Akr1b7

Functionⁱ

Reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. May play a role in the metabolism of xenobiotic aromatic aldehydes.1 Publication

Catalytic activityⁱ

Alditol + NAD(P)⁺ = aldose + NAD(P)H.2 Publications

Enzyme regulationⁱ

Inhibited by tolrestat and epalrestat.1 Publication

Kineticsⁱ

K_M=
1.5 µM for NADPH
2 Publications
Manual assertion based on experiment inⁱ
- Ref.4
  "Rat aldose reductase-like protein (AKR1B14) efficiently reduces the lipid peroxidation product 4-oxo-2-nonenal."
  Endo S., Matsunaga T., Fujita A., Tajima K., El-Kabbani O., Hara A.
  Biol. Pharm. Bull. 33:1886-1890(2010) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
- Ref.5
  "Structure of rat aldose reductase-like protein AKR1B14 holoenzyme: Probing the role of His269 in coenzyme binding by site-directed mutagenesis."
  Sundaram K., Dhagat U., Endo S., Chung R., Matsunaga T., Hara A., El-Kabbani O.
  Bioorg. Med. Chem. Lett. 21:801-804(2011) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH NADP, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-269.
K_M=
220 µM for NADH
2 Publications
Manual assertion based on experiment inⁱ
- Ref.4
  "Rat aldose reductase-like protein (AKR1B14) efficiently reduces the lipid peroxidation product 4-oxo-2-nonenal."
  Endo S., Matsunaga T., Fujita A., Tajima K., El-Kabbani O., Hara A.
  Biol. Pharm. Bull. 33:1886-1890(2010) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
- Ref.5
  "Structure of rat aldose reductase-like protein AKR1B14 holoenzyme: Probing the role of His269 in coenzyme binding by site-directed mutagenesis."
  Sundaram K., Dhagat U., Endo S., Chung R., Matsunaga T., Hara A., El-Kabbani O.
  Bioorg. Med. Chem. Lett. 21:801-804(2011) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH NADP, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-269.
K_M=
0.16 µM for 4-oxo-2-nonenal
2 Publications
Manual assertion based on experiment inⁱ
- Ref.4
  "Rat aldose reductase-like protein (AKR1B14) efficiently reduces the lipid peroxidation product 4-oxo-2-nonenal."
  Endo S., Matsunaga T., Fujita A., Tajima K., El-Kabbani O., Hara A.
  Biol. Pharm. Bull. 33:1886-1890(2010) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
- Ref.5
  "Structure of rat aldose reductase-like protein AKR1B14 holoenzyme: Probing the role of His269 in coenzyme binding by site-directed mutagenesis."
  Sundaram K., Dhagat U., Endo S., Chung R., Matsunaga T., Hara A., El-Kabbani O.
  Bioorg. Med. Chem. Lett. 21:801-804(2011) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH NADP, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-269.
K_M=
37 µM for geraniol
2 Publications
Manual assertion based on experiment inⁱ
- Ref.4
  "Rat aldose reductase-like protein (AKR1B14) efficiently reduces the lipid peroxidation product 4-oxo-2-nonenal."
  Endo S., Matsunaga T., Fujita A., Tajima K., El-Kabbani O., Hara A.
  Biol. Pharm. Bull. 33:1886-1890(2010) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
- Ref.5
  "Structure of rat aldose reductase-like protein AKR1B14 holoenzyme: Probing the role of His269 in coenzyme binding by site-directed mutagenesis."
  Sundaram K., Dhagat U., Endo S., Chung R., Matsunaga T., Hara A., El-Kabbani O.
  Bioorg. Med. Chem. Lett. 21:801-804(2011) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH NADP, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-269.
K_M=
1.5 µM for 4-nitrobenzaldehyde
2 Publications
Manual assertion based on experiment inⁱ
- Ref.4
  "Rat aldose reductase-like protein (AKR1B14) efficiently reduces the lipid peroxidation product 4-oxo-2-nonenal."
  Endo S., Matsunaga T., Fujita A., Tajima K., El-Kabbani O., Hara A.
  Biol. Pharm. Bull. 33:1886-1890(2010) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
- Ref.5
  "Structure of rat aldose reductase-like protein AKR1B14 holoenzyme: Probing the role of His269 in coenzyme binding by site-directed mutagenesis."
  Sundaram K., Dhagat U., Endo S., Chung R., Matsunaga T., Hara A., El-Kabbani O.
  Bioorg. Med. Chem. Lett. 21:801-804(2011) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH NADP, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-269.

pH dependenceⁱ

Optimum pH is 6.5-7.2 Publications

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	44	NADP1 Publication	1
Active siteⁱ	49	Proton donorBy similarity	1
Siteⁱ	78	Lowers pKa of active site TyrBy similarity	1
Binding siteⁱ	184	NADP1 Publication	1
Binding siteⁱ	273	NADP1 Publication	1

Regions

Feature key	Position(s)	DescriptionActions	Length
Nucleotide bindingⁱ	20 – 21	NADP1 Publication	2
Nucleotide bindingⁱ	160 – 161	NADP1 Publication	2
Nucleotide bindingⁱ	210 – 215	NADP1 Publication	6
Nucleotide bindingⁱ	263 – 269	NADP1 Publication	7

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Ligand	NADP

Enzyme and pathway databases

Reactomeⁱ	R-RNO-193144. Estrogen biosynthesis. R-RNO-975634. Retinoid metabolism and transport.

Reactomeⁱ

R-RNO-193144. Estrogen biosynthesis.
R-RNO-975634. Retinoid metabolism and transport.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Aldose reductase-related protein 1 (EC:1.1.1.21) Alternative name(s): Aldehyde reductase Aldo-keto reductase family 1 member B7 Aldose reductase-like protein AKR1B14
Gene namesⁱ	Name:Akr1b7 Synonyms:Akr1b14
Organismⁱ	Rattus norvegicus (Rat)
Taxonomic identifierⁱ	10116 [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 › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Chromosome 4

Organism-specific databases

Rat genome database More...RGDⁱ	620257. Akr1b7.

RGDⁱ

620257. Akr1b7.

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	269	H → F or R: Reduced affinity for NADP. 1 Publication		1
Mutagenesisⁱ	269	H → M: Strongly reduced affinity for NADP. 1 Publication		1

Chemistry databases

ChEMBLⁱ	CHEMBL3421523.

ChEMBLⁱ

CHEMBL3421523.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000415351	1 – 316	Aldose reductase-related protein 1Add BLAST		316

Proteomic databases

PaxDbⁱ	Q5RJP0.
PRIDEⁱ	Q5RJP0.

PTM databases

iPTMnetⁱ	Q5RJP0.
PhosphoSitePlusⁱ	Q5RJP0.

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSRNOG00000009875.
Genevisibleⁱ	Q5RJP0. RN.

Interactionⁱ

Subunit structureⁱ

Monomer.By similarity

Protein-protein interaction databases

STRINGⁱ	10116.ENSRNOP00000013423.

STRINGⁱ

10116.ENSRNOP00000013423.

Chemistry databases

BindingDBⁱ

Q5RJP0.

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	4 – 6	Combined sources	3
Beta strandⁱ	12 – 19	Combined sources	8
Helixⁱ	27 – 37	Combined sources	11
Beta strandⁱ	42 – 44	Combined sources	3
Helixⁱ	47 – 49	Combined sources	3
Helixⁱ	52 – 64	Combined sources	13
Helixⁱ	70 – 72	Combined sources	3
Beta strandⁱ	74 – 79	Combined sources	6
Helixⁱ	81 – 83	Combined sources	3
Helixⁱ	86 – 100	Combined sources	15
Beta strandⁱ	105 – 111	Combined sources	7
Helixⁱ	138 – 150	Combined sources	13
Beta strandⁱ	153 – 161	Combined sources	9
Helixⁱ	164 – 171	Combined sources	8
Beta strandⁱ	182 – 186	Combined sources	5
Helixⁱ	194 – 201	Combined sources	8
Turnⁱ	202 – 204	Combined sources	3
Beta strandⁱ	206 – 210	Combined sources	5
Helixⁱ	228 – 230	Combined sources	3
Helixⁱ	232 – 241	Combined sources	10
Helixⁱ	245 – 254	Combined sources	10
Turnⁱ	255 – 257	Combined sources	3
Helixⁱ	267 – 273	Combined sources	7
Helixⁱ	283 – 290	Combined sources	8
Helixⁱ	302 – 304	Combined sources	3
Helixⁱ	311 – 313	Combined sources	3

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
	3O3R	X-ray	1.86	A/B	1-316	[»]
	3QKZ	X-ray	1.87	A/B	1-316	[»]
ProteinModelPortalⁱ	Q5RJP0.
SMRⁱ	Q5RJP0.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

Q5RJP0.

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGⁱ	KOG1577. Eukaryota. COG0656. LUCA.
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000119041.
HOGENOMⁱ	HOG000250272.
HOVERGENⁱ	HBG000020.
InParanoidⁱ	Q5RJP0.
KEGG Orthology (KO) More...KOⁱ	K00011.
OMAⁱ	THGYEST.
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0D69.
PhylomeDBⁱ	Q5RJP0.
TreeFamⁱ	TF106492.

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd06660. Aldo_ket_red. 1 hit.
Gene3Dⁱ	3.20.20.100. 1 hit.
InterProⁱ	View protein in InterPro IPR018170. Aldo/ket_reductase_CS. IPR020471. Aldo/keto_reductase. IPR023210. NADP_OxRdtase_dom. IPR036812. NADP_OxRdtase_dom_sf.
PANTHERⁱ	PTHR11732. PTHR11732. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00248. Aldo_ket_red. 1 hit.
PIRSFⁱ	PIRSF000097. AKR. 1 hit.
PRINTSⁱ	PR00069. ALDKETRDTASE.
SUPFAMⁱ	SSF51430. SSF51430. 1 hit.
PROSITEⁱ	View protein in PROSITE PS00798. ALDOKETO_REDUCTASE_1. 1 hit. PS00062. ALDOKETO_REDUCTASE_2. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

Q5RJP0-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MTTFVKLRTK AKMPLVGLGT WKSPPGQVKE AVKAAIDAGY RHFDCAYVYQ 
        60         70         80         90        100
NESEVGEAIQ EKIKEKAVRR EDLFIVSKLW STFFEKSLMK EAFQKTLSDL 
       110        120        130        140        150
KLDYLDLYLI HWPQGLQAGK EFLPKDSQGK VLMSKSTFLD AWEGMEELVD 
       160        170        180        190        200
QGLVKALGVS NFNHFQIERL LNKPGLKHKP VTNQVECHPY LTQEKLIQYC 
       210        220        230        240        250
HSKGIAVIAY SPLGSPDRPY AKPEDPVVLE IPKIKEIAAK HKKTIAQVLI 
       260        270        280        290        300
RFHVQRNVAV IPKSVTLSHI KENIQVFDFQ LSEEDMAAIL SLNRNWRACG 
       310 
LFVTSDEEDF PFHEEY

Length:316

Mass (Da):36,122

Last modified:December 21, 2004 - v1

Checksum:ⁱE5733ADA0ED5FF21

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CH473959 Genomic DNA. Translation: EDM15308.1. BC086563 mRNA. Translation: AAH86563.1.
NCBI Reference Sequences More...RefSeqⁱ	NP_446233.2. NM_053781.2.
UniGeneⁱ	Rn.32702.

Genome annotation databases

Ensemblⁱ	ENSRNOT00000013423; ENSRNOP00000013423; ENSRNOG00000009875.
GeneIDⁱ	116463.
KEGGⁱ	rno:116463.
UCSC genome browser More...UCSCⁱ	RGD:620257. rat.

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
Q5RJP0	UPI0004E482D9 Q9QZI2 UPI00025213E3 UPI0004E47681 UPI0003D0FA66	Rattus norvegicus (Rat)	316	UniRef90_Q5RJP0	Cluster: Aldose reductase-related protein 1	6

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
Q5RJP0	UPI0004E482D9 Q9QZI2 UPI00025213E3 UPI0004E47681 UPI0003D0FA66 UPI0005F54A96 P45377 UPI0000029472 UPI000A30E9AD UPI000A319D23 +80	Rattus norvegicus (Rat) Macaca nemestrina (Pig-tailed macaque) Mus musculus (Mouse) Mus pahari (Gairdner's shrew-mouse) (Coelomys pahari) Mus caroli (Ryukyu mouse) (Ricefield mouse) Elephantulus edwardii (Cape long-eared elephant shrew) Callithrix jacchus (White-tufted-ear marmoset) Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby) Chrysochloris asiatica (Cape golden mole) Bos mutus (wild yak) And more	316	UniRef50_Q5RJP0	Cluster: Aldose reductase-related protein 1	91

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CH473959 Genomic DNA. Translation: EDM15308.1. BC086563 mRNA. Translation: AAH86563.1.
NCBI Reference Sequences More...RefSeqⁱ	NP_446233.2. NM_053781.2.
UniGeneⁱ	Rn.32702.

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
	3O3R	X-ray	1.86	A/B	1-316	[»]
	3QKZ	X-ray	1.87	A/B	1-316	[»]
ProteinModelPortalⁱ	Q5RJP0.
SMRⁱ	Q5RJP0.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	10116.ENSRNOP00000013423.

STRINGⁱ

10116.ENSRNOP00000013423.

Chemistry databases

BindingDBⁱ	Q5RJP0.
ChEMBLⁱ	CHEMBL3421523.

PTM databases

iPTMnetⁱ	Q5RJP0.
PhosphoSitePlusⁱ	Q5RJP0.

Proteomic databases

PaxDbⁱ	Q5RJP0.
PRIDEⁱ	Q5RJP0.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSRNOT00000013423; ENSRNOP00000013423; ENSRNOG00000009875.
GeneIDⁱ	116463.
KEGGⁱ	rno:116463.
UCSC genome browser More...UCSCⁱ	RGD:620257. rat.

Organism-specific databases

CTDⁱ	11997.
Rat genome database More...RGDⁱ	620257. Akr1b7.

Phylogenomic databases

eggNOGⁱ	KOG1577. Eukaryota. COG0656. LUCA.
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000119041.
HOGENOMⁱ	HOG000250272.
HOVERGENⁱ	HBG000020.
InParanoidⁱ	Q5RJP0.
KEGG Orthology (KO) More...KOⁱ	K00011.
OMAⁱ	THGYEST.
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0D69.
PhylomeDBⁱ	Q5RJP0.
TreeFamⁱ	TF106492.

Enzyme and pathway databases

Reactomeⁱ	R-RNO-193144. Estrogen biosynthesis. R-RNO-975634. Retinoid metabolism and transport.

Reactomeⁱ

R-RNO-193144. Estrogen biosynthesis.
R-RNO-975634. Retinoid metabolism and transport.

Miscellaneous databases

EvolutionaryTraceⁱ	Q5RJP0.
Protein Ontology More...PROⁱ	PR:Q5RJP0.

Gene expression databases

Bgeeⁱ	ENSRNOG00000009875.
Genevisibleⁱ	Q5RJP0. RN.

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd06660. Aldo_ket_red. 1 hit.
Gene3Dⁱ	3.20.20.100. 1 hit.
InterProⁱ	View protein in InterPro IPR018170. Aldo/ket_reductase_CS. IPR020471. Aldo/keto_reductase. IPR023210. NADP_OxRdtase_dom. IPR036812. NADP_OxRdtase_dom_sf.
PANTHERⁱ	PTHR11732. PTHR11732. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00248. Aldo_ket_red. 1 hit.
PIRSFⁱ	PIRSF000097. AKR. 1 hit.
PRINTSⁱ	PR00069. ALDKETRDTASE.
SUPFAMⁱ	SSF51430. SSF51430. 1 hit.
PROSITEⁱ	View protein in PROSITE PS00798. ALDOKETO_REDUCTASE_1. 1 hit. PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ALD1_RAT
Accessionⁱ	Q5RJP0Primary (citable) accession number: Q5RJP0
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	January 25, 2012
	Last sequence update:	December 21, 2004
	Last modified:	March 28, 2018
	This is version 96 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

UniProtKB

UniParc

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Supporting data

UniProtKB - Q5RJP0 (ALD1_RAT)

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Aldose reductase-related protein 1

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<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 ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi

<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

<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

Sites

Regions

<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

Enzyme and pathway 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

Other locations

Cytosol

Mitochondrion

<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

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

<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

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

Chemistry 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

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Functionⁱ

Enzyme regulationⁱ

Kineticsⁱ

pH dependenceⁱ

GO - Molecular functionⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ