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Protein

Aprataxin

Gene

Aptx

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei247 – 2471Tele-AMP-histidine intermediateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri304 – 32623C2H2-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Aprataxin (EC:3.-.-.-)
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi628740. Aptx.

Subcellular locationi

  • Nucleusnucleoplasm By similarity
  • Nucleusnucleolus By similarity

  • Note: Upon genotoxic stress, colocalizes with XRCC1 at sites of DNA damage. Colocalizes with MDC1 at sites of DNA double-strand breaks. Interaction with NCL is required for nucleolar localization (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 329329AprataxinPRO_0000109842Add
BLAST

Proteomic databases

PRIDEiQ8K4H4.

Expressioni

Gene expression databases

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).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000046400.

Structurei

3D structure databases

ProteinModelPortaliQ8K4H4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 7250FHA-likeAdd
BLAST
Domaini155 – 260106HITPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 9595Interactions with ADPRT and NCLBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi111 – 1155Nuclear localization signalBy similarity
Motifi245 – 2495Histidine triad motif

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

Sequence similaritiesi

Contains 1 C2H2-type zinc finger.PROSITE-ProRule annotation
Contains 1 FHA-like domain.Curated
Contains 1 HIT domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri304 – 32623C2H2-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG278510.
GeneTreeiENSGT00570000079163.
HOGENOMiHOG000248858.
HOVERGENiHBG050555.
InParanoidiQ8K4H4.
KOiK10863.
OMAiPGQVLHM.
OrthoDBiEOG786H3J.
PhylomeDBiQ8K4H4.

Family and domain databases

Gene3Di2.60.200.20. 2 hits.
3.30.428.10. 1 hit.
InterProiIPR026963. Aprataxin.
IPR000253. FHA_dom.
IPR019808. Histidine_triad_CS.
IPR001310. Histidine_triad_HIT.
IPR011146. HIT-like.
IPR008984. SMAD_FHA_domain.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
PANTHERiPTHR12486. PTHR12486. 1 hit.
PTHR12486:SF4. PTHR12486:SF4. 1 hit.
SMARTiSM00355. ZnF_C2H2. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF54197. SSF54197. 1 hit.
PROSITEiPS00892. HIT_1. 1 hit.
PS51084. HIT_2. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]

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_006238027.2.
XP_006238090.1. XM_006238028.2.
UniGeneiRn.50459.

Genome annotation databases

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

Cross-referencesi

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_006238027.2.
XP_006238090.1. XM_006238028.2.
UniGeneiRn.50459.

3D structure databases

ProteinModelPortaliQ8K4H4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000046400.

Proteomic databases

PRIDEiQ8K4H4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi54840.
RGDi628740. Aptx.

Phylogenomic databases

eggNOGiNOG278510.
GeneTreeiENSGT00570000079163.
HOGENOMiHOG000248858.
HOVERGENiHBG050555.
InParanoidiQ8K4H4.
KOiK10863.
OMAiPGQVLHM.
OrthoDBiEOG786H3J.
PhylomeDBiQ8K4H4.

Miscellaneous databases

NextBioi624321.
PROiQ8K4H4.

Gene expression databases

GenevisibleiQ8K4H4. RN.

Family and domain databases

Gene3Di2.60.200.20. 2 hits.
3.30.428.10. 1 hit.
InterProiIPR026963. Aprataxin.
IPR000253. FHA_dom.
IPR019808. Histidine_triad_CS.
IPR001310. Histidine_triad_HIT.
IPR011146. HIT-like.
IPR008984. SMAD_FHA_domain.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
PANTHERiPTHR12486. PTHR12486. 1 hit.
PTHR12486:SF4. PTHR12486:SF4. 1 hit.
SMARTiSM00355. ZnF_C2H2. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF54197. SSF54197. 1 hit.
PROSITEiPS00892. HIT_1. 1 hit.
PS51084. HIT_2. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of FHA-HIT as a novel nuclear protein involved in cell-cycle regulation."
    Huang C.-H., Chen H., Peng J., Chen Y.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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.

Entry informationi

Entry nameiAPTX_RAT
AccessioniPrimary (citable) accession number: Q8K4H4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: October 1, 2002
Last modified: July 22, 2015
This is version 90 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.