UniProtKB - P04995 (EX1_ECOLI)

>sp|P04995|EX1_ECOLI Exodeoxyribonuclease I OS=Escherichia coli (strain K12) OX=83333 GN=sbcB PE=1 SV=2
MMNDGKQQSTFLFHDYETFGTHPALDRPAQFAAIRTDSEFNVIGEPEVFYCKPADDYLPQ
PGAVLITGITPQEARAKGENEAAFAARIHSLFTVPKTCILGYNNVRFDDEVTRNIFYRNF
YDPYAWSWQHDNSRWDLLDVMRACYALRPEGINWPENDDGLPSFRLEHLTKANGIEHSNA
HDAMADVYATIAMAKLVKTRQPRLFDYLFTHRNKHKLMALIDVPQMKPLVHVSGMFGAWR
GNTSWVAPLAWHPENRNAVIMVDLAGDISPLLELDSDTLRERLYTAKTDLGDNAAVPVKL
VHINKCPVLAQANTLRPEDADRLGINRQHCLDNLKILRENPQVREKVVAIFAEAEPFTPS
DNVDAQLYNGFFSDADRAAMKIVLETEPRNLPALDITFVDKRIEKLLFNYRARNFPGTLD
YAEQQRWLEHRRQVFTPEFLQGYADELQMLVQQYADDKEKVALLKALWQYAEEIV

Entry version 185 (07 Apr 2021)
Sequence version 2 (01 Feb 1994)
Previous versions | rss

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Protein

Exodeoxyribonuclease I

Gene

sbcB

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Degrades single-stranded DNA (ssDNA) in a highly processive manner (PubMed:23609540). Also functions as a DNA deoxyribophosphodiesterase that releases deoxyribose-phosphate moieties following the cleavage of DNA at an apurinic/apyrimidinic (AP) site by either an AP endonuclease or AP lyase (PubMed:1329027).2 Publications

Catalytic activityⁱ

Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.9
  "Structural basis of Escherichia coli single-stranded DNA-binding protein stimulation of exonuclease I."
  Lu D., Keck J.L.
  Proc. Natl. Acad. Sci. U.S.A. 105:9169-9174(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF APO FORM AND IN COMPLEX WITH SSB TAIL PEPTIDE AND MAGNESIUM, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH SSB, DOMAIN, SITES, MUTAGENESIS OF ARG-148; GLU-150; TYR-207; LYS-227; GLN-311; ARG-316; GLU-318; ASP-319; ARG-327; LEU-331; ARG-338; GLN-448 AND GLN-452.
- Ref.10
  "Small-molecule tools for dissecting the roles of SSB/protein interactions in genome maintenance."
  Lu D., Bernstein D.A., Satyshur K.A., Keck J.L.
  Proc. Natl. Acad. Sci. U.S.A. 107:633-638(2010) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEXES WITH INHIBITORS AND MAGNESIUM, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH SSB, SITE.
- Ref.12
  "Crystal structures of Escherichia coli exonuclease I in complex with single-stranded DNA provide insights into the mechanism of processive digestion."
  Korada S.K., Johns T.D., Smith C.E., Jones N.D., McCabe K.A., Bell C.E.
  Nucleic Acids Res. 41:5887-5897(2013) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEXES WITH SINGLE-STRANDED DNA SUBSTRATES AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBUNIT, DOMAIN, MUTAGENESIS OF HIS-181.
EC:3.1.11.1

Cofactorⁱ

Mg²⁺4 PublicationsNote: Binds 2 Mg²⁺ ions per monomer.1 Publication

Activity regulationⁱ

Inhibited by 10 mM EDTA.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	15	Magnesium 15 Publications	1
Metal bindingⁱ	17	Magnesium 21 Publication	1
Binding siteⁱ	17	Substrate1 Publication	1
Siteⁱ	148	Important for interaction with ssb1 Publication	1
Binding siteⁱ	165	Substrate1 Publication	1
Siteⁱ	181	Important for activity1 Publication	1
Metal bindingⁱ	186	Magnesium 21 Publication	1
Siteⁱ	207	Important for interaction with ssb1 Publication	1
Siteⁱ	311	Important for interaction with ssb1 Publication	1
Siteⁱ	338	Important for interaction with ssb1 Publication	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding, Exonuclease, Hydrolase, Nuclease
Biological process	DNA damage, DNA repair
Ligand	Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10926-MONOMER MetaCyc:EG10926-MONOMER
BRENDAⁱ	3.1.11.1, 2026

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Exodeoxyribonuclease I (EC:3.1.11.13 Publications) Short name: ExoI1 Publication Short name: Exonuclease I1 Publication Alternative name(s): DNA deoxyribophosphodiesterase Short name: dRPase
Gene namesⁱ	Name:sbcB Synonyms:cpeA, xonA Ordered Locus Names:b2011, JW1993
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

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	148	R → A: Strongly reduced ssb-binding. Reduced ssb-dependent nuclease activity. 1 Publication	1
Mutagenesisⁱ	150	E → A: About 2-fold increased ssb-binding. Weakly increased ssb-independent and ssb-dependent nuclease activity. 1 Publication	1
Mutagenesisⁱ	181	H → A: Residual nuclease activity. 1 Publication	1
Mutagenesisⁱ	207	Y → A: Strongly reduced ssb-binding. Reduced ssb-dependent nuclease activity. 1 Publication	1
Mutagenesisⁱ	227	K → A: 7-fold reduced ssb-binding. Reduced ssb-dependent nuclease activity. 1 Publication	1
Mutagenesisⁱ	311	Q → A: 2-fold reduced ssb-binding. Weakly reduced ssb-dependent nuclease activity. 1 Publication	1
Mutagenesisⁱ	316	R → A: Strongly reduced ssb-binding. Strongly reduced ssb-dependent nuclease activity. 1 Publication	1
Mutagenesisⁱ	318	E → A: About 2-fold increased ssb-binding. No effect on ssb-dependent nuclease activity. 1 Publication	1
Mutagenesisⁱ	319	D → A: 2-fold reduced ssb-binding. No effect on ssb-dependent nuclease activity. 1 Publication	1
Mutagenesisⁱ	327	R → A: No effect on ssb-binding and on ssb-dependent nuclease activity. 1 Publication	1
Mutagenesisⁱ	331	L → A: No effect on ssb-binding and on ssb-dependent nuclease activity. 1 Publication	1
Mutagenesisⁱ	338	R → A: 3-fold reduced ssb-binding. Reduced ssb-dependent nuclease activity. 1 Publication	1
Mutagenesisⁱ	448	Q → A: No effect on ssb-binding and on ssb-dependent nuclease activity. 1 Publication	1
Mutagenesisⁱ	452	Q → A: No effect on ssb-binding and on ssb-dependent nuclease activity. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000087110	1 – 475	Exodeoxyribonuclease IAdd BLAST		475

Proteomic databases

jPOSTⁱ	P04995
PaxDbⁱ	P04995
PRIDEⁱ	P04995

Interactionⁱ

Subunit structureⁱ

Monomer (PubMed:23609540).

Interacts with ssb (via C-terminus); this interaction stimulates the exonuclease activity by recruiting the enzyme to its substrate (PubMed:18591666, PubMed:20018747).

3 Publications

Sites

Feature key	Position(s)	DescriptionActions	Length
Siteⁱ	18	Interaction with single-stranded DNA1 Publication	1
Siteⁱ	66	Interaction with single-stranded DNA1 Publication	1
Siteⁱ	113	Interaction with single-stranded DNA1 Publication	1
Siteⁱ	124	Interaction with single-stranded DNA1 Publication	1
Siteⁱ	128	Interaction with single-stranded DNA1 Publication	1
Siteⁱ	142	Interaction with single-stranded DNA1 Publication	1
Siteⁱ	164	Interaction with single-stranded DNACombined sources1 Publication	1
Siteⁱ	214	Interaction with single-stranded DNA1 Publication	1
Siteⁱ	257	Interaction with single-stranded DNACombined sources1 Publication	1
Siteⁱ	284	Interaction with single-stranded DNA1 Publication	1
Siteⁱ	304	Interaction with single-stranded DNACombined sources1 Publication	1
Siteⁱ	368	Interaction with single-stranded DNA1 Publication	1
Siteⁱ	371	Interaction with single-stranded DNA1 Publication	1

Protein-protein interaction databases

BioGRIDⁱ	4260414, 102 interactors
Database of interacting proteins More...DIPⁱ	DIP-10827N
IntActⁱ	P04995, 7 interactors
STRINGⁱ	511145.b2011

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	10 – 21	Combined sources	12
Turnⁱ	23 – 25	Combined sources	3
Beta strandⁱ	28 – 36	Combined sources	9
Beta strandⁱ	47 – 51	Combined sources	5
Helixⁱ	61 – 67	Combined sources	7
Helixⁱ	71 – 77	Combined sources	7
Helixⁱ	81 – 92	Combined sources	12
Beta strandⁱ	97 – 103	Combined sources	7
Turnⁱ	104 – 107	Combined sources	4
Helixⁱ	108 – 118	Combined sources	11
Helixⁱ	125 – 127	Combined sources	3
Helixⁱ	129 – 131	Combined sources	3
Beta strandⁱ	133 – 136	Combined sources	4
Helixⁱ	137 – 147	Combined sources	11
Beta strandⁱ	160 – 162	Combined sources	3
Helixⁱ	166 – 172	Combined sources	7
Helixⁱ	185 – 200	Combined sources	16
Helixⁱ	202 – 210	Combined sources	9
Helixⁱ	214 – 219	Combined sources	6
Turnⁱ	223 – 226	Combined sources	4
Beta strandⁱ	229 – 232	Combined sources	4
Helixⁱ	234 – 236	Combined sources	3
Helixⁱ	238 – 240	Combined sources	3
Beta strandⁱ	243 – 251	Combined sources	9
Beta strandⁱ	258 – 263	Combined sources	6
Helixⁱ	269 – 273	Combined sources	5
Helixⁱ	276 – 285	Combined sources	10
Helixⁱ	287 – 289	Combined sources	3
Beta strandⁱ	298 – 302	Combined sources	5
Helixⁱ	303 – 305	Combined sources	3
Beta strandⁱ	308 – 311	Combined sources	4
Helixⁱ	312 – 314	Combined sources	3
Helixⁱ	317 – 323	Combined sources	7
Helixⁱ	327 – 339	Combined sources	13
Helixⁱ	343 – 346	Combined sources	4
Helixⁱ	363 – 365	Combined sources	3
Helixⁱ	367 – 369	Combined sources	3
Helixⁱ	374 – 385	Combined sources	12
Turnⁱ	388 – 390	Combined sources	3
Turnⁱ	391 – 393	Combined sources	3
Helixⁱ	402 – 414	Combined sources	13
Helixⁱ	416 – 418	Combined sources	3
Helixⁱ	421 – 434	Combined sources	14
Helixⁱ	437 – 453	Combined sources	17
Turnⁱ	454 – 456	Combined sources	3
Helixⁱ	458 – 473	Combined sources	16

Show more details

3D structure databases

SMRⁱ	P04995
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P04995

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	13 – 192	ExonucleaseSequence analysisAdd BLAST	180
Domainⁱ	202 – 355	ExoI SH3-likePROSITE-ProRule annotationAdd BLAST	154
Domainⁱ	358 – 475	ExoI C-terminalPROSITE-ProRule annotationAdd BLAST	118

Domainⁱ

The N-terminal exonuclease domain and the exonuclease C-terminal domain form a central positively charged groove which binds the DNA.2 Publications2 Publications

Phylogenomic databases

eggNOGⁱ	COG2925, Bacteria
HOGENOMⁱ	CLU_043508_1_1_6
InParanoidⁱ	P04995
PhylomeDBⁱ	P04995

Family and domain databases

Gene3Dⁱ	2.30.30.450, 1 hit 3.30.420.10, 1 hit
InterProⁱ	View protein in InterPro IPR023607, Exodeoxyribonuclease_I IPR034748, EXOI_C IPR034747, EXOI_SH3 IPR038649, EXOI_SH3_sf IPR013620, Exonuc_1_C IPR013520, Exonuclease_RNaseT/DNA_pol3 IPR012337, RNaseH-like_sf IPR036397, RNaseH_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF08411, Exonuc_X-T_C, 1 hit PF00929, RNase_T, 1 hit
PIRSFⁱ	PIRSF000977, Exodeoxyribonuclease_I, 1 hit
SMARTⁱ	View protein in SMART SM00479, EXOIII, 1 hit
SUPFAMⁱ	SSF53098, SSF53098, 1 hit
PROSITEⁱ	View protein in PROSITE PS51785, EXOI_C, 1 hit PS51784, EXOI_SH3, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P04995-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MMNDGKQQST FLFHDYETFG THPALDRPAQ FAAIRTDSEF NVIGEPEVFY 
        60         70         80         90        100
CKPADDYLPQ PGAVLITGIT PQEARAKGEN EAAFAARIHS LFTVPKTCIL 
       110        120        130        140        150
GYNNVRFDDE VTRNIFYRNF YDPYAWSWQH DNSRWDLLDV MRACYALRPE 
       160        170        180        190        200
GINWPENDDG LPSFRLEHLT KANGIEHSNA HDAMADVYAT IAMAKLVKTR 
       210        220        230        240        250
QPRLFDYLFT HRNKHKLMAL IDVPQMKPLV HVSGMFGAWR GNTSWVAPLA 
       260        270        280        290        300
WHPENRNAVI MVDLAGDISP LLELDSDTLR ERLYTAKTDL GDNAAVPVKL 
       310        320        330        340        350
VHINKCPVLA QANTLRPEDA DRLGINRQHC LDNLKILREN PQVREKVVAI 
       360        370        380        390        400
FAEAEPFTPS DNVDAQLYNG FFSDADRAAM KIVLETEPRN LPALDITFVD 
       410        420        430        440        450
KRIEKLLFNY RARNFPGTLD YAEQQRWLEH RRQVFTPEFL QGYADELQML 
       460        470 
VQQYADDKEK VALLKALWQY AEEIV

Length:475

Mass (Da):54,501

Last modified:February 1, 1994 - v2

Checksum:ⁱA6A02AC17922C313

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	210 – 218	Missing in AAA19938 (PubMed:3539937).Curated	9
Sequence conflictⁱ	225	Q → H in AAA19938 (PubMed:3539937).Curated	1
Sequence conflictⁱ	343	V → E in AAA19938 (PubMed:3539937).Curated	1
Sequence conflictⁱ	475	V → A in AAA19938 (PubMed:3539937).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J02641 Unassigned DNA Translation: AAA19938.1 U00009 Genomic DNA Translation: AAA16417.1 U00096 Genomic DNA Translation: AAC75072.1 AP009048 Genomic DNA Translation: BAA15839.1
PIRⁱ	B64966, NCECX1
NCBI Reference Sequences More...RefSeqⁱ	NP_416515.1, NC_000913.3 WP_000980589.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC75072; AAC75072; b2011 BAA15839; BAA15839; BAA15839
GeneIDⁱ	946529
KEGGⁱ	ecj:JW1993 eco:b2011

Protein	Similar proteins		Species	Score	Length	Source
P04995	Exodeoxyribonuclease I		Escherichia coli MS 198-1		499	UniRef100_P04995
Exodeoxyribonuclease I		ECOLI		475
Exodeoxyribonuclease I		ECOLX		475
Exodeoxyribonuclease I		Escherichia coli 3-373-03_S4_C2		475
Exodeoxyribonuclease I		Escherichia coli UMEA 3212-1		475
+9

Protein	Similar proteins		Species	Score	Length	Source
P04995	Exodeoxyribonuclease I		Escherichia coli MS 198-1		499	UniRef90_P04995
Exodeoxyribonuclease I		ECOLI		475
Exodeoxyribonuclease I		ECOLX		475
Exodeoxyribonuclease I		Escherichia coli 3-373-03_S4_C2		475
Exodeoxyribonuclease I		Escherichia coli UMEA 3212-1		475
+2652

Protein	Similar proteins		Species	Score	Length	Source
P04995	Exodeoxyribonuclease I		Escherichia coli MS 198-1		499	UniRef50_P04995
Exodeoxyribonuclease I		ECOLI		475
Exodeoxyribonuclease I		ECOLX		475
Exodeoxyribonuclease I		Escherichia coli 3-373-03_S4_C2		475
Exodeoxyribonuclease I		Escherichia coli UMEA 3212-1		475
+7458

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J02641 Unassigned DNA Translation: AAA19938.1 U00009 Genomic DNA Translation: AAA16417.1 U00096 Genomic DNA Translation: AAC75072.1 AP009048 Genomic DNA Translation: BAA15839.1
PIRⁱ	B64966, NCECX1
RefSeqⁱ	NP_416515.1, NC_000913.3 WP_000980589.1, 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
	1FXX	X-ray	2.40	A	1-475	[»]
	2QXF	X-ray	1.50	A	1-475	[»]
	3C94	X-ray	2.70	A	1-475	[»]
	3C95	X-ray	1.70	A	1-475	[»]
	3HL8	X-ray	1.55	A	1-475	[»]
	3HP9	X-ray	1.60	A	1-475	[»]
	4HCB	X-ray	2.00	A/B	1-475	[»]
	4HCC	X-ray	2.96	A/B	1-475	[»]
	4JRP	X-ray	1.95	A/B	1-475	[»]
	4JRQ	X-ray	3.00	A/B	1-475	[»]
	4JS4	X-ray	3.10	A/B	1-475	[»]
	4JS5	X-ray	3.50	A/B	1-475	[»]
SMRⁱ	P04995
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	4260414, 102 interactors
DIPⁱ	DIP-10827N
IntActⁱ	P04995, 7 interactors
STRINGⁱ	511145.b2011

Proteomic databases

jPOSTⁱ	P04995
PaxDbⁱ	P04995
PRIDEⁱ	P04995

Genome annotation databases

EnsemblBacteriaⁱ	AAC75072; AAC75072; b2011 BAA15839; BAA15839; BAA15839
GeneIDⁱ	946529
KEGGⁱ	ecj:JW1993 eco:b2011

Organism-specific databases

EchoBASEⁱ	EB0919

EchoBASEⁱ

EB0919

Phylogenomic databases

eggNOGⁱ	COG2925, Bacteria
HOGENOMⁱ	CLU_043508_1_1_6
InParanoidⁱ	P04995
PhylomeDBⁱ	P04995

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10926-MONOMER MetaCyc:EG10926-MONOMER
BRENDAⁱ	3.1.11.1, 2026

Miscellaneous databases

EvolutionaryTraceⁱ	P04995
Protein Ontology More...PROⁱ	PR:P04995

Family and domain databases

Gene3Dⁱ	2.30.30.450, 1 hit 3.30.420.10, 1 hit
InterProⁱ	View protein in InterPro IPR023607, Exodeoxyribonuclease_I IPR034748, EXOI_C IPR034747, EXOI_SH3 IPR038649, EXOI_SH3_sf IPR013620, Exonuc_1_C IPR013520, Exonuclease_RNaseT/DNA_pol3 IPR012337, RNaseH-like_sf IPR036397, RNaseH_sf
Pfamⁱ	View protein in Pfam PF08411, Exonuc_X-T_C, 1 hit PF00929, RNase_T, 1 hit
PIRSFⁱ	PIRSF000977, Exodeoxyribonuclease_I, 1 hit
SMARTⁱ	View protein in SMART SM00479, EXOIII, 1 hit
SUPFAMⁱ	SSF53098, SSF53098, 1 hit
PROSITEⁱ	View protein in PROSITE PS51785, EXOI_C, 1 hit PS51784, EXOI_SH3, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	EX1_ECOLI
Accessionⁱ	P04995Primary (citable) accession number: P04995
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
	Last sequence update:	February 1, 1994
	Last modified:	April 7, 2021
	This is version 185 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

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UniProtKB - P04995 (EX1_ECOLI)

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Exodeoxyribonuclease I

sbcB

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<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>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

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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

<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

Sites

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

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

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Proteomic 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

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ