Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

D3ZVH5 (D3ZVH5_RAT) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein names

Transformed mouse 3T3 cell double minute 2 homolog (Mouse) (Predicted), isoform CRA_b EMBL EDM16616.1
Gene names
Name:Mdm2 Ensembl ENSRNOP00000063449 RGD 1305332
Synonyms:Mdm2_predicted EMBL EDM16616.1
ORF Names:rCG_48669 EMBL EDM16616.1
OrganismRattus norvegicus (Rat) [Reference proteome] Ensembl ENSRNOP00000063449
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length458 AA.
Sequence statusComplete.
Protein existencePredicted

Ontologies

Keywords
   DomainZinc-finger RuleBase RU000353
   LigandMetal-binding
Zinc
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest

Inferred from electronic annotation. Source: Ensembl

cellular response to UV-C

Inferred from expression pattern PubMed 14558917. Source: RGD

cellular response to acid

Inferred from expression pattern PubMed 16598789. Source: RGD

cellular response to alkaloid

Inferred from expression pattern PubMed 19136059. Source: RGD

cellular response to antibiotic

Inferred from expression pattern PubMed 18469520. Source: RGD

cellular response to estrogen stimulus

Inferred from expression pattern PubMed 14667141. Source: RGD

cellular response to growth factor stimulus

Inferred from expression pattern PubMed 16091747. Source: RGD

cellular response to hydrogen peroxide

Inferred from expression pattern PubMed 19638633. Source: RGD

cellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

cellular response to organic cyclic compound

Inferred from expression pattern PubMed 19819240. Source: RGD

cellular response to organic substance

Inferred from expression pattern PubMed 19950214. Source: RGD

cellular response to peptide hormone stimulus

Inferred from expression pattern PubMed 19850968. Source: RGD

cellular response to vitamin B1

Inferred from expression pattern PubMed 15656374. Source: RGD

establishment of protein localization

Inferred from electronic annotation. Source: Ensembl

negative regulation of DNA damage response, signal transduction by p53 class mediator

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 17881359. Source: RGD

negative regulation of cell cycle arrest

Inferred from electronic annotation. Source: InterPro

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype PubMed 19850968. Source: RGD

negative regulation of gene expression

Inferred from mutant phenotype PubMed 19850968. Source: RGD

negative regulation of protein processing

Inferred from mutant phenotype PubMed 19638633. Source: RGD

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: InterPro

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 19103650. Source: RGD

peptidyl-lysine modification

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from mutant phenotype PubMed 19103650. Source: RGD

positive regulation of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein export from nucleus

Inferred from mutant phenotype PubMed 17881359. Source: RGD

protein complex assembly

Inferred from electronic annotation. Source: Ensembl

protein destabilization

Inferred from electronic annotation. Source: Ensembl

protein localization to nucleus

Inferred from electronic annotation. Source: Ensembl

protein ubiquitination

Inferred from mutant phenotype PubMed 16330492. Source: RGD

protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

response to carbohydrate

Inferred from expression pattern PubMed 18045764. Source: RGD

response to cocaine

Inferred from expression pattern PubMed 14625023. Source: RGD

response to drug

Inferred from expression pattern PubMed 19136059. Source: RGD

response to ether

Inferred from expression pattern PubMed 16790648. Source: RGD

response to iron ion

Inferred from expression pattern PubMed 20019189. Source: RGD

response to magnesium ion

Inferred from expression pattern PubMed 15165363. Source: RGD

response to morphine

Inferred from expression pattern PubMed 14625023. Source: RGD

response to steroid hormone

Inferred from expression pattern PubMed 17000718. Source: RGD

response to toxic substance

Inferred from expression pattern PubMed 17905399. Source: RGD

traversing start control point of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Inferred from direct assay PubMed 19819240. Source: RGD

nuclear body

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 17107963. Source: RGD

plasma membrane

Inferred from direct assay PubMed 14642282. Source: RGD

protein complex

Inferred from electronic annotation. Source: Ensembl

synapse

Inferred from direct assay PubMed 14642282. Source: RGD

   Molecular_functionp53 binding

Inferred from physical interaction PubMed 16330492. Source: RGD

peroxisome proliferator activated receptor binding

Inferred from physical interaction PubMed 19103650. Source: RGD

ubiquitin-protein ligase activity

Inferred from mutant phenotype PubMed 16330492. Source: RGD

zinc ion binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
D3ZVH5 [UniParc].

Last modified April 20, 2010. Version 1.
Checksum: A521BF918BA6E926

FASTA45851,051
        10         20         30         40         50         60 
MCNTNMSVST EGAAGTSQIP ASEQETLIIF YIGQYIMTKR LYDEKQQHIV YCSNDLLGDV 

        70         80         90        100        110        120 
FGVPSFSVKE HRKIYAMIYR NLVVVSQQDS GTSPSESRCQ PEGGSDLKDP VQASQEEKPS 

       130        140        150        160        170        180 
SSDVVSRPST SSRRRAISET EENTDELPGE RQRKRHRALS FDESLGLCVL REICCERSSS 

       190        200        210        220        230        240 
SEATDTPSHQ DLDDGVSDHS ADCLDQDSVS DQFSVEFEVE SLDSEDYSLS DEGHELSDED 

       250        260        270        280        290        300 
DEVYRVTVYQ AGESDADSFE GDPEISLADY WKCTSCNEMN PPLPSHCNRC WTLRENWLPD 

       310        320        330        340        350        360 
DKGKDKVEIS EKAKLESSDQ AEEGLDVPDG KKVTEDDAKE SSAEDSEEKV AQMLLSQESD 

       370        380        390        400        410        420 
DYSQPSTSSS IVYSSQESGK ELKEDTQDKE ESMESSFSLN AIEPCVICQG RPKNGCIVHG 

       430        440        450 
KTGHLMSCFT CAKKLKKRNK PCPVCRQPIQ MIVLTYFN 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Rat Genome Sequencing Project Consortium
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway Ensembl ENSRNOP00000063449.
[2]"Gene and alternative splicing annotation with AIR."
Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M., Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z., Istrail S., Li P., Sutton G.
Genome Res. 15:54-66(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: BN EMBL EDM16616.1.
[3]Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M., Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F. expand/collapse author list , Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: BN EMBL EDM16616.1.
[4]Ensembl
Submitted (JUL-2011) to UniProtKB
Cited for: IDENTIFICATION.
Strain: Brown Norway Ensembl ENSRNOP00000063449.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR06049829 Genomic DNA. No translation available.
CH473960 Genomic DNA. Translation: EDM16616.1.
CH473960 Genomic DNA. Translation: EDM16617.1.
RefSeqNP_001101569.1. NM_001108099.1.
UniGeneRn.91829.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000066767; ENSRNOP00000063449; ENSRNOG00000006304.
GeneID314856.
KEGGrno:314856.
UCSCRGD:1305332. rat.

Organism-specific databases

CTD4193.
RGD1305332. Mdm2.

Phylogenomic databases

GeneTreeENSGT00530000063539.
KOK06643.
OMALCVIREI.
OrthoDBEOG7RRF7T.

Family and domain databases

Gene3D1.10.245.10. 1 hit.
3.30.40.10. 1 hit.
InterProIPR015459. MDM2_E3_ligase.
IPR016495. p53_neg-reg_MDM_2/4.
IPR003121. SWIB_MDM2_domain.
IPR001876. Znf_RanBP2.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERPTHR10360:SF9. PTHR10360:SF9. 1 hit.
PfamPF02201. SWIB. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view]
PIRSFPIRSF006748. p53_MDM_2/4. 1 hit.
SMARTSM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF47592. SSF47592. 2 hits.
PROSITEPS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio668312.

Entry information

Entry nameD3ZVH5_RAT
AccessionPrimary (citable) accession number: D3ZVH5
Entry history
Integrated into UniProtKB/TrEMBL: April 20, 2010
Last sequence update: April 20, 2010
Last modified: April 16, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)