Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Aprataxin

Gene

Aptx

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

DNA-binding protein involved in single-strand DNA break repair, double-strand DNA break repair and base excision repair. Resolves abortive DNA ligation intermediates formed either at base excision sites, or when DNA ligases attempt to repair non-ligatable breaks induced by reactive oxygen species. Catalyzes the release of adenylate groups covalently linked to 5'-phosphate termini, resulting in the production of 5'-phosphate termini that can be efficiently rejoined. Also able to hydrolyze adenosine 5'-monophosphoramidate (AMP-NH2) and diadenosine tetraphosphate (AppppA), but with lower catalytic activity (By similarity). Likewise, catalyzes the release of 3'-linked guanosine (DNAppG) and inosine (DNAppI) from DNA, but has higher specific activity with 5'-linked adenosine (AppDNA) (By similarity).By similarity

Catalytic activityi

Adenosine-5'-diphospho-5'-(DNA) + H2O = AMP + phospho-5'-(DNA).By similarity
Adenosine-5'-diphospho-5'-(ribonucleotide)-(DNA) + H2O = AMP + 5'-phospho-(ribonucleotide)-(DNA).By similarity
(DNA)-3'-diphospho-5'-guanosine + H2O = (DNA)-3'-phosphate + GMP.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei247Tele-AMP-histidine intermediateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri304 – 326C2H2-typePROSITE-ProRule annotationAdd BLAST23

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, Hydrolase
Biological processDNA damage, DNA repair
LigandMetal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Aprataxin (EC:3.1.11.7By similarity, EC:3.1.12.2By similarity)
Alternative name(s):
Forkhead-associated domain histidine triad-like protein
Short name:
FHA-HIT
Gene namesi
Name:Aptx
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi628740. Aptx.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001098421 – 329AprataxinAdd BLAST329

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei120PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ8K4H4.
PRIDEiQ8K4H4.

PTM databases

PhosphoSitePlusiQ8K4H4.

Expressioni

Gene expression databases

BgeeiENSRNOG00000006582.
GenevisibleiQ8K4H4. RN.

Interactioni

Subunit structurei

Interacts with single-strand break repair proteins XRCC1, XRCC4, ADPRT and p53/TP53. Interacts with NCL. Interacts (via FHA-like domain) with MDC1 (phosphorylated).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei161Interaction with DNA substrateBy similarity1
Sitei238Interaction with DNA substrateBy similarity1
Sitei249Interaction with DNA substrateBy similarity1
Sitei264Interaction with DNA substrateBy similarity1

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000046400.

Structurei

3D structure databases

ProteinModelPortaliQ8K4H4.
SMRiQ8K4H4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini23 – 72FHA-likeAdd BLAST50
Domaini155 – 260HITPROSITE-ProRule annotationAdd BLAST106

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 95Interactions with ADPRT and NCLBy similarityAdd BLAST95
Regioni180 – 184Interaction with DNA substrateBy similarity5
Regioni242 – 243Interaction with DNA substrateBy similarity2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi111 – 115Nuclear localization signalBy similarity5
Motifi245 – 249Histidine triad motifPROSITE-ProRule annotation5

Domaini

The histidine triad, also called HIT motif, forms part of the binding loop for the alpha-phosphate of purine mononucleotide.By similarity
The FHA-like domain mediates interaction with NCL; XRCC1 and XRCC4.By similarity
The HIT domain is required for enzymatic activity.By similarity
The C2H2-type zinc finger mediates DNA-binding.By similarity

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri304 – 326C2H2-typePROSITE-ProRule annotationAdd BLAST23

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0562. Eukaryota.
KOG2134. Eukaryota.
ENOG41102F4. LUCA.
GeneTreeiENSGT00570000079163.
HOGENOMiHOG000248858.
HOVERGENiHBG050555.
InParanoidiQ8K4H4.
KOiK10863.
OMAiTVRDGMP.
PhylomeDBiQ8K4H4.

Family and domain databases

CDDicd00060. FHA. 1 hit.
Gene3Di3.30.428.10. 1 hit.
InterProiView protein in InterPro
IPR026963. Aprataxin.
IPR000253. FHA_dom.
IPR019808. Histidine_triad_CS.
IPR011146. HIT-like.
IPR036265. HIT-like_sf.
IPR008984. SMAD_FHA_dom_sf.
IPR032566. Znf-C2HE.
IPR013087. Znf_C2H2_type.
PANTHERiPTHR12486:SF4. PTHR12486:SF4. 1 hit.
PfamiView protein in Pfam
PF16278. zf-C2HE. 1 hit.
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF54197. SSF54197. 1 hit.
PROSITEiView protein in PROSITE
PS00892. HIT_1. 1 hit.
PS51084. HIT_2. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8K4H4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVCWLVRQD CWHQRIKLPH LEAVVIGRSP ETKITDKKCS RQQVQLKAEC
60 70 80 90 100
NKRYVNVKQM GVNPTSIDEV VIGKDREMKL LPGQVLHMVN ELYPYMVEFE
110 120 130 140 150
EVAESPNVTQ RKRKRPDCDS QEMEAEAGAS PSQCSVSPKT GKHGAAKEES
160 170 180 190 200
LGHWSQGLKI SMKDPKMQVY KDDQVVVIKD KYPKARHHWL VLPWASISSL
210 220 230 240 250
KVVTSEHLEL LKHMHAVGEK VIADFTGSSK LRFRLGYHAI PSMSHVHLHV
260 270 280 290 300
ISQDFDSPCL KNKKHWNSFN TEYFLESQAV IKMVQEAGRV TVKDGTCELL
310 320
KLPLRCHECQ QLLPSIPQLK EHLRKHWGG
Length:329
Mass (Da):37,720
Last modified:October 1, 2002 - v1
Checksum:i636B827F661B14FD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF398235 mRNA. Translation: AAM90583.1.
BC078716 mRNA. Translation: AAH78716.1.
RefSeqiNP_683687.1. NM_148889.2.
XP_006238089.1. XM_006238027.3.
XP_006238090.1. XM_006238028.3.
UniGeneiRn.50459.

Genome annotation databases

EnsembliENSRNOT00000046463; ENSRNOP00000046400; ENSRNOG00000006582.
ENSRNOT00000090891; ENSRNOP00000072443; ENSRNOG00000006582.
GeneIDi259271.
KEGGirno:259271.
UCSCiRGD:628740. rat.

Similar proteinsi

Entry informationi

Entry nameiAPTX_RAT
AccessioniPrimary (citable) accession number: Q8K4H4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: October 1, 2002
Last modified: November 22, 2017
This is version 105 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome