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Q9QXK2 (RAD18_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
E3 ubiquitin-protein ligase RAD18

EC=6.3.2.-
Alternative name(s):
Postreplication repair protein RAD18
Short name=mRAD18Sc
Gene names
Name:Rad18
Synonyms:Rad18sc
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E3 ubiquitin-protein ligase involved in postreplication repair of UV-damaged DNA. Postreplication repair functions in gap-filling of a daughter strand on replication of damaged DNA. Associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. Has ssDNA binding activity.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Homodimer. Interacts with UBE2A and UBE2B, one homodimer binding one molecule of UBE2B. Interacts with HLTF and SHPRH. Interacts with SPRTN; leading to enhance chromatin association of RAD18 and RAD18-mediated PCNA ubiquitination and translesion DNA synthesis By similarity.

Subcellular location

Nucleus.

Tissue specificity

Expressed in thymus, spleen, brain, and ovary.

Sequence similarities

Belongs to the RAD18 family.

Contains 1 RING-type zinc finger.

Contains 1 SAP domain.

Contains 1 UBZ-type zinc finger.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 509509E3 ubiquitin-protein ligase RAD18
PRO_0000056150

Regions

Domain248 – 28235SAP
Zinc finger25 – 6440RING-type
Zinc finger201 – 22424UBZ-type
Motif232 – 2409LR motif

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue991Phosphoserine By similarity
Modified residue1031Phosphoserine By similarity
Modified residue1641Phosphoserine By similarity
Modified residue4851Phosphoserine By similarity

Experimental info

Sequence conflict91W → C in AAF19193. Ref.1
Sequence conflict2681Q → P in AAF19193. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9QXK2 [UniParc].

Last modified June 6, 2002. Version 2.
Checksum: BF7717D1A69738F9

FASTA50957,412
        10         20         30         40         50         60 
MEVLAEPRWP PGLAVMKTID DLLRCGICFE YFNIAVIIPQ CSHNYCSLCI RKFLSYKTQC 

        70         80         90        100        110        120 
PTCCVAVTEP DLRNNRLLDE LVKSMNFART HLLQFALESP PISPVSSTSK KVVVKVHNAD 

       130        140        150        160        170        180 
AAQHPVKQAN RLMDKFLIRE TGDCVFELLG KENERKFSPQ KELSTSAEIK ETSLLGKPVL 

       190        200        210        220        230        240 
GLSDANGPVT PSTSTMKLDT KVSCPVCGVS IPENHINKHL DSCLSREEKK ESLRSSAHKR 

       250        260        270        280        290        300 
KPLPKTVYNL LSDRDLKKKL KQYGLSVQGN KQQLIKRHQE FVHMYNAQCD ALHPKSAAEI 

       310        320        330        340        350        360 
VQEIESMEKT RMRLEASKLN ENVMVFTKNQ TEKEIEEVHS EYRKKHQNAF QLLVDQAKKG 

       370        380        390        400        410        420 
YKKTGRVSQA AAMRTDEPAE TLPSMRTDEP AETLPSMRTD EPAETLPLMR ADEPAETLPS 

       430        440        450        460        470        480 
ECIAQEDNVS FSDTVSVTNH FPQPQLDSPG PSEPERPDDS SSCTDILFSS DSDSCNRNDQ 

       490        500 
NREVSPQQTR RTRASECVEI EPRNKRNKN 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of mRAD18Sc, a mouse homolog of the yeast postreplication repair gene RAD18."
van der Laan R., Roest H.P., Hoogerbrugge J.W., Smit E.M.E., Slater R., Baarends W.M., Hoeijmakers J.H.J., Grootegoed J.A.
Genomics 69:86-94(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[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. 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: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF205278 mRNA. Translation: AAF19193.1.
AK012795 mRNA. Translation: BAB28475.1.
CCDSCCDS39589.1.
RefSeqNP_067360.2. NM_021385.2.
UniGeneMm.103812.

3D structure databases

ProteinModelPortalQ9QXK2.
SMRQ9QXK2. Positions 8-95.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid208379. 2 interactions.
STRING10090.ENSMUSP00000070619.

PTM databases

PhosphoSiteQ9QXK2.

Proteomic databases

MaxQBQ9QXK2.
PRIDEQ9QXK2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000077088; ENSMUSP00000076341; ENSMUSG00000030254.
GeneID58186.
KEGGmmu:58186.
UCSCuc009dec.2. mouse.

Organism-specific databases

CTD56852.
MGIMGI:1890476. Rad18.

Phylogenomic databases

eggNOGCOG5432.
GeneTreeENSGT00390000011230.
HOGENOMHOG000234845.
HOVERGENHBG054721.
KOK10627.
PhylomeDBQ9QXK2.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9QXK2.
BgeeQ9QXK2.
CleanExMM_RAD18.
GenevestigatorQ9QXK2.

Family and domain databases

Gene3D1.10.720.30. 1 hit.
3.30.40.10. 1 hit.
InterProIPR003034. SAP_dom.
IPR018957. Znf_C3HC4_RING-type.
IPR006642. Znf_Rad18_put.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF02037. SAP. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
SM00513. SAP. 1 hit.
SM00734. ZnF_Rad18. 1 hit.
[Graphical view]
PROSITEPS50800. SAP. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio314151.
PROQ9QXK2.
SOURCESearch...

Entry information

Entry nameRAD18_MOUSE
AccessionPrimary (citable) accession number: Q9QXK2
Secondary accession number(s): Q9CZB8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: June 6, 2002
Last modified: July 9, 2014
This is version 102 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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