Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P51612 (XPC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA repair protein complementing XP-C cells homolog
Alternative name(s):
Xeroderma pigmentosum group C-complementing protein homolog
p125
Gene names
Name:Xpc
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length930 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

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 By similarity.

Subunit structure

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 By similarity.

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Note: 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 By similarity.

Post-translational modification

Ubiquitinated upon UV irradiation; the ubiquitination requires the UV-DDB complex, appears to be reversible and does not serve as a signal for degradation By similarity.

Sequence similarities

Belongs to the XPC family.

Sequence caution

The sequence AAC52500.1 differs from that shown. Reason: Frameshift at positions 50, 52 and 61.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 930929DNA repair protein complementing XP-C cells homolog
PRO_0000218294

Regions

Region489 – 727239Interaction with RAD23B By similarity
Region600 – 759160Minimal sensor domain involved in damage recognition By similarity
Region600 – 734135DNA-binding; preference for heteroduplex DNA By similarity
Region760 – 82465DNA-binding; preference for single stranded DNA; required for formation of stable nucleoprotein complex By similarity
Region809 – 930122Interaction with ERCC2 and GTF2H1 By similarity
Region840 – 85920Interaction with CETN2 By similarity
Motif388 – 3936Nuclear localization signal Potential
Compositional bias27 – 173147Glu-rich (acidic)
Compositional bias355 – 39339Lys-rich (basic)
Compositional bias401 – 42424Arg/Lys-rich (basic)
Compositional bias425 – 45430Asp/Glu-rich (acidic)
Compositional bias459 – 48628Arg/Lys-rich (basic)

Amino acid modifications

Modified residue931Phosphoserine By similarity
Modified residue1261Phosphoserine By similarity
Modified residue1651Phosphothreonine By similarity
Modified residue8751Phosphoserine Ref.5 Ref.6
Modified residue8761Phosphoserine Ref.5 Ref.6
Modified residue8831Phosphoserine By similarity

Experimental info

Sequence conflict131K → N in BAB64540. Ref.2
Sequence conflict841L → S in AAC52500. Ref.1
Sequence conflict981F → L in AAC52500. Ref.1
Sequence conflict1011S → L in AAC52500. Ref.1
Sequence conflict148 – 1492AT → CP in BAB64540. Ref.2
Sequence conflict165 – 1662TP → RG in AAC52500. Ref.1
Sequence conflict196 – 2016EVQENM → GVHEDT in AAA82720. Ref.4
Sequence conflict2121S → N in AAA82720. Ref.4
Sequence conflict2181S → N in AAA82720. Ref.4
Sequence conflict221 – 2233RQP → SQL in AAA82720. Ref.4
Sequence conflict373 – 3753GKA → AKP in AAA82720. Ref.4
Sequence conflict3731G → GS in AAC52500. Ref.1
Sequence conflict3971S → R in AAC52500. Ref.1
Sequence conflict4541E → K in BAB64540. Ref.2
Sequence conflict4581R → C in AAA82720. Ref.4
Sequence conflict4971S → C in AAC52500. Ref.1
Sequence conflict6141E → K in AAC52500. Ref.1
Sequence conflict621 – 6222KH → ND in AAC52500. Ref.1
Sequence conflict6831W → R in AAC52500. Ref.1
Sequence conflict712 – 7154LSEP → HLGA in AAC52500. Ref.1
Sequence conflict7511N → K in AAC52500. Ref.1
Sequence conflict7771R → H in AAC52500. Ref.1
Sequence conflict7971C → S in AAC52500. Ref.1
Sequence conflict9211A → P in AAC52500. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P51612 [UniParc].

Last modified August 16, 2004. Version 2.
Checksum: 0C469AB21B4E4EE9

FASTA930104,522
        10         20         30         40         50         60 
MAPKRTADGR RRKRGQKTED NKVARHEESV ADDFEDEKQK PRRKSSFPKV SQGKRKRGCS 

        70         80         90        100        110        120 
DPGDPTNGAA KKKVAKATAK SKNLKVLKEE ALSDGDDFRD SPADCKKAKK HPKSKVVDQG 

       130        140        150        160        170        180 
TDEDDSEDDW EEVEELTEPV LDMGENSATS PSDMPVKAVE IEIETPQQAK ERERSEKIKM 

       190        200        210        220        230        240 
EFETYLRRMM KRFNKEVQEN MHKVHLLCLL ASGFYRNSIC RQPDLLAIGL SIIPIRFTKV 

       250        260        270        280        290        300 
PLQDRDAYYL SNLVKWFIGT FTVNADLSAS EQDDLQTTLE RRIAIYSARD NEELVHIFLL 

       310        320        330        340        350        360 
ILRALQLLTR LVLSLQPIPL KSAVTKGRKS SKETSVEGPG GSSELSSNSP ESHNKPTTSR 

       370        380        390        400        410        420 
RIKEEETLSE GRGKATARGK RGTGTAGSRQ RRKPSCSEGE EAEQKVQGRP HARKRRVAAK 

       430        440        450        460        470        480 
VSYKEESESD GAGSGSDFEP SSGEGQHSSD EDCEPGPRKQ KRASAPQRTK AGSKSASKTQ 

       490        500        510        520        530        540 
RGSQCEPSSF PEASSSSSGC KRGKKVSSGA EEMADRKPAG VDQWLEVYCE PQAKWVCVDC 

       550        560        570        580        590        600 
VHGVVGQPVA CYKYATKPMT YVVGIDSDGW VRDVTQRYDP AWMTATRKCR VDAEWWAETL 

       610        620        630        640        650        660 
RPYRSLLTER EKKEDQEFQA KHLDQPLPTS ISTYKNHPLY ALKRHLLKFQ AIYPETAAVL 

       670        680        690        700        710        720 
GYCRGEAVYS RDCVHTLHSR DTWLKQARVV RLGEVPYKMV KGFSNRARKA RLSEPQLHDH 

       730        740        750        760        770        780 
NDLGLYGHWQ TEEYQPPIAV DGKVPRNEFG NVYLFLPSMM PVGCVQMTLP NLNRVARKLG 

       790        800        810        820        830        840 
IDCVQAITGF DFHGGYCHPV TDGYIVCEEF RDVLLAAWEN EQAIIEKKEK EKKEKRALGN 

       850        860        870        880        890        900 
WKLLVRGLLI RERLKLRYGA KSEAAAPHAA GGGLSSDEEE GTSSQAEAAR VLAASWPQNR 

       910        920        930 
EDPEQKSEYT KMTRKRRAAE ASHLFPFEKL 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of the mouse XPC cDNA and genomic structure of the human XPC gene."
Li L., Peterson C., Legerski R.
Nucleic Acids Res. 24:1026-1028(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-930.
[2]"Molecular cloning of mouse XPC."
Yokoi M., Hanaoka F.
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Lung and Skin.
[4]"High susceptibility to ultraviolet-induced carcinogenesis in mice lacking XPC."
Sands A.T., Abuin A., Sanchez A., Conti C.J., Bradley A.
Nature 377:162-165(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 59-617.
Strain: 129/Sv.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-875 AND SER-876, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-875 AND SER-876, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U27398 mRNA. Translation: AAC52500.1. Frameshift.
AB071144 mRNA. Translation: BAB64540.1.
AK004713 mRNA. Translation: BAB23497.1.
AK028595 mRNA. Translation: BAC26023.1.
AK166981 mRNA. Translation: BAE39163.1.
U40005 mRNA. Translation: AAA82720.1.
CCDSCCDS39569.1.
PIRS70630.
RefSeqNP_033557.2. NM_009531.2.
UniGeneMm.2806.

3D structure databases

ProteinModelPortalP51612.
SMRP51612. Positions 524-817.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204605. 1 interaction.
IntActP51612. 3 interactions.
MINTMINT-4122377.

PTM databases

PhosphoSiteP51612.

Proteomic databases

PaxDbP51612.
PRIDEP51612.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032182; ENSMUSP00000032182; ENSMUSG00000030094.
GeneID22591.
KEGGmmu:22591.
UCSCuc009cyd.2. mouse.

Organism-specific databases

CTD7508.
MGIMGI:103557. Xpc.

Phylogenomic databases

eggNOGCOG5535.
GeneTreeENSGT00390000005194.
HOGENOMHOG000124671.
HOVERGENHBG000407.
InParanoidP51612.
KOK10838.
OMAPQRTKAG.
OrthoDBEOG7BW0J2.
PhylomeDBP51612.
TreeFamTF101242.

Gene expression databases

BgeeP51612.
CleanExMM_XPC.
GenevestigatorP51612.

Family and domain databases

InterProIPR004583. DNA_repair_Rad4.
IPR018026. DNA_repair_Rad4_subgr.
IPR018325. Rad4/PNGase_transGLS-fold.
IPR018326. Rad4_beta-hairpin_dom1.
IPR018327. Rad4_beta-hairpin_dom2.
IPR018328. Rad4_beta-hairpin_dom3.
[Graphical view]
PANTHERPTHR12135. PTHR12135. 1 hit.
PfamPF10403. BHD_1. 1 hit.
PF10404. BHD_2. 1 hit.
PF10405. BHD_3. 1 hit.
PF03835. Rad4. 1 hit.
[Graphical view]
SMARTSM01030. BHD_1. 1 hit.
SM01031. BHD_2. 1 hit.
SM01032. BHD_3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00605. rad4. 1 hit.
ProtoNetSearch...

Other

ChiTaRSXPC. mouse.
NextBio302933.
PROP51612.
SOURCESearch...

Entry information

Entry nameXPC_MOUSE
AccessionPrimary (citable) accession number: P51612
Secondary accession number(s): P54732 expand/collapse secondary AC list , Q3TKI2, Q920M1, Q9DBW7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: August 16, 2004
Last modified: July 9, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot