ileS

Functionⁱ

Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).

Miscellaneous

Strain PS102 is resistant to the antibiotic mupirocin (pseudomonic acid A), an Ile-analog that competitively inhibits activation by Ile-tRNA synthetase, thus inhibiting protein biosynthesis.

Catalytic activityⁱ

ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile).

Cofactorⁱ

Zn²⁺Note: Binds 1 zinc ion per subunit.

Kineticsⁱ

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	561	Aminoacyl-adenylateBy similarity	1
Binding siteⁱ	605	ATPBy similarity	1
Metal bindingⁱ	901	ZincBy similarity	1
Metal bindingⁱ	904	ZincBy similarity	1
Metal bindingⁱ	921	ZincBy similarity	1
Metal bindingⁱ	924	ZincBy similarity	1

GO - Molecular functionⁱ

aminoacyl-tRNA editing activity Source: InterPro
ATP binding Source: UniProtKB-UniRule
isoleucine-tRNA ligase activity
Source: GO_Central
Inferred from direct assayⁱ
- 4581276
tRNA binding Source: InterPro
zinc ion binding
Source: EcoCyc
Inferred from direct assayⁱ
- 8286369

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

isoleucyl-tRNA aminoacylation
Source: EcoCyc
Inferred from direct assayⁱ
- 764868
response to antibiotic Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Aminoacyl-tRNA synthetase, Ligase
Biological process	Antibiotic resistance, Protein biosynthesis
Ligand	ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCycⁱ	EcoCyc:ILES-MONOMER MetaCyc:ILES-MONOMER

BioCycⁱ

EcoCyc:ILES-MONOMER
MetaCyc:ILES-MONOMER

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Isoleucine--tRNA ligase (EC:6.1.1.5) Alternative name(s): Isoleucyl-tRNA synthetase Short name: IleRS
Gene namesⁱ	Name:ileS Synonyms:ilvS Ordered Locus Names:b0026, JW0024
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	EG10492 ileS

EcoGeneⁱ

EG10492 ileS

Subcellular locationⁱ

Cytoplasm

GO - Cellular componentⁱ

cytosol
Source: EcoCyc
Inferred from direct assayⁱ
- 18304323

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	94	G → R: 6000-fold increase in Km for isoleucine and 4-fold increase in Km for ATP, with no effect on activity. 1 Publication	1
Mutagenesisⁱ	97	C → S: No effect on activity. 1 Publication	1
Mutagenesisⁱ	102	I → N: No significant effect on activity. 1 Publication	1
Mutagenesisⁱ	183	K → A: Abolishes translocation from the aminoacylation site to the editing site, without effect on aminoacylation activity and posttransfer editing; when associated with A-421. 1 Publication	1
Mutagenesisⁱ	241	T → A: Nearly the same editing activity as the wild-type. 1 Publication	1
Mutagenesisⁱ	242	T → A: Abolishes editing activity against valine, with little change in aminoacylation activity; when associated with A-250. 1 Publication	1
Mutagenesisⁱ	242	T → P: Abolishes editing activity against valine, with little change in aminoacylation activity. 1 Publication	1
Mutagenesisⁱ	243	T → A: Abolishes editing activity against valine, with little change in aminoacylation activity. 2 Publications	1
Mutagenesisⁱ	243	T → R: Abolishes pretransfer editing. 2 Publications	1
Mutagenesisⁱ	246	T → A: Nearly the same editing activity as the wild-type. 1 Publication	1
Mutagenesisⁱ	250	N → A: Abolishes editing activity against valine, with little change in aminoacylation activity. 2 Publications	1
Mutagenesisⁱ	333	H → A: Alters the specificity for hydrolysis of the aminoacyl tRNA ester, with no effect on pretransfer editing. 1 Publication	1
Mutagenesisⁱ	342	D → A or N: Strong decrease in total editing and deacylation activities. Severely deficient in translocation from the aminoacylation site to the editing site. 1 Publication	1
Mutagenesisⁱ	342	D → E: Reduces 2- to 3-fold the total editing activity and 2-fold the deacylation activity. Moderately reduces translocation from the aminoacylation site to the editing site. 1 Publication	1
Mutagenesisⁱ	421	W → A: Abolishes translocation from the aminoacylation site to the editing site, without effect on aminoacylation activity and posttransfer editing; when associated with A-183. 1 Publication	1

Chemistry databases

ChEMBLⁱ	CHEMBL3657

ChEMBLⁱ

CHEMBL3657

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed1 Publication
ChainⁱPRO_0000098384	2 – 938	Isoleucine--tRNA ligaseAdd BLAST		937

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	183	N6-acetyllysine1 Publication		1

Keywords - PTMⁱ

Acetylation

Proteomic databases

EPDⁱ	P00956
PaxDbⁱ	P00956
PRIDEⁱ	P00956

PTM databases

iPTMnetⁱ	P00956

iPTMnetⁱ

P00956

Interactionⁱ

Subunit structureⁱ

Monomer.

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
hyaD	P19930	3	EBI-552928,EBI-552940
rbsB	P02925	3	EBI-552928,EBI-369930
tufA	P0CE47	2	EBI-552928,EBI-301077
yjgL	P39336	3	EBI-552928,EBI-549937

Protein-protein interaction databases

BioGridⁱ	4261375, 35 interactors 849163, 1 interactor
Database of interacting proteins More...DIPⁱ	DIP-10017N
IntActⁱ	P00956, 17 interactors
STRINGⁱ	316385.ECDH10B_0027

Chemistry databases

BindingDBⁱ

P00956

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P00956
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	58 – 68	"HIGH" regionAdd BLAST		11
Motifⁱ	602 – 606	"KMSKS" region		5

Domainⁱ

IleRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated valine is translocated from the active site to the editing site, which sterically excludes the correctly activated isoleucine. The single editing site contains two valyl binding pockets, one specific for each substrate (Val-AMP or Val-tRNA(Ile)).

Sequence similaritiesⁱ

Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 1 subfamily.Curated

Phylogenomic databases

eggNOGⁱ	ENOG4105C07 Bacteria COG0060 LUCA
HOGENOMⁱ	HOG000246402
InParanoidⁱ	P00956
KEGG Orthology (KO) More...KOⁱ	K01870
PhylomeDBⁱ	P00956

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd07960 Anticodon_Ia_Ile_BEm, 1 hit
Gene3Dⁱ	3.40.50.620, 1 hit 3.90.740.10, 1 hit
HAMAPⁱ	MF_02002 Ile_tRNA_synth_type1, 1 hit
InterProⁱ	View protein in InterPro IPR001412 aa-tRNA-synth_I_CS IPR002300 aa-tRNA-synth_Ia IPR033708 Anticodon_Ile_BEm IPR002301 Ile-tRNA-ligase IPR023585 Ile-tRNA-ligase_type1 IPR013155 M/V/L/I-tRNA-synth_anticd-bd IPR014729 Rossmann-like_a/b/a_fold IPR009080 tRNAsynth_Ia_anticodon-bd IPR009008 Val/Leu/Ile-tRNA-synth_edit IPR010663 Znf_FPG/IleRS
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF08264 Anticodon_1, 1 hit PF00133 tRNA-synt_1, 1 hit PF06827 zf-FPG_IleRS, 1 hit
PRINTSⁱ	PR00984 TRNASYNTHILE
SUPFAMⁱ	SSF47323 SSF47323, 1 hit SSF50677 SSF50677, 1 hit
TIGRFAMsⁱ	TIGR00392 ileS, 1 hit
PROSITEⁱ	View protein in PROSITE PS00178 AA_TRNA_LIGASE_I, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P00956-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MSDYKSTLNL PETGFPMRGD LAKREPGMLA RWTDDDLYGI IRAAKKGKKT 
        60         70         80         90        100
FILHDGPPYA NGSIHIGHSV NKILKDIIVK SKGLSGYDSP YVPGWDCHGL 
       110        120        130        140        150
PIELKVEQEY GKPGEKFTAA EFRAKCREYA ATQVDGQRKD FIRLGVLGDW 
       160        170        180        190        200
SHPYLTMDFK TEANIIRALG KIIGNGHLHK GAKPVHWCVD CRSALAEAEV 
       210        220        230        240        250
EYYDKTSPSI DVAFQAVDQD ALKAKFAVSN VNGPISLVIW TTTPWTLPAN 
       260        270        280        290        300
RAISIAPDFD YALVQIDGQA VILAKDLVES VMQRIGVTDY TILGTVKGAE 
       310        320        330        340        350
LELLRFTHPF MGFDVPAILG DHVTLDAGTG AVHTAPGHGP DDYVIGQKYG 
       360        370        380        390        400
LETANPVGPD GTYLPGTYPT LDGVNVFKAN DIVVALLQEK GALLHVEKMQ 
       410        420        430        440        450
HSYPCCWRHK TPIIFRATPQ WFVSMDQKGL RAQSLKEIKG VQWIPDWGQA 
       460        470        480        490        500
RIESMVANRP DWCISRQRTW GVPMSLFVHK DTEELHPRTL ELMEEVAKRV 
       510        520        530        540        550
EVDGIQAWWD LDAKEILGDE ADQYVKVPDT LDVWFDSGST HSSVVDVRPE 
       560        570        580        590        600
FAGHAADMYL EGSDQHRGWF MSSLMISTAM KGKAPYRQVL THGFTVDGQG 
       610        620        630        640        650
RKMSKSIGNT VSPQDVMNKL GADILRLWVA STDYTGEMAV SDEILKRAAD 
       660        670        680        690        700
SYRRIRNTAR FLLANLNGFD PAKDMVKPEE MVVLDRWAVG CAKAAQEDIL 
       710        720        730        740        750
KAYEAYDFHE VVQRLMRFCS VEMGSFYLDI IKDRQYTAKA DSVARRSCQT 
       760        770        780        790        800
ALYHIAEALV RWMAPILSFT ADEVWGYLPG EREKYVFTGE WYEGLFGLAD 
       810        820        830        840        850
SEAMNDAFWD ELLKVRGEVN KVIEQARADK KVGGSLEAAV TLYAEPELSA 
       860        870        880        890        900
KLTALGDELR FVLLTSGATV ADYNDAPADA QQSEVLKGLK VALSKAEGEK 
       910        920        930 
CPRCWHYTQD VGKVAEHAEI CGRCVSNVAG DGEKRKFA

Length:938

Mass (Da):104,297

Last modified:January 23, 2007 - v5

Checksum:ⁱ238CEDAF461F01D5

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	243 – 264	TPWTL…DYALV → RRGLCLPTAQSLLHQISTMR WW AA sequence (PubMed:6390679).CuratedAdd BLAST	22
Sequence conflictⁱ	300 – 301	EL → DV AA sequence (PubMed:6390679).Curated	2
Sequence conflictⁱ	587	R → C AA sequence (PubMed:6390679).Curated	1
Sequence conflictⁱ	637	E → Q AA sequence (PubMed:6390679).Curated	1
Sequence conflictⁱ	724	G → V AA sequence (PubMed:6390679).Curated	1
Sequence conflictⁱ	738	A → P AA sequence (PubMed:6390679).Curated	1
Sequence conflictⁱ	740 – 743	ADSV → RTVW AA sequence (PubMed:6390679).Curated	4
Sequence conflictⁱ	787	F → L AA sequence (PubMed:6390679).Curated	1
Sequence conflictⁱ	830	K → N AA sequence (PubMed:6390679).Curated	1
Sequence conflictⁱ	867 – 869	GAT → DRRY AA sequence (PubMed:6390679).Curated	3

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱ	594	F → L in strain: PS102.		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U00096 Genomic DNA Translation: AAC73137.1 AP009048 Genomic DNA Translation: BAB96595.2 M10428 Genomic DNA Translation: AAA24606.1 X00776 Genomic DNA Translation: CAA25352.1 K01990 Genomic DNA Translation: AAA24091.1
PIRⁱ	B64723 SYECIT
NCBI Reference Sequences More...RefSeqⁱ	NP_414567.1, NC_000913.3 WP_001286857.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC73137; AAC73137; b0026 BAB96595; BAB96595; BAB96595
GeneIDⁱ	944761
KEGGⁱ	ecj:JW0024 eco:b0026
PATRICⁱ	fig\|1411691.4.peg.2259

Protein	Similar proteins		Species	Score	Length	Source
P00956	Isoleucine--tRNA ligase		ECO55		938	UniRef100_B7L4E8
Isoleucine--tRNA ligase		ECO8A		938
Isoleucine--tRNA ligase		ECOBW		938
Isoleucine--tRNA ligase		ECODH		938
Isoleucine--tRNA ligase		ECOSE		938
+38

Protein	Similar proteins		Species	Score	Length	Source
P00956	Isoleucine--tRNA ligase		ECO57		938	UniRef90_Q8XA49
Isoleucine--tRNA ligase		ECO5E		938
Isoleucine--tRNA ligase		CITK8		938
Isoleucine--tRNA ligase		CROS8		938
Isoleucine--tRNA ligase		ECO24		938
+1788

Protein	Similar proteins		Species	Score	Length	Source
P00956	Isoleucine--tRNA ligase		ECO57		938	UniRef50_Q8XA49
Isoleucine--tRNA ligase		ECO5E		938
Isoleucine--tRNA ligase		KLEP3		938
Isoleucine--tRNA ligase		SHIDS		938
Isoleucine--tRNA ligase		ECO55		938
+3166

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U00096 Genomic DNA Translation: AAC73137.1 AP009048 Genomic DNA Translation: BAB96595.2 M10428 Genomic DNA Translation: AAA24606.1 X00776 Genomic DNA Translation: CAA25352.1 K01990 Genomic DNA Translation: AAA24091.1
PIRⁱ	B64723 SYECIT
RefSeqⁱ	NP_414567.1, NC_000913.3 WP_001286857.1, NZ_LN832404.1

3D structure databases

ProteinModelPortalⁱ	P00956
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4261375, 35 interactors 849163, 1 interactor
DIPⁱ	DIP-10017N
IntActⁱ	P00956, 17 interactors
STRINGⁱ	316385.ECDH10B_0027

Chemistry databases

BindingDBⁱ	P00956
ChEMBLⁱ	CHEMBL3657

PTM databases

iPTMnetⁱ	P00956

iPTMnetⁱ

P00956

Proteomic databases

EPDⁱ	P00956
PaxDbⁱ	P00956
PRIDEⁱ	P00956

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC73137; AAC73137; b0026 BAB96595; BAB96595; BAB96595
GeneIDⁱ	944761
KEGGⁱ	ecj:JW0024 eco:b0026
PATRICⁱ	fig\|1411691.4.peg.2259

Organism-specific databases

EchoBASEⁱ	EB0487
EcoGeneⁱ	EG10492 ileS

Phylogenomic databases

eggNOGⁱ	ENOG4105C07 Bacteria COG0060 LUCA
HOGENOMⁱ	HOG000246402
InParanoidⁱ	P00956
KOⁱ	K01870
PhylomeDBⁱ	P00956

Enzyme and pathway databases

BioCycⁱ	EcoCyc:ILES-MONOMER MetaCyc:ILES-MONOMER

BioCycⁱ

EcoCyc:ILES-MONOMER
MetaCyc:ILES-MONOMER

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P00956

PROⁱ

PR:P00956

Family and domain databases

CDDⁱ	cd07960 Anticodon_Ia_Ile_BEm, 1 hit
Gene3Dⁱ	3.40.50.620, 1 hit 3.90.740.10, 1 hit
HAMAPⁱ	MF_02002 Ile_tRNA_synth_type1, 1 hit
InterProⁱ	View protein in InterPro IPR001412 aa-tRNA-synth_I_CS IPR002300 aa-tRNA-synth_Ia IPR033708 Anticodon_Ile_BEm IPR002301 Ile-tRNA-ligase IPR023585 Ile-tRNA-ligase_type1 IPR013155 M/V/L/I-tRNA-synth_anticd-bd IPR014729 Rossmann-like_a/b/a_fold IPR009080 tRNAsynth_Ia_anticodon-bd IPR009008 Val/Leu/Ile-tRNA-synth_edit IPR010663 Znf_FPG/IleRS
Pfamⁱ	View protein in Pfam PF08264 Anticodon_1, 1 hit PF00133 tRNA-synt_1, 1 hit PF06827 zf-FPG_IleRS, 1 hit
PRINTSⁱ	PR00984 TRNASYNTHILE
SUPFAMⁱ	SSF47323 SSF47323, 1 hit SSF50677 SSF50677, 1 hit
TIGRFAMsⁱ	TIGR00392 ileS, 1 hit
PROSITEⁱ	View protein in PROSITE PS00178 AA_TRNA_LIGASE_I, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	SYI_ECOLI
Accessionⁱ	P00956Primary (citable) accession number: P00956 Secondary accession number(s): P78038, Q59429
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
	Last sequence update:	January 23, 2007
	Last modified:	November 7, 2018
	This is version 184 of the entry and version 5 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
Aminoacyl-tRNA synthetases
List of aminoacyl-tRNA synthetase entries
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

UniProtKB

UniParc

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UniRef

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Supporting data

UniProtKB - P00956 (SYI_ECOLI)

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Isoleucine--tRNA ligase

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 ‘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

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

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

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

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

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM 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

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

Motif

<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

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

PTM 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

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ