ftsW

Functionⁱ

Peptidoglycan polymerase that is essential for cell division (Probable). Functions probably in conjunction with the penicillin-binding protein 3 (ftsI) (PubMed:9603865, PubMed:11807049). Required for localization of FtsI (PubMed:11807049).2 Publications2 Publications

Caution

Has previously been proposed to be a lipid II flippase that transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane (PubMed:21386816, PubMed:24711460), but recent evidence suggests that FtsW may function as a peptidoglycan polymerase (PubMed:27643381). The identity of the lipid II flippase is still controversial with conflicting in vivo and in vitro results, but MurJ (AC P0AF16) is probably the lipid II flippase.Curated

Catalytic activityⁱ

(GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl diphosphate.UniRule annotation

Pathwayⁱ: peptidoglycan biosynthesis

This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

GO - Molecular functionⁱ

lipid-linked peptidoglycan transporter activity
Source: EcoCyc
Inferred from direct assayⁱ
- 21386816
peptidoglycan glycosyltransferase activity Source: UniProtKB-UniRule

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cell division
Source: EcoliWiki
Inferred from mutant phenotypeⁱ
- 9006034
- 9603865
cell wall organization Source: UniProtKB-KW
FtsZ-dependent cytokinesis Source: UniProtKB-UniRule
peptidoglycan biosynthetic process Source: UniProtKB-UniRule
regulation of cell shape
Source: EcoliWiki
Inferred from mutant phenotypeⁱ
- 9006034

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Glycosyltransferase, Transferase
Biological process	Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10344-MONOMER MetaCyc:EG10344-MONOMER
UniPathwayⁱ	UPA00219

Protein family/group databases

TCDBⁱ	2.A.103.1.1 the bacterial murein precursor exporter (mpe) family

TCDBⁱ

2.A.103.1.1 the bacterial murein precursor exporter (mpe) family

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Probable peptidoglycan glycosyltransferase FtsWUniRule annotationBy similarity (EC:2.4.1.129UniRule annotationBy similarity) Short name: PGTUniRule annotationBy similarity Alternative name(s): Cell division protein FtsWUniRule annotationCurated Cell wall polymeraseUniRule annotationBy similarity Lipid II flippase FtsWCurated Peptidoglycan polymeraseUniRule annotationBy similarity Short name: PG polymeraseUniRule annotationBy similarity
Gene namesⁱ	Name:ftsWUniRule annotation Ordered Locus Names:b0089, JW0087
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	EG10344 ftsW

EcoGeneⁱ

EG10344 ftsW

Subcellular locationⁱ

Cell inner membrane
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00913
3 Publications
Manual assertion based on experiment inⁱ
- Ref.9
  "FtsI and FtsW are localized to the septum in Escherichia coli."
  Wang L., Khattar M.K., Donachie W.D., Lutkenhaus J.
  J. Bacteriol. 180:2810-2816(1998) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBCELLULAR LOCATION.
- Ref.10
  "Topological characterization of the essential Escherichia coli cell division protein FtsW."
  Lara B., Ayala J.A.
  FEMS Microbiol. Lett. 216:23-32(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION, TOPOLOGY.
- Ref.11
  "The Escherichia coli cell division protein FtsW is required to recruit its cognate transpeptidase, FtsI (PBP3), to the division site."
  Mercer K.L., Weiss D.S.
  J. Bacteriol. 184:904-912(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBCELLULAR LOCATION.
; Multi-pass membrane protein
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00913
3 Publications
Manual assertion based on experiment inⁱ
- Ref.9
  "FtsI and FtsW are localized to the septum in Escherichia coli."
  Wang L., Khattar M.K., Donachie W.D., Lutkenhaus J.
  J. Bacteriol. 180:2810-2816(1998) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBCELLULAR LOCATION.
- Ref.10
  "Topological characterization of the essential Escherichia coli cell division protein FtsW."
  Lara B., Ayala J.A.
  FEMS Microbiol. Lett. 216:23-32(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION, TOPOLOGY.
- Ref.11
  "The Escherichia coli cell division protein FtsW is required to recruit its cognate transpeptidase, FtsI (PBP3), to the division site."
  Mercer K.L., Weiss D.S.
  J. Bacteriol. 184:904-912(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBCELLULAR LOCATION.

Note:

Localizes to the division septum. Localization requires FtsZ, FtsA, FtsQ and FtsL, but not FtsI.

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 12	CytoplasmicSequence analysisAdd BLAST	12
Transmembraneⁱ	13 – 33	HelicalUniRule annotationAdd BLAST	21
Topological domainⁱ	34 – 47	PeriplasmicSequence analysisAdd BLAST	14
Transmembraneⁱ	48 – 68	HelicalUniRule annotationAdd BLAST	21
Topological domainⁱ	69 – 86	CytoplasmicSequence analysisAdd BLAST	18
Transmembraneⁱ	87 – 107	HelicalUniRule annotationAdd BLAST	21
Topological domainⁱ	108 – 111	PeriplasmicSequence analysis	4
Transmembraneⁱ	112 – 132	HelicalUniRule annotationAdd BLAST	21
Topological domainⁱ	133 – 174	CytoplasmicSequence analysisAdd BLAST	42
Transmembraneⁱ	175 – 194	HelicalUniRule annotationAdd BLAST	20
Topological domainⁱ	195 – 197	PeriplasmicSequence analysis	3
Transmembraneⁱ	198 – 217	HelicalUniRule annotationAdd BLAST	20
Topological domainⁱ	218 – 221	CytoplasmicSequence analysis	4
Transmembraneⁱ	222 – 244	HelicalUniRule annotationAdd BLAST	23
Topological domainⁱ	245 – 301	PeriplasmicSequence analysisAdd BLAST	57
Transmembraneⁱ	302 – 322	HelicalUniRule annotationAdd BLAST	21
Topological domainⁱ	323 – 342	CytoplasmicSequence analysisAdd BLAST	20
Transmembraneⁱ	343 – 363	HelicalUniRule annotationAdd BLAST	21
Topological domainⁱ	364 – 373	PeriplasmicSequence analysis	10
Transmembraneⁱ	374 – 394	HelicalUniRule annotationAdd BLAST	21
Topological domainⁱ	395 – 414	CytoplasmicSequence analysisAdd BLAST	20

GO - Cellular componentⁱ

cell division site
Source: EcoliWiki
Inferred from direct assayⁱ
- 9603865
integral component of plasma membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 21386816
plasma membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 15919996

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	145	R → A: Loss of flippase activity. Does not affect localization at the division site. 1 Publication	1
Mutagenesisⁱ	150 – 152	ELT → AAA: Does not affect flippase activity. 1 Publication	3
Mutagenesisⁱ	153	K → N: Loss of flippase activity. Does not affect localization at the division site. 1 Publication	1
Mutagenesisⁱ	154 – 156	LSL → AAA: Does not affect flippase activity. 1 Publication	3
Mutagenesisⁱ	170	E → K in ftsW201; TS; blocks division at the initiation stage.	1
Mutagenesisⁱ	172	R → S: Does not affect localization, but affects its thermosensitivity. 1 Publication	1
Mutagenesisⁱ	181	P → L in ftsW1640; TS; blocks division at a late stage.	1
Mutagenesisⁱ	243	R → Q: Lack of activity. 1 Publication	1
Mutagenesisⁱ	253	P → L in ftsW263; TS; blocks division at the initiation stage.	1
Mutagenesisⁱ	311	G → D: Thermosensitive. Fails to localize to the division site at 42 degrees Celsius. 1 Publication	1
Mutagenesisⁱ	368	P → A: Cannot recruit FtsI at the division site; when associated with A-375. 1 Publication	1
Mutagenesisⁱ	375	P → A: Cannot recruit FtsI at the division site; when associated with A-368. 1 Publication	1
Mutagenesisⁱ	402	R → Q: Does not affect localization and activity. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000062700	1 – 414	Probable peptidoglycan glycosyltransferase FtsWAdd BLAST		414

Proteomic databases

PaxDbⁱ	P0ABG4
PRIDEⁱ	P0ABG4

Interactionⁱ

Subunit structureⁱ

Forms a complex with FtsI. Interacts also with FtsL, FtsQ and FtsN.4 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
ftsI	P0AD68	7	EBI-1214767,EBI-548564
ftsN	P29131	3	EBI-1214767,EBI-1134233
ftsQ	P06136	3	EBI-1214767,EBI-1130157

Protein-protein interaction databases

BioGridⁱ	4261096, 505 interactors
Database of interacting proteins More...DIPⁱ	DIP-47989N
IntActⁱ	P0ABG4, 14 interactors
Molecular INTeraction database More...MINTⁱ	P0ABG4
STRINGⁱ	316385.ECDH10B_0071

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P0ABG4
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domainⁱ

The periplasmic loop between transmembrane domains 7 and 8 is essential for activity and the loop between transmembrane domains 9 and 10 is involved in the recruitment of FtsI at the division site.1 Publication

Sequence similaritiesⁱ

Belongs to the SEDS family. FtsW subfamily.UniRule annotationCurated

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	ENOG4105CNI Bacteria COG0772 LUCA
HOGENOMⁱ	HOG000282689
InParanoidⁱ	P0ABG4
KEGG Orthology (KO) More...KOⁱ	K03588
OMAⁱ	KGYQLSH
PhylomeDBⁱ	P0ABG4

Family and domain databases

HAMAPⁱ	MF_00913 PGT_FtsW_proteobact, 1 hit
InterProⁱ	View protein in InterPro IPR018365 Cell_cycle_FtsW-rel_CS IPR013437 FtsW IPR001182 FtsW/RodA
PANTHERⁱ	PTHR30474 PTHR30474, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01098 FTSW_RODA_SPOVE, 1 hit
TIGRFAMsⁱ	TIGR02614 ftsW, 1 hit
PROSITEⁱ	View protein in PROSITE PS00428 FTSW_RODA_SPOVE, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P0ABG4-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MRLSLPRLKM PRLPGFSILV WISTALKGWV MGSREKDTDS LIMYDRTLLW 
        60         70         80         90        100
LTFGLAAIGF IMVTSASMPI GQRLTNDPFF FAKRDGVYLI LAFILAIITL 
       110        120        130        140        150
RLPMEFWQRY SATMLLGSII LLMIVLVVGS SVKGASRWID LGLLRIQPAE 
       160        170        180        190        200
LTKLSLFCYI ANYLVRKGDE VRNNLRGFLK PMGVILVLAV LLLAQPDLGT 
       210        220        230        240        250
VVVLFVTTLA MLFLAGAKLW QFIAIIGMGI SAVVLLILAE PYRIRRVTAF 
       260        270        280        290        300
WNPWEDPFGS GYQLTQSLMA FGRGELWGQG LGNSVQKLEY LPEAHTDFIF 
       310        320        330        340        350
AIIGEELGYV GVVLALLMVF FVAFRAMSIG RKALEIDHRF SGFLACSIGI 
       360        370        380        390        400
WFSFQALVNV GAAAGMLPTK GLTLPLISYG GSSLLIMSTA IMMLLRIDYE 
       410 
TRLEKAQAFV RGSR

Length:414

Mass (Da):45,987

Last modified:October 25, 2005 - v1

Checksum:ⁱ7935EC952AD9A1F3

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M30807 Genomic DNA Translation: AAA83859.1 X55034 Genomic DNA Translation: CAA38866.1 U00096 Genomic DNA Translation: AAC73200.1 AP009048 Genomic DNA Translation: BAB96657.1 X52644 Genomic DNA Translation: CAA36866.1
PIRⁱ	A32581 CEECFW
NCBI Reference Sequences More...RefSeqⁱ	NP_414631.1, NC_000913.3 WP_001295532.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC73200; AAC73200; b0089 BAB96657; BAB96657; BAB96657
GeneIDⁱ	946322
KEGGⁱ	ecj:JW0087 eco:b0089
PATRICⁱ	fig\|1411691.4.peg.2191

Protein	Similar proteins		Species	Score	Length	Source
P0ABG4	Probable peptidoglycan glycosyltransferase FtsW		ECO57		414	UniRef100_P0ABG6
Probable peptidoglycan glycosyltransferase FtsW		ECOL6		414
Probable peptidoglycan glycosyltransferase FtsW		Escherichia coli O25b:H4-ST131		415
Probable peptidoglycan glycosyltransferase FtsW		Escherichia coli O25b:H4		415
Probable peptidoglycan glycosyltransferase FtsW		Shigella dysenteriae WRSd3		415
+178

Protein	Similar proteins		Species	Score	Length	Source
P0ABG4	Probable peptidoglycan glycosyltransferase FtsW		ECO57		414	UniRef90_P0ABG6
Probable peptidoglycan glycosyltransferase FtsW		ECOL6		414
Probable peptidoglycan glycosyltransferase FtsW		Escherichia coli O25b:H4-ST131		415
Probable peptidoglycan glycosyltransferase FtsW		Escherichia coli O25b:H4		415
Probable peptidoglycan glycosyltransferase FtsW		Shigella dysenteriae WRSd3		415
+396

Protein	Similar proteins		Species	Score	Length	Source
P0ABG4	Probable peptidoglycan glycosyltransferase FtsW		ECO57		414	UniRef50_P0ABG6
Probable peptidoglycan glycosyltransferase FtsW		ECOL6		414
Probable peptidoglycan glycosyltransferase FtsW		PSEA6		487
Probable peptidoglycan glycosyltransferase FtsW		ALTNA		514
Probable peptidoglycan glycosyltransferase FtsW		Escherichia coli O25b:H4-ST131		415
+1203

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M30807 Genomic DNA Translation: AAA83859.1 X55034 Genomic DNA Translation: CAA38866.1 U00096 Genomic DNA Translation: AAC73200.1 AP009048 Genomic DNA Translation: BAB96657.1 X52644 Genomic DNA Translation: CAA36866.1
PIRⁱ	A32581 CEECFW
RefSeqⁱ	NP_414631.1, NC_000913.3 WP_001295532.1, NZ_LN832404.1

3D structure databases

ProteinModelPortalⁱ	P0ABG4
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4261096, 505 interactors
DIPⁱ	DIP-47989N
IntActⁱ	P0ABG4, 14 interactors
MINTⁱ	P0ABG4
STRINGⁱ	316385.ECDH10B_0071

Protein family/group databases

TCDBⁱ	2.A.103.1.1 the bacterial murein precursor exporter (mpe) family

TCDBⁱ

2.A.103.1.1 the bacterial murein precursor exporter (mpe) family

Proteomic databases

PaxDbⁱ	P0ABG4
PRIDEⁱ	P0ABG4

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC73200; AAC73200; b0089 BAB96657; BAB96657; BAB96657
GeneIDⁱ	946322
KEGGⁱ	ecj:JW0087 eco:b0089
PATRICⁱ	fig\|1411691.4.peg.2191

Organism-specific databases

EchoBASEⁱ	EB0340
EcoGeneⁱ	EG10344 ftsW

Phylogenomic databases

eggNOGⁱ	ENOG4105CNI Bacteria COG0772 LUCA
HOGENOMⁱ	HOG000282689
InParanoidⁱ	P0ABG4
KOⁱ	K03588
OMAⁱ	KGYQLSH
PhylomeDBⁱ	P0ABG4

Enzyme and pathway databases

UniPathwayⁱ	UPA00219
BioCycⁱ	EcoCyc:EG10344-MONOMER MetaCyc:EG10344-MONOMER

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P0ABG4

PROⁱ

PR:P0ABG4

Family and domain databases

HAMAPⁱ	MF_00913 PGT_FtsW_proteobact, 1 hit
InterProⁱ	View protein in InterPro IPR018365 Cell_cycle_FtsW-rel_CS IPR013437 FtsW IPR001182 FtsW/RodA
PANTHERⁱ	PTHR30474 PTHR30474, 1 hit
Pfamⁱ	View protein in Pfam PF01098 FTSW_RODA_SPOVE, 1 hit
TIGRFAMsⁱ	TIGR02614 ftsW, 1 hit
PROSITEⁱ	View protein in PROSITE PS00428 FTSW_RODA_SPOVE, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	FTSW_ECOLI
Accessionⁱ	P0ABG4Primary (citable) accession number: P0ABG4 Secondary accession number(s): P16457
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
	Last sequence update:	October 25, 2005
	Last modified:	October 10, 2018
	This is version 111 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, 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 - P0ABG4 (FTSW_ECOLI)

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Probable peptidoglycan glycosyltransferase FtsW

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

Caution

<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: peptidoglycan biosynthesis

<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

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

<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

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

Pathwayⁱ: peptidoglycan biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ