Description:
DNA-repair protein complementing XP-C cells homolog (Xerodermapigmentosum group C-complementing protein homolog) (p125).
Molecular weight: 10452
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 ) nucleotide-excision repair (and GO:0045001, a synonym)( GO:0006289 )
Important dates:
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 2.
07-MAR-2006, entry version 36.
Phylogenetic order:
Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Glires Rodentia Sciurognathi Muroidea Muridae Murinae Mus.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein XPC_MOUSE:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | U27398 | AAC52500.1 | ALT_FRAME |
| EMBL | AB071144 | BAB64540.1 | - |
| EMBL | AK004713 | BAB23497.1 | - |
| EMBL | AK028595 | BAC26023.1 | - |
| EMBL | U40005 | AAA82720.1 | - |
| PIR | S70630 | S70630. | |
| Ensembl | ENSMUSG00000030094 | Mus musculus.1 | |
| MGI | MGI:103557 | Xpc.1 | |
| GO | GO:0005634 | C:nucleus | IDA. |
| GO | GO:0006289 | P:nucleotide-excision repair | IDA. |
| InterPro | IPR004583 | Rad4. | |
| PANTHER | PTHR12135 | Rad4.1 | 1. |
| Pfam | PF03835 | Rad4 | 1. |
| TIGRFAMs | TIGR00605 | rad4 | 1. |
Keywords:
DNA damage; DNA repair; DNA-binding; Nuclear protein; Phosphorylation.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-930.
RX MEDLINE=96184849; PubMed=8604333; DOI=10.1093/nar/24.6.1026;
RA Li L., Peterson C., Legerski R.;
RT "Sequence of the mouse XPC cDNA and genomic structure of the human XPC
RT gene.";
RL Nucleic Acids Res. 24:1026-1028(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yokoi M., Hanaoka F.;
RT "Molecular cloning of mouse XPC.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schonbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 59-617.
RC STRAIN=129/Sv;
RX MEDLINE=95405469; PubMed=7675084; DOI=10.1038/377162a0;
RA Sands A.T., Abuin A., Sanchez A., Conti C.J., Bradley A.;
RT "High susceptibility to ultraviolet-induced carcinogenesis in mice
RT lacking XPC.";
RL Nature 377:162-165(1995).
Feature:
CHAIN 1 930 DNA-repair protein complementing XP-C
cells homolog.
/FTId=PRO_0000218294.
MOTIF 388 393 Nuclear localization signal (Potential).
COMPBIAS 27 173 Glu-rich (acidic).
COMPBIAS 355 393 Lys-rich (basic).
COMPBIAS 401 424 Arg/Lys-rich (basic).
COMPBIAS 425 454 Asp/Glu-rich (acidic).
COMPBIAS 459 486 Arg/Lys-rich (basic).
MOD_RES 875 875 Phosphoserine (By similarity).
MOD_RES 876 876 Phosphoserine (By similarity).
CONFLICT 13 13 K -> N (in Ref. 2).
CONFLICT 84 84 L -> S (in Ref. 1).
CONFLICT 98 98 F -> L (in Ref. 1).
CONFLICT 101 101 S -> L (in Ref. 1).
CONFLICT 148 149 AT -> CP (in Ref. 2).
CONFLICT 165 166 TP -> RG (in Ref. 1).
CONFLICT 196 201 EVQENM -> GVHEDT (in Ref. 4).
CONFLICT 212 212 S -> N (in Ref. 4).
CONFLICT 218 218 S -> N (in Ref. 4).
CONFLICT 221 223 RQP -> SQL (in Ref. 4).
CONFLICT 373 375 GKA -> AKP (in Ref. 4).
CONFLICT 373 373 G -> GS (in Ref. 1).
CONFLICT 397 397 S -> R (in Ref. 1).
CONFLICT 454 454 E -> K (in Ref. 2).
CONFLICT 458 458 R -> C (in Ref. 4).
CONFLICT 497 497 S -> C (in Ref. 1).
CONFLICT 614 614 E -> K (in Ref. 1).
CONFLICT 621 622 KH -> ND (in Ref. 1).
CONFLICT 683 683 W -> R (in Ref. 1).
CONFLICT 712 715 LSEP -> HLGA (in Ref. 1).
CONFLICT 751 751 N -> K (in Ref. 1).
CONFLICT 777 777 R -> H (in Ref. 1).
CONFLICT 797 797 C -> S (in Ref. 1).
CONFLICT 921 921 A -> P (in Ref. 1).
Comments:
-!- FUNCTION: Involved in DNA excision repair. May play a part in DNA
damage recognition and/or in altering chromatin structure to allow
access by damage-processing enzymes.
-!- SUBUNIT: Heterodimer of a 125 kDa subunit (p125) and of a 58 kDa
subunit (p58).
-!- SUBCELLULAR LOCATION: Nucleus (Probable).
-!- SIMILARITY: Belongs to the XPC family.
-!- CAUTION: Ref.1 sequence differs from that shown due to frameshifts
in positions 50, 52 and 61.
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Sequence length: 930
MAPKRTADGR RRKRGQKTED NKVARHEESV ADDFEDEKQK PRRKSSFPKV SQGKRKRGCS
DPGDPTNGAA KKKVAKATAK SKNLKVLKEE ALSDGDDFRD SPADCKKAKK HPKSKVVDQG
TDEDDSEDDW EEVEELTEPV LDMGENSATS PSDMPVKAVE IEIETPQQAK ERERSEKIKM
EFETYLRRMM KRFNKEVQEN MHKVHLLCLL ASGFYRNSIC RQPDLLAIGL SIIPIRFTKV
PLQDRDAYYL SNLVKWFIGT FTVNADLSAS EQDDLQTTLE RRIAIYSARD NEELVHIFLL
ILRALQLLTR LVLSLQPIPL KSAVTKGRKS SKETSVEGPG GSSELSSNSP ESHNKPTTSR
RIKEEETLSE GRGKATARGK RGTGTAGSRQ RRKPSCSEGE EAEQKVQGRP HARKRRVAAK
VSYKEESESD GAGSGSDFEP SSGEGQHSSD EDCEPGPRKQ KRASAPQRTK AGSKSASKTQ
RGSQCEPSSF PEASSSSSGC KRGKKVSSGA EEMADRKPAG VDQWLEVYCE PQAKWVCVDC
VHGVVGQPVA CYKYATKPMT YVVGIDSDGW VRDVTQRYDP AWMTATRKCR VDAEWWAETL
RPYRSLLTER EKKEDQEFQA KHLDQPLPTS ISTYKNHPLY ALKRHLLKFQ AIYPETAAVL
GYCRGEAVYS RDCVHTLHSR DTWLKQARVV RLGEVPYKMV KGFSNRARKA RLSEPQLHDH
NDLGLYGHWQ TEEYQPPIAV DGKVPRNEFG NVYLFLPSMM PVGCVQMTLP NLNRVARKLG
IDCVQAITGF DFHGGYCHPV TDGYIVCEEF RDVLLAAWEN EQAIIEKKEK EKKEKRALGN
WKLLVRGLLI RERLKLRYGA KSEAAAPHAA GGGLSSDEEE GTSSQAEAAR VLAASWPQNR
EDPEQKSEYT KMTRKRRAAE ASHLFPFEKL