COB

Functionⁱ

Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (Probable). Cytochrome b is a catalytic core subunit containing 2 b-type hemes BL and BH topographically segregated in the quinone reduction (Qi) and quinol oxidation (Q0) sites on opposite sides of the membrane (PubMed:18390544).

3 Publications1 Publication

Miscellaneous

Heme 1 (or BL or b562) is low-potential and absorbs at about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs at about 566 nm.By similarity

Catalytic activityⁱ

a quinol
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+ 2
Fe(III)-[cytochrome c]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
(out) =
a quinone
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+ 2
Fe(II)-[cytochrome c]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
(out) + 2
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
(out)
2 Publications
Manual assertion based on experiment inⁱ
- Ref.8
  "Electron-transfer restoration by vitamin K3 in a complex III-deficient mutant of S. cerevisiae and sequence of the corresponding cytochrome b mutation."
  Brivet-Chevillotte P., di Rago J.-P.
  FEBS Lett. 255:5-9(1989) [PubMed] [Europe PMC] [Abstract]
  Cited for: MUTANT W7, FUNCTION.
- Ref.9
  "Biochemical evidence for the orientation of cytochrome b in the yeast mitochondrial membrane in the eight-helix model."
  Beattie D.S., Jenkins H.C., Howton M.M.
  Arch. Biochem. Biophys. 312:292-300(1994) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, PROTEIN SEQUENCE OF 66-76.
EC:
7.1.1.8
- 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.
2 Publications
Manual assertion based on experiment inⁱ
- Ref.8
  "Electron-transfer restoration by vitamin K3 in a complex III-deficient mutant of S. cerevisiae and sequence of the corresponding cytochrome b mutation."
  Brivet-Chevillotte P., di Rago J.-P.
  FEBS Lett. 255:5-9(1989) [PubMed] [Europe PMC] [Abstract]
  Cited for: MUTANT W7, FUNCTION.
- Ref.9
  "Biochemical evidence for the orientation of cytochrome b in the yeast mitochondrial membrane in the eight-helix model."
  Beattie D.S., Jenkins H.C., Howton M.M.
  Arch. Biochem. Biophys. 312:292-300(1994) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, PROTEIN SEQUENCE OF 66-76.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
a quinol
zoom
+
2
Fe(III)-[cytochrome c](out)
Fe³⁺
zoom
=
a quinone
zoom
+
2
Fe(II)-[cytochrome c](out)
Fe²⁺
zoom
+
2
H⁺(out)

Cofactorⁱ

heme b4 PublicationsNote: Binds 2 heme b groups non-covalently per subunit.4 Publications

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	16	Ubiquinone1 Publication	1
Metal bindingⁱ	82	Iron 1 (heme b562 axial ligand); via tele nitrogenCombined sources4 Publications	1
Metal bindingⁱ	96	Iron 2 (heme b566 axial ligand); via tele nitrogenCombined sources4 Publications	1
Metal bindingⁱ	183	Iron 1 (heme b562 axial ligand); via tele nitrogenCombined sources4 Publications	1
Metal bindingⁱ	197	Iron 2 (heme b566 axial ligand); via tele nitrogenCombined sources4 Publications	1
Binding siteⁱ	202	UbiquinoneBy similarity	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Translocase
Biological process	Electron transport, Respiratory chain, Transport
Ligand	Heme, Iron, Metal-binding, Ubiquinone

Enzyme and pathway databases

Reactomeⁱ	R-SCE-611105, Respiratory electron transport

Reactomeⁱ

R-SCE-611105, Respiratory electron transport

Protein family/group databases

TCDBⁱ	3.D.3.3.1, the proton-translocating quinol:cytochrome c reductase (qcr) superfamily

TCDBⁱ

3.D.3.3.1, the proton-translocating quinol:cytochrome c reductase (qcr) superfamily

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Cytochrome b (EC:7.1.1.82 Publications) Alternative name(s): Complex III subunit 3 Complex III subunit CYTB Complex III subunit III Cytochrome b-c1 complex subunit 3 Cytochrome b-c1 complex subunit CYTB Ubiquinol-cytochrome c oxidoreductase complex cytochrome b subunit
Gene namesⁱ	Name:COB Synonyms:CYTB Ordered Locus Names:Q0105
Encoded onⁱ	Mitochondrion
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: Mitochondrion

Organism-specific databases

Saccharomyces Genome Database More...SGDⁱ	S000007270, COB
VEuPathDBⁱ	FungiDB:Q0105

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 27	Mitochondrial matrix1 Publication2 PublicationsAdd BLAST	27
Transmembraneⁱ	28 – 51	HelicalCombined sources4 PublicationsAdd BLAST	24
Topological domainⁱ	52 – 74	Mitochondrial intermembrane1 Publication2 PublicationsAdd BLAST	23
Transmembraneⁱ	75 – 102	HelicalCombined sources4 PublicationsAdd BLAST	28
Topological domainⁱ	103 – 110	Mitochondrial matrix1 Publication2 Publications	8
Transmembraneⁱ	111 – 135	HelicalCombined sources4 PublicationsAdd BLAST	25
Topological domainⁱ	136 – 172	Mitochondrial intermembrane1 Publication2 PublicationsAdd BLAST	37
Transmembraneⁱ	173 – 204	HelicalCombined sources4 PublicationsAdd BLAST	32
Topological domainⁱ	205 – 223	Mitochondrial matrix1 Publication2 PublicationsAdd BLAST	19
Transmembraneⁱ	224 – 246	HelicalCombined sources4 PublicationsAdd BLAST	23
Topological domainⁱ	247 – 287	Mitochondrial intermembrane1 Publication2 PublicationsAdd BLAST	41
Transmembraneⁱ	288 – 308	HelicalCombined sources4 PublicationsAdd BLAST	21
Topological domainⁱ	309 – 319	Mitochondrial matrix1 Publication2 PublicationsAdd BLAST	11
Transmembraneⁱ	320 – 340	HelicalCombined sources4 PublicationsAdd BLAST	21
Topological domainⁱ	341 – 347	Mitochondrial intermembrane1 Publication2 Publications	7
Transmembraneⁱ	348 – 364	HelicalCombined sources4 PublicationsAdd BLAST	17
Topological domainⁱ	365 – 385	Mitochondrial matrix1 Publication2 PublicationsAdd BLAST	21

Keywords - Cellular componentⁱ

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechⁱ

Chemistry databases

ChEMBLⁱ	CHEMBL4296317

ChEMBLⁱ

CHEMBL4296317

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000061769	1 – 385	Cytochrome bAdd BLAST		385

Proteomic databases

PaxDbⁱ	P00163
TopDownProteomicsⁱ	P00163

Interactionⁱ

Subunit structureⁱ

Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme composed of 10 subunits. The complex is composed of 3 respiratory subunits cytochrome b (COB), cytochrome c1 (CYT1) and Rieske protein (RIP1), 2 core protein subunits COR1 and QCR2, and 5 low-molecular weight protein subunits QCR6, QCR7, QCR8, QCR9 and QCR10 (PubMed:10873857, PubMed:11880631, PubMed:8031140, PubMed:30598554). The complex exists as an obligatory dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with a monomer or a dimer of cytochrome c oxidase (complex IV, CIV), resulting in 2 different assemblies (supercomplexes III₂IV and III₂IV₂) (PubMed:10775262, PubMed:10764779, PubMed:30598556, PubMed:30598554).

7 Publications

Protein-protein interaction databases

BioGRIDⁱ	34779, 37 interactors
ComplexPortalⁱ	CPX-567, Mitochondrial respiratory chain complex III
IntActⁱ	P00163, 4 interactors
STRINGⁱ	4932.Q0105

Miscellaneous databases

RNActⁱ	P00163, protein

RNActⁱ

P00163, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	3 – 6	Combined sources	4
Helixⁱ	10 – 17	Combined sources	8
Beta strandⁱ	21 – 23	Combined sources	3
Helixⁱ	28 – 31	Combined sources	4
Helixⁱ	32 – 51	Combined sources	20
Turnⁱ	58 – 60	Combined sources	3
Helixⁱ	61 – 70	Combined sources	10
Helixⁱ	75 – 102	Combined sources	28
Turnⁱ	103 – 106	Combined sources	4
Turnⁱ	108 – 110	Combined sources	3
Helixⁱ	111 – 135	Combined sources	25
Helixⁱ	138 – 149	Combined sources	12
Helixⁱ	150 – 153	Combined sources	4
Turnⁱ	155 – 157	Combined sources	3
Helixⁱ	158 – 166	Combined sources	9
Beta strandⁱ	168 – 171	Combined sources	4
Helixⁱ	173 – 204	Combined sources	32
Beta strandⁱ	217 – 220	Combined sources	4
Turnⁱ	221 – 223	Combined sources	3
Helixⁱ	224 – 246	Combined sources	23
Turnⁱ	248 – 251	Combined sources	4
Helixⁱ	254 – 257	Combined sources	4
Beta strandⁱ	262 – 264	Combined sources	3
Helixⁱ	273 – 275	Combined sources	3
Helixⁱ	276 – 283	Combined sources	8
Beta strandⁱ	285 – 287	Combined sources	3
Helixⁱ	288 – 300	Combined sources	13
Helixⁱ	301 – 304	Combined sources	4
Helixⁱ	305 – 308	Combined sources	4
Beta strandⁱ	312 – 316	Combined sources	5
Helixⁱ	320 – 340	Combined sources	21
Helixⁱ	348 – 364	Combined sources	17
Helixⁱ	366 – 380	Combined sources	15

Show more details

3D structure databases

AlphaFoldDBⁱ	P00163
SMRⁱ	P00163
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P00163

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the cytochrome b family.PROSITE-ProRule annotation

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG4663, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000017948
HOGENOMⁱ	CLU_031114_3_0_1
InParanoidⁱ	P00163
OMAⁱ	RFFAFHF

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00290, cytochrome_b_C, 1 hit cd00284, Cytochrome_b_N, 1 hit
Gene3Dⁱ	1.20.810.10, 1 hit
InterProⁱ	View protein in InterPro IPR005798, Cyt_b/b6_C IPR036150, Cyt_b/b6_C_sf IPR005797, Cyt_b/b6_N IPR027387, Cytb/b6-like_sf IPR030689, Cytochrome_b IPR016174, Di-haem_cyt_TM
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00032, Cytochrom_B_C, 1 hit PF00033, Cytochrome_B, 1 hit
PIRSFⁱ	PIRSF038885, COB, 1 hit
SUPFAMⁱ	SSF81342, SSF81342, 1 hit SSF81648, SSF81648, 1 hit
PROSITEⁱ	View protein in PROSITE PS51003, CYTB_CTER, 1 hit PS51002, CYTB_NTER, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P00163-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MAFRKSNVYL SLVNSYIIDS PQPSSINYWW NMGSLLGLCL VIQIVTGIFM 
        60         70         80         90        100
AMHYSSNIEL AFSSVEHIMR DVHNGYILRY LHANGASFFF MVMFMHMAKG 
       110        120        130        140        150
LYYGSYRSPR VTLWNVGVII FILTIATAFL GYCCVYGQMS HWGATVITNL 
       160        170        180        190        200
FSAIPFVGND IVSWLWGGFS VSNPTIQRFF ALHYLVPFII AAMVIMHLMA 
       210        220        230        240        250
LHIHGSSNPL GITGNLDRIP MHSYFIFKDL VTVFLFMLIL ALFVFYSPNT 
       260        270        280        290        300
LGHPDNYIPG NPLVTPASIV PEWYLLPFYA ILRSIPDKLL GVITMFAAIL 
       310        320        330        340        350
VLLVLPFTDR SVVRGNTFKV LSKFFFFIFV FNFVLLGQIG ACHVEVPYVL 
       360        370        380 
MGQIATFIYF AYFLIIVPVI STIENVLFYI GRVNK

Length:385

Mass (Da):43,656

Last modified:April 23, 2003 - v3

Checksum:ⁱ1B1B1616BBC2A798

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	122	I → T in CAA58861 (PubMed:7737175).Curated	1
Sequence conflictⁱ	122	I → T in AAA32151 (PubMed:7004642).Curated	1
Sequence conflictⁱ	269	I → ID in CAA24073 (PubMed:6253454).Curated	1
Sequence conflictⁱ	269	I → ID no nucleotide entry (PubMed:6383504).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱ	131	G → S in mutant W7 which is respiratory deficient.		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	V00696 Genomic DNA Translation: CAA24073.2 Sequence problems. X84042 mRNA Translation: CAA58861.1 KP263414 Genomic DNA Translation: AIZ98890.1 J01473, J01472 Genomic DNA Translation: AAA32151.2 J01475, J01474 Genomic DNA Translation: AAA32152.2
PIRⁱ	A00159, CBBY S78660
NCBI Reference Sequences More...RefSeqⁱ	NP_009315.1, NC_001224.1

Genome annotation databases

EnsemblFungiⁱ	Q0105_mRNA; Q0105; Q0105
GeneIDⁱ	854583
KEGGⁱ	sce:Q0105

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P00163	Cytochrome b		YEASX		385	UniRef100_P00163

Protein	Similar proteins		Species	Score	Length	Source
P00163	Cytochrome b		SACPA		385	UniRef90_P00163
Cytochrome b		YEASX		385
Cytochrome b		Saccharomyces cerevisiae x Saccharomyces paradoxus		385
Cytochrome b		SACEU		385
Cytochrome b		SACPW		385
+21

Protein	Similar proteins		Species	Score	Length	Source
P00163	Cytochrome b		SACPA		385	UniRef50_P00163
Cytochrome b		PHYAC		381
Cytochrome b		AKOAF		379
Cytochrome b		AKODO		379
Cytochrome b		AKOMY		379
+1589

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	V00696 Genomic DNA Translation: CAA24073.2 Sequence problems. X84042 mRNA Translation: CAA58861.1 KP263414 Genomic DNA Translation: AIZ98890.1 J01473, J01472 Genomic DNA Translation: AAA32151.2 J01475, J01474 Genomic DNA Translation: AAA32152.2
PIRⁱ	A00159, CBBY S78660
RefSeqⁱ	NP_009315.1, NC_001224.1

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
	1EZV	X-ray	2.30	C	1-385	[»]
	1KB9	X-ray	2.30	C	1-385	[»]
	1KYO	X-ray	2.97	C/N	1-385	[»]
	1P84	X-ray	2.50	C	1-385	[»]
	2IBZ	X-ray	2.30	C	1-385	[»]
	3CX5	X-ray	1.90	C/N	1-385	[»]
	3CXH	X-ray	2.50	C/N	1-385	[»]
	4PD4	X-ray	3.04	C	1-385	[»]
	6GIQ	electron microscopy	3.23	C/N	1-385	[»]
	6HU9	electron microscopy	3.35	C/N	1-385	[»]
	6T0B	electron microscopy	2.80	C/N	1-385	[»]
	6T15	electron microscopy	3.29	C/N	1-385	[»]
	6YMX	electron microscopy	3.17	C/N	1-385	[»]
AlphaFoldDBⁱ	P00163
SMRⁱ	P00163
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	34779, 37 interactors
ComplexPortalⁱ	CPX-567, Mitochondrial respiratory chain complex III
IntActⁱ	P00163, 4 interactors
STRINGⁱ	4932.Q0105

Chemistry databases

ChEMBLⁱ	CHEMBL4296317

ChEMBLⁱ

CHEMBL4296317

Protein family/group databases

TCDBⁱ	3.D.3.3.1, the proton-translocating quinol:cytochrome c reductase (qcr) superfamily

TCDBⁱ

3.D.3.3.1, the proton-translocating quinol:cytochrome c reductase (qcr) superfamily

Proteomic databases

PaxDbⁱ	P00163
TopDownProteomicsⁱ	P00163

Genome annotation databases

EnsemblFungiⁱ	Q0105_mRNA; Q0105; Q0105
GeneIDⁱ	854583
KEGGⁱ	sce:Q0105

Organism-specific databases

SGDⁱ	S000007270, COB
VEuPathDBⁱ	FungiDB:Q0105

Phylogenomic databases

eggNOGⁱ	KOG4663, Eukaryota
GeneTreeⁱ	ENSGT00390000017948
HOGENOMⁱ	CLU_031114_3_0_1
InParanoidⁱ	P00163
OMAⁱ	RFFAFHF

Enzyme and pathway databases

Reactomeⁱ	R-SCE-611105, Respiratory electron transport

Reactomeⁱ

R-SCE-611105, Respiratory electron transport

Miscellaneous databases

EvolutionaryTraceⁱ	P00163
Protein Ontology More...PROⁱ	PR:P00163
RNActⁱ	P00163, protein

Family and domain databases

CDDⁱ	cd00290, cytochrome_b_C, 1 hit cd00284, Cytochrome_b_N, 1 hit
Gene3Dⁱ	1.20.810.10, 1 hit
InterProⁱ	View protein in InterPro IPR005798, Cyt_b/b6_C IPR036150, Cyt_b/b6_C_sf IPR005797, Cyt_b/b6_N IPR027387, Cytb/b6-like_sf IPR030689, Cytochrome_b IPR016174, Di-haem_cyt_TM
Pfamⁱ	View protein in Pfam PF00032, Cytochrom_B_C, 1 hit PF00033, Cytochrome_B, 1 hit
PIRSFⁱ	PIRSF038885, COB, 1 hit
SUPFAMⁱ	SSF81342, SSF81342, 1 hit SSF81648, SSF81648, 1 hit
PROSITEⁱ	View protein in PROSITE PS51003, CYTB_CTER, 1 hit PS51002, CYTB_NTER, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CYB_YEAST
Accessionⁱ	P00163Primary (citable) accession number: P00163 Secondary accession number(s): A0A0A7NYK0 , Q35802, Q35807, Q36301, Q9ZZW9
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
	Last sequence update:	April 23, 2003
	Last modified:	May 25, 2022
	This is version 187 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Fungal Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Direct protein sequencing, Reference proteome

Documents

Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
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 - P00163 (CYB_YEAST)

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Cytochrome b

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%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

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

Mitochondrion

Mitochondrion

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

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

<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

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

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

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

Protein family/group databases

Proteomic 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

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ