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Q8IW19

- APLF_HUMAN

UniProt

Q8IW19 - APLF_HUMAN

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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

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

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. regulation of isotype switching Source: Ensembl
  7. single strand break repair Source: UniProtKB
Complete GO annotation...

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. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB
  3. site of double-strand break Source: MGI
Complete GO annotation...

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

BgeeiQ8IW19.
CleanExiHS_APLF.
ExpressionAtlasiQ8IW19. baseline and differential.
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. 30 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 – 3744Combined sources
Turni380 – 3834Combined sources
Helixi392 – 3954Combined sources
Turni412 – 4143Combined sources
Helixi424 – 4263Combined sources
Helixi432 – 4376Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000010591.
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

        10         20         30         40         50
MSGGFELQPR DGGPRVALAP GETVIGRGPL LGITDKRVSR RHAILEVAGG
60 70 80 90 100
QLRIKPIHTN PCFYQSSEKS QLLPLKPNLW CYLNPGDSFS LLVDKYIFRI
110 120 130 140 150
LSIPSEVEMQ CTLRNSQVLD EDNILNETPK SPVINLPHET TGASQLEGST
160 170 180 190 200
EIAKTQMTPT NSVSFLGENR DCNKQQPILA ERKRILPTWM LAEHLSDQNL
210 220 230 240 250
SVPAISGGNV IQGSGKEEIC KDKSQLNTTQ QGRRQLISSG SSENTSAEQD
260 270 280 290 300
TGEECKNTDQ EESTISSKEM PQSFSAITLS NTEMNNIKTN AQRNKLPIEE
310 320 330 340 350
LGKVSKHKIA TKRTPHKEDE AMSCSENCSS AQGDSLQDES QGSHSESSSN
360 370 380 390 400
PSNPETLHAK ATDSVLQGSE GNKVKRTSCM YGANCYRKNP VHFQHFSHPG
410 420 430 440 450
DSDYGGVQIV GQDETDDRPE CPYGPSCYRK NPQHKIEYRH NTLPVRNVLD
460 470 480 490 500
EDNDNVGQPN EYDLNDSFLD DEEEDYEPTD EDSDWEPGKE DEEKEDVEEL
510
LKEAKRFMKR K
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 30 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.
GeneTreei ENSGT00390000010591.
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

Bgeei Q8IW19.
CleanExi HS_APLF.
ExpressionAtlasi Q8IW19. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 100 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