UniProtKB - P06709 (BIRA_ECOLI)

BLAST

>sp|P06709|BIRA_ECOLI Bifunctional ligase/repressor BirA OS=Escherichia coli (strain K12) OX=83333 GN=birA PE=1 SV=1
MKDNTVPLKLIALLANGEFHSGEQLGETLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSL
PEPIQLLNAKQILGQLDGGSVAVLPVIDSTNQYLLDRIGELKSGDACIAEYQQAGRGRRG
RKWFSPFGANLYLSMFWRLEQGPAAAIGLSLVIGIVMAEVLRKLGADKVRVKWPNDLYLQ
DRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEESVVNQGWITLQEAGINLDRNTLAA
MLIRELRAALELFEQEGLAPYLSRWEKLDNFINRPVKLIIGDKEIFGISRGIDKQGALLL
EQDGIIKPWMGGEISLRSAEK

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History
Entry version 174 (07 Nov 2018)
Sequence version 1 (01 Jan 1988)
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Protein

Bifunctional ligase/repressor BirA

Gene

birA

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon.UniRule annotation4 Publications

Catalytic activityⁱ

ATP + biotin + [biotin carboxyl-carrier protein]-L-lysine = AMP + diphosphate + [biotin carboxyl-carrier protein]-N₆-biotinyl-L-lysine.UniRule annotation2 Publications

Activity regulationⁱ

The switch between the enzymatic activity and the repressor activity is regulated by cellular demand for biotin. The switch occurs by swapping of protein interaction partners by holoBirA. In conditions of high biotin demand, holoBirA associates with apoBCCP to transfer biotin. In conditions of low biotin demand, holoBirA dimerizes, binds DNA and represses transcription of the biotin operon.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Binding siteⁱ	112	BiotinUniRule annotation2 Publications		1
Binding siteⁱ	183	BiotinUniRule annotation2 Publications		1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
DNA bindingⁱ	22 – 41	H-T-H motifUniRule annotationAdd BLAST		20

GO - Molecular functionⁱ

ATP binding
Source: CAFA
Inferred from mutant phenotypeⁱ
- 10497026
- 11124029
bacterial-type RNA polymerase regulatory region sequence-specific DNA binding
Source: CAFA
Inferred from mutant phenotypeⁱ
- 10497026
- 11124029
biotin-[acetyl-CoA-carboxylase] ligase activity
Source: EcoliWiki
Inferred from direct assayⁱ
- 7024555
biotin binding
Source: CAFA
Inferred from direct assayⁱ
- 1409631
DNA binding
Source: EcoliWiki
Inferred from direct assayⁱ
- 6456358
protein homodimerization activity
Source: CAFA
Inferred from mutant phenotypeⁱ
- 11124029

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

biotin biosynthetic process
Source: EcoliWiki
Inferred from mutant phenotypeⁱ
- 6456358
biotin metabolic process
Source: CAFA
Inferred from mutant phenotypeⁱ
- 10497026
- 11124029
protein biotinylation
Source: CACAO
Inferred from direct assayⁱ
- 22412018
regulation of transcription, DNA-templated Source: UniProtKB-UniRule

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding, Ligase, Repressor
Biological process	Transcription, Transcription regulation
Ligand	ATP-binding, Biotin, Nucleotide-binding

Enzyme and pathway databases

BioCycⁱ	EcoCyc:BIOTINLIG-MONOMER MetaCyc:BIOTINLIG-MONOMER
BRENDAⁱ	6.3.4.15 2026

Protein family/group databases

MoonProtⁱ	P06709

MoonProtⁱ

P06709

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Bifunctional ligase/repressor BirAUniRule annotation Alternative name(s): Biotin operon repressorUniRule annotation Biotin--[acetyl-CoA-carboxylase] ligaseUniRule annotation (EC:6.3.4.15UniRule annotation) Biotin--protein ligaseUniRule annotation Biotin-[acetyl-CoA carboxylase] synthetaseUniRule annotation
Gene namesⁱ	Name:birAUniRule annotation Synonyms:bioR, dhbB Ordered Locus Names:b3973, JW3941
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	EG10123 birA

EcoGeneⁱ

EG10123 birA

Subcellular locationⁱ

GO - Cellular componentⁱ

transcriptional repressor complex
Source: CAFA
Inferred from direct assayⁱ
- 10497026

View the complete GO annotation on QuickGO ...

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	52	T → I: Does not affect repressor activity. 1 Publication	1
Mutagenesisⁱ	52	T → S: 5-fold increase of repressor activity. Increases binding to DNA. 1 Publication	1
Mutagenesisⁱ	57	G → S: Lack of repressor activity. Does not bind DNA. 1 Publication	1
Mutagenesisⁱ	58	Y → F: Lack of repressor activity. 1 Publication	1
Mutagenesisⁱ	58	Y → T: Does not affect repressor activity. 1 Publication	1

Chemistry databases

ChEMBLⁱ	CHEMBL3559644
Drug and drug target database More...DrugBankⁱ	DB04651 BIOTINOL-5-AMP

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000064932	1 – 321	Bifunctional ligase/repressor BirAAdd BLAST		321

Proteomic databases

PaxDbⁱ	P06709
PRIDEⁱ	P06709

Interactionⁱ

Subunit structureⁱ

Monomer in solution. Interacts with BCCP. Homodimerizes to bind DNA. Interaction with the corepressor bio-5'-AMP increases dimerization.6 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
nanE	P0A761	2	EBI-545740,EBI-561432

With

Entry

#Exp.

IntAct

Notes

nanE

P0A761

EBI-545740,EBI-561432

GO - Molecular functionⁱ

protein homodimerization activity
Source: CAFA
Inferred from mutant phenotypeⁱ
- 11124029

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	4263391, 269 interactors
Database of interacting proteins More...DIPⁱ	DIP-9224N
IntActⁱ	P06709, 7 interactors
STRINGⁱ	316385.ECDH10B_4162

Chemistry databases

BindingDBⁱ

P06709

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	5 – 14	Combined sources	10
Helixⁱ	22 – 29	Combined sources	8
Helixⁱ	33 – 45	Combined sources	13
Beta strandⁱ	51 – 53	Combined sources	3
Turnⁱ	54 – 56	Combined sources	3
Beta strandⁱ	57 – 59	Combined sources	3
Helixⁱ	69 – 74	Combined sources	6
Beta strandⁱ	76 – 79	Combined sources	4
Beta strandⁱ	81 – 83	Combined sources	3
Beta strandⁱ	85 – 88	Combined sources	4
Helixⁱ	90 – 95	Combined sources	6
Helixⁱ	96 – 100	Combined sources	5
Beta strandⁱ	106 – 110	Combined sources	5
Beta strandⁱ	129 – 139	Combined sources	11
Helixⁱ	143 – 145	Combined sources	3
Helixⁱ	147 – 163	Combined sources	17
Beta strandⁱ	170 – 172	Combined sources	3
Turnⁱ	173 – 175	Combined sources	3
Beta strandⁱ	176 – 179	Combined sources	4
Beta strandⁱ	182 – 192	Combined sources	11
Beta strandⁱ	195 – 197	Combined sources	3
Beta strandⁱ	199 – 208	Combined sources	10
Turnⁱ	216 – 218	Combined sources	3
Turnⁱ	226 – 230	Combined sources	5
Helixⁱ	235 – 256	Combined sources	22
Helixⁱ	259 – 261	Combined sources	3
Helixⁱ	262 – 268	Combined sources	7
Turnⁱ	270 – 273	Combined sources	4
Beta strandⁱ	274 – 280	Combined sources	7
Beta strandⁱ	283 – 292	Combined sources	10
Turnⁱ	294 – 296	Combined sources	3
Beta strandⁱ	298 – 302	Combined sources	5
Beta strandⁱ	305 – 311	Combined sources	7
Beta strandⁱ	313 – 316	Combined sources	4

Show more details

3D structure databases

Database of protein disorder More...DisProtⁱ	DP00349
ProteinModelPortalⁱ	P06709
SMRⁱ	P06709
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P06709

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	67 – 254	BPL/LPL catalyticPROSITE-ProRule annotationAdd BLAST		188

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	89 – 91	Biotin binding		3
Regionⁱ	116 – 118	Biotin binding		3

Domainⁱ

Contains an N-terminal helix-turn-helix DNA-binding domain, connected via a linker to the central catalytic domain and the C-terminal domain, which plays roles in dimerization, catalytic function and DNA binding. The N-terminal domain is required for both ligase and repressor activities. It may orient the active site and thereby play an important role in enzymatic activity.4 Publications

Sequence similaritiesⁱ

Belongs to the biotin--protein ligase family.UniRule annotation

Phylogenomic databases

eggNOGⁱ	ENOG4105HJX Bacteria COG0340 LUCA COG1654 LUCA
HOGENOMⁱ	HOG000041812
InParanoidⁱ	P06709
KEGG Orthology (KO) More...KOⁱ	K03524
PhylomeDBⁱ	P06709

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd16442 BPL, 1 hit
Gene3Dⁱ	1.10.10.10, 1 hit
HAMAPⁱ	MF_00978 Bifunct_BirA, 1 hit
InterProⁱ	View protein in InterPro IPR030855 Bifunct_BirA IPR004408 Biotin_CoA_COase_ligase IPR004409 Biotin_operon_repress_HTH IPR003142 BPL_C IPR004143 BPL_LPL_catalytic IPR013196 HTH_11 IPR008988 Transcriptional_repressor_C IPR036388 WH-like_DNA-bd_sf IPR036390 WH_DNA-bd_sf
PANTHERⁱ	PTHR12835:SF5 PTHR12835:SF5, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02237 BPL_C, 1 hit PF03099 BPL_LplA_LipB, 1 hit PF08279 HTH_11, 1 hit
SUPFAMⁱ	SSF46785 SSF46785, 1 hit SSF50037 SSF50037, 1 hit
TIGRFAMsⁱ	TIGR00121 birA_ligase, 1 hit TIGR00122 birA_repr_reg, 1 hit
PROSITEⁱ	View protein in PROSITE PS51733 BPL_LPL_CATALYTIC, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P06709-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MKDNTVPLKL IALLANGEFH SGEQLGETLG MSRAAINKHI QTLRDWGVDV 
        60         70         80         90        100
FTVPGKGYSL PEPIQLLNAK QILGQLDGGS VAVLPVIDST NQYLLDRIGE 
       110        120        130        140        150
LKSGDACIAE YQQAGRGRRG RKWFSPFGAN LYLSMFWRLE QGPAAAIGLS 
       160        170        180        190        200
LVIGIVMAEV LRKLGADKVR VKWPNDLYLQ DRKLAGILVE LTGKTGDAAQ 
       210        220        230        240        250
IVIGAGINMA MRRVEESVVN QGWITLQEAG INLDRNTLAA MLIRELRAAL 
       260        270        280        290        300
ELFEQEGLAP YLSRWEKLDN FINRPVKLII GDKEIFGISR GIDKQGALLL 
       310        320 
EQDGIIKPWM GGEISLRSAE K

Length:321

Mass (Da):35,312

Last modified:January 1, 1988 - v1

Checksum:ⁱB80AEBCEEE1BD2D4

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱ	61	P → A in strain: RDD012.		1
Natural variantⁱ	70	K → E in strain: RDD012.		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M10123 Genomic DNA Translation: AAA23520.1 M15820 Genomic DNA Translation: AAA23521.1 L14557 Genomic DNA Translation: AAA24186.1 U00006 Genomic DNA Translation: AAC43075.1 U00096 Genomic DNA Translation: AAC76951.1 AP009048 Genomic DNA Translation: BAE77342.1
PIRⁱ	B24029 BVECBF
NCBI Reference Sequences More...RefSeqⁱ	NP_418404.1, NC_000913.3 WP_000654630.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC76951; AAC76951; b3973 BAE77342; BAE77342; BAE77342
GeneIDⁱ	948469
KEGGⁱ	ecj:JW3941 eco:b3973
PATRICⁱ	fig\|1411691.4.peg.2735

Protein	Similar proteins		Species	Score	Length	Source
P06709	Bifunctional biotin--[acetyl-CoA-carboxylase] synthetase/biotin operon repressor		Shigella sp.		321	UniRef100_P06709
Bifunctional ligase/repressor BirA		uncultured bacterium		321
Bifunctional ligase/repressor BirA		ECOLX		321
Bifunctional ligase/repressor BirA		SHIDY		321
Bifunctional ligase/repressor BirA		Shigella dysenteriae 1012		321
+27

Protein	Similar proteins		Species	Score	Length	Source
P06709	Bifunctional ligase/repressor BirA		SALTY		320	UniRef90_P06709
Bifunctional biotin--[acetyl-CoA-carboxylase] synthetase/biotin operon repressor		Shigella sp.		321
Bifunctional ligase/repressor BirA		uncultured bacterium		321
Bifunctional ligase/repressor BirA		ECOLX		321
Bifunctional ligase/repressor BirA		SHIDY		321
+725

Protein	Similar proteins		Species	Score	Length	Source
P06709	Bifunctional ligase/repressor BirA		SALTY		320	UniRef50_P06709
Bifunctional biotin--[acetyl-CoA-carboxylase] synthetase/biotin operon repressor		Shigella sp.		321
Bifunctional ligase/repressor BirA		uncultured bacterium		321
Bifunctional ligase/repressor BirA		ECOLX		321
Bifunctional ligase/repressor BirA		SHIDY		321
+1069

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M10123 Genomic DNA Translation: AAA23520.1 M15820 Genomic DNA Translation: AAA23521.1 L14557 Genomic DNA Translation: AAA24186.1 U00006 Genomic DNA Translation: AAC43075.1 U00096 Genomic DNA Translation: AAC76951.1 AP009048 Genomic DNA Translation: BAE77342.1
PIRⁱ	B24029 BVECBF
RefSeqⁱ	NP_418404.1, NC_000913.3 WP_000654630.1, NZ_LN832404.1

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
	1BIA	X-ray	2.30	A	1-321	[»]
	1BIB	X-ray	2.80	A	1-321	[»]
	1HXD	X-ray	2.40	A/B	1-321	[»]
	1K67	model	-	A	65-317	[»]
	2EWN	X-ray	2.80	A/B	1-321	[»]
	4WF2	X-ray	2.31	A	1-321	[»]
DisProtⁱ	DP00349
ProteinModelPortalⁱ	P06709
SMRⁱ	P06709
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4263391, 269 interactors
DIPⁱ	DIP-9224N
IntActⁱ	P06709, 7 interactors
STRINGⁱ	316385.ECDH10B_4162

Chemistry databases

BindingDBⁱ	P06709
ChEMBLⁱ	CHEMBL3559644
DrugBankⁱ	DB04651 BIOTINOL-5-AMP

Protein family/group databases

MoonProtⁱ	P06709

MoonProtⁱ

P06709

Proteomic databases

PaxDbⁱ	P06709
PRIDEⁱ	P06709

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC76951; AAC76951; b3973 BAE77342; BAE77342; BAE77342
GeneIDⁱ	948469
KEGGⁱ	ecj:JW3941 eco:b3973
PATRICⁱ	fig\|1411691.4.peg.2735

Organism-specific databases

EchoBASEⁱ	EB0121
EcoGeneⁱ	EG10123 birA

Phylogenomic databases

eggNOGⁱ	ENOG4105HJX Bacteria COG0340 LUCA COG1654 LUCA
HOGENOMⁱ	HOG000041812
InParanoidⁱ	P06709
KOⁱ	K03524
PhylomeDBⁱ	P06709

Enzyme and pathway databases

BioCycⁱ	EcoCyc:BIOTINLIG-MONOMER MetaCyc:BIOTINLIG-MONOMER
BRENDAⁱ	6.3.4.15 2026

Miscellaneous databases

EvolutionaryTraceⁱ	P06709
Protein Ontology More...PROⁱ	PR:P06709

Family and domain databases

CDDⁱ	cd16442 BPL, 1 hit
Gene3Dⁱ	1.10.10.10, 1 hit
HAMAPⁱ	MF_00978 Bifunct_BirA, 1 hit
InterProⁱ	View protein in InterPro IPR030855 Bifunct_BirA IPR004408 Biotin_CoA_COase_ligase IPR004409 Biotin_operon_repress_HTH IPR003142 BPL_C IPR004143 BPL_LPL_catalytic IPR013196 HTH_11 IPR008988 Transcriptional_repressor_C IPR036388 WH-like_DNA-bd_sf IPR036390 WH_DNA-bd_sf
PANTHERⁱ	PTHR12835:SF5 PTHR12835:SF5, 1 hit
Pfamⁱ	View protein in Pfam PF02237 BPL_C, 1 hit PF03099 BPL_LplA_LipB, 1 hit PF08279 HTH_11, 1 hit
SUPFAMⁱ	SSF46785 SSF46785, 1 hit SSF50037 SSF50037, 1 hit
TIGRFAMsⁱ	TIGR00121 birA_ligase, 1 hit TIGR00122 birA_repr_reg, 1 hit
PROSITEⁱ	View protein in PROSITE PS51733 BPL_LPL_CATALYTIC, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	BIRA_ECOLI
Accessionⁱ	P06709Primary (citable) accession number: P06709 Secondary accession number(s): Q2M8R4
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
	Last sequence update:	January 1, 1988
	Last modified:	November 7, 2018
	This is version 174 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

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

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UniProtKB - P06709 (BIRA_ECOLI)

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Bifunctional ligase/repressor BirA

birA

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

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

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

GO - 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

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

GO - Molecular functioni

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

Domains and Repeats

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

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

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

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ