APEX1

Functionⁱ

Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6, associates with nCaRE, acting as an activator of transcriptional repression. Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance. Acts also as an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression. Associates, together with YBX1, on the MDR1 promoter. Together with NPM1, associates with rRNA. Binds DNA and RNA.25 Publications

Miscellaneous

Extract of mitochondria, but not of nuclei or cytosol, cleaves recombinant APEX1 to generate a mitochondrial APEX1-sized product (By similarity). The specific activity of the cleaved mitochondrial endodeoxyribonuclease appeared to be about 3-fold higher than that of the full-length form.By similarity

Catalytic activityⁱ

The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU00764
5 Publications
Manual assertion based on experiment inⁱ
- Ref.21
  "Rapid dissociation of human apurinic endonuclease (Ape1) from incised DNA induced by magnesium."
  Masuda Y., Bennett R.A., Demple B.
  J. Biol. Chem. 273:30360-30365(1998) [PubMed] [Europe PMC] [Abstract]
  Cited for: CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF ASP-283; ASP-308 AND HIS-309, COFACTOR.
- Ref.30
  "Novel role of tyrosine in catalysis by human AP endonuclease 1."
  Mundle S.T., Fattal M.H., Melo L.F., Coriolan J.D., O'Regan N.E., Strauss P.R.
  DNA Repair 3:1447-1455(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF TYR-171.
- Ref.39
  "Enzymatic mechanism of human apurinic/apyrimidinic endonuclease against a THF AP site model substrate."
  Mundle S.T., Delaney J.C., Essigmann J.M., Strauss P.R.
  Biochemistry 48:19-26(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: CATALYTIC ACTIVITY, COFACTOR, ENZYME MECHANISM.
- Ref.49
  "Characterization of the endoribonuclease active site of human apurinic/apyrimidinic endonuclease 1."
  Kim W.C., Berquist B.R., Chohan M., Uy C., Wilson D.M. III, Lee C.H.
  J. Mol. Biol. 411:960-971(2011) [PubMed] [Europe PMC] [Abstract]
  Cited for: MUTAGENESIS OF ASN-68; ASP-70; TYR-171; PHE-266; ASP-283; ASP-308 AND HIS-309, CATALYTIC ACTIVITY, ACTIVE SITE, FUNCTION, COFACTOR.
- Ref.55
  "Two divalent metal ions in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1: implications for the catalytic mechanism."
  Beernink P.T., Segelke B.W., Hadi M.Z., Erzberger J.P., Wilson D.M. III, Rupp B.
  J. Mol. Biol. 307:1023-1034(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH METAL IONS, CATALYTIC ACTIVITY, COFACTOR.
EC:4.2.99.18

Cofactorⁱ

Mg²⁺4 Publications, Mn²⁺4 PublicationsNote: Probably binds two magnesium or manganese ions per subunit.4 Publications

Activity regulationⁱ

NPM1 stimulates endodeoxyribonuclease activity on double-stranded DNA with AP sites, but inhibits endoribonuclease activity on single-stranded RNA containing AP sites.

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	70	Magnesium 1	1
Metal bindingⁱ	96	Magnesium 1	1
Active siteⁱ	171		1
Active siteⁱ	210	Proton donor/acceptor	1
Metal bindingⁱ	210	Magnesium 2	1
Metal bindingⁱ	212	Magnesium 2	1
Siteⁱ	212	Transition state stabilizer	1
Siteⁱ	283	Important for catalytic activity	1
Metal bindingⁱ	308	Magnesium 1	1

GO - Molecular functionⁱ

3'-5' exonuclease activity
Source: UniProtKB
Inferred from direct assayⁱ
- 11832948
chromatin DNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 11809897
class I DNA-(apurinic or apyrimidinic site) endonuclease activity Source: UniProtKB-EC
damaged DNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 12524539
- 14706345
DNA-(apurinic or apyrimidinic site) endonuclease activity
Source: UniProtKB
Inferred from direct assayⁱ
DNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 11286553
double-stranded DNA 3'-5' exodeoxyribonuclease activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
double-stranded DNA exodeoxyribonuclease activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 24703901
double-stranded telomeric DNA binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 24703901
endodeoxyribonuclease activity Source: Reactome
endonuclease activity
Source: MGI
Inferred from direct assayⁱ
- 11478795
metal ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 11286553
NF-kappaB binding Source: Ensembl
oxidoreductase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 12524539
- 9119221
phosphodiesterase I activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
phosphoric diester hydrolase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 18973764
protein-containing complex binding Source: Ensembl
RNA binding
Source: UniProtKB
Inferred from high throughput direct assayⁱ
- 22681889
RNA-DNA hybrid ribonuclease activity
Source: UniProtKB
Traceable author statementⁱ
- 11286553
site-specific endodeoxyribonuclease activity, specific for altered base
Source: UniProtKB
Inferred from direct assayⁱ
- 19188445
transcription coactivator activity
Source: UniProtKB
Inferred from direct assayⁱ
- 9119221
transcription corepressor activity
Source: ProtInc
Traceable author statementⁱ
- 7961715
uracil DNA N-glycosylase activity
Source: ProtInc
Traceable author statementⁱ
- 10805771

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

aging Source: Ensembl
base-excision repair
Source: CAFA
Inferred from direct assayⁱ
- 8932386
base-excision repair, base-free sugar-phosphate removal Source: Reactome
cell redox homeostasis Source: Ensembl
cellular response to cAMP Source: Ensembl
cellular response to hydrogen peroxide Source: Ensembl
cellular response to peptide hormone stimulus Source: Ensembl
DNA demethylation
Source: UniProtKB
Inferred from direct assayⁱ
- 21496894
DNA recombination Source: UniProtKB-KW
DNA repair
Source: UniProtKB
Inferred from direct assayⁱ
- 9560228
negative regulation of smooth muscle cell migration Source: Ensembl
positive regulation of G1/S transition of mitotic cell cycle Source: Ensembl
regulation of apoptotic process
Source: UniProtKB
Inferred from direct assayⁱ
- 19934257
regulation of mRNA stability
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 19401441
telomere maintenance
Source: BHF-UCL
Inferred from direct assayⁱ
- 24703901
telomere maintenance via base-excision repair
Source: BHF-UCL
Inferred from direct assayⁱ
- 24703901

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Activator, DNA-binding, Endonuclease, Exonuclease, Hydrolase, Lyase, Nuclease, Repressor, RNA-binding
Biological process	DNA damage, DNA recombination, DNA repair, Transcription, Transcription regulation
Ligand	Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAⁱ	4.2.99.18 2681
Reactomeⁱ	R-HSA-110357 Displacement of DNA glycosylase by APEX1 R-HSA-110362 POLB-Dependent Long Patch Base Excision Repair R-HSA-110373 Resolution of AP sites via the multiple-nucleotide patch replacement pathway R-HSA-5651801 PCNA-Dependent Long Patch Base Excision Repair R-HSA-73930 Abasic sugar-phosphate removal via the single-nucleotide replacement pathway R-HSA-73933 Resolution of Abasic Sites (AP sites)
SIGNORⁱ	P27695

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: DNA-(apurinic or apyrimidinic site) lyase (EC:3.1.-.-, EC:4.2.99.18) Alternative name(s): APEX nuclease Short name: APEN Apurinic-apyrimidinic endonuclease 1 Short name: AP endonuclease 1 Short name: APE-1 REF-1 Redox factor-1 Cleaved into the following chain: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial
Gene namesⁱ	Name:APEX1 Synonyms:APE, APE1, APEX, APX, HAP1, REF1
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 14

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000100823.11
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:587 APEX1
MIMⁱ	107748 gene
neXtProtⁱ	NX_P27695

Keywords - Cellular componentⁱ

Cytoplasm, Endoplasmic reticulum, Mitochondrion, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	6	K → R: Lack of acetylation, does not stimulate the YBX1-mediated MDR1 promoter activity and alter nuclear subcellular localization; when associated with R-7. Does not inhibit interaction with HDAC1, HDAC2 and HDAC3. Absence of increase in nCaRE binding activity. 4 Publications	1
Mutagenesisⁱ	7	K → R: Lack of acetylation and does not stimulate the YBX1-mediated MDR1 promoter activity and alter nuclear subcellular localization; when associated with R-6. 4 Publications	1
Mutagenesisⁱ	12	E → A: Reduces nuclear localization; when associated with A-13. 1 Publication	1
Mutagenesisⁱ	13	D → A: Reduces nuclear localization; when associated with A-12. 1 Publication	1
Mutagenesisⁱ	24	K → A: Enhances the interaction with TOMM20. Inhibits rRNA binding, interaction with NPM1, nuclear localization and modulates its endodeoxyribonuclease activity; when associated with A-25; A-27; A-31 and A-32. Inhibits ubiquitination; when associated with K-25 and K-27. 3 Publications	1
Mutagenesisⁱ	25	K → A: Enhances the interaction with TOMM20. Inhibits rRNA binding, interaction with NPM1, nuclear localization and modulates its endodeoxyribonuclease activity; when associated with A-24; A-27; A-31 and A-32. Inhibits ubiquitination; when associated with K-24 and K-27. 3 Publications	1
Mutagenesisⁱ	27	K → A: Enhances the interaction with TOMM20. Inhibits rRNA binding, interaction with NPM1, nuclear localization and modulates its endodeoyribonuclease activity; when associated with A-24; A-25; A-31 and A-32. Inhibits ubiquitination; when associated with K-24 and K-25. 3 Publications	1
Mutagenesisⁱ	31	K → A: Enhances the interaction with TOMM20. Does not inhibit redox and AP endodeoyribonuclease activities. Inhibits rRNA binding, interaction with NPM1, nuclear localization and modulates its endodeoxyribonuclease activity; when associated with A-24; A-25; A-27 and A-32. Reduces protection from granzyme A-mediated cell death; when associated with A-65 and A-210. 3 Publications	1
Mutagenesisⁱ	32	K → A: Inhibits rRNA binding, interaction with NPM1, nuclear localization and modulates its endodeoxyribonuclease activity; when associated with A-24; A-25; A-27 and A-31. 1 Publication	1
Mutagenesisⁱ	65	C → A: Abolishes the redox activity. Does not abolish the AP endodeoxyribonuclease and phosphodiesterase activities. Reduces protection from granzyme A-mediated cell death; when associated with A-31 and A-210. 3 Publications	1
Mutagenesisⁱ	65	C → S: Does not abolish NO-induced nitrosylation. Enhances NO-induced nuclear export. 3 Publications	1
Mutagenesisⁱ	68	N → A: Nearly abolishes AP endodeoxyribonuclease activity. 1 Publication	1
Mutagenesisⁱ	70	D → A: Strongly reduces AP endodeoxyribonuclease activity. 1 Publication	1
Mutagenesisⁱ	93	C → A: Abolishes partially the redox activity. 2 Publications	1
Mutagenesisⁱ	93	C → S: Does not abolish NO-induced nitrosylation. Abolishes NO-induced nitrosylation and translocation from the nucleus to the cytoplasm; when associated with S-310. 2 Publications	1
Mutagenesisⁱ	96	E → A: Lacks MYC CRD RNA cleavage activity. 1 Publication	1
Mutagenesisⁱ	99	C → A: Does not abolish the redox activity. 2 Publications	1
Mutagenesisⁱ	138	C → A: Does not abolish the redox activity. 2 Publications	1
Mutagenesisⁱ	171	Y → A, F or H: Abolishes the AP endodeoxyribonuclease activity. 2 Publications	1
Mutagenesisⁱ	208	C → A: Does not abolish the redox activity. 2 Publications	1
Mutagenesisⁱ	210	D → A or N: Abolishes the AP endodeoxyribonuclease activity. Reduces protection from granzyme A-mediated cell death; when associated with A-31 and A-65. 1 Publication	1
Mutagenesisⁱ	212	N → A: Abolishes AP endodeoxyribonuclease activity. 1 Publication	1
Mutagenesisⁱ	212	N → Q or D: Decreases AP endodeoxyribonuclease activity. 1 Publication	1
Mutagenesisⁱ	266	F → A: Strongly reduces AP endodeoxyribonuclease activity. 1 Publication	1
Mutagenesisⁱ	283	D → A: Strongly reduces AP endodeoxyribonuclease activity, but does not affect RNA cleavage activity. Nearly abolishes AP endodeoxyribonuclease activity; when associated with A-308. 2 Publications	1
Mutagenesisⁱ	296	C → A: Does not abolish the redox activity. 2 Publications	1
Mutagenesisⁱ	299	K → A: Reduces the interaction with TOMM20. Abolishes localization in the mitochondria; when associated with A-301. 1 Publication	1
Mutagenesisⁱ	301	R → A: Reduces the interaction with TOMM20. Abolishes localization in the mitochondria; when associated with A-299. 1 Publication	1
Mutagenesisⁱ	303	K → A: Reduces the interaction with TOMM20. 1 Publication	1
Mutagenesisⁱ	308	D → A: Reduces AP endodeoxyribonuclease activity. Nearly abolishes AP endodeoxyribonuclease activity; when associated with A-283. 2 Publications	1
Mutagenesisⁱ	309	H → N or S: Abolishes AP endodeoxyribonuclease activity. Lacks MYC CRD RNA cleavage activity. 3 Publications	1
Mutagenesisⁱ	310	C → A: Does not abolish the redox activity. 2 Publications	1
Mutagenesisⁱ	310	C → S: Does not abolish NO-induced nitrosylation. Abolishes NO-induced nitrosylation and translocation from the nucleus to the cytoplasm; when associated with S-93. 2 Publications	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	328
Open Targets More...OpenTargetsⁱ	ENSG00000100823
PharmGKBⁱ	PA201059

Chemistry databases

ChEMBLⁱ	CHEMBL5619
Drug and drug target database More...DrugBankⁱ	DB04967 Lucanthone

Polymorphism and mutation databases

BioMutaⁱ	APEX1
DMDMⁱ	113984

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Length
Initiator methionineⁱ		Removed2 Publications
ChainⁱPRO_0000200010	2 – 318	DNA-(apurinic or apyrimidinic site) lyaseAdd BLAST	317
ChainⁱPRO_0000402572	32 – 318	DNA-(apurinic or apyrimidinic site) lyase, mitochondrialBy similarityAdd BLAST	287

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	6	N6-acetyllysine; by EP3001 Publication	1
Modified residueⁱ	7	N6-acetyllysine; by EP3001 Publication	1
Modified residueⁱ	27	N6-acetyllysine1 Publication	1
Modified residueⁱ	31	N6-acetyllysine1 Publication	1
Modified residueⁱ	32	N6-acetyllysine1 Publication	1
Modified residueⁱ	35	N6-acetyllysine1 Publication	1
Modified residueⁱ	54	PhosphoserineCombined sources	1
Disulfide bondⁱ	65 ↔ 93	AlternateCurated
Modified residueⁱ	65	S-nitrosocysteine; alternate1 Publication	1
Modified residueⁱ	93	S-nitrosocysteine; alternate1 Publication	1
Modified residueⁱ	197	N6-acetyllysineCombined sources	1
Modified residueⁱ	233	Phosphothreonine; by CDK5By similarity	1
Modified residueⁱ	310	S-nitrosocysteine1 Publication	1

Post-translational modificationⁱ

Phosphorylated. Phosphorylation by kinase PKC or casein kinase CK2 results in enhanced redox activity that stimulates binding of the FOS/JUN AP-1 complex to its cognate binding site. AP-endodeoxyribonuclease activity is not affected by CK2-mediated phosphorylation. Phosphorylation of Thr-233 by CDK5 reduces AP-endodeoxyribonuclease activity resulting in accumulation of DNA damage and contributing to neuronal death.2 Publications

Acetylated on Lys-6 and Lys-7. Acetylation is increased by the transcriptional coactivator EP300 acetyltransferase, genotoxic agents like H₂O₂ and methyl methanesulfonate (MMS). Acetylation increases its binding affinity to the negative calcium response element (nCaRE) DNA promoter. The acetylated form induces a stronger binding of YBX1 to the Y-box sequence in the MDR1 promoter than the unacetylated form. Deacetylated on lysines. Lys-6 and Lys-7 are deacetylated by SIRT1.2 Publications

Cleaved at Lys-31 by granzyme A to create the mitochondrial form; leading in reduction of binding to DNA, AP endodeoxynuclease activity, redox activation of transcription factors and to enhanced cell death. Cleaved by granzyme K; leading to intracellular ROS accumulation and enhanced cell death after oxidative stress.

Cys-65 and Cys-93 are nitrosylated in response to nitric oxide (NO) and lead to the exposure of the nuclear export signal (NES).1 Publication

Ubiquitinated by MDM2; leading to translocation to the cytoplasm and proteasomal degradation.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	31 – 32	Cleavage; by granzyme A		2

Keywords - PTMⁱ

Acetylation, Cleavage on pair of basic residues, Disulfide bond, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

EPDⁱ	P27695
PaxDbⁱ	P27695
PeptideAtlas More...PeptideAtlasⁱ	P27695
PRIDEⁱ	P27695
ProteomicsDBⁱ	54406
TopDownProteomicsⁱ	P27695

PTM databases

iPTMnetⁱ	P27695
PhosphoSitePlusⁱ	P27695
SwissPalmⁱ	P27695

Miscellaneous databases

PMAP-CutDBⁱ	P27695

PMAP-CutDBⁱ

P27695

Expressionⁱ

Inductionⁱ

Up-regulated in presence of reactive oxygen species (ROS), like bleomycin, H₂O₂ and phenazine methosulfate.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000100823 Expressed in 229 organ(s), highest expression level in embryo
CleanExⁱ	HS_APEX1 HS_HAP1
ExpressionAtlasⁱ	P27695 baseline and differential
Genevisibleⁱ	P27695 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB004294 CAB047307 HPA000956 HPA002564

HPAⁱ

CAB004294
CAB047307
HPA000956
HPA002564

Interactionⁱ

Subunit structureⁱ

Monomer. Homodimer; disulfide-linked. Component of the SET complex, composed of at least APEX1, SET, ANP32A, HMGB2, NME1 and TREX1. Associates with the dimer XRCC5/XRCC6 in a DNA-dependent manner. Interacts with SIRT1; the interaction is increased in the context of genotoxic stress. Interacts with HDAC1, HDAC2 and HDAC3; the interactions are not dependent on the APEX1 acetylation status. Interacts with XRCC1; the interaction is induced by SIRT1 and increased with the APEX1 acetylated form. Interacts with NPM1 (via N-terminal domain); the interaction is RNA-dependent and decreases in hydrogen peroxide-damaged cells. Interacts (via N-terminus) with YBX1 (via C-terminus); the interaction is increased in presence of APEX1 acetylated at Lys-6 and Lys-7. Interacts with HNRNPL; the interaction is DNA-dependent. Interacts (via N-terminus) with KPNA1 and KPNA2. Interacts with TXN; the interaction stimulates the FOS/JUN AP-1 complex DNA-binding activity in a redox-dependent manner. Interacts with GZMA, KRT8, MDM2, POLB, PRDX6, PRPF19, RPLP0, TOMM20 and WDR77. Binds to CDK5.17 Publications

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	309	Interaction with DNA substrate		1

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
EP300	Q09472	8	EBI-1048805,EBI-447295
Rnf4	O88846	2	EBI-1048805,EBI-7258907	From Rattus norvegicus.
SIRT1	Q96EB6	6	EBI-1048805,EBI-1802965

GO - Molecular functionⁱ

NF-kappaB binding Source: Ensembl

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	106825, 92 interactors
CORUMⁱ	P27695
Database of interacting proteins More...DIPⁱ	DIP-6130N
IntActⁱ	P27695, 42 interactors
Molecular INTeraction database More...MINTⁱ	P27695
STRINGⁱ	9606.ENSP00000216714

Chemistry databases

BindingDBⁱ

P27695

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	62 – 68	Combined sources	7
Helixⁱ	72 – 77	Combined sources	6
Helixⁱ	80 – 87	Combined sources	8
Beta strandⁱ	90 – 95	Combined sources	6
Helixⁱ	101 – 103	Combined sources	3
Helixⁱ	106 – 110	Combined sources	5
Helixⁱ	112 – 114	Combined sources	3
Beta strandⁱ	116 – 120	Combined sources	5
Beta strandⁱ	123 – 125	Combined sources	3
Beta strandⁱ	127 – 129	Combined sources	3
Beta strandⁱ	131 – 137	Combined sources	7
Beta strandⁱ	140 – 145	Combined sources	6
Helixⁱ	149 – 151	Combined sources	3
Beta strandⁱ	152 – 154	Combined sources	3
Beta strandⁱ	157 – 161	Combined sources	5
Beta strandⁱ	166 – 171	Combined sources	6
Helixⁱ	177 – 179	Combined sources	3
Helixⁱ	182 – 200	Combined sources	19
Beta strandⁱ	205 – 210	Combined sources	6
Helixⁱ	217 – 219	Combined sources	3
Turnⁱ	224 – 228	Combined sources	5
Turnⁱ	230 – 232	Combined sources	3
Helixⁱ	234 – 246	Combined sources	13
Beta strandⁱ	249 – 251	Combined sources	3
Helixⁱ	252 – 256	Combined sources	5
Beta strandⁱ	257 – 259	Combined sources	3
Helixⁱ	270 – 272	Combined sources	3
Helixⁱ	273 – 276	Combined sources	4
Beta strandⁱ	283 – 287	Combined sources	5
Helixⁱ	289 – 294	Combined sources	6
Beta strandⁱ	295 – 300	Combined sources	6
Beta strandⁱ	306 – 309	Combined sources	4
Beta strandⁱ	312 – 316	Combined sources	5

Show more details

3D structure databases

Database of protein disorder More...DisProtⁱ	DP00007
ProteinModelPortalⁱ	P27695
SMRⁱ	P27695
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P27695

EvolutionaryTraceⁱ

P27695

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	2 – 33	Necessary for interaction with YBX1, binding to RNA, NPM1-dependent association with rRNA, endoribonuclease activity on abasic RNA and localization in the nucleoli1 PublicationAdd BLAST	32
Regionⁱ	23 – 33	Necessary for interaction with NPM1 and for efficient rRNA bindingAdd BLAST	11
Regionⁱ	289 – 318	Mitochondrial targeting sequence (MTS)Add BLAST	30

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	8 – 13	Nuclear localization signal (NLS)		6
Motifⁱ	64 – 80	Nuclear export signal (NES)Add BLAST		17

Domainⁱ

The N-terminus contains the redox activity while the C-terminus exerts the DNA AP-endodeoxyribonuclease activity; both function are independent in their actions. An unconventional mitochondrial targeting sequence (MTS) is harbored within the C-terminus, that appears to be masked by the N-terminal sequence containing the nuclear localization signal (NLS), that probably blocks the interaction between the MTS and Tom proteins.

Sequence similaritiesⁱ

Belongs to the DNA repair enzymes AP/ExoA family.Curated

Phylogenomic databases

eggNOGⁱ	KOG1294 Eukaryota COG0708 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00530000063540
HOGENOMⁱ	HOG000034586
HOVERGENⁱ	HBG050531
InParanoidⁱ	P27695
KEGG Orthology (KO) More...KOⁱ	K10771
OMAⁱ	GTAVFTK
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0FDG
PhylomeDBⁱ	P27695
TreeFamⁱ	TF315048

Family and domain databases

Gene3Dⁱ	3.60.10.10, 1 hit
InterProⁱ	View protein in InterPro IPR004808 AP_endonuc_1 IPR020847 AP_endonuclease_F1_BS IPR020848 AP_endonuclease_F1_CS IPR036691 Endo/exonu/phosph_ase_sf IPR005135 Endo/exonuclease/phosphatase
PANTHERⁱ	PTHR22748 PTHR22748, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF03372 Exo_endo_phos, 1 hit
SUPFAMⁱ	SSF56219 SSF56219, 1 hit
TIGRFAMsⁱ	TIGR00633 xth, 1 hit
PROSITEⁱ	View protein in PROSITE PS00726 AP_NUCLEASE_F1_1, 1 hit PS00727 AP_NUCLEASE_F1_2, 1 hit PS00728 AP_NUCLEASE_F1_3, 1 hit PS51435 AP_NUCLEASE_F1_4, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

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

This entry has 1 described isoform and 11 potential isoforms that are computationally mapped.Show all Align All

P27695-1 [UniParc]FASTA Add to basket

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        10         20         30         40         50
MPKRGKKGAV AEDGDELRTE PEAKKSKTAA KKNDKEAAGE GPALYEDPPD 
        60         70         80         90        100
QKTSPSGKPA TLKICSWNVD GLRAWIKKKG LDWVKEEAPD ILCLQETKCS 
       110        120        130        140        150
ENKLPAELQE LPGLSHQYWS APSDKEGYSG VGLLSRQCPL KVSYGIGDEE 
       160        170        180        190        200
HDQEGRVIVA EFDSFVLVTA YVPNAGRGLV RLEYRQRWDE AFRKFLKGLA 
       210        220        230        240        250
SRKPLVLCGD LNVAHEEIDL RNPKGNKKNA GFTPQERQGF GELLQAVPLA 
       260        270        280        290        300
DSFRHLYPNT PYAYTFWTYM MNARSKNVGW RLDYFLLSHS LLPALCDSKI 
       310 
RSKALGSDHC PITLYLAL

Length:318

Mass (Da):35,555

Last modified:January 23, 2007 - v2

Checksum:ⁱB88579C01BAF80C6

GO

Computationally mapped potential isoform sequencesⁱ

There are 11 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name	Protein names	Gene names	Length	Annotation

	G3V5Q1	G3V5Q1_HUMAN	DNA-(apurinic or apyrimidinic site)... DNA-(apurinic or apyrimidinic site) lyase, EC 4.2.99.18	APEX1	242	Annotation score:
	G3V3M6	G3V3M6_HUMAN	DNA-(apurinic or apyrimidinic site)... DNA-(apurinic or apyrimidinic site) lyase, EC 4.2.99.18	APEX1	263	Annotation score:
	G3V359	G3V359_HUMAN	DNA-(apurinic or apyrimidinic site)... DNA-(apurinic or apyrimidinic site) lyase, EC 4.2.99.18	APEX1	172	Annotation score:
	G3V5M0	G3V5M0_HUMAN	DNA-(apurinic or apyrimidinic site)... DNA-(apurinic or apyrimidinic site) lyase, EC 4.2.99.18	APEX1	162	Annotation score:
	G3V3C7	G3V3C7_HUMAN	DNA-(apurinic or apyrimidinic site)... DNA-(apurinic or apyrimidinic site) lyase, EC 4.2.99.18	APEX1	174	Annotation score:
	H7C4A8	H7C4A8_HUMAN	DNA-(apurinic or apyrimidinic site)... DNA-(apurinic or apyrimidinic site) lyase, EC 4.2.99.18	APEX1	150	Annotation score:
	A0A0C4DGK8	A0A0C4DGK8_HUMAN	DNA-(apurinic or apyrimidinic site)... DNA-(apurinic or apyrimidinic site) lyase, EC 4.2.99.18	APEX1	146	Annotation score:
	G3V5D9	G3V5D9_HUMAN	DNA-(apurinic or apyrimidinic site)... DNA-(apurinic or apyrimidinic site) lyase	APEX1	107	Annotation score:
	G3V2D9	G3V2D9_HUMAN	DNA-(apurinic or apyrimidinic site)... DNA-(apurinic or apyrimidinic site) lyase	APEX1	49	Annotation score:
	G3V3Y6	G3V3Y6_HUMAN	DNA-(apurinic or apyrimidinic site)... DNA-(apurinic or apyrimidinic site) lyase	APEX1	41	Annotation score:
There is more potential isoformShow all

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	57	G → A in AAA58371 (PubMed:1722334).Curated		1
Sequence conflictⁱ	306	G → A in AAA58371 (PubMed:1722334).Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_013455	51	Q → H1 PublicationCorresponds to variant dbSNP:rs1048945Ensembl.	1
Natural variantⁱVAR_014823	64	I → V1 PublicationCorresponds to variant dbSNP:rs2307486Ensembl.	1
Natural variantⁱVAR_019790	148	D → E2 PublicationsCorresponds to variant dbSNP:rs1130409Ensembl.	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X59764 mRNA Translation: CAA42437.1 M80261 mRNA Translation: AAA58371.1 D90373 mRNA Translation: BAA14381.1 S43127 mRNA Translation: AAB22977.1 M81955 mRNA Translation: AAA58372.1 M92444 Genomic DNA Translation: AAA58629.1 X66133 Genomic DNA Translation: CAA46925.1 D13370 Genomic DNA Translation: BAA02633.1 U79268 mRNA Translation: AAB50212.1 BT007236 mRNA Translation: AAP35900.1 AF488551 Genomic DNA Translation: AAL86909.1 AL355075 Genomic DNA No translation available. BC002338 mRNA Translation: AAH02338.1 BC004979 mRNA Translation: AAH04979.1 BC008145 mRNA Translation: AAH08145.1 BC019291 mRNA Translation: AAH19291.1 M99703 Genomic DNA Translation: AAA58373.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS9550.1
PIRⁱ	S23550
NCBI Reference Sequences More...RefSeqⁱ	NP_001231178.1, NM_001244249.1 NP_001632.2, NM_001641.3 NP_542379.1, NM_080648.2 NP_542380.1, NM_080649.2
UniGeneⁱ	Hs.73722

Genome annotation databases

Ensemblⁱ	ENST00000216714; ENSP00000216714; ENSG00000100823 ENST00000398030; ENSP00000381111; ENSG00000100823 ENST00000555414; ENSP00000451979; ENSG00000100823
GeneIDⁱ	328
KEGGⁱ	hsa:328
UCSC genome browser More...UCSCⁱ	uc058yte.1 human

Keywords - Coding sequence diversityⁱ

Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P27695	DNA-(apurinic or apyrimidinic site) lyase		HUMAN		318	UniRef100_P27695
DNA-(apurinic or apyrimidinic site) lyase (Fragment)		PANTR		146
DNA-(apurinic or apyrimidinic site) lyase (Fragment)		HUMAN		174
DNA-(apurinic or apyrimidinic site) lyase (Fragment)		HUMAN		146
DNA-(apurinic or apyrimidinic site) lyase (Fragment)		HUMAN		263
+6

Protein	Similar proteins		Species	Score	Length	Source
P27695	DNA-(apurinic or apyrimidinic site) lyase		PONPY		318	UniRef90_P27695
DNA-(apurinic or apyrimidinic site) lyase		PANPA		318
DNA-(apurinic or apyrimidinic site) lyase		PANTR		318
DNA-(apurinic or apyrimidinic site) lyase		GORGO		318
DNA-(apurinic or apyrimidinic site) lyase	)	BOVIN		318
+138

Protein	Similar proteins		Species	Score	Length	Source
P27695	DNA-(apurinic or apyrimidinic site) lyase		PANPA		318	UniRef50_P27695
DNA-(apurinic or apyrimidinic site) lyase		PANTR		318
DNA-(apurinic or apyrimidinic site) lyase		GORGO		318
DNA-(apurinic or apyrimidinic site) lyase	)	BOVIN		318
DNA-(apurinic or apyrimidinic site) lyase		PONPY		318
+220

Cross-referencesⁱ

Web resourcesⁱ

NIEHS-SNPs

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X59764 mRNA Translation: CAA42437.1 M80261 mRNA Translation: AAA58371.1 D90373 mRNA Translation: BAA14381.1 S43127 mRNA Translation: AAB22977.1 M81955 mRNA Translation: AAA58372.1 M92444 Genomic DNA Translation: AAA58629.1 X66133 Genomic DNA Translation: CAA46925.1 D13370 Genomic DNA Translation: BAA02633.1 U79268 mRNA Translation: AAB50212.1 BT007236 mRNA Translation: AAP35900.1 AF488551 Genomic DNA Translation: AAL86909.1 AL355075 Genomic DNA No translation available. BC002338 mRNA Translation: AAH02338.1 BC004979 mRNA Translation: AAH04979.1 BC008145 mRNA Translation: AAH08145.1 BC019291 mRNA Translation: AAH19291.1 M99703 Genomic DNA Translation: AAA58373.1
CCDSⁱ	CCDS9550.1
PIRⁱ	S23550
RefSeqⁱ	NP_001231178.1, NM_001244249.1 NP_001632.2, NM_001641.3 NP_542379.1, NM_080648.2 NP_542380.1, NM_080649.2
UniGeneⁱ	Hs.73722

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
	1BIX	X-ray	2.20	A	32-318	[»]
	1CQG	NMR	-	B	59-71	[»]
	1CQH	NMR	-	B	59-71	[»]
	1DE8	X-ray	2.95	A/B	43-318	[»]
	1DE9	X-ray	3.00	A/B	43-318	[»]
	1DEW	X-ray	2.65	A/B	40-318	[»]
	1E9N	X-ray	2.20	A/B	2-318	[»]
	1HD7	X-ray	1.95	A	2-318	[»]
	2ISI	X-ray	2.76	A/B/C	2-318	[»]
	2O3H	X-ray	1.90	A	40-318	[»]
	3U8U	X-ray	2.15	A/B/C/D/E/F	1-318	[»]
	4IEM	X-ray	2.39	A/B/C/D	2-318	[»]
	4LND	X-ray	1.92	A/B/C	39-318	[»]
	4QH9	X-ray	2.18	A	38-318	[»]
	4QHD	X-ray	1.65	A	38-318	[»]
	4QHE	X-ray	1.40	A	38-318	[»]
	5CFG	X-ray	1.80	A	44-318	[»]
	5DFF	X-ray	1.57	A/B	43-318	[»]
	5DFH	X-ray	1.95	A/B	43-318	[»]
	5DFI	X-ray	1.63	A/B	43-318	[»]
	5DFJ	X-ray	1.85	A/B	43-318	[»]
	5DG0	X-ray	1.80	A/B	43-318	[»]
	5WN0	X-ray	2.60	A/B	43-318	[»]
	5WN1	X-ray	2.30	A/B	43-318	[»]
	5WN2	X-ray	2.29	A/B	43-318	[»]
	5WN3	X-ray	2.00	A/B	43-318	[»]
	5WN4	X-ray	2.10	A/B	43-318	[»]
	5WN5	X-ray	2.20	A/B	43-318	[»]
	6BOQ	X-ray	1.96	A/B	1-318	[»]
	6BOR	X-ray	1.84	A/B	1-318	[»]
	6BOS	X-ray	2.30	A/B	1-318	[»]
	6BOT	X-ray	2.30	A/B	1-318	[»]
	6BOU	X-ray	2.54	A/B	1-318	[»]
	6BOV	X-ray	1.98	A/B	1-318	[»]
	6BOW	X-ray	1.59	A/B	1-318	[»]
DisProtⁱ	DP00007
ProteinModelPortalⁱ	P27695
SMRⁱ	P27695
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	106825, 92 interactors
CORUMⁱ	P27695
DIPⁱ	DIP-6130N
IntActⁱ	P27695, 42 interactors
MINTⁱ	P27695
STRINGⁱ	9606.ENSP00000216714

Chemistry databases

BindingDBⁱ	P27695
ChEMBLⁱ	CHEMBL5619
DrugBankⁱ	DB04967 Lucanthone

PTM databases

iPTMnetⁱ	P27695
PhosphoSitePlusⁱ	P27695
SwissPalmⁱ	P27695

Polymorphism and mutation databases

BioMutaⁱ	APEX1
DMDMⁱ	113984

Proteomic databases

EPDⁱ	P27695
PaxDbⁱ	P27695
PeptideAtlasⁱ	P27695
PRIDEⁱ	P27695
ProteomicsDBⁱ	54406
TopDownProteomicsⁱ	P27695

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	328
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000216714; ENSP00000216714; ENSG00000100823 ENST00000398030; ENSP00000381111; ENSG00000100823 ENST00000555414; ENSP00000451979; ENSG00000100823
GeneIDⁱ	328
KEGGⁱ	hsa:328
UCSCⁱ	uc058yte.1 human

Organism-specific databases

CTDⁱ	328
DisGeNETⁱ	328
EuPathDBⁱ	HostDB:ENSG00000100823.11
GeneCardsⁱ	APEX1
HGNCⁱ	HGNC:587 APEX1
HPAⁱ	CAB004294 CAB047307 HPA000956 HPA002564
MIMⁱ	107748 gene
neXtProtⁱ	NX_P27695
OpenTargetsⁱ	ENSG00000100823
PharmGKBⁱ	PA201059
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG1294 Eukaryota COG0708 LUCA
GeneTreeⁱ	ENSGT00530000063540
HOGENOMⁱ	HOG000034586
HOVERGENⁱ	HBG050531
InParanoidⁱ	P27695
KOⁱ	K10771
OMAⁱ	GTAVFTK
OrthoDBⁱ	EOG091G0FDG
PhylomeDBⁱ	P27695
TreeFamⁱ	TF315048

Enzyme and pathway databases

BRENDAⁱ	4.2.99.18 2681
Reactomeⁱ	R-HSA-110357 Displacement of DNA glycosylase by APEX1 R-HSA-110362 POLB-Dependent Long Patch Base Excision Repair R-HSA-110373 Resolution of AP sites via the multiple-nucleotide patch replacement pathway R-HSA-5651801 PCNA-Dependent Long Patch Base Excision Repair R-HSA-73930 Abasic sugar-phosphate removal via the single-nucleotide replacement pathway R-HSA-73933 Resolution of Abasic Sites (AP sites)
SIGNORⁱ	P27695

Miscellaneous databases

ChiTaRSⁱ	APEX1 human
EvolutionaryTraceⁱ	P27695
GeneWikiⁱ	APEX1
GenomeRNAiⁱ	328
PMAP-CutDBⁱ	P27695
Protein Ontology More...PROⁱ	PR:P27695
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000100823 Expressed in 229 organ(s), highest expression level in embryo
CleanExⁱ	HS_APEX1 HS_HAP1
ExpressionAtlasⁱ	P27695 baseline and differential
Genevisibleⁱ	P27695 HS

Family and domain databases

Gene3Dⁱ	3.60.10.10, 1 hit
InterProⁱ	View protein in InterPro IPR004808 AP_endonuc_1 IPR020847 AP_endonuclease_F1_BS IPR020848 AP_endonuclease_F1_CS IPR036691 Endo/exonu/phosph_ase_sf IPR005135 Endo/exonuclease/phosphatase
PANTHERⁱ	PTHR22748 PTHR22748, 1 hit
Pfamⁱ	View protein in Pfam PF03372 Exo_endo_phos, 1 hit
SUPFAMⁱ	SSF56219 SSF56219, 1 hit
TIGRFAMsⁱ	TIGR00633 xth, 1 hit
PROSITEⁱ	View protein in PROSITE PS00726 AP_NUCLEASE_F1_1, 1 hit PS00727 AP_NUCLEASE_F1_2, 1 hit PS00728 AP_NUCLEASE_F1_3, 1 hit PS51435 AP_NUCLEASE_F1_4, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	APEX1_HUMAN
Accessionⁱ	P27695Primary (citable) accession number: P27695 Secondary accession number(s): Q969L5, Q99775
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
	Last sequence update:	January 23, 2007
	Last modified:	December 5, 2018
	This is version 228 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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
Human chromosome 14
Human chromosome 14: entries, gene names and cross-references to MIM
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

UniProtKB

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Help

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UniProtKB - P27695 (APEX1_HUMAN)

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DNA-(apurinic or apyrimidinic site) lyase

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

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

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

Endoplasmic reticulum

Nucleus

Other locations

Mitochondrion

Cytoskeleton

Endoplasmic reticulum

Mitochondrion

Nucleus

Other locations

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

Organism-specific databases

Chemistry databases

Polymorphism and mutation 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

Amino acid modifications

Sites

Keywords - PTMi

Proteomic databases

PTM databases

Miscellaneous 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

Gene expression databases

Organism-specific 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

GO - Molecular functioni

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

Region

Motif

<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

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

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Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ