UniProtKB - P17169 (GLMS_ECOLI)

BLAST

>sp|P17169|GLMS_ECOLI Glutamine--fructose-6-phosphate aminotransferase [isomerizing] OS=Escherichia coli (strain K12) OX=83333 GN=glmS PE=1 SV=4
MCGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDAEGHMTRLRRLGKVQMLAQAAE
EHPLHGGTGIAHTRWATHGEPSEVNAHPHVSEHIVVVHNGIIENHEPLREELKARGYTFV
SETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYGTVIMDSRHPDTLLAARSGSPLV
IGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIFDKTGAEVKRQDIESNLQ
YDAGDKGIYRHYMQKEIYEQPNAIKNTLTGRISHGQVDLSELGPNADELLSKVEHIQILA
CGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGL
RLSKELGYLGSLAICNVPGSSLVRESDLALMTNAGTEIGVASTKAFTTQLTVLLMLVAKL
SRLKGLDASIEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQYPIA
LEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRAR
GGQLYVFADQDAGFVSSDNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPR
NLAKSVTVE

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History
Entry version 183 (10 Oct 2018)
Sequence version 4 (23 Jan 2007)
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Protein

Glutamine--fructose-6-phosphate aminotransferase [isomerizing]

Gene

glmS

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.

Catalytic activityⁱ

L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate.

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Active siteⁱ	2	Nucleophile; for GATase activityBy similarity		1
Active siteⁱ	604	For Fru-6P isomerization activity		1

GO - Molecular functionⁱ

carbohydrate derivative binding Source: InterPro
glutamine-fructose-6-phosphate transaminase (isomerizing) activity
Source: EcoCyc
Inferred from direct assayⁱ
- 3297136

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

carbohydrate metabolic process Source: UniProtKB-UniRule
fructose 6-phosphate metabolic process Source: GO_Central
glutamine metabolic process Source: UniProtKB-KW
protein N-linked glycosylation Source: GO_Central
UDP-N-acetylglucosamine biosynthetic process
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 5541523

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Aminotransferase, Transferase

Molecular function

Aminotransferase, Transferase

Enzyme and pathway databases

BioCycⁱ	EcoCyc:L-GLN-FRUCT-6-P-AMINOTRANS-MONOMER MetaCyc:L-GLN-FRUCT-6-P-AMINOTRANS-MONOMER
BRENDAⁱ	2.6.1.16 2026

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Glutamine--fructose-6-phosphate aminotransferase [isomerizing] (EC:2.6.1.16) Alternative name(s): D-fructose-6-phosphate amidotransferase GFAT Glucosamine-6-phosphate synthase Hexosephosphate aminotransferase L-glutamine--D-fructose-6-phosphate amidotransferase
Gene namesⁱ	Name:glmS Ordered Locus Names:b3729, JW3707
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	EG10382 glmS

EcoGeneⁱ

EG10382 glmS

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

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB03814 2-(N-Morpholino)-Ethanesulfonic Acid DB02445 2-Deoxy-2-Amino Glucitol-6-Phosphate DB02007 alpha-D-glucose 6-phosphate DB02657 Glucosamine 6-Phosphate DB03581 Glucose-6-Phosphate DB02446 Glutamine Hydroxamate

DrugBankⁱ

DB03814 2-(N-Morpholino)-Ethanesulfonic Acid
DB02445 2-Deoxy-2-Amino Glucitol-6-Phosphate
DB02007 alpha-D-glucose 6-phosphate
DB02657 Glucosamine 6-Phosphate
DB03581 Glucose-6-Phosphate
DB02446 Glutamine Hydroxamate

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed
ChainⁱPRO_0000135328	2 – 609	Glutamine--fructose-6-phosphate aminotransferase [isomerizing]Add BLAST		608

Proteomic databases

EPDⁱ	P17169
PaxDbⁱ	P17169
PRIDEⁱ	P17169

Expressionⁱ

Inductionⁱ

Post-transcriptionally regulated by the GlmY/GlmZ sRNA regulatory cascade. The sRNA GlmZ, together with Hfq, directly activates glmS mRNA translation through base-pairing. A second sRNA, GlmY, positively regulates glmS indirectly, by sequestering the adapter protein RapZ and protecting GlmZ from RNA cleavage.3 Publications

Interactionⁱ

Subunit structureⁱ

Homodimer.

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
ispE	P62615	2	EBI-551022,EBI-562202
ynbD	P76093	4	EBI-551022,EBI-551038

Protein-protein interaction databases

BioGridⁱ	4262136, 528 interactors
Database of interacting proteins More...DIPⁱ	DIP-9775N
IntActⁱ	P17169, 8 interactors
STRINGⁱ	316407.85676309

Chemistry databases

BindingDBⁱ

P17169

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	3 – 8	Combined sources	6
Helixⁱ	14 – 24	Combined sources	11
Helixⁱ	25 – 27	Combined sources	3
Beta strandⁱ	30 – 37	Combined sources	8
Beta strandⁱ	43 – 50	Combined sources	8
Helixⁱ	52 – 61	Combined sources	10
Beta strandⁱ	67 – 74	Combined sources	8
Beta strandⁱ	77 – 79	Combined sources	3
Turnⁱ	83 – 85	Combined sources	3
Beta strandⁱ	89 – 91	Combined sources	3
Beta strandⁱ	94 – 102	Combined sources	9
Helixⁱ	105 – 114	Combined sources	10
Helixⁱ	125 – 137	Combined sources	13
Helixⁱ	142 – 149	Combined sources	8
Helixⁱ	150 – 152	Combined sources	3
Beta strandⁱ	155 – 163	Combined sources	9
Beta strandⁱ	170 – 177	Combined sources	8
Beta strandⁱ	180 – 183	Combined sources	4
Beta strandⁱ	188 – 193	Combined sources	6
Helixⁱ	194 – 196	Combined sources	3
Turnⁱ	197 – 200	Combined sources	4
Beta strandⁱ	202 – 206	Combined sources	5
Beta strandⁱ	212 – 215	Combined sources	4
Beta strandⁱ	220 – 223	Combined sources	4
Beta strandⁱ	225 – 227	Combined sources	3
Beta strandⁱ	234 – 236	Combined sources	3
Turnⁱ	241 – 244	Combined sources	4
Helixⁱ	252 – 258	Combined sources	7
Helixⁱ	260 – 268	Combined sources	9
Beta strandⁱ	271 – 273	Combined sources	3
Beta strandⁱ	274 – 277	Combined sources	4
Helixⁱ	280 – 282	Combined sources	3
Helixⁱ	286 – 292	Combined sources	7
Beta strandⁱ	295 – 300	Combined sources	6
Helixⁱ	302 – 318	Combined sources	17
Beta strandⁱ	323 – 327	Combined sources	5
Helixⁱ	328 – 332	Combined sources	5
Beta strandⁱ	342 – 351	Combined sources	10
Helixⁱ	354 – 363	Combined sources	10
Turnⁱ	364 – 367	Combined sources	4
Beta strandⁱ	369 – 377	Combined sources	9
Helixⁱ	381 – 385	Combined sources	5
Beta strandⁱ	386 – 391	Combined sources	6
Beta strandⁱ	399 – 401	Combined sources	3
Helixⁱ	404 – 423	Combined sources	20
Helixⁱ	428 – 448	Combined sources	21
Helixⁱ	449 – 451	Combined sources	3
Helixⁱ	454 – 462	Combined sources	9
Beta strandⁱ	466 – 472	Combined sources	7
Helixⁱ	474 – 476	Combined sources	3
Helixⁱ	477 – 491	Combined sources	15
Beta strandⁱ	494 – 499	Combined sources	6
Helixⁱ	500 – 505	Combined sources	6
Helixⁱ	507 – 510	Combined sources	4
Beta strandⁱ	517 – 521	Combined sources	5
Helixⁱ	524 – 536	Combined sources	13
Helixⁱ	537 – 540	Combined sources	4
Beta strandⁱ	544 – 549	Combined sources	6
Helixⁱ	550 – 552	Combined sources	3
Beta strandⁱ	560 – 565	Combined sources	6
Helixⁱ	570 – 572	Combined sources	3
Helixⁱ	573 – 592	Combined sources	20
Beta strandⁱ	596 – 598	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	P17169
SMRⁱ	P17169
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P17169

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	2 – 218	Glutamine amidotransferase type-2Add BLAST	217
Domainⁱ	286 – 426	SIS 1Add BLAST	141
Domainⁱ	458 – 599	SIS 2Add BLAST	142

Keywords - Domainⁱ

Glutamine amidotransferase, Repeat

Phylogenomic databases

eggNOGⁱ	ENOG4105C46 Bacteria COG0449 LUCA
HOGENOMⁱ	HOG000258898
InParanoidⁱ	P17169
KEGG Orthology (KO) More...KOⁱ	K00820
OMAⁱ	ASEYRYA
PhylomeDBⁱ	P17169

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd05008 SIS_GlmS_GlmD_1, 1 hit cd05009 SIS_GlmS_GlmD_2, 1 hit
Gene3Dⁱ	3.60.20.10, 1 hit
HAMAPⁱ	MF_00164 GlmS, 1 hit
InterProⁱ	View protein in InterPro IPR017932 GATase_2_dom IPR035466 GlmS/AgaS_SIS IPR035490 GlmS/FrlB_SIS IPR005855 GlmS_trans IPR029055 Ntn_hydrolases_N IPR001347 SIS
PANTHERⁱ	PTHR10937:SF0 PTHR10937:SF0, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01380 SIS, 2 hits
SUPFAMⁱ	SSF56235 SSF56235, 1 hit
TIGRFAMsⁱ	TIGR01135 glmS, 1 hit
PROSITEⁱ	View protein in PROSITE PS51278 GATASE_TYPE_2, 1 hit PS51464 SIS, 2 hits

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P17169-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MCGIVGAIAQ RDVAEILLEG LRRLEYRGYD SAGLAVVDAE GHMTRLRRLG 
        60         70         80         90        100
KVQMLAQAAE EHPLHGGTGI AHTRWATHGE PSEVNAHPHV SEHIVVVHNG 
       110        120        130        140        150
IIENHEPLRE ELKARGYTFV SETDTEVIAH LVNWELKQGG TLREAVLRAI 
       160        170        180        190        200
PQLRGAYGTV IMDSRHPDTL LAARSGSPLV IGLGMGENFI ASDQLALLPV 
       210        220        230        240        250
TRRFIFLEEG DIAEITRRSV NIFDKTGAEV KRQDIESNLQ YDAGDKGIYR 
       260        270        280        290        300
HYMQKEIYEQ PNAIKNTLTG RISHGQVDLS ELGPNADELL SKVEHIQILA 
       310        320        330        340        350
CGTSYNSGMV SRYWFESLAG IPCDVEIASE FRYRKSAVRR NSLMITLSQS 
       360        370        380        390        400
GETADTLAGL RLSKELGYLG SLAICNVPGS SLVRESDLAL MTNAGTEIGV 
       410        420        430        440        450
ASTKAFTTQL TVLLMLVAKL SRLKGLDASI EHDIVHGLQA LPSRIEQMLS 
       460        470        480        490        500
QDKRIEALAE DFSDKHHALF LGRGDQYPIA LEGALKLKEI SYIHAEAYAA 
       510        520        530        540        550
GELKHGPLAL IDADMPVIVV APNNELLEKL KSNIEEVRAR GGQLYVFADQ 
       560        570        580        590        600
DAGFVSSDNM HIIEMPHVEE VIAPIFYTVP LQLLAYHVAL IKGTDVDQPR 

NLAKSVTVE

Length:609

Mass (Da):66,894

Last modified:January 23, 2007 - v4

Checksum:ⁱA1CB929E839436E0

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	419 – 420	KL → NV in CAA25785 (PubMed:6395859).Curated		2

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X01631 Genomic DNA Translation: CAA25785.1 L10328 Genomic DNA Translation: AAA62080.1 U00096 Genomic DNA Translation: AAC76752.1 AP009048 Genomic DNA Translation: BAE77559.1 V00620 Genomic DNA Translation: CAA23894.1 M18980 Genomic DNA Translation: AAA23836.1
PIRⁱ	B65176 XNECGM
NCBI Reference Sequences More...RefSeqⁱ	NP_418185.1, NC_000913.3 WP_000334099.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC76752; AAC76752; b3729 BAE77559; BAE77559; BAE77559
GeneIDⁱ	948241
KEGGⁱ	ecj:JW3707 eco:b3729
PATRICⁱ	fig\|1411691.4.peg.2971

Protein	Similar proteins		Species	Score	Length	Source
P17169	Glutamine--fructose-6-phosphate aminotransferase [isomerizing]		Escherichia coli NCCP15648		609	UniRef100_P17169
Glutamine--fructose-6-phosphate aminotransferase [isomerizing]		Klebsiella pneumoniae IS22		609
Glutamine--fructose-6-phosphate aminotransferase [isomerizing]		Escherichia coli D6-113.11		609
Glutamine--fructose-6-phosphate aminotransferase [isomerizing]		Escherichia coli M8		609
Glutamine--fructose-6-phosphate aminotransferase [isomerizing]		ECOLX		609
+84

Protein	Similar proteins		Species	Score	Length	Source
P17169	Glutamine--fructose-6-phosphate aminotransferase [isomerizing]		SHIFL		609	UniRef90_P17169
Glutamine--fructose-6-phosphate aminotransferase [isomerizing]		ECOL6		609
Glutamine--fructose-6-phosphate aminotransferase [isomerizing]		SALPA		609
Glutamine--fructose-6-phosphate aminotransferase [isomerizing]		ECO57		609
Glutamine--fructose-6-phosphate aminotransferase [isomerizing]		SALTI		609
+1493

Protein	Similar proteins		Species	Score	Length	Source
P17169	Glutamine--fructose-6-phosphate aminotransferase [isomerizing]		ECO57		609	UniRef50_P17169
Glutamine--fructose-6-phosphate aminotransferase [isomerizing]		SALPA		609
Glutamine--fructose-6-phosphate aminotransferase [isomerizing]		SALTY		609
Glutamine--fructose-6-phosphate aminotransferase [isomerizing]		ECOL6		609
Glutamine--fructose-6-phosphate aminotransferase [isomerizing]		SHIFL		609
+5203

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X01631 Genomic DNA Translation: CAA25785.1 L10328 Genomic DNA Translation: AAA62080.1 U00096 Genomic DNA Translation: AAC76752.1 AP009048 Genomic DNA Translation: BAE77559.1 V00620 Genomic DNA Translation: CAA23894.1 M18980 Genomic DNA Translation: AAA23836.1
PIRⁱ	B65176 XNECGM
RefSeqⁱ	NP_418185.1, NC_000913.3 WP_000334099.1, 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
	1JXA	X-ray	3.10	A/B/C	2-609	[»]
	1MOQ	X-ray	1.57	A	242-609	[»]
	1MOR	X-ray	1.90	A	242-609	[»]
	1MOS	X-ray	2.00	A	242-609	[»]
	1XFF	X-ray	1.80	A/B	2-241	[»]
	1XFG	X-ray	1.85	A/B	2-241	[»]
	2J6H	X-ray	2.35	A/B	2-609	[»]
	2VF4	X-ray	2.95	X	2-609	[»]
	2VF5	X-ray	2.90	X	2-609	[»]
	3OOJ	X-ray	2.50	A/B/C/D/E/F/G/H	3-609	[»]
	4AMV	X-ray	2.05	A/B/C	1-609	[»]
ProteinModelPortalⁱ	P17169
SMRⁱ	P17169
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4262136, 528 interactors
DIPⁱ	DIP-9775N
IntActⁱ	P17169, 8 interactors
STRINGⁱ	316407.85676309

Chemistry databases

BindingDBⁱ	P17169
DrugBankⁱ	DB03814 2-(N-Morpholino)-Ethanesulfonic Acid DB02445 2-Deoxy-2-Amino Glucitol-6-Phosphate DB02007 alpha-D-glucose 6-phosphate DB02657 Glucosamine 6-Phosphate DB03581 Glucose-6-Phosphate DB02446 Glutamine Hydroxamate

Proteomic databases

EPDⁱ	P17169
PaxDbⁱ	P17169
PRIDEⁱ	P17169

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC76752; AAC76752; b3729 BAE77559; BAE77559; BAE77559
GeneIDⁱ	948241
KEGGⁱ	ecj:JW3707 eco:b3729
PATRICⁱ	fig\|1411691.4.peg.2971

Organism-specific databases

EchoBASEⁱ	EB0377
EcoGeneⁱ	EG10382 glmS

Phylogenomic databases

eggNOGⁱ	ENOG4105C46 Bacteria COG0449 LUCA
HOGENOMⁱ	HOG000258898
InParanoidⁱ	P17169
KOⁱ	K00820
OMAⁱ	ASEYRYA
PhylomeDBⁱ	P17169

Enzyme and pathway databases

BioCycⁱ	EcoCyc:L-GLN-FRUCT-6-P-AMINOTRANS-MONOMER MetaCyc:L-GLN-FRUCT-6-P-AMINOTRANS-MONOMER
BRENDAⁱ	2.6.1.16 2026

Miscellaneous databases

EvolutionaryTraceⁱ	P17169
Protein Ontology More...PROⁱ	PR:P17169

Family and domain databases

CDDⁱ	cd05008 SIS_GlmS_GlmD_1, 1 hit cd05009 SIS_GlmS_GlmD_2, 1 hit
Gene3Dⁱ	3.60.20.10, 1 hit
HAMAPⁱ	MF_00164 GlmS, 1 hit
InterProⁱ	View protein in InterPro IPR017932 GATase_2_dom IPR035466 GlmS/AgaS_SIS IPR035490 GlmS/FrlB_SIS IPR005855 GlmS_trans IPR029055 Ntn_hydrolases_N IPR001347 SIS
PANTHERⁱ	PTHR10937:SF0 PTHR10937:SF0, 1 hit
Pfamⁱ	View protein in Pfam PF01380 SIS, 2 hits
SUPFAMⁱ	SSF56235 SSF56235, 1 hit
TIGRFAMsⁱ	TIGR01135 glmS, 1 hit
PROSITEⁱ	View protein in PROSITE PS51278 GATASE_TYPE_2, 1 hit PS51464 SIS, 2 hits
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	GLMS_ECOLI
Accessionⁱ	P17169Primary (citable) accession number: P17169 Secondary accession number(s): P76745, Q2M847
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
	Last sequence update:	January 23, 2007
	Last modified:	October 10, 2018
	This is version 183 of the entry and version 4 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

Proteomes

Annotation systems

Supporting data

UniProtKB - P17169 (GLMS_ECOLI)

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Glutamine--fructose-6-phosphate aminotransferase [isomerizing]

glmS

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

<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

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 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

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

Domains and Repeats

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

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

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ