C/D	2-364	[»]
	1EWD	X-ray	2.46	A/B/C/D	2-364	[»]
	1EWE	X-ray	2.60	A/B/C/D	2-364	[»]
	1EX5	X-ray	2.20	A/B/C/D	2-364	[»]
	1J4E	X-ray	2.65	A/B/C/D	2-364	[»]
	1ZAH	X-ray	1.80	A/B/C/D	2-364	[»]
	1ZAI	X-ray	1.76	A/B/C/D	2-364	[»]
	1ZAJ	X-ray	1.89	A/B/C/D	2-364	[»]
	1ZAL	X-ray	1.89	A/B/C/D	2-364	[»]
	2OT0	X-ray	2.05	A/B/C/D	2-364	[»]
	2OT1	X-ray	2.05	A/B/C/D	2-364	[»]
	2QUT	X-ray	1.88	A/B/C/D	2-364	[»]
	2QUU	X-ray	1.98	A/B/C/D	2-364	[»]
	2QUV	X-ray	2.22	A/B/C/D	2-364	[»]
	3B8D	X-ray	2.00	A/B/C/D	2-364	[»]
	3BV4	X-ray	1.70	A	5-344	[»]
	3DFN	X-ray	1.86	A/B/C/D	2-364	[»]
	3DFO	X-ray	1.94	A/B/C/D	2-364	[»]
	3DFP	X-ray	2.05	A/B/C/D	2-364	[»]
	3DFQ	X-ray	1.82	A/B/C/D	2-364	[»]
	3DFS	X-ray	2.03	A/B/C/D	2-364	[»]
	3DFT	X-ray	1.94	A/B/C/D	2-364	[»]
	3LGE	X-ray	2.20	A/B/C/D	2-364	[»]
	3TU9	X-ray	2.09	A/B/C/D	2-364	[»]
	5F4X	X-ray	1.84	A/B/C/D	2-364	[»]
	5TLE	X-ray	1.58	A/B/C/D	2-364	[»]
	5TLH	X-ray	2.20	A/B/C/D	2-364	[»]
	5TLW	X-ray	2.29	A/B/C/D	2-364	[»]
	5TLZ	X-ray	1.97	A/B/C/D	2-364	[»]
	5VY5	electron microscopy	2.60	A/B/C/D	2-364	[»]
	6ALD	X-ray	2.30	A/B/C/D	2-364	[»]
ProteinModelPortalⁱ	P00883
SMRⁱ	P00883
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	1172078, 2 interactors
IntActⁱ	P00883, 1 interactor
MINTⁱ	P00883
STRINGⁱ	9986.ENSOCUP00000020204

Chemistry databases

BindingDBⁱ	P00883
ChEMBLⁱ	CHEMBL4695

Protein family/group databases

MoonProtⁱ	P00883

MoonProtⁱ

P00883

PTM databases

iPTMnetⁱ	P00883

iPTMnetⁱ

P00883

Proteomic databases

PRIDEⁱ	P00883

PRIDEⁱ

P00883

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSOCUT00000009869; ENSOCUP00000008499; ENSOCUG00000006329
GeneIDⁱ	100009055
KEGGⁱ	ocu:100009055

Organism-specific databases

CTDⁱ	226

CTDⁱ

226

Phylogenomic databases

eggNOGⁱ	KOG1557 Eukaryota COG3588 LUCA
GeneTreeⁱ	ENSGT00390000010235
HOGENOMⁱ	HOG000220876
HOVERGENⁱ	HBG002386
InParanoidⁱ	P00883
KOⁱ	K01623
OMAⁱ	DYREMLF
OrthoDBⁱ	EOG091G0A9T

Enzyme and pathway databases

UniPathwayⁱ	UPA00109;UER00183
BRENDAⁱ	4.1.2.13 1749
SABIO-RKⁱ	P00883

Miscellaneous databases

EvolutionaryTraceⁱ	P00883
Protein Ontology More...PROⁱ	PR:P00883

Gene expression databases

Bgeeⁱ	ENSOCUG00000006329 Expressed in 3 organ(s), highest expression level in prefrontal cortex

Bgeeⁱ

ENSOCUG00000006329 Expressed in 3 organ(s), highest expression level in prefrontal cortex

Family and domain databases

Gene3Dⁱ	3.20.20.70, 1 hit
InterProⁱ	View protein in InterPro IPR029768 Aldolase_I_AS IPR013785 Aldolase_TIM IPR000741 FBA_I
Pfamⁱ	View protein in Pfam PF00274 Glycolytic, 1 hit
PROSITEⁱ	View protein in PROSITE PS00158 ALDOLASE_CLASS_I, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ALDOA_RABIT
Accessionⁱ	P00883Primary (citable) accession number: P00883 Secondary accession number(s): Q28671
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
	Last sequence update:	January 23, 2007
	Last modified:	December 5, 2018
	This is version 163 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P00883 (ALDOA_RABIT)

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Fructose-bisphosphate aldolase A

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

Miscellaneous

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

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

<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

Other locations

Other locations

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

Mutagenesis

Chemistry databases

<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

PTM 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

Chemistry 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

Miscellaneous 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

Region

<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

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry 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

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

Pathwayⁱ: glycolysis

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

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ