UniProtKB - P08191 (FIMH_ECOLI)

>sp|P08191|FIMH_ECOLI Type 1 fimbrin D-mannose specific adhesin OS=Escherichia coli (strain K12) OX=83333 GN=fimH PE=1 SV=2
MKRVITLFAVLLMGWSVNAWSFACKTANGTAIPIGGGSANVYVNLAPVVNVGQNLVVDLS
TQIFCHNDYPETITDYVTLQRGSAYGGVLSNFSGTVKYSGSSYPFPTTSETPRVVYNSRT
DKPWPVALYLTPVSSAGGVAIKAGSLIAVLILRQTNNYNSDDFQFVWNIYANNDVVVPTG
GCDVSARDVTVTLPDYPGSVPIPLTVYCAKSQNLGYYLSGTTADAGNSIFTNTASFSPAQ
GVGVQLTRNGTIIPANNTVSLGAVGTSAVSLGLTANYARTGGQVTAGNVQSIIGVTFVYQ

Entry version 162 (08 May 2019)
Sequence version 2 (01 Feb 1995)
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Protein

Type 1 fimbrin D-mannose specific adhesin

Gene

fimH

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed.1 Publication

GO - Molecular functionⁱ

mannose binding
Source: EcoCyc
Inferred from direct assayⁱ
- Ref.7
  "Direct evidence that the FimH protein is the mannose-specific adhesin of Escherichia coli type 1 fimbriae."
  Krogfelt K.A., Bergmans H., Klemm P.
  Infect. Immun. 58:1995-1998(1990) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBCELLULAR LOCATION.

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

View the complete GO annotation on QuickGO ...

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10315-MONOMER ECOL316407:JW4283-MONOMER

BioCycⁱ

EcoCyc:EG10315-MONOMER
ECOL316407:JW4283-MONOMER

Protein family/group databases

UniLectinⁱ	P08191

UniLectinⁱ

P08191

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Type 1 fimbrin D-mannose specific adhesin Alternative name(s): Protein FimH
Gene namesⁱ	Name:fimH Ordered Locus Names:b4320, JW4283
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	EG10315 fimH

EcoGeneⁱ

EG10315 fimH

Subcellular locationⁱ

Fimbrium
1 Publication
Manual assertion based on experiment inⁱ
- Ref.7
  "Direct evidence that the FimH protein is the mannose-specific adhesin of Escherichia coli type 1 fimbriae."
  Krogfelt K.A., Bergmans H., Klemm P.
  Infect. Immun. 58:1995-1998(1990) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBCELLULAR LOCATION.

GO - Cellular componentⁱ

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Fimbrium

Pathology & Biotechⁱ

Chemistry databases

ChEMBLⁱ	CHEMBL3124740

ChEMBLⁱ

CHEMBL3124740

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 21	1 PublicationAdd BLAST		21
ChainⁱPRO_0000009211	22 – 300	Type 1 fimbrin D-mannose specific adhesinAdd BLAST		279

Proteomic databases

PaxDbⁱ	P08191
PRIDEⁱ	P08191

Interactionⁱ

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
fimC	P31697	11	EBI-1028015,EBI-1028005
UPK1A	O00322	2	EBI-1028015,EBI-14031976	From Homo sapiens.

Protein-protein interaction databases

BioGridⁱ	4262737, 8 interactors
ComplexPortalⁱ	CPX-2855 Fimbrial Tip Complex FimFGH
Database of interacting proteins More...DIPⁱ	DIP-9616N
IntActⁱ	P08191, 3 interactors
STRINGⁱ	511145.b4320

Chemistry databases

BindingDBⁱ

P08191

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	23 – 26	Combined sources	4
Beta strandⁱ	37 – 43	Combined sources	7
Beta strandⁱ	48 – 50	Combined sources	3
Beta strandⁱ	55 – 58	Combined sources	4
Helixⁱ	59 – 61	Combined sources	3
Beta strandⁱ	63 – 66	Combined sources	4
Turnⁱ	70 – 72	Combined sources	3
Beta strandⁱ	75 – 84	Combined sources	10
Helixⁱ	86 – 91	Combined sources	6
Beta strandⁱ	92 – 98	Combined sources	7
Beta strandⁱ	101 – 106	Combined sources	6
Beta strandⁱ	114 – 116	Combined sources	3
Beta strandⁱ	118 – 120	Combined sources	3
Beta strandⁱ	126 – 132	Combined sources	7
Beta strandⁱ	134 – 136	Combined sources	3
Beta strandⁱ	138 – 141	Combined sources	4
Beta strandⁱ	146 – 159	Combined sources	14
Beta strandⁱ	163 – 173	Combined sources	11
Beta strandⁱ	175 – 177	Combined sources	3
Beta strandⁱ	180 – 185	Combined sources	6
Beta strandⁱ	187 – 192	Combined sources	6
Beta strandⁱ	195 – 197	Combined sources	3
Beta strandⁱ	200 – 202	Combined sources	3
Beta strandⁱ	205 – 210	Combined sources	6
Beta strandⁱ	212 – 220	Combined sources	9
Beta strandⁱ	222 – 224	Combined sources	3
Beta strandⁱ	235 – 238	Combined sources	4
Beta strandⁱ	240 – 248	Combined sources	9
Beta strandⁱ	259 – 264	Combined sources	6
Beta strandⁱ	273 – 279	Combined sources	7
Beta strandⁱ	281 – 283	Combined sources	3
Beta strandⁱ	286 – 299	Combined sources	14

Show more details

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
	1KIU	X-ray	3.00	B/D/F/H/J/L/N/P	22-300	[»]
	1KLF	X-ray	2.79	B/D/F/H/J/L/N/P	22-300	[»]
	1QUN	X-ray	2.80	B/D/F/H/J/L/N/P	22-300	[»]
	1TR7	X-ray	2.10	A/B	22-179	[»]
	1UWF	X-ray	1.69	A	22-179	[»]
	1ZE3	X-ray	1.84	H	179-300	[»]
	2VCO	X-ray	2.10	A/B	22-179	[»]
	3RFZ	X-ray	2.80	A/D	22-300	[»]
	3ZL1	X-ray	1.55	A/B	22-179	[»]
	3ZL2	X-ray	1.25	A	22-179	[»]
	4ATT	X-ray	1.25	A	22-179	[»]
	4AUJ	X-ray	1.53	A	22-179	[»]
	4AUU	X-ray	1.60	A/B	22-179	[»]
	4AUY	X-ray	2.10	A/B	22-179	[»]
	4AV0	X-ray	2.10	A/B	22-179	[»]
	4AV4	X-ray	1.90	A	22-179	[»]
	4AV5	X-ray	1.40	A/B/C/D	22-179	[»]
	4AVH	X-ray	2.10	A/B	22-179	[»]
	4AVI	X-ray	2.40	A/B	22-179	[»]
	4AVJ	X-ray	2.10	A/B	22-179	[»]
	4AVK	X-ray	2.40	A/B	22-179	[»]
	4CSS	X-ray	1.07	A	22-180	[»]
	4CST	X-ray	1.10	A	22-180	[»]
	4J3O	X-ray	3.80	H	22-300	[»]
	4LOV	X-ray	1.50	A	22-179	[»]
	4X50	X-ray	2.00	A/B	22-180	[»]
	4X5P	X-ray	1.00	A	22-180	[»]
	4X5Q	X-ray	1.12	A	22-180	[»]
	4X5R	X-ray	1.65	A/B/C	22-180	[»]
	4XO8	X-ray	1.70	A/B	22-179	[»]
	4XO9	X-ray	1.14	A	22-300	[»]
	4XOA	X-ray	2.54	A/C/E/G	22-300	[»]
	4XOB	X-ray	3.00	A/C/E/G	22-300	[»]
	4XOD	X-ray	1.14	A	22-300	[»]
	5AB1	X-ray	1.96	A/B	1-300	[»]
	5ABZ	X-ray	2.40	A/B	22-179	[»]
	5CGB	X-ray	1.60	A/B	22-179	[»]
	5F2F	X-ray	1.67	A	22-179	[»]
	5F3F	X-ray	1.76	A	22-179	[»]
	5FS5	X-ray	1.42	A	22-179	[»]
	5FWR	X-ray	2.13	A/B/C/D/E/F/G/H	22-179	[»]
	5FX3	X-ray	1.90	A	22-179	[»]
	5JCQ	X-ray	1.60	A/B	22-179	[»]
	5JCR	X-ray	1.70	A/B	22-179	[»]
	5L4T	X-ray	1.90	A/B	22-179	[»]
	5L4U	X-ray	2.10	A/B	22-179	[»]
	5L4V	X-ray	2.99	A/B/C	22-179	[»]
	5L4W	X-ray	1.90	A/B/C	22-179	[»]
	5L4X	X-ray	1.90	A/B	22-179	[»]
	5L4Y	X-ray	1.90	A/B	22-179	[»]
	5MCA	X-ray	1.60	A	22-180	[»]
	5MTS	X-ray	2.60	A/B	1-300	[»]
	5MUC	X-ray	2.60	A/B	22-179	[»]
	6E14	electron microscopy	4.00	H	1-300	[»]
	6E15	electron microscopy	6.20	H	1-300	[»]
	6GTX	X-ray	2.50	A/B/C/D	22-179	[»]
	6GTY	X-ray	1.90	A/B/C/D/E	22-179	[»]
SMRⁱ	P08191
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P08191

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the fimbrial protein family.Curated

Keywords - Domainⁱ

Signal

Phylogenomic databases

eggNOGⁱ	ENOG410643X Bacteria ENOG410Y3E1 LUCA
HOGENOMⁱ	HOG000120719
KEGG Orthology (KO) More...KOⁱ	K07350

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd10466 FimH_man-bind, 1 hit
Gene3Dⁱ	2.60.40.1090, 2 hits
InterProⁱ	View protein in InterPro IPR000259 Adhesion_dom_fimbrial IPR036937 Adhesion_dom_fimbrial_sf IPR008966 Adhesion_dom_sf IPR015243 FimH_man-bd
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00419 Fimbrial, 1 hit PF09160 FimH_man-bind, 1 hit
SUPFAMⁱ	SSF49401 SSF49401, 2 hits

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P08191-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MKRVITLFAV LLMGWSVNAW SFACKTANGT AIPIGGGSAN VYVNLAPVVN 
        60         70         80         90        100
VGQNLVVDLS TQIFCHNDYP ETITDYVTLQ RGSAYGGVLS NFSGTVKYSG 
       110        120        130        140        150
SSYPFPTTSE TPRVVYNSRT DKPWPVALYL TPVSSAGGVA IKAGSLIAVL 
       160        170        180        190        200
ILRQTNNYNS DDFQFVWNIY ANNDVVVPTG GCDVSARDVT VTLPDYPGSV 
       210        220        230        240        250
PIPLTVYCAK SQNLGYYLSG TTADAGNSIF TNTASFSPAQ GVGVQLTRNG 
       260        270        280        290        300
TIIPANNTVS LGAVGTSAVS LGLTANYART GGQVTAGNVQ SIIGVTFVYQ

Length:300

Mass (Da):31,473

Last modified:February 1, 1995 - v2

Checksum:ⁱ939204A51658747D

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	79	L → R no nucleotide entry (PubMed:7905476).Curated	1
Sequence conflictⁱ	197	P → R in CAA29156 (PubMed:2890081).Curated	1
Sequence conflictⁱ	222	T → H in CAA29156 (PubMed:2890081).Curated	1
Sequence conflictⁱ	222	T → H no nucleotide entry (PubMed:7905476).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X05672 Genomic DNA Translation: CAA29156.1 U14003 Genomic DNA Translation: AAA97216.1 U00096 Genomic DNA Translation: AAC77276.1 AP009048 Genomic DNA Translation: BAE78313.1
PIRⁱ	S56545
NCBI Reference Sequences More...RefSeqⁱ	NP_418740.1, NC_000913.3 WP_000832247.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC77276; AAC77276; b4320 BAE78313; BAE78313; BAE78313
GeneIDⁱ	948847
KEGGⁱ	ecj:JW4283 eco:b4320
PATRICⁱ	fig\|1411691.4.peg.2372

Protein	Similar proteins		Species	Score	Length	Source
P08191	Protein FimH		ECOLX		303	UniRef100_P08191
Protein FimH		Escherichia coli MS 115-1		303
Protein FimH		Escherichia coli 113290		303
Protein FimH		Escherichia coli 907713		303
Protein FimH		Escherichia coli MS 198-1		303
+13

Protein	Similar proteins		Species	Score	Length	Source
P08191	Protein FimH		ECOLX		303	UniRef90_P08191
Protein FimH		Escherichia coli MS 115-1		303
Protein FimH		Escherichia coli 113290		303
Protein FimH		Escherichia coli 907713		303
Protein FimH		Escherichia coli MS 198-1		303
+938

Protein	Similar proteins		Species	Score	Length	Source
P08191	Protein FimH		ECOLX		303	UniRef50_P08191
Protein FimH		Escherichia coli MS 115-1		303
Protein FimH		Escherichia coli 113290		303
Protein FimH		Escherichia coli 907713		303
Protein FimH		Escherichia coli MS 198-1		303
+967

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X05672 Genomic DNA Translation: CAA29156.1 U14003 Genomic DNA Translation: AAA97216.1 U00096 Genomic DNA Translation: AAC77276.1 AP009048 Genomic DNA Translation: BAE78313.1
PIRⁱ	S56545
RefSeqⁱ	NP_418740.1, NC_000913.3 WP_000832247.1, NZ_LN832404.1

3D structure databases

Select the link destinations: PDBeⁱ RCSB PDBⁱ PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1KIU	X-ray	3.00	B/D/F/H/J/L/N/P	22-300	[»]
	1KLF	X-ray	2.79	B/D/F/H/J/L/N/P	22-300	[»]
	1QUN	X-ray	2.80	B/D/F/H/J/L/N/P	22-300	[»]
	1TR7	X-ray	2.10	A/B	22-179	[»]
	1UWF	X-ray	1.69	A	22-179	[»]
	1ZE3	X-ray	1.84	H	179-300	[»]
	2VCO	X-ray	2.10	A/B	22-179	[»]
	3RFZ	X-ray	2.80	A/D	22-300	[»]
	3ZL1	X-ray	1.55	A/B	22-179	[»]
	3ZL2	X-ray	1.25	A	22-179	[»]
	4ATT	X-ray	1.25	A	22-179	[»]
	4AUJ	X-ray	1.53	A	22-179	[»]
	4AUU	X-ray	1.60	A/B	22-179	[»]
	4AUY	X-ray	2.10	A/B	22-179	[»]
	4AV0	X-ray	2.10	A/B	22-179	[»]
	4AV4	X-ray	1.90	A	22-179	[»]
	4AV5	X-ray	1.40	A/B/C/D	22-179	[»]
	4AVH	X-ray	2.10	A/B	22-179	[»]
	4AVI	X-ray	2.40	A/B	22-179	[»]
	4AVJ	X-ray	2.10	A/B	22-179	[»]
	4AVK	X-ray	2.40	A/B	22-179	[»]
	4CSS	X-ray	1.07	A	22-180	[»]
	4CST	X-ray	1.10	A	22-180	[»]
	4J3O	X-ray	3.80	H	22-300	[»]
	4LOV	X-ray	1.50	A	22-179	[»]
	4X50	X-ray	2.00	A/B	22-180	[»]
	4X5P	X-ray	1.00	A	22-180	[»]
	4X5Q	X-ray	1.12	A	22-180	[»]
	4X5R	X-ray	1.65	A/B/C	22-180	[»]
	4XO8	X-ray	1.70	A/B	22-179	[»]
	4XO9	X-ray	1.14	A	22-300	[»]
	4XOA	X-ray	2.54	A/C/E/G	22-300	[»]
	4XOB	X-ray	3.00	A/C/E/G	22-300	[»]
	4XOD	X-ray	1.14	A	22-300	[»]
	5AB1	X-ray	1.96	A/B	1-300	[»]
	5ABZ	X-ray	2.40	A/B	22-179	[»]
	5CGB	X-ray	1.60	A/B	22-179	[»]
	5F2F	X-ray	1.67	A	22-179	[»]
	5F3F	X-ray	1.76	A	22-179	[»]
	5FS5	X-ray	1.42	A	22-179	[»]
	5FWR	X-ray	2.13	A/B/C/D/E/F/G/H	22-179	[»]
	5FX3	X-ray	1.90	A	22-179	[»]
	5JCQ	X-ray	1.60	A/B	22-179	[»]
	5JCR	X-ray	1.70	A/B	22-179	[»]
	5L4T	X-ray	1.90	A/B	22-179	[»]
	5L4U	X-ray	2.10	A/B	22-179	[»]
	5L4V	X-ray	2.99	A/B/C	22-179	[»]
	5L4W	X-ray	1.90	A/B/C	22-179	[»]
	5L4X	X-ray	1.90	A/B	22-179	[»]
	5L4Y	X-ray	1.90	A/B	22-179	[»]
	5MCA	X-ray	1.60	A	22-180	[»]
	5MTS	X-ray	2.60	A/B	1-300	[»]
	5MUC	X-ray	2.60	A/B	22-179	[»]
	6E14	electron microscopy	4.00	H	1-300	[»]
	6E15	electron microscopy	6.20	H	1-300	[»]
	6GTX	X-ray	2.50	A/B/C/D	22-179	[»]
	6GTY	X-ray	1.90	A/B/C/D/E	22-179	[»]
SMRⁱ	P08191
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4262737, 8 interactors
ComplexPortalⁱ	CPX-2855 Fimbrial Tip Complex FimFGH
DIPⁱ	DIP-9616N
IntActⁱ	P08191, 3 interactors
STRINGⁱ	511145.b4320

Chemistry databases

BindingDBⁱ	P08191
ChEMBLⁱ	CHEMBL3124740

Protein family/group databases

UniLectinⁱ	P08191

UniLectinⁱ

P08191

Proteomic databases

PaxDbⁱ	P08191
PRIDEⁱ	P08191

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC77276; AAC77276; b4320 BAE78313; BAE78313; BAE78313
GeneIDⁱ	948847
KEGGⁱ	ecj:JW4283 eco:b4320
PATRICⁱ	fig\|1411691.4.peg.2372

Organism-specific databases

EchoBASEⁱ	EB0311
EcoGeneⁱ	EG10315 fimH

Phylogenomic databases

eggNOGⁱ	ENOG410643X Bacteria ENOG410Y3E1 LUCA
HOGENOMⁱ	HOG000120719
KOⁱ	K07350

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10315-MONOMER ECOL316407:JW4283-MONOMER

BioCycⁱ

EcoCyc:EG10315-MONOMER
ECOL316407:JW4283-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P08191
Protein Ontology More...PROⁱ	PR:P08191

Family and domain databases

CDDⁱ	cd10466 FimH_man-bind, 1 hit
Gene3Dⁱ	2.60.40.1090, 2 hits
InterProⁱ	View protein in InterPro IPR000259 Adhesion_dom_fimbrial IPR036937 Adhesion_dom_fimbrial_sf IPR008966 Adhesion_dom_sf IPR015243 FimH_man-bd
Pfamⁱ	View protein in Pfam PF00419 Fimbrial, 1 hit PF09160 FimH_man-bind, 1 hit
SUPFAMⁱ	SSF49401 SSF49401, 2 hits
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	FIMH_ECOLI
Accessionⁱ	P08191Primary (citable) accession number: P08191 Secondary accession number(s): Q2M5Z3
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
	Last sequence update:	February 1, 1995
	Last modified:	May 8, 2019
	This is version 162 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
SIMILARITY comments
Index of protein domains and families
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P08191 (FIMH_ECOLI)

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Type 1 fimbrin D-mannose specific adhesin

fimH

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

<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

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

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

<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

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

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

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ