manX

Functionⁱ

The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane (PubMed:2951378, PubMed:2999119, PubMed:2681202, PubMed:8262947). The enzyme II ManXYZ PTS system is involved in mannose transport (PubMed:2951378, PubMed:2999119, PubMed:2681202, PubMed:8262947). Also functions as a receptor for bacterial chemotaxis and is required for infection of the cell by bacteriophage lambda where it most likely functions as a pore for penetration of lambda DNA (PubMed:4604906, PubMed:353494).6 Publications

Manual assertion based on experiment inⁱ

Ref.2
"The mannose permease of Escherichia coli consists of three different proteins. Amino acid sequence and function in sugar transport, sugar phosphorylation, and penetration of phage lambda DNA."
Erni B., Zanolari B., Kocher H.P.
J. Biol. Chem. 262:5238-5247(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
Ref.7
"Phosphotransferase-system enzymes as chemoreceptors for certain sugars in Escherichia coli chemotaxis."
Adler J., Epstein W.
Proc. Natl. Acad. Sci. U.S.A. 71:2895-2899(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Ref.8
"E. coli K-12 pel mutants, which block phage lambda DNA injection, coincide with ptsM, which determines a component of a sugar transport system."
Elliott J., Arber W.
Mol. Gen. Genet. 161:1-8(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Ref.9
"The mannose-permease of the bacterial phosphotransferase system. Gene cloning and purification of the enzyme IIMan/IIIMan complex of Escherichia coli."
Erni B., Zanolari B.
J. Biol. Chem. 260:15495-15503(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
Ref.10
"Mannose permease of Escherichia coli. Domain structure and function of the phosphorylating subunit."
Erni B., Zanolari B., Graff P., Kocher H.P.
J. Biol. Chem. 264:18733-18741(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, PHOSPHORYLATION AT HIS-10 AND HIS-175.
Ref.11
"The mannose transporter of Escherichia coli. Structure and function of the IIABMan subunit."
Stolz B., Huber M., Markovic-Housley Z., Erni B.
J. Biol. Chem. 268:27094-27099(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-10; TRP-12; LYS-48; SER-72; HIS-86; SER-110; HIS-175 AND HIS-219, ACTIVE SITE, PHOSPHORYLATION AT HIS-10 AND HIS-175, SUBUNIT.

Catalytic activityⁱ

[Protein]-N(pi)-phospho-L-histidine + D-mannose(Side 1) = [protein]-L-histidine + D-mannose 6-phosphate(Side 2).2 Publications

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	10	Tele-phosphohistidine intermediate; for EIIA activityPROSITE-ProRule annotation4 Publications	1
Siteⁱ	89	Involved in the phosphoryl transfer between H-10 and H-1751 Publication	1
Active siteⁱ	175	Pros-phosphohistidine intermediate; for EIIB activity2 Publications	1

GO - Molecular functionⁱ

kinase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 2999119
protein-N(PI)-phosphohistidine-mannose phosphotransferase system transporter activity
Source: EcoCyc
Inferred from direct assayⁱ
- 5545083

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

glucose import across plasma membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 5545083
mannose transmembrane transport
Source: EcoCyc
Inferred from direct assayⁱ
- 5545083
phosphoenolpyruvate-dependent sugar phosphotransferase system
Source: EcoCyc
Inferred from direct assayⁱ
- 2999119

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Kinase, Transferase
Biological process	Phosphotransferase system, Sugar transport, Transport

Enzyme and pathway databases

BioCycⁱ	EcoCyc:MANX-MONOMER MetaCyc:MANX-MONOMER

BioCycⁱ

EcoCyc:MANX-MONOMER
MetaCyc:MANX-MONOMER

Protein family/group databases

TCDBⁱ	4.A.6.1.1 the pts mannose-fructose-sorbose (man) family

TCDBⁱ

4.A.6.1.1 the pts mannose-fructose-sorbose (man) family

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: PTS system mannose-specific EIIAB component1 Publication (EC:2.7.1.1912 Publications) Alternative name(s): EIIAB-Man1 Publication EIII-Man1 Publication Including the following 2 domains: Mannose-specific phosphotransferase enzyme IIA component1 Publication Alternative name(s): PTS system mannose-specific EIIA component1 Publication Mannose-specific phosphotransferase enzyme IIB component1 Publication Alternative name(s): PTS system mannose-specific EIIB component1 Publication
Gene namesⁱ	Name:manX1 Publication Synonyms:gptB, ptsL1 Publication Ordered Locus Names:b1817, JW1806
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	EG10567 manX

EcoGeneⁱ

EG10567 manX

Subcellular locationⁱ

GO - Cellular componentⁱ

cytoplasm
Source: EcoCyc
Inferred from direct assayⁱ
- 2999119
cytosol
Source: EcoCyc
Inferred from direct assayⁱ
- 2999119
integral component of plasma membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 2999119
membrane
Source: UniProtKB
Inferred from high throughput direct assayⁱ
- 16858726

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell inner membrane, Cell membrane, Cytoplasm, Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	10	H → C: Loss of phosphotransferase activity. Unable to dimerize. 1 Publication	1
Mutagenesisⁱ	10	H → E: Results in the formation of a single complex corresponding to the productive phosphoryl transfer complex. 1 Publication	1
Mutagenesisⁱ	12	W → F: Slight phosphotransferase activity. Unable to dimerize. 1 Publication	1
Mutagenesisⁱ	48	K → C: Retains more than 50% of phosphotransferase activity. 1 Publication	1
Mutagenesisⁱ	72	S → C: Slight phosphotransferase activity. Unable to dimerize. 1 Publication	1
Mutagenesisⁱ	86	H → N: Loss of phosphotransferase activity. 1 Publication	1
Mutagenesisⁱ	110	S → C: Retains more than 50% of phosphotransferase activity. 1 Publication	1
Mutagenesisⁱ	175	H → C: Loss of phosphotransferase activity. 1 Publication	1
Mutagenesisⁱ	219	H → Q: Slight phosphotransferase activity. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed1 Publication1 Publication
ChainⁱPRO_0000186653	2 – 323	PTS system mannose-specific EIIAB componentAdd BLAST		322

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	10	Phosphohistidine; by HPr2 Publications	1
Modified residueⁱ	55	N6-acetyllysine1 Publication	1
Modified residueⁱ	175	Phosphohistidine; by EIIAPROSITE-ProRule annotation2 Publications	1
Modified residueⁱ	234	N6-acetyllysine1 Publication	1

Keywords - PTMⁱ

Acetylation, Phosphoprotein

Proteomic databases

EPDⁱ	P69797
PaxDbⁱ	P69797
PRIDEⁱ	P69797

2D gel databases

SWISS-2DPAGEⁱ	P69797

SWISS-2DPAGEⁱ

P69797

PTM databases

iPTMnetⁱ	P69797

iPTMnetⁱ

P69797

Interactionⁱ

Subunit structureⁱ

Homodimer.1 Publication4 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
cytR	P0ACN7	2	EBI-554089,EBI-1125696

With

Entry

#Exp.

IntAct

Notes

cytR

P0ACN7

2

EBI-554089,EBI-1125696

Protein-protein interaction databases

BioGridⁱ	4259144, 308 interactors 850691, 1 interactor
Database of interacting proteins More...DIPⁱ	DIP-35846N
IntActⁱ	P69797, 15 interactors
Molecular INTeraction database More...MINTⁱ	P69797
STRINGⁱ	316385.ECDH10B_1955

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	4 – 8	Combined sources	5
Helixⁱ	13 – 25	Combined sources	13
Beta strandⁱ	29 – 34	Combined sources	6
Helixⁱ	42 – 53	Combined sources	12
Beta strandⁱ	62 – 68	Combined sources	7
Helixⁱ	72 – 81	Combined sources	10
Beta strandⁱ	87 – 92	Combined sources	6
Helixⁱ	95 – 105	Combined sources	11
Helixⁱ	111 – 124	Combined sources	14
Beta strandⁱ	163 – 170	Combined sources	8
Helixⁱ	178 – 185	Combined sources	8
Beta strandⁱ	189 – 194	Combined sources	6
Helixⁱ	196 – 199	Combined sources	4
Helixⁱ	202 – 210	Combined sources	9
Beta strandⁱ	217 – 221	Combined sources	5
Helixⁱ	223 – 230	Combined sources	8
Helixⁱ	233 – 235	Combined sources	3
Beta strandⁱ	239 – 246	Combined sources	8
Helixⁱ	247 – 255	Combined sources	9
Beta strandⁱ	261 – 267	Combined sources	7
Beta strandⁱ	274 – 276	Combined sources	3
Beta strandⁱ	278 – 280	Combined sources	3
Helixⁱ	285 – 296	Combined sources	12
Beta strandⁱ	300 – 303	Combined sources	4
Helixⁱ	314 – 319	Combined sources	6

Show more details

3D structure databases

ProteinModelPortalⁱ	P69797
SMRⁱ	P69797
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P69797

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	2 – 124	PTS EIIA type-4PROSITE-ProRule annotation2 PublicationsAdd BLAST		123
Domainⁱ	157 – 320	PTS EIIB type-4PROSITE-ProRule annotation1 PublicationAdd BLAST		164

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	137 – 155	Hinge1 PublicationAdd BLAST		19

Domainⁱ

The PTS EIIA type-4 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-4 domain.2 Publications

The PTS EIIB type-4 domain is phosphorylated by phospho-EIIA on a histidyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-4 domain.PROSITE-ProRule annotation1 Publication

Phylogenomic databases

eggNOGⁱ	ENOG4105DAS Bacteria COG2893 LUCA COG3444 LUCA
HOGENOMⁱ	HOG000140047
InParanoidⁱ	P69797
KEGG Orthology (KO) More...KOⁱ	K02793 K02794
OMAⁱ	EMIFGKQ
PhylomeDBⁱ	P69797

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00006 PTS_IIA_man, 1 hit cd00001 PTS_IIB_man, 1 hit
Gene3Dⁱ	3.40.35.10, 1 hit 3.40.50.510, 1 hit
InterProⁱ	View protein in InterPro IPR013789 PTS_EIIA_man IPR004701 PTS_EIIA_man-typ IPR036662 PTS_EIIA_man-typ_sf IPR033887 PTS_IIA_man IPR004720 PTS_IIB_sorbose-sp IPR036667 PTS_IIB_sorbose-sp_sf IPR018455 PTS_IIB_sorbose-sp_subgr
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF03610 EIIA-man, 1 hit PF03830 PTSIIB_sorb, 1 hit
SUPFAMⁱ	SSF52728 SSF52728, 1 hit SSF53062 SSF53062, 1 hit
TIGRFAMsⁱ	TIGR00824 EIIA-man, 1 hit TIGR00854 pts-sorbose, 1 hit
PROSITEⁱ	View protein in PROSITE PS51096 PTS_EIIA_TYPE_4, 1 hit PS51101 PTS_EIIB_TYPE_4, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P69797-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MTIAIVIGTH GWAAEQLLKT AEMLLGEQEN VGWIDFVPGE NAETLIEKYN 
        60         70         80         90        100
AQLAKLDTTK GVLFLVDTWG GSPFNAASRI VVDKEHYEVI AGVNIPMLVE 
       110        120        130        140        150
TLMARDDDPS FDELVALAVE TGREGVKALK AKPVEKAAPA PAAAAPKAAP 
       160        170        180        190        200
TPAKPMGPND YMVIGLARID DRLIHGQVAT RWTKETNVSR IIVVSDEVAA 
       210        220        230        240        250
DTVRKTLLTQ VAPPGVTAHV VDVAKMIRVY NNPKYAGERV MLLFTNPTDV 
       260        270        280        290        300
ERLVEGGVKI TSVNVGGMAF RQGKTQVNNA VSVDEKDIEA FKKLNARGIE 
       310        320 
LEVRKVSTDP KLKMMDLISK IDK

Length:323

Mass (Da):35,048

Last modified:January 23, 2007 - v2

Checksum:ⁱA446B79421B8C040

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	2 – 23	TIAIV…KTAEM → GWGCRAGCLKRQKW in AAA24110 (Ref. 1) CuratedAdd BLAST	22
Sequence conflictⁱ	35	D → N in AAA24110 (Ref. 1) Curated	1
Sequence conflictⁱ	101	T → R in AAA24110 (Ref. 1) Curated	1
Sequence conflictⁱ	142	A → G in AAA24110 (Ref. 1) Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M36404 Genomic DNA Translation: AAA24110.1 J02699 Genomic DNA Translation: AAA24443.1 U00096 Genomic DNA Translation: AAC74887.1 AP009048 Genomic DNA Translation: BAA15624.1
PIRⁱ	A30286 WQECM3
NCBI Reference Sequences More...RefSeqⁱ	NP_416331.1, NC_000913.3 WP_000150543.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC74887; AAC74887; b1817 BAA15624; BAA15624; BAA15624
GeneIDⁱ	946334
KEGGⁱ	ecj:JW1806 eco:b1817
PATRICⁱ	fig\|1411691.4.peg.434

Protein	Similar proteins		Species	Score	Length	Source
P69797	PTS system mannose-specific EIIAB component		ECO57		323	UniRef100_P69799
PTS system mannose-specific EIIAB component		ECOL6		323
PTS system mannose-specific EIIAB component		SHIFL		323
Fused mannose-specific PTS enzymes: IIA component IIB component		Escherichia coli NCCP15648		323
PTS system, mannose-specific IIA component / PTS system, mannose-specific IIB component		Klebsiella pneumoniae IS22		323
+130

Protein	Similar proteins		Species	Score	Length	Source
P69797	PTS system mannose-specific EIIAB component		ECO57		323	UniRef90_P69799
PTS system mannose-specific EIIAB component		ECOL6		323
PTS system mannose-specific EIIAB component		SHIFL		323
Fused mannose-specific PTS enzymes: IIA component IIB component		Escherichia coli NCCP15648		323
PTS system, mannose-specific IIA component / PTS system, mannose-specific IIB component		Klebsiella pneumoniae IS22		323
+1173

Protein	Similar proteins		Species	Score	Length	Source
P69797	PTS system mannose-specific EIIAB component		ECO57		323	UniRef50_P69799
PTS system mannose-specific EIIAB component		ECOL6		323
PTS system mannose-specific EIIAB component		SHIFL		323
Fused mannose-specific PTS enzymes: IIA component IIB component		Escherichia coli NCCP15648		323
PTS system, mannose-specific IIA component / PTS system, mannose-specific IIB component		Klebsiella pneumoniae IS22		323
+1813

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M36404 Genomic DNA Translation: AAA24110.1 J02699 Genomic DNA Translation: AAA24443.1 U00096 Genomic DNA Translation: AAC74887.1 AP009048 Genomic DNA Translation: BAA15624.1
PIRⁱ	A30286 WQECM3
RefSeqⁱ	NP_416331.1, NC_000913.3 WP_000150543.1, 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
	1PDO	X-ray	1.70	A	2-133	[»]
	1VRC	NMR	-	A/B	1-133	[»]
	1VSQ	NMR	-	A/B	2-134	[»]
				C	159-323	[»]
	2JZH	NMR	-	A	154-323	[»]
	2JZN	NMR	-	A/B	2-134	[»]
				C	159-323	[»]
	2JZO	NMR	-	A/B	2-134	[»]
				D	159-323	[»]
ProteinModelPortalⁱ	P69797
SMRⁱ	P69797
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4259144, 308 interactors 850691, 1 interactor
DIPⁱ	DIP-35846N
IntActⁱ	P69797, 15 interactors
MINTⁱ	P69797
STRINGⁱ	316385.ECDH10B_1955

Protein family/group databases

TCDBⁱ	4.A.6.1.1 the pts mannose-fructose-sorbose (man) family

TCDBⁱ

4.A.6.1.1 the pts mannose-fructose-sorbose (man) family

PTM databases

iPTMnetⁱ	P69797

iPTMnetⁱ

P69797

2D gel databases

SWISS-2DPAGEⁱ	P69797

SWISS-2DPAGEⁱ

P69797

Proteomic databases

EPDⁱ	P69797
PaxDbⁱ	P69797
PRIDEⁱ	P69797

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC74887; AAC74887; b1817 BAA15624; BAA15624; BAA15624
GeneIDⁱ	946334
KEGGⁱ	ecj:JW1806 eco:b1817
PATRICⁱ	fig\|1411691.4.peg.434

Organism-specific databases

EchoBASEⁱ	EB0562
EcoGeneⁱ	EG10567 manX

Phylogenomic databases

eggNOGⁱ	ENOG4105DAS Bacteria COG2893 LUCA COG3444 LUCA
HOGENOMⁱ	HOG000140047
InParanoidⁱ	P69797
KOⁱ	K02793 K02794
OMAⁱ	EMIFGKQ
PhylomeDBⁱ	P69797

Enzyme and pathway databases

BioCycⁱ	EcoCyc:MANX-MONOMER MetaCyc:MANX-MONOMER

BioCycⁱ

EcoCyc:MANX-MONOMER
MetaCyc:MANX-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P69797
Protein Ontology More...PROⁱ	PR:P69797

Family and domain databases

CDDⁱ	cd00006 PTS_IIA_man, 1 hit cd00001 PTS_IIB_man, 1 hit
Gene3Dⁱ	3.40.35.10, 1 hit 3.40.50.510, 1 hit
InterProⁱ	View protein in InterPro IPR013789 PTS_EIIA_man IPR004701 PTS_EIIA_man-typ IPR036662 PTS_EIIA_man-typ_sf IPR033887 PTS_IIA_man IPR004720 PTS_IIB_sorbose-sp IPR036667 PTS_IIB_sorbose-sp_sf IPR018455 PTS_IIB_sorbose-sp_subgr
Pfamⁱ	View protein in Pfam PF03610 EIIA-man, 1 hit PF03830 PTSIIB_sorb, 1 hit
SUPFAMⁱ	SSF52728 SSF52728, 1 hit SSF53062 SSF53062, 1 hit
TIGRFAMsⁱ	TIGR00824 EIIA-man, 1 hit TIGR00854 pts-sorbose, 1 hit
PROSITEⁱ	View protein in PROSITE PS51096 PTS_EIIA_TYPE_4, 1 hit PS51101 PTS_EIIB_TYPE_4, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	PTNAB_ECOLI
Accessionⁱ	P69797Primary (citable) accession number: P69797 Secondary accession number(s): P08186, Q47350
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
	Last sequence update:	January 23, 2007
	Last modified:	April 25, 2018
	This is version 129 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

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

UniProtKB

UniParc

Help

UniRef

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Supporting data

UniProtKB - P69797 (PTNAB_ECOLI)

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PTS system mannose-specific EIIAB component

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

<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

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

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel 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

<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

Phylogenomic databases

Family and domain databases

Experimental Info

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

PTM databases

2D gel 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

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ