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P51612

- XPC_MOUSE

UniProt

P51612 - XPC_MOUSE

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Protein
DNA repair protein complementing XP-C cells homolog
Gene
Xpc
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. damaged DNA binding Source: Ensembl
  2. single-stranded DNA binding Source: Ensembl

GO - Biological processi

  1. DNA repair Source: MGI
  2. cellular response to DNA damage stimulus Source: MGI
  3. intra-S DNA damage checkpoint Source: MGI
  4. nucleotide-excision repair Source: MGI
  5. nucleotide-excision repair, DNA damage recognition Source: Ensembl
  6. response to UV-B Source: MGI
  7. response to drug Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_210532. DNA Damage Recognition in GG-NER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair protein complementing XP-C cells homolog
Alternative name(s):
Xeroderma pigmentosum group C-complementing protein homolog
p125
Gene namesi
Name:Xpc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:103557. Xpc.

Subcellular locationi

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.

GO - Cellular componenti

  1. XPC complex Source: UniProtKB
  2. cytoplasm Source: UniProtKB-SubCell
  3. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 930929DNA repair protein complementing XP-C cells homolog
PRO_0000218294Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei93 – 931Phosphoserine By similarity
Modified residuei126 – 1261Phosphoserine By similarity
Modified residuei165 – 1651Phosphothreonine By similarity
Modified residuei875 – 8751Phosphoserine2 Publications
Modified residuei876 – 8761Phosphoserine2 Publications
Modified residuei883 – 8831Phosphoserine By similarity

Post-translational modificationi

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.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP51612.
PRIDEiP51612.

PTM databases

PhosphoSiteiP51612.

Expressioni

Gene expression databases

BgeeiP51612.
CleanExiMM_XPC.
GenevestigatoriP51612.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi204605. 1 interaction.
IntActiP51612. 3 interactions.
MINTiMINT-4122377.

Structurei

3D structure databases

ProteinModelPortaliP51612.
SMRiP51612. Positions 524-817.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni489 – 727239Interaction with RAD23B By similarity
Add
BLAST
Regioni600 – 759160Minimal sensor domain involved in damage recognition By similarity
Add
BLAST
Regioni600 – 734135DNA-binding; preference for heteroduplex DNA By similarity
Add
BLAST
Regioni760 – 82465DNA-binding; preference for single stranded DNA; required for formation of stable nucleoprotein complex By similarity
Add
BLAST
Regioni809 – 930122Interaction with ERCC2 and GTF2H1 By similarity
Add
BLAST
Regioni840 – 85920Interaction with CETN2 By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi388 – 3936Nuclear localization signal Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi27 – 173147Glu-rich (acidic)
Add
BLAST
Compositional biasi355 – 39339Lys-rich (basic)
Add
BLAST
Compositional biasi401 – 42424Arg/Lys-rich (basic)
Add
BLAST
Compositional biasi425 – 45430Asp/Glu-rich (acidic)
Add
BLAST
Compositional biasi459 – 48628Arg/Lys-rich (basic)
Add
BLAST

Sequence similaritiesi

Belongs to the XPC family.

Phylogenomic databases

eggNOGiCOG5535.
GeneTreeiENSGT00390000005194.
HOGENOMiHOG000124671.
HOVERGENiHBG000407.
InParanoidiP51612.
KOiK10838.
OMAiPQRTKAG.
OrthoDBiEOG7BW0J2.
PhylomeDBiP51612.
TreeFamiTF101242.

Family and domain databases

InterProiIPR004583. 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]
PANTHERiPTHR12135. PTHR12135. 1 hit.
PfamiPF10403. BHD_1. 1 hit.
PF10404. BHD_2. 1 hit.
PF10405. BHD_3. 1 hit.
PF03835. Rad4. 1 hit.
[Graphical view]
SMARTiSM01030. BHD_1. 1 hit.
SM01031. BHD_2. 1 hit.
SM01032. BHD_3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00605. rad4. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P51612-1 [UniParc]FASTAAdd to Basket

« Hide

MAPKRTADGR RRKRGQKTED NKVARHEESV ADDFEDEKQK PRRKSSFPKV    50
SQGKRKRGCS DPGDPTNGAA KKKVAKATAK SKNLKVLKEE ALSDGDDFRD 100
SPADCKKAKK HPKSKVVDQG TDEDDSEDDW EEVEELTEPV LDMGENSATS 150
PSDMPVKAVE IEIETPQQAK ERERSEKIKM EFETYLRRMM KRFNKEVQEN 200
MHKVHLLCLL ASGFYRNSIC RQPDLLAIGL SIIPIRFTKV PLQDRDAYYL 250
SNLVKWFIGT FTVNADLSAS EQDDLQTTLE RRIAIYSARD NEELVHIFLL 300
ILRALQLLTR LVLSLQPIPL KSAVTKGRKS SKETSVEGPG GSSELSSNSP 350
ESHNKPTTSR RIKEEETLSE GRGKATARGK RGTGTAGSRQ RRKPSCSEGE 400
EAEQKVQGRP HARKRRVAAK VSYKEESESD GAGSGSDFEP SSGEGQHSSD 450
EDCEPGPRKQ KRASAPQRTK AGSKSASKTQ RGSQCEPSSF PEASSSSSGC 500
KRGKKVSSGA EEMADRKPAG VDQWLEVYCE PQAKWVCVDC VHGVVGQPVA 550
CYKYATKPMT YVVGIDSDGW VRDVTQRYDP AWMTATRKCR VDAEWWAETL 600
RPYRSLLTER EKKEDQEFQA KHLDQPLPTS ISTYKNHPLY ALKRHLLKFQ 650
AIYPETAAVL GYCRGEAVYS RDCVHTLHSR DTWLKQARVV RLGEVPYKMV 700
KGFSNRARKA RLSEPQLHDH NDLGLYGHWQ TEEYQPPIAV DGKVPRNEFG 750
NVYLFLPSMM PVGCVQMTLP NLNRVARKLG IDCVQAITGF DFHGGYCHPV 800
TDGYIVCEEF RDVLLAAWEN EQAIIEKKEK EKKEKRALGN WKLLVRGLLI 850
RERLKLRYGA KSEAAAPHAA GGGLSSDEEE GTSSQAEAAR VLAASWPQNR 900
EDPEQKSEYT KMTRKRRAAE ASHLFPFEKL 930
Length:930
Mass (Da):104,522
Last modified:August 16, 2004 - v2
Checksum:i0C469AB21B4E4EE9
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131K → N in BAB64540. 1 Publication
Sequence conflicti84 – 841L → S in AAC52500. 1 Publication
Sequence conflicti98 – 981F → L in AAC52500. 1 Publication
Sequence conflicti101 – 1011S → L in AAC52500. 1 Publication
Sequence conflicti148 – 1492AT → CP in BAB64540. 1 Publication
Sequence conflicti165 – 1662TP → RG in AAC52500. 1 Publication
Sequence conflicti196 – 2016EVQENM → GVHEDT in AAA82720. 1 Publication
Sequence conflicti212 – 2121S → N in AAA82720. 1 Publication
Sequence conflicti218 – 2181S → N in AAA82720. 1 Publication
Sequence conflicti221 – 2233RQP → SQL in AAA82720. 1 Publication
Sequence conflicti373 – 3753GKA → AKP in AAA82720. 1 Publication
Sequence conflicti373 – 3731G → GS in AAC52500. 1 Publication
Sequence conflicti397 – 3971S → R in AAC52500. 1 Publication
Sequence conflicti454 – 4541E → K in BAB64540. 1 Publication
Sequence conflicti458 – 4581R → C in AAA82720. 1 Publication
Sequence conflicti497 – 4971S → C in AAC52500. 1 Publication
Sequence conflicti614 – 6141E → K in AAC52500. 1 Publication
Sequence conflicti621 – 6222KH → ND in AAC52500. 1 Publication
Sequence conflicti683 – 6831W → R in AAC52500. 1 Publication
Sequence conflicti712 – 7154LSEP → HLGA in AAC52500. 1 Publication
Sequence conflicti751 – 7511N → K in AAC52500. 1 Publication
Sequence conflicti777 – 7771R → H in AAC52500. 1 Publication
Sequence conflicti797 – 7971C → S in AAC52500. 1 Publication
Sequence conflicti921 – 9211A → P in AAC52500. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS39569.1.
PIRiS70630.
RefSeqiNP_033557.2. NM_009531.2.
UniGeneiMm.2806.

Genome annotation databases

EnsembliENSMUST00000032182; ENSMUSP00000032182; ENSMUSG00000030094.
GeneIDi22591.
KEGGimmu:22591.
UCSCiuc009cyd.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS39569.1.
PIRi S70630.
RefSeqi NP_033557.2. NM_009531.2.
UniGenei Mm.2806.

3D structure databases

ProteinModelPortali P51612.
SMRi P51612. Positions 524-817.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204605. 1 interaction.
IntActi P51612. 3 interactions.
MINTi MINT-4122377.

PTM databases

PhosphoSitei P51612.

Proteomic databases

PaxDbi P51612.
PRIDEi P51612.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000032182 ; ENSMUSP00000032182 ; ENSMUSG00000030094 .
GeneIDi 22591.
KEGGi mmu:22591.
UCSCi uc009cyd.2. mouse.

Organism-specific databases

CTDi 7508.
MGIi MGI:103557. Xpc.

Phylogenomic databases

eggNOGi COG5535.
GeneTreei ENSGT00390000005194.
HOGENOMi HOG000124671.
HOVERGENi HBG000407.
InParanoidi P51612.
KOi K10838.
OMAi PQRTKAG.
OrthoDBi EOG7BW0J2.
PhylomeDBi P51612.
TreeFami TF101242.

Enzyme and pathway databases

Reactomei REACT_210532. DNA Damage Recognition in GG-NER.

Miscellaneous databases

ChiTaRSi XPC. mouse.
NextBioi 302933.
PROi P51612.
SOURCEi Search...

Gene expression databases

Bgeei P51612.
CleanExi MM_XPC.
Genevestigatori P51612.

Family and domain databases

InterProi IPR004583. 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 ]
PANTHERi PTHR12135. PTHR12135. 1 hit.
Pfami PF10403. BHD_1. 1 hit.
PF10404. BHD_2. 1 hit.
PF10405. BHD_3. 1 hit.
PF03835. Rad4. 1 hit.
[Graphical view ]
SMARTi SM01030. BHD_1. 1 hit.
SM01031. BHD_2. 1 hit.
SM01032. BHD_3. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00605. rad4. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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].

Entry informationi

Entry nameiXPC_MOUSE
AccessioniPrimary (citable) accession number: P51612
Secondary accession number(s): P54732
, Q3TKI2, Q920M1, Q9DBW7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: August 16, 2004
Last modified: September 3, 2014
This is version 111 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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