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Q8IW19

- APLF_HUMAN

UniProt

Q8IW19 - APLF_HUMAN

Protein

Aprataxin and PNK-like factor

Gene

APLF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Nuclease involved in single-strand and double-strand DNA break repair. Recruited to sites of DNA damage through interaction with poly(ADP-ribose), a polymeric post-translational modification synthesized transiently at sites of chromosomal damage to accelerate DNA strand break repair reactions. Displays apurinic-apyrimidinic (AP) endonuclease and 3'-5' exonuclease activities in vitro. Also able to introduce nicks at hydroxyuracil and other types of pyrimidine base damage.2 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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei376 – 3761Poly-ADP-ribose
    Binding sitei381 – 3811Poly-ADP-ribose
    Binding sitei386 – 3861Poly-ADP-ribose
    Binding sitei387 – 3871Poly-ADP-ribose
    Binding sitei423 – 4231Poly-ADP-ribose
    Binding sitei428 – 4281Poly-ADP-ribose
    Binding sitei429 – 4291Poly-ADP-ribose

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri377 – 39822PBZ-type 1Add
    BLAST
    Zinc fingeri419 – 44022PBZ-type 2Add
    BLAST

    GO - Molecular functioni

    1. 3'-5' exonuclease activity Source: UniProtKB
    2. DNA-(apurinic or apyrimidinic site) lyase activity Source: UniProtKB
    3. endodeoxyribonuclease activity Source: UniProtKB
    4. metal ion binding Source: UniProtKB-KW
    5. nucleotide binding Source: UniProtKB
    6. protein binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: UniProtKB
    2. DNA catabolic process, endonucleolytic Source: GOC
    3. double-strand break repair Source: UniProtKB
    4. nucleic acid phosphodiester bond hydrolysis Source: GOC
    5. positive regulation of DNA ligation Source: MGI
    6. single strand break repair Source: UniProtKB

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    Metal-binding, Nucleotide-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aprataxin and PNK-like factor (EC:4.2.99.18)
    Alternative name(s):
    Apurinic-apyrimidinic endonuclease APLF
    PNK and APTX-like FHA domain-containing protein
    XRCC1-interacting protein 1
    Gene namesi
    Name:APLF
    Synonyms:C2orf13, PALF, XIP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:28724. APLF.

    Subcellular locationi

    Nucleus. Cytoplasmcytosol
    Note: Localizes to DNA damage sites. Accumulates at single-strand breaks and double-strand breaks via the PBZ-type zinc fingers.

    GO - Cellular componenti

    1. cytosol Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB
    3. site of double-strand break Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi116 – 1161S → A: Decreases phosphorylation by ATM. 1 Publication
    Mutagenesisi376 – 3761R → A: Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-421 and A-427. 1 Publication
    Mutagenesisi379 – 3791C → A: Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-385; A-421 and A-427. 1 Publication
    Mutagenesisi385 – 3851C → A: Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-379; A-421 and A-427. 1 Publication
    Mutagenesisi421 – 4211C → A: Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-379; A-385 and A-427. Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-376 and A-427. 1 Publication
    Mutagenesisi427 – 4271C → A: Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-379; A-385 and A-421. Abolishes poly(ADP-ribose)-binding and poly-ADP-ribosylation by PARP1; when associated with A-376 and A-421. 1 Publication

    Organism-specific databases

    PharmGKBiPA164715842.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 511511Aprataxin and PNK-like factorPRO_0000089342Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei116 – 1161Phosphoserine; by ATM1 Publication

    Post-translational modificationi

    Poly-ADP-ribosylated. In addition to binding non covalently poly(ADP-ribose) via its PBZ-type zinc fingers, the protein is also covalently poly-ADP-ribosylated by PARP1.
    Phosphorylated in an ATM-dependent manner upon double-strand DNA break.3 Publications

    Keywords - PTMi

    ADP-ribosylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8IW19.
    PaxDbiQ8IW19.
    PRIDEiQ8IW19.

    PTM databases

    PhosphoSiteiQ8IW19.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8IW19.
    BgeeiQ8IW19.
    CleanExiHS_APLF.
    GenevestigatoriQ8IW19.

    Organism-specific databases

    HPAiHPA034642.
    HPA034643.

    Interactioni

    Subunit structurei

    Interacts with LIG4, PARP1, XRCC1, XRCC4 and XRCC5.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LIG4P499172EBI-1256044,EBI-847896
    PARP1P098743EBI-1256044,EBI-355676
    XRCC1P1888710EBI-1256044,EBI-947466
    XRCC4Q134264EBI-1256044,EBI-717592
    XRCC5P1301012EBI-1256044,EBI-357997

    Protein-protein interaction databases

    BioGridi128334. 8 interactions.
    DIPiDIP-39136N.
    IntActiQ8IW19. 14 interactions.
    MINTiMINT-3037419.
    STRINGi9606.ENSP00000307004.

    Structurei

    Secondary structure

    1
    511
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi371 – 3744
    Turni380 – 3834
    Helixi392 – 3954
    Turni412 – 4143
    Helixi424 – 4263
    Helixi432 – 4376

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KQBNMR-A368-451[»]
    2KQCNMR-A368-451[»]
    2KQDNMR-A368-451[»]
    2KQENMR-A368-451[»]
    2KUONMR-A360-448[»]
    ProteinModelPortaliQ8IW19.
    SMRiQ8IW19. Positions 359-451.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8IW19.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 108108FHA-likeAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni406 – 41611Flexible linkerAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili487 – 51125Sequence AnalysisAdd
    BLAST

    Domaini

    The PBZ-type zinc fingers (also named CYR) mediate non-covalent poly(ADP-ribose)-binding. Poly(ADP-ribose)-binding is dependent on the presence of zinc and promotes its recruitment to DNA damage sites.1 Publication
    The FHA-like domain mediates interaction with XRCC1 and XRCC4.1 Publication

    Sequence similaritiesi

    Belongs to the APLF family.Curated
    Contains 1 FHA-like domain.Curated
    Contains 2 PBZ-type zinc fingers.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri377 – 39822PBZ-type 1Add
    BLAST
    Zinc fingeri419 – 44022PBZ-type 2Add
    BLAST

    Keywords - Domaini

    Coiled coil, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG85452.
    HOGENOMiHOG000033995.
    HOVERGENiHBG095728.
    InParanoidiQ8IW19.
    KOiK13295.
    OMAiHIINCES.
    OrthoDBiEOG73805W.
    PhylomeDBiQ8IW19.
    TreeFamiTF326160.

    Family and domain databases

    Gene3Di2.60.200.20. 1 hit.
    InterProiIPR000253. FHA_dom.
    IPR008984. SMAD_FHA_domain.
    IPR019406. Znf_C2H2_APLF-like.
    [Graphical view]
    PfamiPF10283. zf-CCHH. 2 hits.
    [Graphical view]
    SUPFAMiSSF49879. SSF49879. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q8IW19-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGGFELQPR DGGPRVALAP GETVIGRGPL LGITDKRVSR RHAILEVAGG    50
    QLRIKPIHTN PCFYQSSEKS QLLPLKPNLW CYLNPGDSFS LLVDKYIFRI 100
    LSIPSEVEMQ CTLRNSQVLD EDNILNETPK SPVINLPHET TGASQLEGST 150
    EIAKTQMTPT NSVSFLGENR DCNKQQPILA ERKRILPTWM LAEHLSDQNL 200
    SVPAISGGNV IQGSGKEEIC KDKSQLNTTQ QGRRQLISSG SSENTSAEQD 250
    TGEECKNTDQ EESTISSKEM PQSFSAITLS NTEMNNIKTN AQRNKLPIEE 300
    LGKVSKHKIA TKRTPHKEDE AMSCSENCSS AQGDSLQDES QGSHSESSSN 350
    PSNPETLHAK ATDSVLQGSE GNKVKRTSCM YGANCYRKNP VHFQHFSHPG 400
    DSDYGGVQIV GQDETDDRPE CPYGPSCYRK NPQHKIEYRH NTLPVRNVLD 450
    EDNDNVGQPN EYDLNDSFLD DEEEDYEPTD EDSDWEPGKE DEEKEDVEEL 500
    LKEAKRFMKR K 511
    Length:511
    Mass (Da):56,956
    Last modified:March 1, 2003 - v1
    Checksum:iCBBF0096843298DA
    GO

    Sequence cautioni

    The sequence AAY14945.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti313 – 3131Missing in BAF83530. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti100 – 1001I → V.
    Corresponds to variant rs11902811 [ dbSNP | Ensembl ].
    VAR_032299
    Natural varianti224 – 2241S → T.
    Corresponds to variant rs35002937 [ dbSNP | Ensembl ].
    VAR_061557
    Natural varianti336 – 3361L → F.
    Corresponds to variant rs13404469 [ dbSNP | Ensembl ].
    VAR_032300

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK290841 mRNA. Translation: BAF83530.1.
    AC105054 Genomic DNA. Translation: AAY24113.1.
    AC127383 Genomic DNA. Translation: AAY24008.1.
    AC130709 Genomic DNA. Translation: AAY14945.1. Different initiation.
    BC041144 mRNA. Translation: AAH41144.1.
    CCDSiCCDS1888.1.
    RefSeqiNP_775816.1. NM_173545.2.
    UniGeneiHs.720369.

    Genome annotation databases

    EnsembliENST00000303795; ENSP00000307004; ENSG00000169621.
    GeneIDi200558.
    KEGGihsa:200558.
    UCSCiuc002sep.3. human.

    Polymorphism databases

    DMDMi73619699.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK290841 mRNA. Translation: BAF83530.1 .
    AC105054 Genomic DNA. Translation: AAY24113.1 .
    AC127383 Genomic DNA. Translation: AAY24008.1 .
    AC130709 Genomic DNA. Translation: AAY14945.1 . Different initiation.
    BC041144 mRNA. Translation: AAH41144.1 .
    CCDSi CCDS1888.1.
    RefSeqi NP_775816.1. NM_173545.2.
    UniGenei Hs.720369.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KQB NMR - A 368-451 [» ]
    2KQC NMR - A 368-451 [» ]
    2KQD NMR - A 368-451 [» ]
    2KQE NMR - A 368-451 [» ]
    2KUO NMR - A 360-448 [» ]
    ProteinModelPortali Q8IW19.
    SMRi Q8IW19. Positions 359-451.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 128334. 8 interactions.
    DIPi DIP-39136N.
    IntActi Q8IW19. 14 interactions.
    MINTi MINT-3037419.
    STRINGi 9606.ENSP00000307004.

    PTM databases

    PhosphoSitei Q8IW19.

    Polymorphism databases

    DMDMi 73619699.

    Proteomic databases

    MaxQBi Q8IW19.
    PaxDbi Q8IW19.
    PRIDEi Q8IW19.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000303795 ; ENSP00000307004 ; ENSG00000169621 .
    GeneIDi 200558.
    KEGGi hsa:200558.
    UCSCi uc002sep.3. human.

    Organism-specific databases

    CTDi 200558.
    GeneCardsi GC02P068694.
    HGNCi HGNC:28724. APLF.
    HPAi HPA034642.
    HPA034643.
    MIMi 611035. gene.
    neXtProti NX_Q8IW19.
    PharmGKBi PA164715842.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG85452.
    HOGENOMi HOG000033995.
    HOVERGENi HBG095728.
    InParanoidi Q8IW19.
    KOi K13295.
    OMAi HIINCES.
    OrthoDBi EOG73805W.
    PhylomeDBi Q8IW19.
    TreeFami TF326160.

    Miscellaneous databases

    ChiTaRSi APLF. human.
    EvolutionaryTracei Q8IW19.
    GenomeRNAii 200558.
    NextBioi 89940.
    PROi Q8IW19.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IW19.
    Bgeei Q8IW19.
    CleanExi HS_APLF.
    Genevestigatori Q8IW19.

    Family and domain databases

    Gene3Di 2.60.200.20. 1 hit.
    InterProi IPR000253. FHA_dom.
    IPR008984. SMAD_FHA_domain.
    IPR019406. Znf_C2H2_APLF-like.
    [Graphical view ]
    Pfami PF10283. zf-CCHH. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49879. SSF49879. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Liver.
    2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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: Testis.
    4. "A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses."
      Kanno S., Kuzuoka H., Sasao S., Hong Z., Lan L., Nakajima S., Yasui A.
      EMBO J. 26:2094-2103(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, POLY-ADP-RIBOSYLATION, INTERACTION WITH LIG4; PARP1; XRCC4 AND XRCC5.
    5. "Human Xip1 (C2orf13) is a novel regulator of cellular responses to DNA strand breaks."
      Bekker-Jensen S., Fugger K., Danielsen J.R., Gromova I., Sehested M., Celis J., Bartek J., Lukas J., Mailand N.
      J. Biol. Chem. 282:19638-19643(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH XRCC1, PHOSPHORYLATION AT SER-116, MUTAGENESIS OF SER-116.
    6. "APLF (C2orf13) is a novel human protein involved in the cellular response to chromosomal DNA strand breaks."
      Iles N., Rulten S., El-Khamisy S.F., Caldecott K.W.
      Mol. Cell. Biol. 27:3793-3803(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PARP1; XRCC1; XRCC4 AND XRCC5, SUBCELLULAR LOCATION, PHOSPHORYLATION.
    7. "APLF (C2orf13) facilitates nonhomologous end-joining and undergoes ATM-dependent hyperphosphorylation following ionizing radiation."
      Macrae C.J., McCulloch R.D., Ylanko J., Durocher D., Koch C.A.
      DNA Repair 7:292-302(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH XRCC4, PHOSPHORYLATION.
    8. "APLF (C2orf13) is a novel component of poly(ADP-ribose) signaling in mammalian cells."
      Rulten S.L., Cortes-Ledesma F., Guo L., Iles N.J., Caldecott K.W.
      Mol. Cell. Biol. 28:4620-4628(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, ADP-RIBOSE-BINDING.
    9. "Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins."
      Ahel I., Ahel D., Matsusaka T., Clark A.J., Pines J., Boulton S.J., West S.C.
      Nature 451:81-85(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DOMAIN PBZ-TYPE, POLY-ADP-RIBOSYLATION, ADP-RIBOSE-BINDING, MUTAGENESIS OF ARG-376; CYS-379; CYS-385; CYS-421 AND CYS-427.
    10. "Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose)."
      Eustermann S., Brockmann C., Mehrotra P.V., Yang J.C., Loakes D., West S.C., Ahel I., Neuhaus D.
      Nat. Struct. Mol. Biol. 17:241-243(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 368-451 ALONE AND IN COMPLEX WITH ADP-RIBOSE ANALOG, POLY-ADP-RIBOSE BINDING SITES.
    11. "Structure and identification of ADP-ribose recognition motifs of APLF and role in the DNA damage response."
      Li G.Y., McCulloch R.D., Fenton A.L., Cheung M., Meng L., Ikura M., Koch C.A.
      Proc. Natl. Acad. Sci. U.S.A. 107:9129-9134(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 360-448, LINKER REGION, POLY-ADP-RIBOSE BINDING SITES.

    Entry informationi

    Entry nameiAPLF_HUMAN
    AccessioniPrimary (citable) accession number: Q8IW19
    Secondary accession number(s): A8K476
    , Q53P47, Q53PB9, Q53QU0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2005
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 98 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3