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USC-OGP 2-DE database

Two-dimensional polyacrylamide gel electrophoresis database
USC-OGP 2-DE database 
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Searching in 'USC-OGP 2-DE database' for entry matching: P27695




USC-OGP 2-DE database:  P27695

P27695


General information about the entry
View entry in simple text format
Entry nameAPEX1_HUMAN
Primary accession numberP27695
integrated into USC-OGP 2-DE database on January 17, 2017 (release 1)
2D Annotations were last modified onJanuary 17, 2017 (version 1)
General Annotations were last modified on April 5, 2017 (version 2)
Name and origin of the protein
DescriptionRecName: Full=DNA-(apurinic or apyrimidinic site) lyase; EC=3.1.-.-; EC=4.2.99.18; AltName: Full=APEX nuclease; Short=APEN; AltName: Full=Apurinic-apyrimidinic endonuclease 1; Short=AP endonuclease 1; Short=APE-1; AltName: Full=REF-1; AltName: Full=Redox factor-1; Contains: RecName: Full=DNA-(apurinic or apyrimidinic site) lyase, mitochondrial;.
Gene nameName=APEX1
Synonyms=APE, APE1, APEX, APX, HAP1, REF1
Annotated speciesHomo sapiens (Human) [TaxID: 9606]
TaxonomyEukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
References
[1]   2D GEL CHARACTERIZATION
Author 1., Author 2.
Submitted (Mar-2011) to Current
2D PAGE maps for identified proteins
How to interpret a protein

UVEAL_MELANOMA_3-10 {UVEAL MELANOMA 3-10}
Homo sapiens (Human)
UVEAL_MELANOMA_3-10
  map experimental info 		 
UVEAL_MELANOMA_3-10

MAP LOCATIONS:
pI=6.93; Mw=22446

Cross-references
UniProtKB/Swiss-ProtP27695; APEX1_HUMAN.



2D PAGE maps for identified proteins
  • How to interpret a protein map
  • You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw.
  • Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly.
  • Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed.



External data extracted from UniProtKB/Swiss-Prot
Extracted from UniProtKB/Swiss-Prot, release: 0.0
Entry nameAPEX1_HUMAN
Primary accession numberP27695
Secondary accession number(s) Q969L5 Q99775
Sequence was last modified on January 23, 2007 (version 2)
Annotations were last modified on March 15, 2017 (version 212)
Name and origin of the protein
DescriptionRecName: Full=DNA-(apurinic or apyrimidinic site) lyase; EC=3.1.-.-; EC=4.2.99.18; AltName: Full=APEX nuclease; Short=APEN; AltName: Full=Apurinic-apyrimidinic endonuclease 1; Short=AP endonuclease 1; Short=APE-1; AltName: Full=REF-1; AltName: Full=Redox factor-1; Contains: RecName: Full=DNA-(apurinic or apyrimidinic site) lyase, mitochondrial;
Gene nameName=APEX1
Synonyms=APE, APE1, APEX, APX, HAP1, REF1
Encoded onName=APEX1; Synonyms=APE, APE1, APEX, APX, HAP1, REF1
Keywords3D-structure; Acetylation; Activator; Cleavage on pair of basic residues; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; DNA damage; DNA recombination; DNA repair; DNA-binding; Endonuclease; Endoplasmic reticulum; Exonuclease; Hydrolase; Lyase; Magnesium; Metal-binding; Mitochondrion; Nuclease; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repressor; RNA-binding; S-nitrosylation; Transcription; Transcription regulation; Ubl conjugation.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLX59764; CAA42437.1; -; mRNA
EMBLM80261; AAA58371.1; -; mRNA
EMBLD90373; BAA14381.1; -; mRNA
EMBLS43127; AAB22977.1; -; mRNA
EMBLM81955; AAA58372.1; -; mRNA
EMBLM92444; AAA58629.1; -; Genomic_DNA
EMBLX66133; CAA46925.1; -; Genomic_DNA
EMBLD13370; BAA02633.1; -; Genomic_DNA
EMBLU79268; AAB50212.1; -; mRNA
EMBLBT007236; AAP35900.1; -; mRNA
EMBLAF488551; AAL86909.1; -; Genomic_DNA
EMBLAL355075; -; NOT_ANNOTATED_CDS; Genomic_DNA
EMBLBC002338; AAH02338.1; -; mRNA
EMBLBC004979; AAH04979.1; -; mRNA
EMBLBC008145; AAH08145.1; -; mRNA
EMBLBC019291; AAH19291.1; -; mRNA
EMBLM99703; AAA58373.1; -; Genomic_DNA
CCDSCCDS9550.1; -; .
PIRS23550; S23550; .
RefSeqNP_001231178.1; NM_001244249.1; .
RefSeqNP_001632.2; NM_001641.3; .
RefSeqNP_542379.1; NM_080648.2; .
RefSeqNP_542380.1; NM_080649.2; .
UniGeneHs.73722; -; .
PDB1BIX; X-ray; 2.20 A; A=32-318
PDB1CQG; NMR; -; B=59-71
PDB1CQH; NMR; -; B=59-71
PDB1DE8; X-ray; 2.95 A; A/B=43-318
PDB1DE9; X-ray; 3.00 A; A/B=43-318
PDB1DEW; X-ray; 2.65 A; A/B=40-318
PDB1E9N; X-ray; 2.20 A; A/B=2-318
PDB1HD7; X-ray; 1.95 A; A=2-318
PDB2ISI; X-ray; 2.76 A; A/B/C=2-318
PDB2O3H; X-ray; 1.90 A; A=40-318
PDB3U8U; X-ray; 2.15 A; A/B/C/D/E/F=1-318
PDB4IEM; X-ray; 2.39 A; A/B/C/D=2-318
PDB4LND; X-ray; 1.92 A; A/B/C=39-318
PDB4QH9; X-ray; 2.18 A; A=38-318
PDB4QHD; X-ray; 1.65 A; A=38-318
PDB4QHE; X-ray; 1.40 A; A=38-318
PDB5CFG; X-ray; 1.80 A; A=44-318
PDB5DFF; X-ray; 1.57 A; A/B=43-318
PDB5DFH; X-ray; 1.95 A; A/B=43-318
PDB5DFI; X-ray; 1.63 A; A/B=43-318
PDB5DFJ; X-ray; 1.85 A; A/B=43-318
PDB5DG0; X-ray; 1.80 A; A/B=43-318
PDBsum1BIX; -; .
PDBsum1CQG; -; .
PDBsum1CQH; -; .
PDBsum1DE8; -; .
PDBsum1DE9; -; .
PDBsum1DEW; -; .
PDBsum1E9N; -; .
PDBsum1HD7; -; .
PDBsum2ISI; -; .
PDBsum2O3H; -; .
PDBsum3U8U; -; .
PDBsum4IEM; -; .
PDBsum4LND; -; .
PDBsum4QH9; -; .
PDBsum4QHD; -; .
PDBsum4QHE; -; .
PDBsum5CFG; -; .
PDBsum5DFF; -; .
PDBsum5DFH; -; .
PDBsum5DFI; -; .
PDBsum5DFJ; -; .
PDBsum5DG0; -; .
DisProtDP00007; -; .
ProteinModelPortalP27695; -; .
SMRP27695; -; .
BioGrid106825; 86; .
DIPDIP-6130N; -; .
IntActP27695; 37; .
MINTMINT-119189; -; .
STRING9606.ENSP00000216714; -; .
BindingDBP27695; -; .
ChEMBLCHEMBL5619; -; .
DrugBankDB04967; Lucanthone; .
iPTMnetP27695; -; .
PhosphoSitePlusP27695; -; .
SwissPalmP27695; -; .
BioMutaAPEX1; -; .
DMDM113984; -; .
EPDP27695; -; .
PaxDbP27695; -; .
PeptideAtlasP27695; -; .
PRIDEP27695; -; .
TopDownProteomicsP27695; -; .
DNASU328; -; .
EnsemblENST00000216714; ENSP00000216714; ENSG00000100823; .
EnsemblENST00000398030; ENSP00000381111; ENSG00000100823; .
EnsemblENST00000555414; ENSP00000451979; ENSG00000100823; .
GeneID328; -; .
KEGGhsa:328; -; .
UCSCuc058yte.1; human; .
CTD328; -; .
DisGeNET328; -; .
GeneCardsAPEX1; -; .
HGNCHGNC:587; APEX1; .
HPACAB004294; -; .
HPACAB047307; -; .
HPAHPA000956; -; .
HPAHPA002564; -; .
MalaCardsAPEX1; -; .
MIM107748; gene; .
neXtProtNX_P27695; -; .
OpenTargetsENSG00000100823; -; .
PharmGKBPA201059; -; .
eggNOGKOG1294; Eukaryota; .
eggNOGCOG0708; LUCA; .
GeneTreeENSGT00530000063540; -; .
HOGENOMHOG000034586; -; .
HOVERGENHBG050531; -; .
InParanoidP27695; -; .
KOK10771; -; .
OMAYTPNSQQ; -; .
OrthoDBEOG091G0FDG; -; .
PhylomeDBP27695; -; .
TreeFamTF315048; -; .
BRENDA4.2.99.18; 2681; .
ReactomeR-HSA-110357; Displacement of DNA glycosylase by APEX1; .
ReactomeR-HSA-110362; POLB-Dependent Long Patch Base Excision Repair; .
ReactomeR-HSA-110373; Resolution of AP sites via the multiple-nucleotide patch replacement pathway; .
ReactomeR-HSA-5651801; PCNA-Dependent Long Patch Base Excision Repair; .
ReactomeR-HSA-73930; Abasic sugar-phosphate removal via the single-nucleotide replacement pathway; .
ReactomeR-HSA-73933; Resolution of Abasic Sites (AP sites); .
SIGNORP27695; -; .
ChiTaRSAPEX1; human; .
EvolutionaryTraceP27695; -; .
GeneWikiAPEX1; -; .
GenomeRNAi328; -; .
PMAP-CutDBP27695; -; .
PROPR:P27695; -; .
ProteomesUP000005640; Chromosome 14; .
BgeeENSG00000100823; -; .
CleanExHS_APEX1; -; .
CleanExHS_HAP1; -; .
ExpressionAtlasP27695; baseline and differential; .
GenevisibleP27695; HS; .
GOGO:0005813; C:centrosome; IDA:HPA; .
GOGO:0005737; C:cytoplasm; IDA:UniProtKB; .
GOGO:0005783; C:endoplasmic reticulum; TAS:UniProtKB; .
GOGO:0005739; C:mitochondrion; IDA:UniProtKB; .
GOGO:0000784; C:nuclear chromosome; telomeric region; IC:BHF-UCL
GOGO:0016607; C:nuclear speck; IDA:UniProtKB; .
GOGO:0005730; C:nucleolus; IDA:UniProtKB; .
GOGO:0005654; C:nucleoplasm; IDA:UniProtKB; .
GOGO:0005634; C:nucleus; IDA:UniProtKB; .
GOGO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB; .
GOGO:0005840; C:ribosome; TAS:UniProtKB; .
GOGO:0005667; C:transcription factor complex; IEA:Ensembl; .
GOGO:0008408; F:3'-5' exonuclease activity; IDA:UniProtKB; .
GOGO:0031490; F:chromatin DNA binding; IDA:UniProtKB; .
GOGO:0003684; F:damaged DNA binding; IDA:UniProtKB; .
GOGO:0003677; F:DNA binding; IDA:UniProtKB; .
GOGO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IDA:UniProtKB; .
GOGO:0008311; F:double-stranded DNA 3'-5' exodeoxyribonuclease activity; IBA:GO_Central; .
GOGO:0008309; F:double-stranded DNA exodeoxyribonuclease activity; IDA:BHF-UCL; .
GOGO:0003691; F:double-stranded telomeric DNA binding; IDA:BHF-UCL; .
GOGO:0004520; F:endodeoxyribonuclease activity; TAS:Reactome; .
GOGO:0004519; F:endonuclease activity; IDA:MGI; .
GOGO:0046872; F:metal ion binding; IDA:UniProtKB; .
GOGO:0016491; F:oxidoreductase activity; IDA:UniProtKB; .
GOGO:0004528; F:phosphodiesterase I activity; TAS:UniProtKB; .
GOGO:0008081; F:phosphoric diester hydrolase activity; IDA:UniProtKB; .
GOGO:0003723; F:RNA binding; IDA:UniProtKB; .
GOGO:0004523; F:RNA-DNA hybrid ribonuclease activity; TAS:UniProtKB; .
GOGO:0016890; F:site-specific endodeoxyribonuclease activity; specific for altered base; IDA:UniProtKB
GOGO:0003713; F:transcription coactivator activity; IDA:UniProtKB; .
GOGO:0003714; F:transcription corepressor activity; TAS:ProtInc; .
GOGO:0004844; F:uracil DNA N-glycosylase activity; TAS:ProtInc; .
GOGO:0007568; P:aging; IEA:Ensembl; .
GOGO:0006284; P:base-excision repair; IDA:BHF-UCL; .
GOGO:0006286; P:base-excision repair; base-free sugar-phosphate removal; TAS:Reactome
GOGO:0045454; P:cell redox homeostasis; IEA:Ensembl; .
GOGO:0071320; P:cellular response to cAMP; IEA:Ensembl; .
GOGO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl; .
GOGO:0071375; P:cellular response to peptide hormone stimulus; IEA:Ensembl; .
GOGO:0080111; P:DNA demethylation; IDA:UniProtKB; .
GOGO:0006310; P:DNA recombination; IEA:UniProtKB-KW; .
GOGO:0006281; P:DNA repair; IDA:UniProtKB; .
GOGO:0014912; P:negative regulation of smooth muscle cell migration; IEA:Ensembl; .
GOGO:0045739; P:positive regulation of DNA repair; IDA:UniProtKB; .
GOGO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl; .
GOGO:0043488; P:regulation of mRNA stability; IMP:UniProtKB; .
GOGO:0006355; P:regulation of transcription; DNA-templated; IEA:UniProtKB-KW
GOGO:0042493; P:response to drug; IEA:Ensembl; .
GOGO:0000723; P:telomere maintenance; IDA:BHF-UCL; .
GOGO:0006351; P:transcription; DNA-templated; IEA:UniProtKB-KW
Gene3D3.60.10.10; -; 1; .
InterProIPR004808; AP_endonuc_1; .
InterProIPR020847; AP_endonuclease_F1_BS; .
InterProIPR020848; AP_endonuclease_F1_CS; .
InterProIPR005135; Endo/exonuclease/phosphatase; .
PANTHERPTHR22748; PTHR22748; 1; .
PfamPF03372; Exo_endo_phos; 1; .
SUPFAMSSF56219; SSF56219; 1; .
TIGRFAMsTIGR00633; xth; 1; .
PROSITEPS00726; AP_NUCLEASE_F1_1; 1; .
PROSITEPS00727; AP_NUCLEASE_F1_2; 1; .
PROSITEPS00728; AP_NUCLEASE_F1_3; 1; .
PROSITEPS51435; AP_NUCLEASE_F1_4; 1; .


USC-OGP 2-DE database image

Gateways to other related servers

Database constructed and maintained by Angel Garcia, using the Make2D-DB II package (ver. 3.10.2) from the World-2DPAGE Constellation of the ExPASy web server

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