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A0JNH9

- APLF_BOVIN

UniProt

A0JNH9 - APLF_BOVIN

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Protein

Aprataxin and PNK-like factor

Gene

APLF

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript 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 (By similarity).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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei350 – 3501Poly-ADP-riboseBy similarity
Binding sitei355 – 3551Poly-ADP-riboseBy similarity
Binding sitei360 – 3601Poly-ADP-riboseBy similarity
Binding sitei361 – 3611Poly-ADP-riboseBy similarity
Binding sitei397 – 3971Poly-ADP-riboseBy similarity
Binding sitei402 – 4021Poly-ADP-riboseBy similarity
Binding sitei403 – 4031Poly-ADP-riboseBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri351 – 37222PBZ-type 1Add
BLAST
Zinc fingeri393 – 41422PBZ-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. 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
Gene namesi
Name:APLF
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 11

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 (By similarity).By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 485485Aprataxin and PNK-like factorPRO_0000287355Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei92 – 921Phosphoserine; by ATMBy similarity

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 (By similarity).By similarity
Phosphorylated in an ATM-dependent manner upon double-strand DNA break.By similarity

Keywords - PTMi

ADP-ribosylation, Phosphoprotein

Proteomic databases

PRIDEiA0JNH9.

Expressioni

Gene expression databases

ExpressionAtlasiA0JNH9. baseline.

Interactioni

Subunit structurei

Interacts with LIG4, PARP1, XRCC1, XRCC4 and XRCC5.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000042099.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8484FHA-likeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni380 – 39011Flexible linkerBy similarityAdd
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 (By similarity).By similarity
The FHA-like domain mediates interaction with XRCC1 and XRCC4.By similarity

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 fingeri351 – 37222PBZ-type 1Add
BLAST
Zinc fingeri393 – 41422PBZ-type 2Add
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG85452.
GeneTreeiENSGT00390000010591.
HOGENOMiHOG000033995.
HOVERGENiHBG095728.
InParanoidiA0JNH9.
KOiK13295.

Family and domain databases

InterProiIPR008984. 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.

A0JNH9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGGFELQPQ DGGPRVALAP GETVIGRGPL LGLHRNPCYY QSSEKSQLLP
60 70 80 90 100
LKTNIWCWLN PGDHFSLLVD KYIFCVLSTH SEMEMECTLR NSQMLDEDDI
110 120 130 140 150
LNEIPKSSSA DLPDKTPSAP RRERSTETAK PQAAANNMSF IGESRDLSKQ
160 170 180 190 200
QPNPSERKRI LPAWMLTENS SDQNLSVISG GNNVTWESEK ERVCKDKTQV
210 220 230 240 250
NITQPGKKRL ISSGSSESTS AKQDTGKKCK NDDQEESIIS SKEMPQSFSA
260 270 280 290 300
AMLHNTEIDN TKTNPQRSKV PVEALGKVSE HKIITKGSSN EDSTARSCSE
310 320 330 340 350
SYSSTQSKSF CDKPQKSHPE PSSNPPSPEC VQAKATDSVP NGSEENKVQR
360 370 380 390 400
TSCMYGANCY RKNPVHFQHF SHPGDSDYGG VNITCQDEAD DRPECPYGAS
410 420 430 440 450
CYRKNPQHKI EYRHSTFPVR SISDEDDNVG QPNEYNLNDS FIDDEEEEYE
460 470 480
PTDEDSDWEP EKEDLEKEDM EGLLKEAKKF MKRKK
Length:485
Mass (Da):54,326
Last modified:December 12, 2006 - v1
Checksum:iD88D75D4D7C9D456
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC126691 mRNA. Translation: AAI26692.1.
RefSeqiNP_001071342.1. NM_001077874.1.
UniGeneiBt.63859.

Genome annotation databases

EnsembliENSBTAT00000044615; ENSBTAP00000042099; ENSBTAG00000018401.
GeneIDi507989.
KEGGibta:507989.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC126691 mRNA. Translation: AAI26692.1 .
RefSeqi NP_001071342.1. NM_001077874.1.
UniGenei Bt.63859.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000042099.

Proteomic databases

PRIDEi A0JNH9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000044615 ; ENSBTAP00000042099 ; ENSBTAG00000018401 .
GeneIDi 507989.
KEGGi bta:507989.

Organism-specific databases

CTDi 200558.

Phylogenomic databases

eggNOGi NOG85452.
GeneTreei ENSGT00390000010591.
HOGENOMi HOG000033995.
HOVERGENi HBG095728.
InParanoidi A0JNH9.
KOi K13295.

Miscellaneous databases

NextBioi 20868301.

Gene expression databases

ExpressionAtlasi A0JNH9. baseline.

Family and domain databases

InterProi 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. NIH - Mammalian Gene Collection (MGC) project
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Hypothalamus.

Entry informationi

Entry nameiAPLF_BOVIN
AccessioniPrimary (citable) accession number: A0JNH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: December 12, 2006
Last modified: October 29, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3