cydA

Functionⁱ

A terminal oxidase that produces a proton motive force by the vectorial transfer of protons across the inner membrane. It is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H₂O, transferring 1 proton/electron.5 Publications

Catalytic activityⁱ

2 ubiquinol + O₂(Side 2) + 4 H⁺(Side 2) = 2 ubiquinone + 2 H₂O(Side 2) + 4 H⁺(Side 1).2 Publications

Cofactorⁱ

Protein has several cofactor binding sites:

Activity regulationⁱ

90% inhibited by cyanide and 2-heptyl-4-hydroxyquinoline N-oxide, at 1 mM and 40 µM respectively.1 Publication

Kineticsⁱ

pH 7.0, 37 degrees Celsius.

K_M=
0.1 mM for ubiquinol-1
1 Publication
Manual assertion based on experiment inⁱ
- Ref.6
  "The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain."
  Miller M.J., Gennis R.B.
  J. Biol. Chem. 258:9159-9165(1983) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION AS AN OXIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, SUBUNIT, INDUCTION.
K_M=
0.28 mM for 2,3,5,6-tetramethyl-p-phenylenediamine
1 Publication
Manual assertion based on experiment inⁱ
- Ref.6
  "The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain."
  Miller M.J., Gennis R.B.
  J. Biol. Chem. 258:9159-9165(1983) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION AS AN OXIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, SUBUNIT, INDUCTION.
K_M=
0.68 mM for N,N,N',N'-tetramethyl-p-phenylenediamine
1 Publication
Manual assertion based on experiment inⁱ
- Ref.6
  "The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain."
  Miller M.J., Gennis R.B.
  J. Biol. Chem. 258:9159-9165(1983) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION AS AN OXIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, SUBUNIT, INDUCTION.

V_max=
383 µmol/min/mg enzyme for ubiquinol-1
1 Publication
Manual assertion based on experiment inⁱ
- Ref.6
  "The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain."
  Miller M.J., Gennis R.B.
  J. Biol. Chem. 258:9159-9165(1983) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION AS AN OXIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, SUBUNIT, INDUCTION.
V_max=
270 µmol/min/mg enzyme for 2,3,5,6-tetramethyl-p-phenylenediamine
1 Publication
Manual assertion based on experiment inⁱ
- Ref.6
  "The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain."
  Miller M.J., Gennis R.B.
  J. Biol. Chem. 258:9159-9165(1983) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION AS AN OXIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, SUBUNIT, INDUCTION.
V_max=
126 µmol/min/mg enzyme for N,N,N',N'-tetramethyl-p-phenylenediamine
1 Publication
Manual assertion based on experiment inⁱ
- Ref.6
  "The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain."
  Miller M.J., Gennis R.B.
  J. Biol. Chem. 258:9159-9165(1983) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION AS AN OXIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, SUBUNIT, INDUCTION.

Pathwayⁱ: oxidative phosphorylation

This protein is involved in the pathway oxidative phosphorylation, which is part of Energy metabolism.
View all proteins of this organism that are known to be involved in the pathway oxidative phosphorylation and in Energy metabolism.

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	19	Iron (heme b595 axial ligand)Sequence analysis	1
Metal bindingⁱ	186	Iron (heme b558 axial ligand)	1
Metal bindingⁱ	393	Iron (heme b558 axial ligand)	1

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

aerobic electron transport chain
Source: EcoCyc
Inferred from direct assayⁱ
- 2414286
- 6321507
oxidative phosphorylation Source: UniProtKB-UniPathway

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Biological process	Electron transport, Transport
Ligand	Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCycⁱ	EcoCyc:CYDA-MONOMER MetaCyc:CYDA-MONOMER
BRENDAⁱ	1.10.3.14 2026
UniPathwayⁱ	UPA00705

Protein family/group databases

TCDBⁱ	3.D.4.3.2 the proton-translocating cytochrome oxidase (cox) superfamily

TCDBⁱ

3.D.4.3.2 the proton-translocating cytochrome oxidase (cox) superfamily

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Cytochrome bd-I ubiquinol oxidase subunit 1 (EC:1.10.3.141 Publication) Alternative name(s): Cytochrome bd-I oxidase subunit I Cytochrome d ubiquinol oxidase subunit I
Gene namesⁱ	Name:cydA Synonyms:cyd-1 Ordered Locus Names:b0733, JW0722
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG10173 cydA

EcoGeneⁱ

EG10173 cydA

Subcellular locationⁱ

Cell inner membrane
2 Publications
Manual assertion based on experiment inⁱ
- Ref.15
  "Gene fusions with beta-lactamase show that subunit I of the cytochrome bd quinol oxidase from E. coli has nine transmembrane helices with the O2 reactive site near the periplasmic surface."
  Zhang J., Barquera B., Gennis R.B.
  FEBS Lett. 561:58-62(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION, TOPOLOGY.
- Ref.16
  "Protein complexes of the Escherichia coli cell envelope."
  Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
  J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBUNIT, SUBCELLULAR LOCATION.
; Multi-pass membrane protein
2 Publications
Manual assertion based on experiment inⁱ
- Ref.15
  "Gene fusions with beta-lactamase show that subunit I of the cytochrome bd quinol oxidase from E. coli has nine transmembrane helices with the O2 reactive site near the periplasmic surface."
  Zhang J., Barquera B., Gennis R.B.
  FEBS Lett. 561:58-62(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION, TOPOLOGY.
- Ref.16
  "Protein complexes of the Escherichia coli cell envelope."
  Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
  J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBUNIT, SUBCELLULAR LOCATION.

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 15	PeriplasmicCuratedAdd BLAST	15
Transmembraneⁱ	16 – 35	HelicalCuratedAdd BLAST	20
Topological domainⁱ	36 – 54	CytoplasmicCuratedAdd BLAST	19
Transmembraneⁱ	55 – 69	HelicalCuratedAdd BLAST	15
Topological domainⁱ	70 – 96	PeriplasmicCuratedAdd BLAST	27
Transmembraneⁱ	97 – 114	HelicalCuratedAdd BLAST	18
Topological domainⁱ	115 – 128	CytoplasmicCuratedAdd BLAST	14
Transmembraneⁱ	129 – 146	HelicalCuratedAdd BLAST	18
Topological domainⁱ	147 – 186	PeriplasmicCuratedAdd BLAST	40
Transmembraneⁱ	187 – 203	HelicalCuratedAdd BLAST	17
Topological domainⁱ	204 – 219	CytoplasmicCuratedAdd BLAST	16
Transmembraneⁱ	220 – 235	HelicalCuratedAdd BLAST	16
Topological domainⁱ	236 – 390	PeriplasmicCuratedAdd BLAST	155
Transmembraneⁱ	391 – 407	HelicalCuratedAdd BLAST	17
Topological domainⁱ	408 – 423	CytoplasmicCuratedAdd BLAST	16
Transmembraneⁱ	424 – 441	HelicalCuratedAdd BLAST	18
Topological domainⁱ	442 – 472	PeriplasmicCuratedAdd BLAST	31
Transmembraneⁱ	473 – 487	HelicalCuratedAdd BLAST	15
Topological domainⁱ	488 – 522	CytoplasmicCuratedAdd BLAST	35

GO - Cellular componentⁱ

cytochrome complex
Source: EcoCyc
Inferred from direct assayⁱ
- 6307994
- 6321507
integral component of plasma membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 3013298
membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 1851043
plasma membrane
Source: EcoCyc
Inferred from direct assayⁱ

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechⁱ

Disruption phenotypeⁱ

A double cydA/cydB deletion shows increased sensitivity to reductant (beta-mercapoethanol).3 Publications

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	19	H → L or R: Loss of cytochrome b595 and heme d, no aerobic growth, complex assembles. 1 Publication	1
Mutagenesisⁱ	86	H → R: No effect. 1 Publication	1
Mutagenesisⁱ	126	H → P: Loss of all cofactors, no aerobic growth, complex assembles. 1 Publication	1
Mutagenesisⁱ	126	H → R: No effect. 1 Publication	1
Mutagenesisⁱ	186	H → L: Loss of cytochrome b558, no aerobic growth, complex assembles, this subunit is more susceptible to proteolysis. 1 Publication	1
Mutagenesisⁱ	314	H → L: Grows aerobically, has altered cytochrome b/d ratio, complex assembles. 1 Publication	1
Mutagenesisⁱ	314	H → P: Loss of cytochrome b595 and heme d, no aerobic growth, loss of complex. 1 Publication	1
Mutagenesisⁱ	393	M → L: Cytochrome b558 shifts to a high spin configuration, complex assembles. Retains about 1% quinol oxidoreductase activity after purification.	1
Mutagenesisⁱ	510	H → L: No effect. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000183919	1 – 522	Cytochrome bd-I ubiquinol oxidase subunit 1Add BLAST		522

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	1	N-formylmethionine1 Publication		1

Post-translational modificationⁱ

The N-terminus is blocked.

Keywords - PTMⁱ

Formylation

Proteomic databases

EPDⁱ	P0ABJ9
PaxDbⁱ	P0ABJ9
PRIDEⁱ	P0ABJ9

Expressionⁱ

Inductionⁱ

Under conditions of low aeration, in stationary phase (at protein level).1 Publication

Interactionⁱ

Subunit structureⁱ

Heterodimer of subunits I and II. Probably interacts with CydX, and overexpressed AppX.4 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
cydB	P0ABK2	5	EBI-906928,EBI-1213195

With

Entry

#Exp.

IntAct

Notes

cydB

P0ABK2

5

EBI-906928,EBI-1213195

Protein-protein interaction databases

BioGridⁱ	4263539, 372 interactors
ComplexPortalⁱ	CPX-268 Cytochrome bd-I ubiquinol oxidase complex
Database of interacting proteins More...DIPⁱ	DIP-36181N
IntActⁱ	P0ABJ9, 4 interactors
Molecular INTeraction database More...MINTⁱ	P0ABJ9
STRINGⁱ	316385.ECDH10B_0799

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P0ABJ9
SMRⁱ	P0ABJ9
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the cytochrome ubiquinol oxidase subunit 1 family.Curated

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	ENOG4105C4M Bacteria COG1271 LUCA
HOGENOMⁱ	HOG000084938
InParanoidⁱ	P0ABJ9
KEGG Orthology (KO) More...KOⁱ	K00425
PhylomeDBⁱ	P0ABJ9

Family and domain databases

InterProⁱ	View protein in InterPro IPR002585 Cyt-d_ubiquinol_oxidase_su_1
PANTHERⁱ	PTHR30365 PTHR30365, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01654 Cyt_bd_oxida_I, 1 hit
PIRSFⁱ	PIRSF006446 Cyt_quinol_oxidase_1, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P0ABJ9-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MLDIVELSRL QFALTAMYHF LFVPLTLGMA FLLAIMETVY VLSGKQIYKD 
        60         70         80         90        100
MTKFWGKLFG INFALGVATG LTMEFQFGTN WSYYSHYVGD IFGAPLAIEG 
       110        120        130        140        150
LMAFFLESTF VGLFFFGWDR LGKVQHMCVT WLVALGSNLS ALWILVANGW 
       160        170        180        190        200
MQNPIASDFN FETMRMEMVS FSELVLNPVA QVKFVHTVAS GYVTGAMFIL 
       210        220        230        240        250
GISAWYMLKG RDFAFAKRSF AIAASFGMAA VLSVIVLGDE SGYEMGDVQK 
       260        270        280        290        300
TKLAAIEAEW ETQPAPAAFT LFGIPDQEEE TNKFAIQIPY ALGIIATRSV 
       310        320        330        340        350
DTPVIGLKEL MVQHEERIRN GMKAYSLLEQ LRSGSTDQAV RDQFNSMKKD 
       360        370        380        390        400
LGYGLLLKRY TPNVADATEA QIQQATKDSI PRVAPLYFAF RIMVACGFLL 
       410        420        430        440        450
LAIIALSFWS VIRNRIGEKK WLLRAALYGI PLPWIAVEAG WFVAEYGRQP 
       460        470        480        490        500
WAIGEVLPTA VANSSLTAGD LIFSMVLICG LYTLFLVAEL FLMFKFARLG 
       510        520 
PSSLKTGRYH FEQSSTTTQP AR

Length:522

Mass (Da):58,205

Last modified:October 25, 2005 - v1

Checksum:ⁱE757442068BCFCFE

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	213	F → L in AAA18804 (PubMed:2843510).Curated		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J03939 Unassigned DNA Translation: AAA18804.1 U00096 Genomic DNA Translation: AAC73827.2 AP009048 Genomic DNA Translation: BAA35399.1
NCBI Reference Sequences More...RefSeqⁱ	NP_415261.2, NC_000913.3 WP_000884361.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC73827; AAC73827; b0733 BAA35399; BAA35399; BAA35399
GeneIDⁱ	945341
KEGGⁱ	ecj:JW0722 eco:b0733
PATRICⁱ	fig\|1411691.4.peg.1540

Protein	Similar proteins		Species	Score	Length	Source
P0ABJ9	Cytochrome bd-I ubiquinol oxidase subunit 1		ECOL6		522	UniRef100_P0ABK0
Cytochrome bd-I ubiquinol oxidase subunit 1		SHIFL		522
Cytochrome D ubiquinol oxidase subunit I		ECOLX		523
Cytochrome D ubiquinol oxidase subunit I		Escherichia coli 907672		523
Cytochrome D ubiquinol oxidase subunit I		Escherichia coli MS 145-7		523
+194

Protein	Similar proteins		Species	Score	Length	Source
P0ABJ9	Cytochrome bd-I ubiquinol oxidase subunit 1		ECOL6		522	UniRef90_P0ABK0
Cytochrome bd-I ubiquinol oxidase subunit 1		SHIFL		522
Cytochrome D ubiquinol oxidase subunit I		ECOLX		523
Cytochrome D ubiquinol oxidase subunit I		Escherichia coli 907672		523
Cytochrome D ubiquinol oxidase subunit I		Escherichia coli MS 145-7		523
+1016

Protein	Similar proteins		Species	Score	Length	Source
P0ABJ9	Cytochrome bd ubiquinol oxidase subunit 1		AZOVI		537	UniRef50_Q09049
Cytochrome bd-I ubiquinol oxidase subunit 1		ECOL6		522
Cytochrome bd-I ubiquinol oxidase subunit 1		SHIFL		522
Probable cytochrome oxidase subunit 1		HAEIN		521
Cytochrome bd ubiquinol oxidase, subunit I		Azotobacter chroococcum NCIMB 8003		537
+7541

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J03939 Unassigned DNA Translation: AAA18804.1 U00096 Genomic DNA Translation: AAC73827.2 AP009048 Genomic DNA Translation: BAA35399.1
RefSeqⁱ	NP_415261.2, NC_000913.3 WP_000884361.1, NZ_LN832404.1

3D structure databases

ProteinModelPortalⁱ	P0ABJ9
SMRⁱ	P0ABJ9
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4263539, 372 interactors
ComplexPortalⁱ	CPX-268 Cytochrome bd-I ubiquinol oxidase complex
DIPⁱ	DIP-36181N
IntActⁱ	P0ABJ9, 4 interactors
MINTⁱ	P0ABJ9
STRINGⁱ	316385.ECDH10B_0799

Protein family/group databases

TCDBⁱ	3.D.4.3.2 the proton-translocating cytochrome oxidase (cox) superfamily

TCDBⁱ

3.D.4.3.2 the proton-translocating cytochrome oxidase (cox) superfamily

Proteomic databases

EPDⁱ	P0ABJ9
PaxDbⁱ	P0ABJ9
PRIDEⁱ	P0ABJ9

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC73827; AAC73827; b0733 BAA35399; BAA35399; BAA35399
GeneIDⁱ	945341
KEGGⁱ	ecj:JW0722 eco:b0733
PATRICⁱ	fig\|1411691.4.peg.1540

Organism-specific databases

EchoBASEⁱ	EB0170
EcoGeneⁱ	EG10173 cydA

Phylogenomic databases

eggNOGⁱ	ENOG4105C4M Bacteria COG1271 LUCA
HOGENOMⁱ	HOG000084938
InParanoidⁱ	P0ABJ9
KOⁱ	K00425
PhylomeDBⁱ	P0ABJ9

Enzyme and pathway databases

UniPathwayⁱ	UPA00705
BioCycⁱ	EcoCyc:CYDA-MONOMER MetaCyc:CYDA-MONOMER
BRENDAⁱ	1.10.3.14 2026

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P0ABJ9

PROⁱ

PR:P0ABJ9

Family and domain databases

InterProⁱ	View protein in InterPro IPR002585 Cyt-d_ubiquinol_oxidase_su_1
PANTHERⁱ	PTHR30365 PTHR30365, 1 hit
Pfamⁱ	View protein in Pfam PF01654 Cyt_bd_oxida_I, 1 hit
PIRSFⁱ	PIRSF006446 Cyt_quinol_oxidase_1, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CYDA_ECOLI
Accessionⁱ	P0ABJ9Primary (citable) accession number: P0ABJ9 Secondary accession number(s): P11026, P75754, P76823
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
	Last sequence update:	October 25, 2005
	Last modified:	November 7, 2018
	This is version 112 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
PATHWAY comments
Index of metabolic and biosynthesis pathways
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P0ABJ9 (CYDA_ECOLI)

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Cytochrome bd-I ubiquinol oxidase subunit 1

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 ‘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 <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: oxidative phosphorylation

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

Topology

GO - Cellular componenti

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

<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

<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

<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

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

Kineticsⁱ

Pathwayⁱ: oxidative phosphorylation

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ