dnaG

Functionⁱ

RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.UniRule annotation2 Publications

Cofactorⁱ

Protein has several cofactor binding sites:

Zn²⁺
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00974
2 Publications
Manual assertion based on experiment inⁱ
- Ref.7
  "Enriched sources of Escherichia coli replication proteins. The dnaG primase is a zinc metalloprotein."
  Stamford N.P.J., Lilley P.E., Dixon N.E.
  Biochim. Biophys. Acta 1132:17-25(1992) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, COFACTOR, SUBUNIT, ZINC-BINDING.
- Ref.8
  "The role of zinc and the reactivity of cysteines in Escherichia coli primase."
  Griep M.A., Lokey E.R.
  Biochemistry 35:8260-8267(1996) [PubMed] [Europe PMC] [Abstract]
  Cited for: COFACTOR, ZINC-BINDING.
Note: Binds 1 zinc ion per monomer.
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00974
2 Publications
Manual assertion based on experiment inⁱ
- Ref.7
  "Enriched sources of Escherichia coli replication proteins. The dnaG primase is a zinc metalloprotein."
  Stamford N.P.J., Lilley P.E., Dixon N.E.
  Biochim. Biophys. Acta 1132:17-25(1992) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, COFACTOR, SUBUNIT, ZINC-BINDING.
- Ref.8
  "The role of zinc and the reactivity of cysteines in Escherichia coli primase."
  Griep M.A., Lokey E.R.
  Biochemistry 35:8260-8267(1996) [PubMed] [Europe PMC] [Abstract]
  Cited for: COFACTOR, ZINC-BINDING.
Mg²⁺
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00974
Note: Binds two Mg²⁺ per subunit.
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00974

Activity regulationⁱ

Activity can be regulated by an intermolecular trans association between the zinc-binding domain and the catalytic core domain of two different primase molecules.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	265	Magnesium 1; catalyticUniRule annotation	1
Metal bindingⁱ	309	Magnesium 1; catalyticUniRule annotation	1
Metal bindingⁱ	309	Magnesium 2UniRule annotation	1
Metal bindingⁱ	311	Magnesium 2UniRule annotation	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	40 – 64	CHC2-typeUniRule annotationAdd BLAST		25

GO - Molecular functionⁱ

DNA binding Source: UniProtKB-KW
DNA primase activity
Source: EcoliWiki
Inferred from direct assayⁱ
- 340457
zinc ion binding
Source: EcoliWiki
Inferred from direct assayⁱ
- 1511009

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

DNA replication, synthesis of RNA primer
Source: EcoliWiki
Inferred from direct assayⁱ
- 340457

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding, Nucleotidyltransferase, Transferase
Biological process	DNA replication, Transcription
Ligand	Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10239-MONOMER MetaCyc:EG10239-MONOMER

BioCycⁱ

EcoCyc:EG10239-MONOMER
MetaCyc:EG10239-MONOMER

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: DNA primaseUniRule annotation (EC:2.7.7.-UniRule annotation)
Gene namesⁱ	Name:dnaGUniRule annotation Synonyms:dnaP, parB Ordered Locus Names:b3066, JW3038
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	EG10239 dnaG

EcoGeneⁱ

EG10239 dnaG

Subcellular locationⁱ

GO - Cellular componentⁱ

cytoplasm
Source: EcoliWiki
Inferred from direct assayⁱ
- 340457
primosome complex Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

DNA-directed RNA polymerase, Primosome

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	165	W → A: Abolishes DNA-binding and primer synthesis. 1 Publication	1
Mutagenesisⁱ	199	R → A: Abolishes primer synthesis but can still bind DNA. Abolishes DNA-binding; when associated with A-201. 1 Publication	1
Mutagenesisⁱ	201	R → A: Abolishes primer synthesis but can still bind DNA. Abolishes DNA-binding; when associated with A-199. 1 Publication	1
Mutagenesisⁱ	576	Q → A: Decreases interaction with DnaB and primase activity. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000180490	1 – 581	DNA primaseAdd BLAST		581

Proteomic databases

PaxDbⁱ	P0ABS5
PRIDEⁱ	P0ABS5

Interactionⁱ

Subunit structureⁱ

Monomer. Interacts with DnaB. The primase-helicase complex is composed of up to three DnaG bound to one DnaB hexamer.UniRule annotation6 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
dnaB	P0ACB0	3	EBI-549259,EBI-548978
rplA	P0A7L0	2	EBI-549259,EBI-543771
ssb	P0AGE0	2	EBI-549259,EBI-1118620

Protein-protein interaction databases

BioGridⁱ	4262146, 230 interactors
ComplexPortalⁱ	CPX-1933 DnaB-DnaG complex
Database of interacting proteins More...DIPⁱ	DIP-47954N
IntActⁱ	P0ABS5, 17 interactors
STRINGⁱ	316385.ECDH10B_3241

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	116 – 131	Combined sources	16
Helixⁱ	134 – 136	Combined sources	3
Helixⁱ	137 – 145	Combined sources	9
Helixⁱ	150 – 156	Combined sources	7
Beta strandⁱ	159 – 161	Combined sources	3
Beta strandⁱ	163 – 165	Combined sources	3
Helixⁱ	167 – 172	Combined sources	6
Helixⁱ	176 – 184	Combined sources	9
Beta strandⁱ	187 – 190	Combined sources	4
Beta strandⁱ	196 – 199	Combined sources	4
Beta strandⁱ	202 – 209	Combined sources	8
Beta strandⁱ	211 – 213	Combined sources	3
Beta strandⁱ	215 – 225	Combined sources	11
Beta strandⁱ	229 – 232	Combined sources	4
Turnⁱ	241 – 243	Combined sources	3
Helixⁱ	248 – 253	Combined sources	6
Beta strandⁱ	261 – 266	Combined sources	6
Helixⁱ	267 – 275	Combined sources	9
Beta strandⁱ	281 – 283	Combined sources	3
Beta strandⁱ	285 – 288	Combined sources	4
Helixⁱ	291 – 300	Combined sources	10
Beta strandⁱ	302 – 311	Combined sources	10
Helixⁱ	312 – 325	Combined sources	14
Helixⁱ	326 – 328	Combined sources	3
Beta strandⁱ	334 – 340	Combined sources	7
Helixⁱ	346 – 362	Combined sources	17
Helixⁱ	368 – 376	Combined sources	9
Helixⁱ	377 – 379	Combined sources	3
Helixⁱ	385 – 399	Combined sources	15
Helixⁱ	405 – 419	Combined sources	15
Helixⁱ	424 – 427	Combined sources	4
Helixⁱ	448 – 460	Combined sources	13
Helixⁱ	462 – 467	Combined sources	6
Turnⁱ	472 – 474	Combined sources	3
Helixⁱ	476 – 478	Combined sources	3
Helixⁱ	482 – 493	Combined sources	12
Helixⁱ	500 – 505	Combined sources	6
Turnⁱ	507 – 509	Combined sources	3
Helixⁱ	510 – 512	Combined sources	3
Helixⁱ	513 – 540	Combined sources	28
Turnⁱ	541 – 543	Combined sources	3
Helixⁱ	544 – 558	Combined sources	15
Turnⁱ	559 – 561	Combined sources	3
Helixⁱ	565 – 577	Combined sources	13

Show more details

3D structure databases

ProteinModelPortalⁱ	P0ABS5
SMRⁱ	P0ABS5
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P0ABS5

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	259 – 341	ToprimUniRule annotationAdd BLAST		83

Domainⁱ

Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.UniRule annotation3 Publications

Sequence similaritiesⁱ

Belongs to the DnaG primase family.UniRule annotation

Zinc finger

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	40 – 64	CHC2-typeUniRule annotationAdd BLAST		25

Keywords - Domainⁱ

Zinc-finger

Phylogenomic databases

eggNOGⁱ	ENOG4105C9G Bacteria COG0358 LUCA
HOGENOMⁱ	HOG000014483
InParanoidⁱ	P0ABS5
KEGG Orthology (KO) More...KOⁱ	K02316
PhylomeDBⁱ	P0ABS5

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd03364 TOPRIM_DnaG_primases, 1 hit
Gene3Dⁱ	1.10.860.10, 1 hit 3.90.580.10, 1 hit 3.90.980.10, 1 hit
HAMAPⁱ	MF_00974 DNA_primase_DnaG, 1 hit
InterProⁱ	View protein in InterPro IPR016136 DNA_helicase_N/primase_C IPR013264 DNA_primase_core_N IPR037068 DNA_primase_core_N_sf IPR019475 DNA_primase_DnaB-bd IPR006295 DNA_primase_DnaG IPR013173 DNA_primase_DnaG_DnaB-bd_dom IPR036977 DNA_primase_Znf_CHC2 IPR030846 DnaG_bac IPR034151 TOPRIM_DnaG_bac IPR006171 TOPRIM_domain IPR002694 Znf_CHC2
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF10410 DnaB_bind, 1 hit PF08278 DnaG_DnaB_bind, 1 hit PF08275 Toprim_N, 1 hit PF01807 zf-CHC2, 1 hit
PIRSFⁱ	PIRSF002811 DnaG, 1 hit
SMARTⁱ	View protein in SMART SM00766 DnaG_DnaB_bind, 1 hit SM00493 TOPRIM, 1 hit SM00400 ZnF_CHCC, 1 hit
TIGRFAMsⁱ	TIGR01391 dnaG, 1 hit
PROSITEⁱ	View protein in PROSITE PS50880 TOPRIM, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P0ABS5-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MAGRIPRVFI NDLLARTDIV DLIDARVKLK KQGKNFHACC PFHNEKTPSF 
        60         70         80         90        100
TVNGEKQFYH CFGCGAHGNA IDFLMNYDKL EFVETVEELA AMHNLEVPFE 
       110        120        130        140        150
AGSGPSQIER HQRQTLYQLM DGLNTFYQQS LQQPVATSAR QYLEKRGLSH 
       160        170        180        190        200
EVIARFAIGF APPGWDNVLK RFGGNPENRQ SLIDAGMLVT NDQGRSYDRF 
       210        220        230        240        250
RERVMFPIRD KRGRVIGFGG RVLGNDTPKY LNSPETDIFH KGRQLYGLYE 
       260        270        280        290        300
AQQDNAEPNR LLVVEGYMDV VALAQYGINY AVASLGTSTT ADHIQLLFRA 
       310        320        330        340        350
TNNVICCYDG DRAGRDAAWR ALETALPYMT DGRQLRFMFL PDGEDPDTLV 
       360        370        380        390        400
RKEGKEAFEA RMEQAMPLSA FLFNSLMPQV DLSTPDGRAR LSTLALPLIS 
       410        420        430        440        450
QVPGETLRIY LRQELGNKLG ILDDSQLERL MPKAAESGVS RPVPQLKRTT 
       460        470        480        490        500
MRILIGLLVQ NPELATLVPP LENLDENKLP GLGLFRELVN TCLSQPGLTT 
       510        520        530        540        550
GQLLEHYRGT NNAATLEKLS MWDDIADKNI AEQTFTDSLN HMFDSLLELR 
       560        570        580 
QEELIARERT HGLSNEERLE LWTLNQELAK K

Length:581

Mass (Da):65,565

Last modified:July 21, 1986 - v1

Checksum:ⁱ294CF020E7B45D94

GO

Sequence cautionⁱ

The sequence CAA23531 differs from that shown. Reason: Frameshift at positions 106 and 169.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	24	D → N in CAA23636 (PubMed:6222240).Curated		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J01687 Genomic DNA Translation: AAA24600.1 V00274 Genomic DNA Translation: CAA23531.1 Frameshift. U28379 Genomic DNA Translation: AAA89146.1 U00096 Genomic DNA Translation: AAC76102.1 AP009048 Genomic DNA Translation: BAE77117.1 V00346 Genomic DNA Translation: CAA23636.1
PIRⁱ	A03423 RYEC2
NCBI Reference Sequences More...RefSeqⁱ	NP_417538.1, NC_000913.3 WP_000918827.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC76102; AAC76102; b3066 BAE77117; BAE77117; BAE77117
GeneIDⁱ	947570
KEGGⁱ	ecj:JW3038 eco:b3066
PATRICⁱ	fig\|1411691.4.peg.3664

Protein	Similar proteins		Species	Score	Length	Source
P0ABS5	DNA primase		ECO57		581	UniRef100_P0ABS6
DNA primase		SHIFL		581
DNA primase		Shigella sp.		581
DNA primase		Escherichia coli O145 str. RM9872		581
DNA primase		KLEPN		581
+129

Protein	Similar proteins		Species	Score	Length	Source
P0ABS5	DNA primase		ECO57		581	UniRef90_P0ABS6
DNA primase		SHIFL		581
DNA primase		Shigella sp.		581
DNA primase		Escherichia coli O145 str. RM9872		581
DNA primase		KLEPN		581
+209

Protein	Similar proteins		Species	Score	Length	Source
P0ABS5	DNA primase		HAEIN		593	UniRef50_Q08346
DNA primase		SALTY		581
DNA primase		ECOL6		581
DNA primase		PASMU		582
DNA primase		ECO57		581
+3093

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J01687 Genomic DNA Translation: AAA24600.1 V00274 Genomic DNA Translation: CAA23531.1 Frameshift. U28379 Genomic DNA Translation: AAA89146.1 U00096 Genomic DNA Translation: AAC76102.1 AP009048 Genomic DNA Translation: BAE77117.1 V00346 Genomic DNA Translation: CAA23636.1
PIRⁱ	A03423 RYEC2
RefSeqⁱ	NP_417538.1, NC_000913.3 WP_000918827.1, 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
	1DD9	X-ray	1.60	A	111-433	[»]
	1DDE	X-ray	1.70	A	111-433	[»]
	1EQN	X-ray	2.90	A/B/C/D/E	111-429	[»]
	1T3W	X-ray	2.80	A/B	434-581	[»]
	2HAJ	NMR	-	A	434-581	[»]
	3B39	X-ray	2.35	A/B	111-429	[»]
ProteinModelPortalⁱ	P0ABS5
SMRⁱ	P0ABS5
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4262146, 230 interactors
ComplexPortalⁱ	CPX-1933 DnaB-DnaG complex
DIPⁱ	DIP-47954N
IntActⁱ	P0ABS5, 17 interactors
STRINGⁱ	316385.ECDH10B_3241

Proteomic databases

PaxDbⁱ	P0ABS5
PRIDEⁱ	P0ABS5

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC76102; AAC76102; b3066 BAE77117; BAE77117; BAE77117
GeneIDⁱ	947570
KEGGⁱ	ecj:JW3038 eco:b3066
PATRICⁱ	fig\|1411691.4.peg.3664

Organism-specific databases

EchoBASEⁱ	EB0235
EcoGeneⁱ	EG10239 dnaG

Phylogenomic databases

eggNOGⁱ	ENOG4105C9G Bacteria COG0358 LUCA
HOGENOMⁱ	HOG000014483
InParanoidⁱ	P0ABS5
KOⁱ	K02316
PhylomeDBⁱ	P0ABS5

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10239-MONOMER MetaCyc:EG10239-MONOMER

BioCycⁱ

EcoCyc:EG10239-MONOMER
MetaCyc:EG10239-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P0ABS5
Protein Ontology More...PROⁱ	PR:P0ABS5

Family and domain databases

CDDⁱ	cd03364 TOPRIM_DnaG_primases, 1 hit
Gene3Dⁱ	1.10.860.10, 1 hit 3.90.580.10, 1 hit 3.90.980.10, 1 hit
HAMAPⁱ	MF_00974 DNA_primase_DnaG, 1 hit
InterProⁱ	View protein in InterPro IPR016136 DNA_helicase_N/primase_C IPR013264 DNA_primase_core_N IPR037068 DNA_primase_core_N_sf IPR019475 DNA_primase_DnaB-bd IPR006295 DNA_primase_DnaG IPR013173 DNA_primase_DnaG_DnaB-bd_dom IPR036977 DNA_primase_Znf_CHC2 IPR030846 DnaG_bac IPR034151 TOPRIM_DnaG_bac IPR006171 TOPRIM_domain IPR002694 Znf_CHC2
Pfamⁱ	View protein in Pfam PF10410 DnaB_bind, 1 hit PF08278 DnaG_DnaB_bind, 1 hit PF08275 Toprim_N, 1 hit PF01807 zf-CHC2, 1 hit
PIRSFⁱ	PIRSF002811 DnaG, 1 hit
SMARTⁱ	View protein in SMART SM00766 DnaG_DnaB_bind, 1 hit SM00493 TOPRIM, 1 hit SM00400 ZnF_CHCC, 1 hit
TIGRFAMsⁱ	TIGR01391 dnaG, 1 hit
PROSITEⁱ	View protein in PROSITE PS50880 TOPRIM, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	DNAG_ECOLI
Accessionⁱ	P0ABS5Primary (citable) accession number: P0ABS5 Secondary accession number(s): P02922 , P02923, Q2M9D9, Q47613
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
	Last sequence update:	July 21, 1986
	Last modified:	November 7, 2018
	This is version 113 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

3D-structure, Complete proteome, 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 - P0ABS5 (DNAG_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>

DNA primase

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 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

<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

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

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

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ