UniProtKB - P08622 (DNAJ_ECOLI)

BLAST

>sp|P08622|DNAJ_ECOLI Chaperone protein DnaJ OS=Escherichia coli (strain K12) OX=83333 GN=dnaJ PE=1 SV=3
MAKQDYYEILGVSKTAEEREIRKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDS
QKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYN
MELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQ
QTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAP
AGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTG
KLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNERQKQLLQELQESFGGPTGEHNSPRS
KSFFDGVKKFFDDLTR

Align
Format
Add to basket Added to basket
History
Entry version 194 (07 Nov 2018)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
Other tutorials and videos
Help video
Feedback

Protein

Chaperone protein DnaJ

Gene

dnaJ

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Interacts with DnaK and GrpE to disassemble a protein complex at the origins of replication of phage lambda and several plasmids. Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.4 Publications

Cofactorⁱ

Zn²⁺Note: Binds 2 Zn²⁺ ions per monomer.

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	144	Zinc 1	1
Metal bindingⁱ	147	Zinc 1	1
Metal bindingⁱ	161	Zinc 2	1
Metal bindingⁱ	164	Zinc 2	1
Metal bindingⁱ	183	Zinc 2	1
Metal bindingⁱ	186	Zinc 2	1
Metal bindingⁱ	197	Zinc 1	1
Metal bindingⁱ	200	Zinc 1	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	131 – 209	CR-typeAdd BLAST		79

GO - Molecular functionⁱ

ATP binding Source: InterPro
chaperone binding
Source: CAFA
Inferred from physical interactionⁱ
- 9103205
heat shock protein binding Source: InterPro
protein disulfide isomerase activity
Source: EcoliWiki
Inferred from direct assayⁱ
- 7559385
protein disulfide oxidoreductase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 11732919
sigma factor antagonist activity
Source: EcoCyc
Inferred from direct assayⁱ
- 8599944
unfolded protein binding
Source: CAFA
Inferred from direct assayⁱ
- 9103205
zinc ion binding
Source: EcoliWiki
Inferred from direct assayⁱ
- 11985624
- 8662861

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

chaperone cofactor-dependent protein refolding
Source: CAFA
Inferred from direct assayⁱ
- 9103205
DNA replication
Source: EcoliWiki
Inferred from mutant phenotypeⁱ
- 2144273
protein-containing complex assembly
Source: CAFA
Inferred from direct assayⁱ
- 9103205
protein folding
Source: EcoliWiki
Inferred from direct assayⁱ
- 7559385
protein refolding
Source: EcoliWiki
Inferred from direct assayⁱ
- 7559385
response to heat
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 2144273
viral process
Source: EcoCyc
Inferred from direct assayⁱ
- 1361234
- 3889001

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Chaperone
Biological process	DNA replication, Stress response
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10240-MONOMER MetaCyc:EG10240-MONOMER

BioCycⁱ

EcoCyc:EG10240-MONOMER
MetaCyc:EG10240-MONOMER

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Chaperone protein DnaJ Alternative name(s): HSP40 Heat shock protein J
Gene namesⁱ	Name:dnaJ Synonyms:groP Ordered Locus Names:b0015, JW0014
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	EG10240 dnaJ

EcoGeneⁱ

EG10240 dnaJ

Subcellular locationⁱ

Cytoplasm

GO - Cellular componentⁱ

cytoplasm
Source: EcoliWiki
Inferred from direct assayⁱ
- 6220698
cytosol
Source: EcoCyc
Inferred from direct assayⁱ
- 6220698
membrane
Source: EcoliWiki
Inferred from direct assayⁱ
- 3889001
- 6220698
protein-containing complex
Source: CAFA
Inferred from direct assayⁱ
- 9103205

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Disruption phenotypeⁱ

Single dnaJ and double dnaK-dnaJ disruption are non-essential; synthetic lethality is seen in a triple tig-dnaK-dnaJ disruption, although this depends on temperature (triple disruptions grow slowly at 20 and 34 degrees Celsius but not at 43 degrees) and strain background.1 Publication

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	19 – 20	RE → AA: No effect.	2
Mutagenesisⁱ	25	Y → A: Loss of activity.	1
Mutagenesisⁱ	26	K → A: Loss of activity.	1
Mutagenesisⁱ	27	R → A: No effect.	1
Mutagenesisⁱ	28	L → A: No effect.	1
Mutagenesisⁱ	29	A → G: No effect.	1
Mutagenesisⁱ	30 – 31	MK → AA: No effect.	2
Mutagenesisⁱ	32	Y → A: No effect.	1
Mutagenesisⁱ	33	H → Q: Loss of ability to stimulate DnaK ATPase activity. 1 Publication	1
Mutagenesisⁱ	34	P → F: Loss of function.	1
Mutagenesisⁱ	35	D → N: Loss of ability to bind DnaK. 1 Publication	1
Mutagenesisⁱ	36	R → A: Decrease in chaperone function.	1
Mutagenesisⁱ	37	N → A: Decrease in chaperone function.	1
Mutagenesisⁱ	38	Q → A: No effect.	1
Mutagenesisⁱ	41 – 42	KE → AA: No effect.	2
Mutagenesisⁱ	44	E → A: No effect. 1 Publication	1
Mutagenesisⁱ	46	K → A: No effect.	1
Mutagenesisⁱ	47	F → A: Loss of function.	1
Mutagenesisⁱ	48 – 49	KE → AA: No effect.	2
Mutagenesisⁱ	51 – 52	KE → AA: No effect.	2
Mutagenesisⁱ	54	Y → A: No effect. 1 Publication	1
Mutagenesisⁱ	55	E → A: No effect. 1 Publication	1
Mutagenesisⁱ	58 – 59	TD → AA: No effect.	2
Mutagenesisⁱ	60 – 61	SQ → AA: No effect.	2
Mutagenesisⁱ	62 – 63	KR → AA: No effect.	2
Mutagenesisⁱ	67 – 68	DQ → AA: No effect.	2
Mutagenesisⁱ	144	C → S: Loss of DnaK-independent chaperone activity; when associated with S-147; S-197 and S-200. 1 Publication	1
Mutagenesisⁱ	147	C → S: Loss of DnaK-independent chaperone activity; when associated with S-144; S-197 and S-200. 1 Publication	1
Mutagenesisⁱ	161	C → H: No effect on chaperone function; when associated with H-183. 2 Publications	1
Mutagenesisⁱ	161	C → S: Loss of function; when associated with S-164; S-183 and S-186. 2 Publications	1
Mutagenesisⁱ	164	C → H: No effect on chaperone function; when associated with H-183. 2 Publications	1
Mutagenesisⁱ	164	C → S: Loss of function; when associated with S-161; S-183 and S-186. 2 Publications	1
Mutagenesisⁱ	183	C → H: No effect on chaperone function. Same effect; when associated with H-161 or H-164. 2 Publications	1
Mutagenesisⁱ	183	C → S: Loss of function; when associated with S-161; S-164 and S-186. 2 Publications	1
Mutagenesisⁱ	186	C → H: No effect on chaperone function. 2 Publications	1
Mutagenesisⁱ	186	C → S: Loss of function; when associated with S-161; S-164 and S-184. 2 Publications	1
Mutagenesisⁱ	197	C → S: Loss of DnaK-independent chaperone activity; when associated with S-144; S-147 and S-200. 1 Publication	1
Mutagenesisⁱ	200	C → S: Loss of DnaK-independent chaperone activity; when associated with S-144; S-147 and S-197. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed1 Publication
ChainⁱPRO_0000070777	2 – 376	Chaperone protein DnaJAdd BLAST		375

Proteomic databases

EPDⁱ	P08622
PaxDbⁱ	P08622
PRIDEⁱ	P08622

Expressionⁱ

Inductionⁱ

By heat shock under the control of the HtpR regulatory protein.

Interactionⁱ

Subunit structureⁱ

Homodimer.

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
dnaK	P0A6Y8	8	EBI-545285,EBI-542092
malT	P06993	5	EBI-545285,EBI-542934

GO - Molecular functionⁱ

chaperone binding
Source: CAFA
Inferred from physical interactionⁱ
- 9103205
heat shock protein binding Source: InterPro
unfolded protein binding
Source: CAFA
Inferred from direct assayⁱ
- 9103205

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	4259725, 278 interactors 849156, 2 interactors
Database of interacting proteins More...DIPⁱ	DIP-9460N
IntActⁱ	P08622, 101 interactors
Molecular INTeraction database More...MINTⁱ	P08622
STRINGⁱ	316385.ECDH10B_0015

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	6 – 10	Combined sources	5
Beta strandⁱ	13 – 15	Combined sources	3
Helixⁱ	18 – 32	Combined sources	15
Helixⁱ	34 – 37	Combined sources	4
Turnⁱ	38 – 40	Combined sources	3
Helixⁱ	41 – 58	Combined sources	18
Helixⁱ	60 – 64	Combined sources	5
Turnⁱ	66 – 68	Combined sources	3
Turnⁱ	70 – 72	Combined sources	3
Turnⁱ	132 – 134	Combined sources	3
Beta strandⁱ	141 – 143	Combined sources	3
Helixⁱ	145 – 147	Combined sources	3
Turnⁱ	148 – 150	Combined sources	3
Beta strandⁱ	154 – 156	Combined sources	3
Turnⁱ	162 – 166	Combined sources	5
Beta strandⁱ	167 – 174	Combined sources	8
Beta strandⁱ	177 – 182	Combined sources	6
Turnⁱ	184 – 188	Combined sources	5
Beta strandⁱ	189 – 192	Combined sources	4
Beta strandⁱ	194 – 196	Combined sources	3
Helixⁱ	198 – 200	Combined sources	3
Beta strandⁱ	203 – 207	Combined sources	5

Show more details

3D structure databases

ProteinModelPortalⁱ	P08622
SMRⁱ	P08622
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P08622

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	3 – 72	JAdd BLAST	70
Repeatⁱ	144 – 151	CXXCXGXG motif	8
Repeatⁱ	161 – 168	CXXCXGXG motif	8
Repeatⁱ	183 – 190	CXXCXGXG motif	8
Repeatⁱ	197 – 204	CXXCXGXG motif	8

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	77 – 114	Gly-richAdd BLAST		38

Domainⁱ

The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.

Sequence similaritiesⁱ

Belongs to the DnaJ family.Curated

Zinc finger

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	131 – 209	CR-typeAdd BLAST		79

Keywords - Domainⁱ

Repeat, Zinc-finger

Phylogenomic databases

eggNOGⁱ	ENOG4105BZ5 Bacteria COG0484 LUCA
HOGENOMⁱ	HOG000226717
InParanoidⁱ	P08622
KEGG Orthology (KO) More...KOⁱ	K03686
PhylomeDBⁱ	P08622

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd06257 DnaJ, 1 hit cd10719 DnaJ_zf, 1 hit
Gene3Dⁱ	1.10.287.110, 1 hit
HAMAPⁱ	MF_01152 DnaJ, 1 hit
InterProⁱ	View protein in InterPro IPR012724 DnaJ IPR002939 DnaJ_C IPR001623 DnaJ_domain IPR018253 DnaJ_domain_CS IPR008971 HSP40/DnaJ_pept-bd IPR001305 HSP_DnaJ_Cys-rich_dom IPR036410 HSP_DnaJ_Cys-rich_dom_sf IPR036869 J_dom_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00226 DnaJ, 1 hit PF01556 DnaJ_C, 1 hit PF00684 DnaJ_CXXCXGXG, 1 hit
PRINTSⁱ	PR00625 JDOMAIN
SMARTⁱ	View protein in SMART SM00271 DnaJ, 1 hit
SUPFAMⁱ	SSF46565 SSF46565, 1 hit SSF49493 SSF49493, 2 hits SSF57938 SSF57938, 1 hit
TIGRFAMsⁱ	TIGR02349 DnaJ_bact, 1 hit
PROSITEⁱ	View protein in PROSITE PS00636 DNAJ_1, 1 hit PS50076 DNAJ_2, 1 hit PS51188 ZF_CR, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P08622-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MAKQDYYEIL GVSKTAEERE IRKAYKRLAM KYHPDRNQGD KEAEAKFKEI 
        60         70         80         90        100
KEAYEVLTDS QKRAAYDQYG HAAFEQGGMG GGGFGGGADF SDIFGDVFGD 
       110        120        130        140        150
IFGGGRGRQR AARGADLRYN MELTLEEAVR GVTKEIRIPT LEECDVCHGS 
       160        170        180        190        200
GAKPGTQPQT CPTCHGSGQV QMRQGFFAVQ QTCPHCQGRG TLIKDPCNKC 
       210        220        230        240        250
HGHGRVERSK TLSVKIPAGV DTGDRIRLAG EGEAGEHGAP AGDLYVQVQV 
       260        270        280        290        300
KQHPIFEREG NNLYCEVPIN FAMAALGGEI EVPTLDGRVK LKVPGETQTG 
       310        320        330        340        350
KLFRMRGKGV KSVRGGAQGD LLCRVVVETP VGLNERQKQL LQELQESFGG 
       360        370 
PTGEHNSPRS KSFFDGVKKF FDDLTR

Length:376

Mass (Da):41,100

Last modified:January 23, 2007 - v3

Checksum:ⁱ05FA762EF9844532

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M12544 Genomic DNA Translation: AAA00009.1 M12565 Genomic DNA Translation: AAA23693.1 U00096 Genomic DNA Translation: AAC73126.1 AP009048 Genomic DNA Translation: BAB96590.1
PIRⁱ	A92572 HHECDJ
NCBI Reference Sequences More...RefSeqⁱ	NP_414556.1, NC_000913.3 WP_001118476.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC73126; AAC73126; b0015 BAB96590; BAB96590; BAB96590
GeneIDⁱ	944753
KEGGⁱ	ecj:JW0014 eco:b0015
PATRICⁱ	fig\|1411691.4.peg.2269

Protein	Similar proteins		Species	Score	Length	Source
P08622	Chaperone protein DnaJ		ECODH		376	UniRef100_B1XBE0
Chaperone protein DnaJ		ECOLX		386
Molecular chaperone DnaJ		Shigella sp.		376
Chaperone protein DnaJ		KLEOX		376
Chaperone protein DnaJ		Achromobacter sp.		376
+5

Protein	Similar proteins		Species	Score	Length	Source
P08622	Chaperone protein DnaJ		SHIFL		376	UniRef90_Q7UDU1
Chaperone protein DnaJ		CROS8		379
Chaperone protein DnaJ		ECODH		376
Chaperone protein DnaJ		ECO24		376
Chaperone protein DnaJ		ECO27		376
+322

Protein	Similar proteins		Species	Score	Length	Source
P08622	Chaperone protein DnaJ		SHIFL		376	UniRef50_Q7UDU1
Chaperone protein DnaJ		CROS8		379
Chaperone protein DnaJ		SHIF8		376
Chaperone protein DnaJ		ECODH		376
Chaperone protein DnaJ		SHIDS		376
+10212

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M12544 Genomic DNA Translation: AAA00009.1 M12565 Genomic DNA Translation: AAA23693.1 U00096 Genomic DNA Translation: AAC73126.1 AP009048 Genomic DNA Translation: BAB96590.1
PIRⁱ	A92572 HHECDJ
RefSeqⁱ	NP_414556.1, NC_000913.3 WP_001118476.1, 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
	1BQ0	NMR	-	A	2-104	[»]
	1BQZ	NMR	-	A	2-78	[»]
	1EXK	NMR	-	A	131-209	[»]
	1XBL	NMR	-	A	2-108	[»]
	5NRO	X-ray	3.25	B	1-105	[»]
ProteinModelPortalⁱ	P08622
SMRⁱ	P08622
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4259725, 278 interactors 849156, 2 interactors
DIPⁱ	DIP-9460N
IntActⁱ	P08622, 101 interactors
MINTⁱ	P08622
STRINGⁱ	316385.ECDH10B_0015

Proteomic databases

EPDⁱ	P08622
PaxDbⁱ	P08622
PRIDEⁱ	P08622

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC73126; AAC73126; b0015 BAB96590; BAB96590; BAB96590
GeneIDⁱ	944753
KEGGⁱ	ecj:JW0014 eco:b0015
PATRICⁱ	fig\|1411691.4.peg.2269

Organism-specific databases

EchoBASEⁱ	EB0236
EcoGeneⁱ	EG10240 dnaJ

Phylogenomic databases

eggNOGⁱ	ENOG4105BZ5 Bacteria COG0484 LUCA
HOGENOMⁱ	HOG000226717
InParanoidⁱ	P08622
KOⁱ	K03686
PhylomeDBⁱ	P08622

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10240-MONOMER MetaCyc:EG10240-MONOMER

BioCycⁱ

EcoCyc:EG10240-MONOMER
MetaCyc:EG10240-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P08622
Protein Ontology More...PROⁱ	PR:P08622

Family and domain databases

CDDⁱ	cd06257 DnaJ, 1 hit cd10719 DnaJ_zf, 1 hit
Gene3Dⁱ	1.10.287.110, 1 hit
HAMAPⁱ	MF_01152 DnaJ, 1 hit
InterProⁱ	View protein in InterPro IPR012724 DnaJ IPR002939 DnaJ_C IPR001623 DnaJ_domain IPR018253 DnaJ_domain_CS IPR008971 HSP40/DnaJ_pept-bd IPR001305 HSP_DnaJ_Cys-rich_dom IPR036410 HSP_DnaJ_Cys-rich_dom_sf IPR036869 J_dom_sf
Pfamⁱ	View protein in Pfam PF00226 DnaJ, 1 hit PF01556 DnaJ_C, 1 hit PF00684 DnaJ_CXXCXGXG, 1 hit
PRINTSⁱ	PR00625 JDOMAIN
SMARTⁱ	View protein in SMART SM00271 DnaJ, 1 hit
SUPFAMⁱ	SSF46565 SSF46565, 1 hit SSF49493 SSF49493, 2 hits SSF57938 SSF57938, 1 hit
TIGRFAMsⁱ	TIGR02349 DnaJ_bact, 1 hit
PROSITEⁱ	View protein in PROSITE PS00636 DNAJ_1, 1 hit PS50076 DNAJ_2, 1 hit PS51188 ZF_CR, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	DNAJ_ECOLI
Accessionⁱ	P08622Primary (citable) accession number: P08622
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
	Last sequence update:	January 23, 2007
	Last modified:	November 7, 2018
	This is version 194 of the entry and version 3 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

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P08622 (DNAJ_ECOLI)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Chaperone protein DnaJ

dnaJ

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

<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

Proteomic databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<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

<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

Compositional bias

<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

Zinc finger

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

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

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ