DNA repair protein complementing XP-C cells (Protein name
), XPC_HUMAN from NCBI database.
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General Annotation
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Antigen Annotation
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Gene name:
XPC(XPCC);
Protein name:
DNA repair protein complementing XP-C cells;
Alternative:
p125;Xeroderma pigmentosum group C-complementing protein;
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
Component of the XPC complex composed of XPC, RAD23B and CETN2. Interacts with RAD23A; the interaction is suggesting the existence of a functional equivalent variant XPC complex. Interacts with TDG; the interaction is demonstrated using the XPC:RAD23B dimer. Interacts with SMUG1; the interaction is demonstrated using the XPC:RAD23B dimer. Interacts with DDB2. Interacts with CCNH, GTF2H1 and ERCC3.
Function:
The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1.
Subcellular Location:
Nucleus
Cytoplasm
Omnipresent in the nucleus and consistently associates with and dissociates from DNA in the absence of DNA damage. Continuously shuttles between the cytoplasm and the nucleus, which is impeded by the presence of NER lesions.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);PROTEIN SEQUENCE OF 2-55;VARIANTS VAL-499 AND LYS-939
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA];VARIANTS VAL-499 AND LYS-939;ALTERNATIVE SPLICING
NIEHS SNPs program
Submitted (2002-07) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA];VARIANTS VAL-16; PHE-48; ARG-86; GLN-314; HIS-492; VAL-499; ILE-513; GLU-632; HIS-671; MET-689; GLN-928 AND LYS-939
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2)
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 69-940 (ISOFORM 1)
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 119-940 (ISOFORM 1)
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Cited for: FUNCTION;SUBUNIT;INTERACTION WITH CCNH; GTF2H1 AND ERCC3
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Cited for: INTERACTION WITH CETN2 AND RAD23B;SUBCELLULAR LOCATION;CHARACTERIZATION OF THE XPC COMPLEX
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Cited for: DNA-BINDING;INTERACTION WITH RAD23B; ERCC2 AND GTF2H1
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Cited for: INTERACTION WITH CETN2 AND RAD23B;MUTAGENESIS OF TRP-848; LEU-851 AND LEU-855
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND SER-129;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94; THR-169; SER-883; SER-884 AND SER-891;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94; SER-129; SER-883 AND SER-884;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94; THR-876; SER-883 AND SER-884;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: CHARACTERIZATION OF VARIANT XP-C SER-690;MUTAGENESIS OF PHE-733
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Cited for: FUNCTION;CHARACTERIZATION OF VARIANT OF VARIANT XP-C SER-690;MUTAGENESIS OF TRP-531; TRP-542; PHE-733 AND GLU-755
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Cited for: FUNCTION;MUTAGENESIS OF ASN-754; PHE-756; PHE-797 AND PHE-799
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Cited for: FUNCTION OF THE XPC COMPLEX;INTERACTION WITH TDG AND SMUG1
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Cited for: STRUCTURE BY NMR OF 847-863 IN COMPLEX WITH CETN2
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Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 847-863 IN COMPLEX WITH CETN2
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Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 847-863 IN COMPLEX WITH CETN2