Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9UBZ4

- APEX2_HUMAN

UniProt

Q9UBZ4 - APEX2_HUMAN

Protein

DNA-(apurinic or apyrimidinic site) lyase 2

Gene

APEX2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Function as a weak 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. Displays also double-stranded DNA 3'-5' exonuclease, 3'-phosphodiesterase activities. Shows robust 3'-5' exonuclease activity on 3'-recessed heteroduplex DNA and is able to remove mismatched nucleotides preferentially. Shows fairly strong 3'-phosphodiesterase activity involved in the removal of 3'-damaged termini formed in DNA by oxidative agents. In the nucleus functions in the PCNA-dependent BER pathway. Required for somatic hypermutation (SHM) and DNA cleavage step of class switch recombination (CSR) of immunoglobulin genes. Required for proper cell cycle progression during proliferation of peripheral lymphocytes.3 Publications

    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

    Cofactori

    Magnesium. Can also utilize manganese. Probably binds two magnesium or manganese ions per subunit By similarity.By similarity

    Enzyme regulationi

    3'-5' exonuclease activity is activated by sodium and manganese. 3'-5' exonuclease and 3'-phosphodiesterase activities are stimulated in presence of PCNA.

    pH dependencei

    Optimum pH is 6.0-8.0.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi8 – 81Magnesium 1By similarity
    Metal bindingi48 – 481Magnesium 1By similarity
    Active sitei156 – 1561By similarity
    Active sitei197 – 1971Proton donor/acceptorBy similarity
    Metal bindingi197 – 1971Magnesium 2By similarity
    Metal bindingi199 – 1991Magnesium 2By similarity
    Sitei199 – 1991Transition state stabilizerBy similarity
    Sitei277 – 2771Important for catalytic activityBy similarity
    Metal bindingi303 – 3031Magnesium 1By similarity
    Sitei304 – 3041Interaction with DNA substrateBy similarity

    GO - Molecular functioni

    1. DNA-(apurinic or apyrimidinic site) lyase activity Source: RefGenome
    2. DNA binding Source: UniProtKB-KW
    3. double-stranded DNA 3'-5' exodeoxyribonuclease activity Source: RefGenome
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. base-excision repair Source: RefGenome
    2. cell cycle Source: UniProtKB-KW
    3. DNA catabolic process, endonucleolytic Source: GOC
    4. DNA catabolic process, exonucleolytic Source: GOC
    5. DNA recombination Source: UniProtKB-KW

    Keywords - Molecular functioni

    Endonuclease, Exonuclease, Hydrolase, Lyase, Nuclease

    Keywords - Biological processi

    Cell cycle, DNA damage, DNA recombination, DNA repair

    Keywords - Ligandi

    DNA-binding, Magnesium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA-(apurinic or apyrimidinic site) lyase 2 (EC:3.1.-.-, EC:4.2.99.18)
    Alternative name(s):
    AP endonuclease XTH2
    APEX nuclease 2
    APEX nuclease-like 2
    Apurinic-apyrimidinic endonuclease 2
    Short name:
    AP endonuclease 2
    Gene namesi
    Name:APEX2
    Synonyms:APE2, APEXL2, XTH2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:17889. APEX2.

    Subcellular locationi

    Nucleus. Cytoplasm. Mitochondrion Curated
    Note: Together with PCNA, is redistributed in discrete nuclear foci in presence of oxidative DNA damaging agents.

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: Ensembl
    2. nucleus Source: RefGenome

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi269 – 2691H → A: Abolishes AP endodeoxyribonuclease, 3'-5' exonuclease activity and 3'-phosphodiesterase activities.
    Mutagenesisi277 – 2771D → A: Abolishes AP endodeoxyribonuclease, 3'-5' exonuclease activity and 3'-phosphodiesterase activities. 1 Publication
    Mutagenesisi396 – 3961Y → A: Reduces 3'-5' exonuclease activity in presence of PCNA. Does not abolish the 3'-5' exonuclease activity. Does only partially redistributes together with PCNA in nuclear foci in presence of oxidative-induced DNA damaging agents. 1 Publication
    Mutagenesisi397 – 3971F → A: Reduces 3'-5' exonuclease activity in presence of PCNA. Does not abolish the 3'-5' exonuclease activity. Does only partially redistributes together with PCNA in nuclear foci in presence of oxidative-induced DNA damaging agents. 1 Publication

    Organism-specific databases

    PharmGKBiPA38474.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 518518DNA-(apurinic or apyrimidinic site) lyase 2PRO_0000200014Add
    BLAST

    Proteomic databases

    MaxQBiQ9UBZ4.
    PaxDbiQ9UBZ4.
    PeptideAtlasiQ9UBZ4.
    PRIDEiQ9UBZ4.

    PTM databases

    PhosphoSiteiQ9UBZ4.

    Expressioni

    Tissue specificityi

    Highly expressed in brain and kidney. Weakly expressed in the fetal brain.1 Publication

    Gene expression databases

    ArrayExpressiQ9UBZ4.
    BgeeiQ9UBZ4.
    CleanExiHS_APEX2.
    GenevestigatoriQ9UBZ4.

    Organism-specific databases

    HPAiHPA030872.

    Interactioni

    Subunit structurei

    Interacts with PCNA; this interaction is triggered by reactive oxygen species and increased by misincorporation of uracil in nuclear DNA.1 Publication

    Protein-protein interaction databases

    BioGridi118124. 13 interactions.
    IntActiQ9UBZ4. 7 interactions.
    MINTiMINT-1439290.
    STRINGi9606.ENSP00000364126.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UBZ4.
    SMRiQ9UBZ4. Positions 1-308.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni390 – 3978Required for the colocalization with PCNA in nuclear foci in presence of oxidative-induced DNA damaging agents

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0708.
    HOGENOMiHOG000231386.
    HOVERGENiHBG054715.
    InParanoidiQ9UBZ4.
    KOiK10772.
    OMAiDHWDAVN.
    OrthoDBiEOG7NKKJZ.
    PhylomeDBiQ9UBZ4.
    TreeFamiTF328442.

    Family and domain databases

    Gene3Di3.60.10.10. 1 hit.
    InterProiIPR004808. AP_endonuc_1.
    IPR020847. AP_endonuclease_F1_BS.
    IPR005135. Endo/exonuclease/phosphatase.
    IPR010666. Znf_GRF.
    [Graphical view]
    PANTHERiPTHR22748. PTHR22748. 1 hit.
    PfamiPF03372. Exo_endo_phos. 1 hit.
    PF06839. zf-GRF. 1 hit.
    [Graphical view]
    SUPFAMiSSF56219. SSF56219. 1 hit.
    TIGRFAMsiTIGR00633. xth. 1 hit.
    PROSITEiPS00726. AP_NUCLEASE_F1_1. 1 hit.
    PS51435. AP_NUCLEASE_F1_4. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9UBZ4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRVVSWNIN GIRRPLQGVA NQEPSNCAAV AVGRILDELD ADIVCLQETK    50
    VTRDALTEPL AIVEGYNSYF SFSRNRSGYS GVATFCKDNA TPVAAEEGLS 100
    GLFATQNGDV GCYGNMDEFT QEELRALDSE GRALLTQHKI RTWEGKEKTL 150
    TLINVYCPHA DPGRPERLVF KMRFYRLLQI RAEALLAAGS HVIILGDLNT 200
    AHRPIDHWDA VNLECFEEDP GRKWMDSLLS NLGCQSASHV GPFIDSYRCF 250
    QPKQEGAFTC WSAVTGARHL NYGSRLDYVL GDRTLVIDTF QASFLLPEVM 300
    GSDHCPVGAV LSVSSVPAKQ CPPLCTRFLP EFAGTQLKIL RFLVPLEQSP 350
    VLEQSTLQHN NQTRVQTCQN KAQVRSTRPQ PSQVGSSRGQ KNLKSYFQPS 400
    PSCPQASPDI ELPSLPLMSA LMTPKTPEEK AVAKVVKGQA KTSEAKDEKE 450
    LRTSFWKSVL AGPLRTPLCG GHREPCVMRT VKKPGPNLGR RFYMCARPRG 500
    PPTDPSSRCN FFLWSRPS 518
    Length:518
    Mass (Da):57,401
    Last modified:May 1, 2000 - v1
    Checksum:i08464806153F8832
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti399 – 3991P → S in AAD43041. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti141 – 1411R → C.1 Publication
    Corresponds to variant rs2301416 [ dbSNP | Ensembl ].
    VAR_023390
    Natural varianti141 – 1411R → W.
    Corresponds to variant rs2301416 [ dbSNP | Ensembl ].
    VAR_048261
    Natural varianti269 – 2691H → Y Identified in a patient with mtDNA maintenance disorders. 1 Publication
    VAR_064033
    Natural varianti392 – 3921N → H Identified in a patient with mtDNA maintenance disorders. 1 Publication
    VAR_064034

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB049211 mRNA. Translation: BAB13764.1.
    AJ011311 mRNA. Translation: CAB45242.1.
    AB021260 mRNA. Translation: BAA78422.1.
    AF119046 mRNA. Translation: AAD43041.1.
    AY884244 Genomic DNA. Translation: AAW56941.1.
    AL020991 Genomic DNA. Translation: CAI43126.1.
    BC002959 mRNA. Translation: AAH02959.1.
    CCDSiCCDS14365.1.
    RefSeqiNP_055296.2. NM_014481.3.
    UniGeneiHs.659558.

    Genome annotation databases

    EnsembliENST00000374987; ENSP00000364126; ENSG00000169188.
    GeneIDi27301.
    KEGGihsa:27301.
    UCSCiuc004dtz.4. human.

    Polymorphism databases

    DMDMi73921676.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB049211 mRNA. Translation: BAB13764.1 .
    AJ011311 mRNA. Translation: CAB45242.1 .
    AB021260 mRNA. Translation: BAA78422.1 .
    AF119046 mRNA. Translation: AAD43041.1 .
    AY884244 Genomic DNA. Translation: AAW56941.1 .
    AL020991 Genomic DNA. Translation: CAI43126.1 .
    BC002959 mRNA. Translation: AAH02959.1 .
    CCDSi CCDS14365.1.
    RefSeqi NP_055296.2. NM_014481.3.
    UniGenei Hs.659558.

    3D structure databases

    ProteinModelPortali Q9UBZ4.
    SMRi Q9UBZ4. Positions 1-308.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118124. 13 interactions.
    IntActi Q9UBZ4. 7 interactions.
    MINTi MINT-1439290.
    STRINGi 9606.ENSP00000364126.

    PTM databases

    PhosphoSitei Q9UBZ4.

    Polymorphism databases

    DMDMi 73921676.

    Proteomic databases

    MaxQBi Q9UBZ4.
    PaxDbi Q9UBZ4.
    PeptideAtlasi Q9UBZ4.
    PRIDEi Q9UBZ4.

    Protocols and materials databases

    DNASUi 27301.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374987 ; ENSP00000364126 ; ENSG00000169188 .
    GeneIDi 27301.
    KEGGi hsa:27301.
    UCSCi uc004dtz.4. human.

    Organism-specific databases

    CTDi 27301.
    GeneCardsi GC0XP055043.
    HGNCi HGNC:17889. APEX2.
    HPAi HPA030872.
    MIMi 300773. gene.
    neXtProti NX_Q9UBZ4.
    PharmGKBi PA38474.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0708.
    HOGENOMi HOG000231386.
    HOVERGENi HBG054715.
    InParanoidi Q9UBZ4.
    KOi K10772.
    OMAi DHWDAVN.
    OrthoDBi EOG7NKKJZ.
    PhylomeDBi Q9UBZ4.
    TreeFami TF328442.

    Miscellaneous databases

    GenomeRNAii 27301.
    NextBioi 50285.
    PROi Q9UBZ4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UBZ4.
    Bgeei Q9UBZ4.
    CleanExi HS_APEX2.
    Genevestigatori Q9UBZ4.

    Family and domain databases

    Gene3Di 3.60.10.10. 1 hit.
    InterProi IPR004808. AP_endonuc_1.
    IPR020847. AP_endonuclease_F1_BS.
    IPR005135. Endo/exonuclease/phosphatase.
    IPR010666. Znf_GRF.
    [Graphical view ]
    PANTHERi PTHR22748. PTHR22748. 1 hit.
    Pfami PF03372. Exo_endo_phos. 1 hit.
    PF06839. zf-GRF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56219. SSF56219. 1 hit.
    TIGRFAMsi TIGR00633. xth. 1 hit.
    PROSITEi PS00726. AP_NUCLEASE_F1_1. 1 hit.
    PS51435. AP_NUCLEASE_F1_4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human APE2 protein is mostly localized in the nuclei and to some extent in the mitochondria, while nuclear APE2 is partly associated with proliferating cell nuclear antigen."
      Tsuchimoto D., Sakai Y., Sakumi K., Nishioka K., Sasaki M., Fujiwara T., Nakabeppu Y.
      Nucleic Acids Res. 29:2349-2360(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PCNA, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Leukemia.
    2. "Putative human AP endonuclease XTH2."
      Luna L., Rognes T., Henriksen A.C., Bjoras M., Seeberg E.
      Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lung tumor.
    3. "cDNA cloning and characterization of human APEX nuclease-like 2 (APEXL2) protein."
      Akiyama K., Sarker A.H., Yao M., Tsutsui K., Seki S.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Bone marrow.
    4. Hadi M.Z., Erzberger J.P., Ramirez M.H., Thelen M.P., Wilson D.M. III
      Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lung tumor.
    5. NIEHS SNPs program
      Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT CYS-141.
    6. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung.
    8. "Human Ape2 protein has a 3'-5' exonuclease activity that acts preferentially on mismatched base pairs."
      Burkovics P., Szukacsov V., Unk I., Haracska L.
      Nucleic Acids Res. 34:2508-2515(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-277.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Role of PCNA-dependent stimulation of 3'-phosphodiesterase and 3'-5' exonuclease activities of human Ape2 in repair of oxidative DNA damage."
      Burkovics P., Hajdu I., Szukacsov V., Unk I., Haracska L.
      Nucleic Acids Res. 37:4247-4255(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-396 AND PHE-397.
    11. "Identification of rare DNA variants in mitochondrial disorders with improved array-based sequencing."
      Wang W., Shen P., Thiyagarajan S., Lin S., Palm C., Horvath R., Klopstock T., Cutler D., Pique L., Schrijver I., Davis R.W., Mindrinos M., Speed T.P., Scharfe C.
      Nucleic Acids Res. 39:44-58(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TYR-269 AND HIS-392.

    Entry informationi

    Entry nameiAPEX2_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBZ4
    Secondary accession number(s): Q9Y5X7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 118 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3