Tag | Content |
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CPLM ID | CPLM-008396 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | DNA repair protein complementing XP-C cells homolog |
Protein Synonyms/Alias | Xeroderma pigmentosum group C-complementing protein homolog; p125 |
Gene Name | Xpc |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
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170 | IETPQQAKERERSEK | ubiquitination | [1] | 643 | NHPLYALKRHLLKFQ | ubiquitination | [1] | 685 | HSRDTWLKQARVVRL | ubiquitination | [1] | 743 | PPIAVDGKVPRNEFG | ubiquitination | [1] |
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Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by Rad23b and Rad23a. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA- binding activity. |
Sequence Annotation | REGION 489 727 Interaction with RAD23B (By similarity). REGION 600 759 Minimal sensor domain involved in damage REGION 600 734 DNA-binding; preference for heteroduplex REGION 760 824 DNA-binding; preference for single REGION 809 930 Interaction with ERCC2 and GTF2H1 (By REGION 840 859 Interaction with CETN2 (By similarity). MOTIF 388 393 Nuclear localization signal (Potential). MOD_RES 93 93 Phosphoserine. MOD_RES 126 126 Phosphoserine (By similarity). MOD_RES 165 165 Phosphothreonine (By similarity). MOD_RES 395 395 Phosphoserine. MOD_RES 397 397 Phosphoserine. MOD_RES 875 875 Phosphoserine. MOD_RES 876 876 Phosphoserine. MOD_RES 883 883 Phosphoserine (By similarity). |
Keyword | Complete proteome; Cytoplasm; DNA damage; DNA repair; DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 930 AA |
Protein Sequence | MAPKRTADGR RRKRGQKTED NKVARHEESV ADDFEDEKQK PRRKSSFPKV SQGKRKRGCS 60 DPGDPTNGAA KKKVAKATAK SKNLKVLKEE ALSDGDDFRD SPADCKKAKK HPKSKVVDQG 120 TDEDDSEDDW EEVEELTEPV LDMGENSATS PSDMPVKAVE IEIETPQQAK ERERSEKIKM 180 EFETYLRRMM KRFNKEVQEN MHKVHLLCLL ASGFYRNSIC RQPDLLAIGL SIIPIRFTKV 240 PLQDRDAYYL SNLVKWFIGT FTVNADLSAS EQDDLQTTLE RRIAIYSARD NEELVHIFLL 300 ILRALQLLTR LVLSLQPIPL KSAVTKGRKS SKETSVEGPG GSSELSSNSP ESHNKPTTSR 360 RIKEEETLSE GRGKATARGK RGTGTAGSRQ RRKPSCSEGE EAEQKVQGRP HARKRRVAAK 420 VSYKEESESD GAGSGSDFEP SSGEGQHSSD EDCEPGPRKQ KRASAPQRTK AGSKSASKTQ 480 RGSQCEPSSF PEASSSSSGC KRGKKVSSGA EEMADRKPAG VDQWLEVYCE PQAKWVCVDC 540 VHGVVGQPVA CYKYATKPMT YVVGIDSDGW VRDVTQRYDP AWMTATRKCR VDAEWWAETL 600 RPYRSLLTER EKKEDQEFQA KHLDQPLPTS ISTYKNHPLY ALKRHLLKFQ AIYPETAAVL 660 GYCRGEAVYS RDCVHTLHSR DTWLKQARVV RLGEVPYKMV KGFSNRARKA RLSEPQLHDH 720 NDLGLYGHWQ TEEYQPPIAV DGKVPRNEFG NVYLFLPSMM PVGCVQMTLP NLNRVARKLG 780 IDCVQAITGF DFHGGYCHPV TDGYIVCEEF RDVLLAAWEN EQAIIEKKEK EKKEKRALGN 840 WKLLVRGLLI RERLKLRYGA KSEAAAPHAA GGGLSSDEEE GTSSQAEAAR VLAASWPQNR 900 EDPEQKSEYT KMTRKRRAAE ASHLFPFEKL 930 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0071942; C:XPC complex; ISS:UniProtKB. GO:0003684; F:damaged DNA binding; IEA:Compara. GO:0003697; F:single-stranded DNA binding; IEA:Compara. GO:0031573; P:intra-S DNA damage checkpoint; IGI:MGI. GO:0006289; P:nucleotide-excision repair; IDA:MGI. GO:0000715; P:nucleotide-excision repair, DNA damage recognition; IEA:Compara. GO:0042493; P:response to drug; IEA:Compara. GO:0010224; P:response to UV-B; IMP:MGI. |
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