bfr

Functionⁱ

Iron-storage protein, whose ferroxidase center binds Fe²⁺ ions, oxidizes them by dioxygen to Fe³⁺, and participates in the subsequent Fe³⁺ oxide mineral core formation within the central cavity of the protein complex. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.2 Publications

Miscellaneous

The internal surface iron site that binds iron 3 is important for the mineralization phase but not for Fe²⁺ binding and oxidation at the ferroxidase center.

Catalytic activityⁱ

4
Fe²⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+ 4
H⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
O₂
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
= 4
Fe³⁺
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+ 2
H₂O
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.9
  "The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin."
  Yang X., Le Brun N.E., Thomson A.J., Moore G.R., Chasteen N.D.
  Biochemistry 39:4915-4923(2000) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
- Ref.10
  "Core formation in Escherichia coli bacterioferritin requires a functional ferroxidase center."
  Baaghil S., Lewin A., Moore G.R., Le Brun N.E.
  Biochemistry 42:14047-14056(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, ROLE OF THE FERROXIDASE CENTER IN CORE FORMATION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, MUTAGENESIS OF GLU-18; GLU-127 AND HIS-130.
- Ref.14
  "Monitoring the iron status of the ferroxidase center of Escherichia coli bacterioferritin using fluorescence spectroscopy."
  Lawson T.L., Crow A., Lewin A., Yasmin S., Moore G.R., Le Brun N.E.
  Biochemistry 48:9031-9039(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF MUTANTS PHE-35 AND PHE-133 IN COMPLEX WITH HEME AND IRON IONS, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
EC:
1.16.3.1
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.9
  "The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin."
  Yang X., Le Brun N.E., Thomson A.J., Moore G.R., Chasteen N.D.
  Biochemistry 39:4915-4923(2000) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
- Ref.10
  "Core formation in Escherichia coli bacterioferritin requires a functional ferroxidase center."
  Baaghil S., Lewin A., Moore G.R., Le Brun N.E.
  Biochemistry 42:14047-14056(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, ROLE OF THE FERROXIDASE CENTER IN CORE FORMATION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, MUTAGENESIS OF GLU-18; GLU-127 AND HIS-130.
- Ref.14
  "Monitoring the iron status of the ferroxidase center of Escherichia coli bacterioferritin using fluorescence spectroscopy."
  Lawson T.L., Crow A., Lewin A., Yasmin S., Moore G.R., Le Brun N.E.
  Biochemistry 48:9031-9039(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF MUTANTS PHE-35 AND PHE-133 IN COMPLEX WITH HEME AND IRON IONS, CATALYTIC ACTIVITY, ACTIVITY REGULATION.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
4
Fe²⁺
zoom
+
4
H⁺
+
O₂
=
4
Fe³⁺
zoom
+
2
H₂O

Cofactorⁱ

Protein has several cofactor binding sites:

Activity regulationⁱ

Iron oxidation is inhibited by Zn²⁺, which binds at the ferroxidase center with a higher affinity that Fe²⁺. The occupation of the ferroxidase center by Zn²⁺ also severely restricts the ability of BFR to form an iron core.3 Publications

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	18	Iron 1PROSITE-ProRule annotation1 Publication	1
Metal bindingⁱ	46	Iron 3PROSITE-ProRule annotation1 Publication	1
Metal bindingⁱ	50	Iron 3PROSITE-ProRule annotation1 Publication	1
Metal bindingⁱ	51	Iron 1PROSITE-ProRule annotation1 Publication	1
Metal bindingⁱ	51	Iron 2PROSITE-ProRule annotation1 Publication	1
Metal bindingⁱ	52	Iron (heme axial ligand); shared with dimeric partnerPROSITE-ProRule annotation1 Publication	1
Metal bindingⁱ	54	Iron 1PROSITE-ProRule annotation1 Publication	1
Metal bindingⁱ	94	Iron 2PROSITE-ProRule annotation1 Publication	1
Metal bindingⁱ	127	Iron 1PROSITE-ProRule annotation1 Publication	1
Metal bindingⁱ	127	Iron 2PROSITE-ProRule annotation1 Publication	1
Metal bindingⁱ	130	Iron 2PROSITE-ProRule annotation1 Publication	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Biological process	Iron storage
Ligand	Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10113-MONOMER MetaCyc:EG10113-MONOMER
BRENDAⁱ	1.16.3.1, 2026

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Bacterioferritin (EC:1.16.3.1) Short name: BFR Alternative name(s): Cytochrome b-1 Cytochrome b-557
Gene namesⁱ	Name:bfr Ordered Locus Names:b3336, JW3298
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

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	18	E → A: Highly decreased Fe(2+) oxidation activity. Is also severely restricted in its ability to lay down an iron core. 1 Publication	1
Mutagenesisⁱ	31	M → H or L: No loss of heme binding. 1 Publication	1
Mutagenesisⁱ	46	H → A: Fe(2+)-binding and single turnover oxidation at the ferroxidase center occur normally but iron mineralization within the cavity is significantly impaired. 1 Publication	1
Mutagenesisⁱ	50	D → A: Fe(2+)-binding and single turnover oxidation at the ferroxidase center occur normally but iron mineralization within the cavity is significantly impaired. 1 Publication	1
Mutagenesisⁱ	52	M → H or L: Loss of heme binding. Is still capable of accumulating iron. 1 Publication	1
Mutagenesisⁱ	86	M → L: No loss of heme binding. 1 Publication	1
Mutagenesisⁱ	127	E → Q: Decreased Fe(2+) oxidation activity. Is also affected in its ability to lay down an iron core. 1 Publication	1
Mutagenesisⁱ	130	H → E: Decreased Fe(2+) oxidation activity. Is also severely restricted in its ability to lay down an iron core. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000192592	1 – 158	BacterioferritinAdd BLAST		158

Proteomic databases

jPOSTⁱ	P0ABD3
PaxDbⁱ	P0ABD3
PRIDEⁱ	P0ABD3

Interactionⁱ

Subunit structureⁱ

Homooligomer of 24 subunits, arranged as 12 dimers, that are packed together to form an approximately spherical molecule with a central cavity, in which large amounts of iron can be deposited as a ferric-oxy-hydroxide mineral core.

7 Publications

Binary interactionsⁱ

P0ABD3

With	#Exp.	IntAct
itself	2	EBI-907496,EBI-907496

GO - Molecular functionⁱ

identical protein binding
Source: EcoCyc
Inferred from direct assayⁱ
- "The composition and the structure of bacterioferritin of Escherichia coli."
  Yariv J., Kalb A.J., Sperling R., Bauminger E.R., Cohen S.G., Ofer S.
  Biochem J 197:171-175(1981) [PubMed] [Europe PMC] [Abstract]

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	4262466, 23 interactors
Database of interacting proteins More...DIPⁱ	DIP-36167N
IntActⁱ	P0ABD3, 3 interactors
STRINGⁱ	511145.b3336

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	5 – 34	Combined sources	30
Helixⁱ	38 – 64	Combined sources	27
Helixⁱ	83 – 110	Combined sources	28
Helixⁱ	114 – 144	Combined sources	31
Helixⁱ	146 – 152	Combined sources	7

Show more details

3D structure databases

SMRⁱ	P0ABD3
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P0ABD3

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	1 – 145	Ferritin-like diironPROSITE-ProRule annotationAdd BLAST		145

Sequence similaritiesⁱ

Belongs to the bacterioferritin family.Curated

Phylogenomic databases

eggNOGⁱ	COG2193, Bacteria
HOGENOMⁱ	CLU_104506_2_0_6
InParanoidⁱ	P0ABD3
PhylomeDBⁱ	P0ABD3

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00907, Bacterioferritin, 1 hit
Gene3Dⁱ	1.20.1260.10, 1 hit
InterProⁱ	View protein in InterPro IPR002024, Bacterioferritin IPR012347, Ferritin-like IPR009040, Ferritin-like_diiron IPR009078, Ferritin-like_SF IPR008331, Ferritin_DPS_dom
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00210, Ferritin, 1 hit
PIRSFⁱ	PIRSF002560, Bacterioferritin, 1 hit
PRINTSⁱ	PR00601, BACFERRITIN
SUPFAMⁱ	SSF47240, SSF47240, 1 hit
TIGRFAMsⁱ	TIGR00754, bfr, 1 hit
PROSITEⁱ	View protein in PROSITE PS00549, BACTERIOFERRITIN, 1 hit PS50905, FERRITIN_LIKE, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P0ABD3-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MKGDTKVINY LNKLLGNELV AINQYFLHAR MFKNWGLKRL NDVEYHESID 
        60         70         80         90        100
EMKHADRYIE RILFLEGLPN LQDLGKLNIG EDVEEMLRSD LALELDGAKN 
       110        120        130        140        150
LREAIGYADS VHDYVSRDMM IEILRDEEGH IDWLETELDL IQKMGLQNYL 

QAQIREEG

Length:158

Mass (Da):18,495

Last modified:October 25, 2005 - v1

Checksum:ⁱA6C86CE1CD8F865A

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	53	K → M AA sequence (PubMed:2644932).Curated		1

Mass spectrometryⁱ

Molecular mass is 18496±2 Da. Determined by ESI. 1 Publication

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱ	5 – 7	TKV → VKI in strain: ECOR 30.	3
Natural variantⁱ	38	K → M in strain: ECOR 30.	1
Natural variantⁱ	57	R → K in strain: ECOR 30.	1
Natural variantⁱ	68	L → I in strain: ECOR 30.	1
Natural variantⁱ	78	N → G in strain: ECOR 30.	1
Natural variantⁱ	88	R → Q in strain: ECOR 30.	1
Natural variantⁱ	92	A → R in strain: ECOR 30.	1
Natural variantⁱ	96	D → E in strain: ECOR 30.	1
Natural variantⁱ	100	N → D in strain: ECOR 30.	1
Natural variantⁱ	106	G → A in strain: ECOR 30.	1
Natural variantⁱ	125	R → A in strain: ECOR 30.	1
Natural variantⁱ	142 – 144	QKM → GKI in strain: ECOR 30.	3
Natural variantⁱ	152 – 158	AQIREEG → SQIKVKD in strain: ECOR 30.	7

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M27176 mRNA Translation: AAC13987.1 AF058450 Genomic DNA Translation: AAC14288.1 U18997 Genomic DNA Translation: AAA58133.1 U00096 Genomic DNA Translation: AAC76361.1 AP009048 Genomic DNA Translation: BAE77955.1 L28106 Genomic DNA Translation: AAC36929.1
PIRⁱ	JV0032, FREC
NCBI Reference Sequences More...RefSeqⁱ	NP_417795.1, NC_000913.3 WP_000675504.1, NZ_STEB01000038.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC76361; AAC76361; b3336 BAE77955; BAE77955; BAE77955
GeneIDⁱ	58459569 947839
KEGGⁱ	ecj:JW3298 eco:b3336
PATRICⁱ	fig\|1411691.4.peg.3395

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P0ABD3	Bacterioferritin		ECOL6		158	UniRef100_P0ABD4
Bacterioferritin		Escherichia coli HVH 101 (4-6859844)		158
Bacterioferritin		Escherichia coli O25b:H4		158
Bacterioferritin		SHIBO		158
Bacterioferritin		Escherichia coli O25b:H4-ST131		158
+84

Protein	Similar proteins		Species	Score	Length	Source
P0ABD3	Bacterioferritin		ECOL6		158	UniRef90_P0ABD4
Bacterioferritin		Escherichia coli HVH 101 (4-6859844)		158
Bacterioferritin		Escherichia coli O25b:H4		158
Bacterioferritin		SHIBO		158
Bacterioferritin		Escherichia coli O25b:H4-ST131		158
+170

Protein	Similar proteins		Species	Score	Length	Source
P0ABD3	Bacterioferritin		SALTY		158	UniRef50_O68926
Bacterioferritin		ECOL6		158
Bacterioferritin (Fragment)		NITWI		50
Putative bacterioferritin subunit 2		MAGMG		160
Bacterioferritin		SALBL		158
+2975

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M27176 mRNA Translation: AAC13987.1 AF058450 Genomic DNA Translation: AAC14288.1 U18997 Genomic DNA Translation: AAA58133.1 U00096 Genomic DNA Translation: AAC76361.1 AP009048 Genomic DNA Translation: BAE77955.1 L28106 Genomic DNA Translation: AAC36929.1
PIRⁱ	JV0032, FREC
RefSeqⁱ	NP_417795.1, NC_000913.3 WP_000675504.1, NZ_STEB01000038.1

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
	1BCF	X-ray	2.90	A/B/C/D/E/F/G/H/I/J/K/L	1-158	[»]
	1BFR	X-ray	2.94	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X	1-158	[»]
	2HTN	X-ray	2.50	A/B/C/D/E/F/G/H	1-158	[»]
	2VXI	X-ray	1.91	A/B/C/D/E/F/G/H/I/J/K/L	1-158	[»]
	2Y3Q	X-ray	1.55	A/B/C/D/E/F/G/H/I/J/K/L	1-158	[»]
	3E1J	X-ray	2.70	A/B/C/D/E/F/G/H/I/J/K/L	1-158	[»]
	3E1L	X-ray	2.50	A/B/C/D/E/F/G/H/I/J/K/L	1-158	[»]
	3E1M	X-ray	2.70	A/B/C/D/E/F/G/H/I/J/K/L	1-158	[»]
	3E1N	X-ray	2.80	A/B/C/D/E/F/G/H/I/J/K/L	1-158	[»]
	3E1O	X-ray	2.95	A/B/C/D/E/F/G/H/I/J/K/L	1-158	[»]
	3E1P	X-ray	2.40	A/B/C/D/E/F/G/H/I/J/K/L	1-158	[»]
	3E1Q	X-ray	2.60	A/B/C/D/E/F/G/H/I/J/K/L	1-158	[»]
	3E2C	X-ray	1.80	A/B	1-158	[»]
	3GHQ	X-ray	2.70	A/B/C/D/E/F/G/H/I/J/K/L	1-158	[»]
	4CVP	X-ray	2.11	A	1-158	[»]
	4CVR	X-ray	1.10	A	1-158	[»]
	4CVS	X-ray	1.39	A	1-158	[»]
	4CVT	X-ray	1.79	A	1-158	[»]
	4U3G	X-ray	2.00	A/B/C/D/E/F/G/H/I/J/K/L	1-158	[»]
	4XKS	X-ray	1.57	A/B/C/D/E/F/G/H/I/J/K/L	1-158	[»]
	4XKT	X-ray	1.82	A/B/C/D/E/F/G/H/I/J/K/L	1-158	[»]
	4XKU	X-ray	1.78	A/B/C/D/E/F/G/H/I/J/K/L	1-158	[»]
	5XGO	X-ray	1.99	A/B/C/D/E/F/G/H/I/J/K/L	138-158	[»]
	6P8K	X-ray	1.70	A/B/C/D/E/F/G/H/I/J/K/L	1-158	[»]
	6P8L	X-ray	2.10	A/B/C/D/E/F/G/H/I/J/K/L	1-158	[»]
SMRⁱ	P0ABD3
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	4262466, 23 interactors
DIPⁱ	DIP-36167N
IntActⁱ	P0ABD3, 3 interactors
STRINGⁱ	511145.b3336

Proteomic databases

jPOSTⁱ	P0ABD3
PaxDbⁱ	P0ABD3
PRIDEⁱ	P0ABD3

Genome annotation databases

EnsemblBacteriaⁱ	AAC76361; AAC76361; b3336 BAE77955; BAE77955; BAE77955
GeneIDⁱ	58459569 947839
KEGGⁱ	ecj:JW3298 eco:b3336
PATRICⁱ	fig\|1411691.4.peg.3395

Organism-specific databases

EchoBASEⁱ	EB0111

EchoBASEⁱ

EB0111

Phylogenomic databases

eggNOGⁱ	COG2193, Bacteria
HOGENOMⁱ	CLU_104506_2_0_6
InParanoidⁱ	P0ABD3
PhylomeDBⁱ	P0ABD3

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10113-MONOMER MetaCyc:EG10113-MONOMER
BRENDAⁱ	1.16.3.1, 2026

Miscellaneous databases

EvolutionaryTraceⁱ	P0ABD3
Protein Ontology More...PROⁱ	PR:P0ABD3

Family and domain databases

CDDⁱ	cd00907, Bacterioferritin, 1 hit
Gene3Dⁱ	1.20.1260.10, 1 hit
InterProⁱ	View protein in InterPro IPR002024, Bacterioferritin IPR012347, Ferritin-like IPR009040, Ferritin-like_diiron IPR009078, Ferritin-like_SF IPR008331, Ferritin_DPS_dom
Pfamⁱ	View protein in Pfam PF00210, Ferritin, 1 hit
PIRSFⁱ	PIRSF002560, Bacterioferritin, 1 hit
PRINTSⁱ	PR00601, BACFERRITIN
SUPFAMⁱ	SSF47240, SSF47240, 1 hit
TIGRFAMsⁱ	TIGR00754, bfr, 1 hit
PROSITEⁱ	View protein in PROSITE PS00549, BACTERIOFERRITIN, 1 hit PS50905, FERRITIN_LIKE, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	BFR_ECOLI
Accessionⁱ	P0ABD3Primary (citable) accession number: P0ABD3 Secondary accession number(s): O68931, P11056, Q2M701
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
	Last sequence update:	October 25, 2005
	Last modified:	April 7, 2021
	This is version 122 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

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UniProtKB - P0ABD3 (BFR_ECOLI)

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Bacterioferritin

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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

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

<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

Cytosol

Other locations

<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

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

P0ABD3

GO - Molecular functioni

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

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

Domains and Repeats

<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

<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

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

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

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Mass spectrometryⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ