Q60596 (XRCC1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA repair protein XRCC1

Alternative name(s):
X-ray repair cross-complementing protein 1

Gene names

Name:	Xrcc1
Synonyms:	Xrcc-1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	631 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Corrects defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents.
Subunit structure	Homodimer. Interacts with polynucleotide kinase (PNK), DNA polymerase-beta (POLB) and DNA ligase III (LIG3). Interacts with APTX and APLF. Interacts with APEX1; the interaction is induced by SIRT1 and increases with the acetylated form of APEX1 By similarity.
Subcellular location	Nucleus Probable.
Post-translational modification	Phosphorylation of Ser-371 causes dimer dissociation. Phosphorylation by CK2 promotes interaction with APTX and APLF By similarity. Sumoylated.
Sequence similarities	Contains 2 BRCT domains.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Domain	Repeat
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from mutant phenotype PubMed 19633665. Source: MGI hippocampus development Inferred from mutant phenotype PubMed 19633665. Source: MGI response to drug Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara response to organic substance Inferred from electronic annotation. Source: Compara single strand break repair Inferred from electronic annotation. Source: InterPro
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	damaged DNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 631

631

DNA repair protein XRCC1

PRO_0000066045

Regions

Domain

315 – 403

89

BRCT 1

Domain

536 – 627

92

BRCT 2

Amino acid modifications

Modified residue

142

1

Phosphoserine By similarity

Modified residue

200

1

Phosphothreonine By similarity

Modified residue

201

1

Phosphoserine By similarity

Modified residue

206

1

Phosphoserine By similarity

Modified residue

213

1

Phosphotyrosine By similarity

Modified residue

228

1

Phosphoserine By similarity

Modified residue

261

1

Phosphoserine By similarity

Modified residue

371

1

Phosphoserine By similarity

Modified residue

408

1

Phosphoserine By similarity

Modified residue

409

1

Phosphoserine By similarity

Modified residue

410

1

Phosphoserine By similarity

Modified residue

416

1

Phosphoserine By similarity

Modified residue

418

1

Phosphoserine By similarity

Modified residue

445

1

Phosphoserine By similarity

Modified residue

446

1

Phosphoserine Ref.4 Ref.7

Modified residue

452

1

Phosphothreonine Ref.4 Ref.5 Ref.7

Modified residue

456

1

Phosphothreonine By similarity

Modified residue

460

1

Phosphoserine By similarity

Modified residue

484

1

Phosphoserine Ref.6

Modified residue

487

1

Phosphothreonine Ref.6

Modified residue

517

1

Phosphoserine By similarity

Modified residue

518

1

Phosphothreonine By similarity

Modified residue

522

1

Phosphothreonine By similarity

Experimental info

Sequence conflict

28

1

D → G in AAH85281. Ref.3

Sequence conflict

68

1

V → L in BAE40272. Ref.2

Sequence conflict

108

1

N → S in AAH85281. Ref.3

Sequence conflict

172

1

L → F in AAH85281. Ref.3

Sequence conflict

197

1

I → V in AAH85281. Ref.3

Sequence conflict

263

1

P → H in BAE40272. Ref.2

Sequence conflict

295

1

V → I in AAA93115. Ref.1

Sequence conflict

379

1

R → G in BAE40272. Ref.2

Sequence conflict

391

1

H → R in AAA93115. Ref.1

Sequence conflict

582

1

V → A in AAH85281. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

631

Helix Strand Turn

Details...

Turn

540 – 543

4

Beta strand

545 – 550

6

Helix

556 – 566

11

Beta strand

573 – 575

3

Beta strand

581 – 586

6

Helix

590 – 596

7

Beta strand

603 – 605

3

Helix

607 – 616

10

Helix

622 – 625

4

Sequences

	Sequence		Length	Mass (Da)
	Q60596 [UniParc]. Last modified December 20, 2005. Version 2. Checksum: 1A730F206E5B8879	FASTA	631	68,971
	10 20 30 40 50 60 MPEISLRHVV SCSSQDSTHC AENLLKADTY RKWRAAKAGE KTISVVLQLE KEEQIHSVDI 70 80 90 100 110 120 GNDGSAFVEV LVGSSAGGAT AGEQDYEVLL VTSSFMSPSE SRSGSNPNRV RIFGPDKLVR 130 140 150 160 170 180 AAAEKRWDRV KIVCSQPYSK DSPYGLSFVK FHSPPDKDEA EATSQKVTVT KLGQFRVKEE 190 200 210 220 230 240 DDSANSLKPG ALFFSRINKT SSASTSDPAG PSYAAATLQA SSAASSASPV PKVVGSSSKP 250 260 270 280 290 300 QEPPKGKRKL DLSLEDRKPP SKPSAGPSTL KRPKLSVPSR TPAAAPASTP AQRAVPGKPR 310 320 330 340 350 360 GEGTEPRGAR TGPQELGKIL QGVVVVLSGF QNPFRSELRD KALELGAKYR PDWTPDSTHL 370 380 390 400 410 420 ICAFANTPKY SQVLGLGGRI VRKEWVLDCH HMRRRLPSRR YLMAGLGSSS EDEGDSHSES 430 440 450 460 470 480 GEDEAPKLPQ KRPQPKAKTQ AAGPSSPPRP PTPKETKAPS PGPQDNSDTE GEESEGRDNG 490 500 510 520 530 540 AEDSGDTEDE LRRVAKQREQ RQPPAPEENG EDPYAGSTDE NTDSETPSEA DLPIPELPDF 550 560 570 580 590 600 FEGKHFFLYG EFPGDERRRL IRYVTAFNGE LEDYMNERVQ FVITAQEWDP NFEEALMENP 610 620 630 SLAFVRPRWI YSCNEKQKLL PHQLYGVVPQ A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of mouse Xrcc-1, a DNA repair gene affecting ligation." Brookman K.W., Tebbs R.S., Allen S.A., Tucker J.D., Swiger R.R., Lamerdin J.E., Carrano A.V., Thompson L.H. Genomics 22:180-188(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"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: DBA/2.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and FVB/N. Tissue: Colon and Egg.
[4]	"Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line." Shu H., Chen S., Bi Q., Mumby M., Brekken D.L. Mol. Cell. Proteomics 3:279-286(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-446 AND THR-452, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[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 THR-452, MASS SPECTROMETRY. Tissue: Liver.
[6]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484 AND THR-487, MASS SPECTROMETRY. Tissue: Melanoma.
[7]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-446 AND THR-452, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U02887 mRNA. Translation: AAA93115.1.
AK168334 mRNA. Translation: BAE40272.1.
BC055900 mRNA. Translation: AAH55900.1.
BC085281 mRNA. Translation: AAH85281.1.

IPI

IPI00118139.

PIR

A54659.

RefSeq

NP_033558.3. NM_009532.4.

UniGene

Mm.4347.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3PC6	X-ray	1.90	A/B	535-631	[»]
3PC8	X-ray	2.31	A/B	535-631	[»]
3QVG	X-ray	2.26	B/D	531-631	[»]

ProteinModelPortal

Q60596.

SMR

Q60596. Positions 2-155, 301-413, 536-631.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q60596. 2 interactions.

PTM databases

PhosphoSite

Q60596.

Proteomic databases

PaxDb

Q60596.

PRIDE

Q60596.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000063249; ENSMUSP00000070995; ENSMUSG00000051768.

GeneID

22594.

KEGG

mmu:22594.

UCSC

uc009fpx.2. mouse.

Organism-specific databases

CTD

7515.

MGI

MGI:99137. Xrcc1.

Phylogenomic databases

eggNOG

NOG295271.

GeneTree

ENSGT00390000004140.

HOGENOM

HOG000111006.

HOVERGEN

HBG052992.

InParanoid

Q60596.

KO

K10803.

OMA

YSCNEKQ.

OrthoDB

EOG4C87SH.

Gene expression databases

Bgee

Q60596.

Genevestigator

Q60596.

GermOnline

ENSMUSG00000051768. Mus musculus.

Family and domain databases

InterPro

IPR001357. BRCT_dom.
IPR008979. Galactose-bd-like.
IPR002706. Xrcc1_N.
[Graphical view]

Pfam

PF00533. BRCT. 2 hits.
PF01834. XRCC1_N. 1 hit.
[Graphical view]

SMART

SM00292. BRCT. 2 hits.
[Graphical view]

SUPFAM

SSF52113. BRCT. 2 hits.
SSF49785. Gal_bind_like. 1 hit.

PROSITE

PS50172. BRCT. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q60596.

NextBio

302941.

SOURCE

Search...

Entry information

Entry name

XRCC1_MOUSE

Accession

Primary (citable) accession number: Q60596
Secondary accession number(s): Q3THC5, Q5U435, Q7TNQ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	December 20, 2005
Last modified:	April 3, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program