Q59HH7 · Q59HH7_HUMAN
- ProteinX-ray repair cross complementing protein 1 variant
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids647 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score1/5
Function
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | nucleoplasm | |
Molecular Function | damaged DNA binding | |
Biological Process | base-excision repair | |
Biological Process | double-strand break repair via nonhomologous end joining | |
Biological Process | single strand break repair |
Names & Taxonomy
Protein names
- Submitted names
Organism names
- Organism
- Taxonomic lineagecellular organisms > Eukaryota (eucaryotes) > Opisthokonta > Metazoa (metazoans) > Eumetazoa > Bilateria > Deuterostomia > Chordata (chordates) > Craniata > Vertebrata (vertebrates) > Gnathostomata (jawed vertebrates) > Teleostomi > Euteleostomi (bony vertebrates) > Sarcopterygii > Dipnotetrapodomorpha > Tetrapoda (tetrapods) > Amniota (amniotes) > Mammalia (mammals) > Theria > Eutheria (placentals) > Boreoeutheria > Euarchontoglires > Primates > Haplorrhini > Simiiformes > Catarrhini > Hominoidea (apes) > Hominidae (great apes) > Homininae > Homo
Accessions
- Primary accessionQ59HH7
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 235-253 | Polar residues | ||||
Sequence: AASSASPVSRAIGSTSKPQ | ||||||
Region | 235-327 | Disordered | ||||
Sequence: AASSASPVSRAIGSTSKPQESPKGKRKLDLNQEEKKTPSKPPAQLSPSVPKRPKLPAPTRTPATAPVPARAQGAVTGKPRGEGTEPRRPRAGP | ||||||
Compositional bias | 254-270 | Basic and acidic residues | ||||
Sequence: ESPKGKRKLDLNQEEKK | ||||||
Compositional bias | 277-297 | Pro residues | ||||
Sequence: AQLSPSVPKRPKLPAPTRTPA | ||||||
Domain | 329-417 | BRCT | ||||
Sequence: ELGKILQGVVVVLSGFQNPFRSELRDKALELGAKYRPDWTRDSTHLICAFANTPKYSQVLGLGGRIVRKEWVLDCHRMRRRLPSQRYLM | ||||||
Region | 414-476 | Disordered | ||||
Sequence: RYLMAGPGSSSEEDEASHSGGSGDEAPKLPQKQPQTKTKPTQAAGPSSPQKPPTPEETKAASP | ||||||
Compositional bias | 442-458 | Polar residues | ||||
Sequence: LPQKQPQTKTKPTQAAG | ||||||
Region | 485-504 | Disordered | ||||
Sequence: EGVQSEGQDNGAEDSGDTED | ||||||
Region | 512-550 | Disordered | ||||
Sequence: QKEHRLPPGQEENGEDPYAGSTDENTDSEEHQEPPDLPV | ||||||
Domain | 552-643 | BRCT | ||||
Sequence: ELPDFFQGKHFFLYGEFPGDERRKLIRYVTAFNGELEDYMSDRVQFVITAQEWDPSFEEALMDNPSLAFVRPRWIYSCNEKQKLLPHQLYGV |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusFragment
- Length647
- Mass (Da)71,014
- Last updated2005-04-26 v1
- Checksum881FBDB515E9926E
Features
Showing features for non-terminal residue, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: S | ||||||
Compositional bias | 235-253 | Polar residues | ||||
Sequence: AASSASPVSRAIGSTSKPQ | ||||||
Compositional bias | 254-270 | Basic and acidic residues | ||||
Sequence: ESPKGKRKLDLNQEEKK | ||||||
Compositional bias | 277-297 | Pro residues | ||||
Sequence: AQLSPSVPKRPKLPAPTRTPA | ||||||
Compositional bias | 442-458 | Polar residues | ||||
Sequence: LPQKQPQTKTKPTQAAG |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB208781 EMBL· GenBank· DDBJ | BAD92018.1 EMBL· GenBank· DDBJ | mRNA |