Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P27641

- XRCC5_MOUSE

UniProt

P27641 - XRCC5_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

X-ray repair cross-complementing protein 5

Gene

Xrcc5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Single-stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. In association with NAA15, the XRCC5/6 dimer binds to the osteocalcin promoter and activates osteocalcin expression. expression. The XRCC5/6 dimer probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks. XRCC5 probably acts as the catalytic subunit of 5'-dRP activity, and allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription (By similarity).By similarity

GO - Molecular functioni

  1. 5'-deoxyribose-5-phosphate lyase activity Source: Ensembl
  2. ATP binding Source: UniProtKB-KW
  3. ATP-dependent DNA helicase activity Source: InterPro
  4. damaged DNA binding Source: InterPro
  5. double-stranded telomeric DNA binding Source: Ensembl
  6. poly(A) RNA binding Source: Ensembl
  7. transcription regulatory region DNA binding Source: Ensembl

GO - Biological processi

  1. brain development Source: Ensembl
  2. cell proliferation Source: MGI
  3. cellular hyperosmotic salinity response Source: Ensembl
  4. cellular response to fatty acid Source: Ensembl
  5. cellular response to X-ray Source: Ensembl
  6. DNA recombination Source: UniProtKB-KW
  7. double-strand break repair Source: MGI
  8. double-strand break repair via nonhomologous end joining Source: UniProtKB
  9. hematopoietic stem cell differentiation Source: MGI
  10. negative regulation of transcription, DNA-templated Source: UniProtKB
  11. positive regulation of neurogenesis Source: MGI
  12. response to drug Source: Ensembl
  13. telomere maintenance Source: InterPro
  14. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Helicase, Hydrolase

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_196447. IRF3-mediated induction of type I IFN.
REACT_224809. Processing of DNA ends prior to end rejoining.
REACT_254501. Nonhomologous End-joining (NHEJ).

Names & Taxonomyi

Protein namesi
Recommended name:
X-ray repair cross-complementing protein 5 (EC:3.6.4.-)
Alternative name(s):
ATP-dependent DNA helicase 2 subunit 2
ATP-dependent DNA helicase II 80 kDa subunit
CTC box-binding factor 85 kDa subunit
Short name:
CTC85
Short name:
CTCBF
DNA repair protein XRCC5
Ku autoantigen protein p86 homolog
Ku80
Nuclear factor IV
Gene namesi
Name:Xrcc5
Synonyms:G22p2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:104517. Xrcc5.

Subcellular locationi

Nucleus. Nucleusnucleolus By similarity. Chromosome

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. Ku70:Ku80 complex Source: UniProtKB
  3. nonhomologous end joining complex Source: UniProtKB
  4. nuclear chromosome, telomeric region Source: Ensembl
  5. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 732731X-ray repair cross-complementing protein 5PRO_0000084341Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei265 – 2651N6-acetyllysineBy similarity
Modified residuei332 – 3321N6-acetyllysineBy similarity
Modified residuei578 – 5781Phosphoserine; by PRKDCBy similarity
Modified residuei580 – 5801Phosphoserine; by PRKDCBy similarity
Modified residuei581 – 5811Phosphoserine; by PRKDCBy similarity
Modified residuei666 – 6661N6-acetyllysineBy similarity
Modified residuei716 – 7161Phosphothreonine; by PRKDCBy similarity

Post-translational modificationi

Phosphorylated on serine residues. Phosphorylation by PRKDC may enhance helicase activity (By similarity).By similarity
Sumoylated.By similarity
Ubiquitinated by RNF8 via 'Lys-48'-linked ubiquitination following DNA damage, leading to its degradation and removal from DNA damage sites.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP27641.
PaxDbiP27641.
PRIDEiP27641.

PTM databases

PhosphoSiteiP27641.

Expressioni

Developmental stagei

Expression increases during promyelocyte differentiation.1 Publication

Inductioni

Up-regulation during myogenesis is inhibited by cAMP, 3-aminobenzamide and sodium butyrate. Expression in myoblasts is unaffected by X-rays and UV light.1 Publication

Gene expression databases

BgeeiP27641.
ExpressionAtlasiP27641. baseline and differential.
GenevestigatoriP27641.

Interactioni

Subunit structurei

Heterodimer of a 70 kDa and a 80 kDa subunit. The dimer associates in a DNA-dependent manner with PRKDC to form the DNA-dependent protein kinase complex DNA-PK, and with the LIG4-XRCC4 complex. The dimer also associates with NAA15, and this complex displays DNA binding activity towards the osteocalcin FGF response element (OCFRE). In addition, the 80 kDa subunit binds to the osteoblast-specific transcription factors MSX2 and RUNX2. Interacts with ELF3. May interact with APLF. The XRCC5/6 dimer associates in a DNA-dependent manner with APEX1 (By similarity). Identified in a complex with DEAF1 and XRCC6 (By similarity).By similarity

Protein-protein interaction databases

BioGridi204608. 6 interactions.
IntActiP27641. 4 interactions.

Structurei

3D structure databases

ProteinModelPortaliP27641.
SMRiP27641. Positions 6-545, 591-710.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini251 – 460210KuAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni138 – 16528Leucine-zipperAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi720 – 7289EEXXXDL motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi478 – 52043Pro-richAdd
BLAST

Domaini

The EEXXXDDL motif is required for the interaction with catalytic subunit PRKDC and its recruitment to sites of DNA damage.By similarity

Sequence similaritiesi

Belongs to the ku80 family.Curated
Contains 1 Ku domain.Curated

Phylogenomic databases

eggNOGiNOG299744.
GeneTreeiENSGT00390000015674.
HOVERGENiHBG006237.
InParanoidiP27641.
KOiK10885.
OMAiGYMLGGT.
OrthoDBiEOG7DVD9X.
PhylomeDBiP27641.
TreeFamiTF101205.

Family and domain databases

Gene3Di1.10.1600.10. 1 hit.
1.25.40.240. 1 hit.
2.40.290.10. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR006164. Ku70/Ku80_beta-barrel_dom.
IPR024193. Ku80.
IPR005160. Ku_C.
IPR005161. Ku_N.
IPR014893. Ku_PK_bind.
IPR016194. SPOC_like_C_dom.
IPR002035. VWF_A.
[Graphical view]
PANTHERiPTHR12604:SF3. PTHR12604:SF3. 1 hit.
PfamiPF02735. Ku. 1 hit.
PF03730. Ku_C. 1 hit.
PF03731. Ku_N. 1 hit.
PF08785. Ku_PK_bind. 1 hit.
[Graphical view]
PIRSFiPIRSF016570. Ku80. 1 hit.
SMARTiSM00559. Ku78. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF100939. SSF100939. 1 hit.
SSF101420. SSF101420. 1 hit.
SSF53300. SSF53300. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P27641-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAWSGNKAAV VLCVDVGVAM GNSFPGEESP IEQAKKVMTM FVQRQVFSES
60 70 80 90 100
KDEIALVLYG TDGTDNALAG KDQYQNITVC RHLMLPDFDL LEDIGNKIQP
110 120 130 140 150
SSQQADFLDA LIVCMDLIQR ETIGKKFGKK HIEVFTDLSS PFSQDQLDVI
160 170 180 190 200
ICNLKKSGIS LQFFLPFPID KNGEPGERGD LDSGLDHLKP SFPQKGLTEQ
210 220 230 240 250
QKEGIRMVTR VMLSLEGEDG LDEIYSFSES LRQLCVFKKI ERRSMPWPCQ
260 270 280 290 300
LTIGPNLSIK IVAYKSIVQE KFKKSWVVVD ARTLKKEDIQ KETVYCLNDD
310 320 330 340 350
DETEVSKEDT IQGYRYGSDI IPFSKVDEEQ MKYKSEGKCF SVLGFCKSSQ
360 370 380 390 400
VHRRFFMGHQ VLKVFAAKDD EAAAVALSSL VHALDELNMV AIVRYAYDKR
410 420 430 440 450
SNPQVGVAFP YIKDAYECLV YVQLPFMEDL RQYMFSSLKN NKKCTPTEAQ
460 470 480 490 500
LSAIDDLIDS MSLVKKNEEE DIVEDLFPTS KIPNPEFQRL YQCLLHRALH
510 520 530 540 550
LQERLPPIQQ HILNMLDPPT EMKAKCESPL SKVKTLFPLT EVIKKKNQVT
560 570 580 590 600
AQDVFQDNHE EGPAAKKYKT EKEEDHISIS SLAEGNITKV GSVNPVENFR
610 620 630 640 650
FLVRQKIASF EEASLQLISH IEQFLDTNET LYFMKSMDCI KAFREEAIQF
660 670 680 690 700
SEEQRFNSFL EALREKVEIK QLNHFWEIVV QDGVTLITKD EGPGSSITAE
710 720 730
EATKFLAPKD KAKEDTTGPE EAGDVDDLLD MI
Length:732
Mass (Da):83,057
Last modified:February 5, 2008 - v4
Checksum:i391F0FAF7EB04288
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51G → V in CAA46999. (PubMed:1641347)Curated
Sequence conflicti24 – 241F → I in CAA46999. (PubMed:1641347)Curated
Sequence conflicti57 – 571V → A in CAA46999. (PubMed:1641347)Curated
Sequence conflicti66 – 694NALA → MPLS in CAA46999. (PubMed:1641347)Curated
Sequence conflicti120 – 1201R → H in AAD49720. 1 PublicationCurated
Sequence conflicti139 – 1391S → G in BAE38207. (PubMed:16141072)Curated
Sequence conflicti139 – 1391S → R in CAA46999. (PubMed:1641347)Curated
Sequence conflicti144 – 1441Q → K in CAA46999. (PubMed:1641347)Curated
Sequence conflicti157 – 1571S → C in CAA46999. (PubMed:1641347)Curated
Sequence conflicti226 – 2261S → F in AAD49720. 1 PublicationCurated
Sequence conflicti409 – 4102FP → SL in CAA46999. (PubMed:1641347)Curated
Sequence conflicti414 – 4141D → G in BAC38276. (PubMed:16141072)Curated
Sequence conflicti415 – 4151A → T in AAD49720. 1 PublicationCurated
Sequence conflicti418 – 4181C → R in CAA46999. (PubMed:1641347)Curated
Sequence conflicti442 – 4421K → M in AAD49720. 1 PublicationCurated
Sequence conflicti479 – 4791T → A in CAA46999. (PubMed:1641347)Curated
Sequence conflicti515 – 5162ML → IW in CAA46999. (PubMed:1641347)Curated
Sequence conflicti524 – 5241A → Q in CAA46999. (PubMed:1641347)Curated
Sequence conflicti530 – 5312LS → PL in CAA46999. (PubMed:1641347)Curated
Sequence conflicti558 – 5581N → H in AAD49720. 1 PublicationCurated
Sequence conflicti692 – 6921G → A in CAA46999. (PubMed:1641347)Curated
Sequence conflicti703 – 7031T → K in CAA46999. (PubMed:1641347)Curated
Sequence conflicti708 – 7081P → H in BAE39415. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66323 mRNA. Translation: CAA46999.1.
AF166486 mRNA. Translation: AAD49720.1.
AK081633 mRNA. Translation: BAC38276.1.
AK165470 mRNA. Translation: BAE38207.1.
AK167312 mRNA. Translation: BAE39415.1.
AK168913 mRNA. Translation: BAE40726.1.
AK169838 mRNA. Translation: BAE41402.1.
BC029218 mRNA. Translation: AAH29218.1.
BC051660 mRNA. Translation: AAH51660.1.
CCDSiCCDS35608.1.
PIRiS26303.
RefSeqiNP_033559.2. NM_009533.2.
UniGeneiMm.246952.

Genome annotation databases

EnsembliENSMUST00000027379; ENSMUSP00000027379; ENSMUSG00000026187.
GeneIDi22596.
KEGGimmu:22596.
UCSCiuc007bkl.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66323 mRNA. Translation: CAA46999.1 .
AF166486 mRNA. Translation: AAD49720.1 .
AK081633 mRNA. Translation: BAC38276.1 .
AK165470 mRNA. Translation: BAE38207.1 .
AK167312 mRNA. Translation: BAE39415.1 .
AK168913 mRNA. Translation: BAE40726.1 .
AK169838 mRNA. Translation: BAE41402.1 .
BC029218 mRNA. Translation: AAH29218.1 .
BC051660 mRNA. Translation: AAH51660.1 .
CCDSi CCDS35608.1.
PIRi S26303.
RefSeqi NP_033559.2. NM_009533.2.
UniGenei Mm.246952.

3D structure databases

ProteinModelPortali P27641.
SMRi P27641. Positions 6-545, 591-710.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204608. 6 interactions.
IntActi P27641. 4 interactions.

PTM databases

PhosphoSitei P27641.

Proteomic databases

MaxQBi P27641.
PaxDbi P27641.
PRIDEi P27641.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000027379 ; ENSMUSP00000027379 ; ENSMUSG00000026187 .
GeneIDi 22596.
KEGGi mmu:22596.
UCSCi uc007bkl.2. mouse.

Organism-specific databases

CTDi 7520.
MGIi MGI:104517. Xrcc5.

Phylogenomic databases

eggNOGi NOG299744.
GeneTreei ENSGT00390000015674.
HOVERGENi HBG006237.
InParanoidi P27641.
KOi K10885.
OMAi GYMLGGT.
OrthoDBi EOG7DVD9X.
PhylomeDBi P27641.
TreeFami TF101205.

Enzyme and pathway databases

Reactomei REACT_196447. IRF3-mediated induction of type I IFN.
REACT_224809. Processing of DNA ends prior to end rejoining.
REACT_254501. Nonhomologous End-joining (NHEJ).

Miscellaneous databases

NextBioi 302945.
PROi P27641.
SOURCEi Search...

Gene expression databases

Bgeei P27641.
ExpressionAtlasi P27641. baseline and differential.
Genevestigatori P27641.

Family and domain databases

Gene3Di 1.10.1600.10. 1 hit.
1.25.40.240. 1 hit.
2.40.290.10. 1 hit.
3.40.50.410. 1 hit.
InterProi IPR006164. Ku70/Ku80_beta-barrel_dom.
IPR024193. Ku80.
IPR005160. Ku_C.
IPR005161. Ku_N.
IPR014893. Ku_PK_bind.
IPR016194. SPOC_like_C_dom.
IPR002035. VWF_A.
[Graphical view ]
PANTHERi PTHR12604:SF3. PTHR12604:SF3. 1 hit.
Pfami PF02735. Ku. 1 hit.
PF03730. Ku_C. 1 hit.
PF03731. Ku_N. 1 hit.
PF08785. Ku_PK_bind. 1 hit.
[Graphical view ]
PIRSFi PIRSF016570. Ku80. 1 hit.
SMARTi SM00559. Ku78. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view ]
SUPFAMi SSF100939. SSF100939. 1 hit.
SSF101420. SSF101420. 1 hit.
SSF53300. SSF53300. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of a mouse cDNA encoding the 80 kDa subunit of the Ku (p70/p80) autoantigen."
    Falzon M., Kuff E.L.
    Nucleic Acids Res. 20:3784-3784(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  2. "Ku gene mutation of radiosensitive mouse mammary carcinoma cell line SX-9."
    Jiang G.C., Yuan L.Z., Wei K.
    Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Mammary carcinoma.
  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 and NOD.
    Tissue: Embryonic head, Embryonic heart, Embryonic liver, Kidney and Thymus.
  4. "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: 129/Sv X 129SvCp and FVB/N.
    Tissue: Embryonic stem cell and Mammary tumor.
  5. "Non-histone protein 1 (NHP1) is a member of the Ku protein family which is upregulated in differentiating mouse myoblasts and human promyelocytes."
    Oderwald H., Hughes M.J., Jost J.-P.
    FEBS Lett. 382:313-318(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE, INDUCTION.

Entry informationi

Entry nameiXRCC5_MOUSE
AccessioniPrimary (citable) accession number: P27641
Secondary accession number(s): Q3TE46
, Q3TJT0, Q3TN82, Q80UT1, Q8C4N6, Q8K1K7, Q9R169
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 5, 2008
Last modified: November 26, 2014
This is version 134 of the entry and version 4 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