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Protein
Submitted name:

Protein Mdm2

Gene

Mdm2

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 5 out of 5-Protein predictedi

Functioni

GO - Molecular functioni

  1. p53 binding Source: RGD
  2. peroxisome proliferator activated receptor binding Source: RGD
  3. ubiquitin-protein transferase activity Source: RGD
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. cellular response to alkaloid Source: RGD
  2. cellular response to antibiotic Source: RGD
  3. cellular response to estrogen stimulus Source: RGD
  4. cellular response to growth factor stimulus Source: RGD
  5. cellular response to hydrogen peroxide Source: RGD
  6. cellular response to hypoxia Source: Ensembl
  7. cellular response to organic cyclic compound Source: RGD
  8. cellular response to organic substance Source: RGD
  9. cellular response to peptide hormone stimulus Source: RGD
  10. cellular response to UV-C Source: RGD
  11. cellular response to vitamin B1 Source: RGD
  12. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Ensembl
  13. establishment of protein localization Source: Ensembl
  14. negative regulation of apoptotic process Source: RGD
  15. negative regulation of cell cycle arrest Source: InterPro
  16. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: RGD
  17. negative regulation of DNA damage response, signal transduction by p53 class mediator Source: Ensembl
  18. negative regulation of gene expression Source: RGD
  19. negative regulation of protein processing Source: RGD
  20. negative regulation of transcription, DNA-templated Source: RGD
  21. negative regulation of transcription from RNA polymerase II promoter Source: InterPro
  22. peptidyl-lysine modification Source: Ensembl
  23. positive regulation of gene expression Source: RGD
  24. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
  25. positive regulation of protein export from nucleus Source: RGD
  26. protein complex assembly Source: Ensembl
  27. protein destabilization Source: Ensembl
  28. protein localization to nucleus Source: Ensembl
  29. protein ubiquitination Source: RGD
  30. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: Ensembl
  31. response to carbohydrate Source: RGD
  32. response to cocaine Source: RGD
  33. response to drug Source: RGD
  34. response to ether Source: RGD
  35. response to iron ion Source: RGD
  36. response to magnesium ion Source: RGD
  37. response to morphine Source: RGD
  38. response to steroid hormone Source: RGD
  39. response to toxic substance Source: RGD
  40. traversing start control point of mitotic cell cycle Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_198729. Constitutive PI3K/AKT Signaling in Cancer.
REACT_203770. Oxidative Stress Induced Senescence.
REACT_207379. Stabilization of p53.
REACT_215142. Oncogene Induced Senescence.
REACT_252972. AKT phosphorylates targets in the cytosol.
REACT_258022. Trafficking of AMPA receptors.

Names & Taxonomyi

Protein namesi
Submitted name:
Protein Mdm2Imported
Submitted name:
Transformed mouse 3T3 cell double minute 2 homolog (Mouse) (Predicted), isoform CRA_bImported
Gene namesi
Name:Mdm2Imported
Synonyms:Mdm2_predictedImported
ORF Names:rCG_48669Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 7

Organism-specific databases

RGDi1305332. Mdm2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: RGD
  2. nuclear body Source: Ensembl
  3. nucleolus Source: Ensembl
  4. nucleus Source: RGD
  5. plasma membrane Source: RGD
  6. protein complex Source: Ensembl
  7. synapse Source: RGD
Complete GO annotation...

Family & Domainsi

Keywords - Domaini

Zinc-fingerUniRule annotation

Phylogenomic databases

GeneTreeiENSGT00530000063539.
KOiK06643.
OMAiFEREETQ.
OrthoDBiEOG7RRF7T.

Family and domain databases

Gene3Di1.10.245.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR015459. 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]
PANTHERiPTHR10360:SF11. PTHR10360:SF11. 1 hit.
PfamiPF02201. SWIB. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view]
PIRSFiPIRSF006748. p53_MDM_2/4. 1 hit.
SMARTiSM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF47592. SSF47592. 2 hits.
PROSITEiPS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D3ZVH5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCNTNMSVST EGAAGTSQIP ASEQETLIIF YIGQYIMTKR LYDEKQQHIV
60 70 80 90 100
YCSNDLLGDV FGVPSFSVKE HRKIYAMIYR NLVVVSQQDS GTSPSESRCQ
110 120 130 140 150
PEGGSDLKDP VQASQEEKPS SSDVVSRPST SSRRRAISET EENTDELPGE
160 170 180 190 200
RQRKRHRALS FDESLGLCVL REICCERSSS SEATDTPSHQ DLDDGVSDHS
210 220 230 240 250
ADCLDQDSVS DQFSVEFEVE SLDSEDYSLS DEGHELSDED DEVYRVTVYQ
260 270 280 290 300
AGESDADSFE GDPEISLADY WKCTSCNEMN PPLPSHCNRC WTLRENWLPD
310 320 330 340 350
DKGKDKVEIS EKAKLESSDQ AEEGLDVPDG KKVTEDDAKE SSAEDSEEKV
360 370 380 390 400
AQMLLSQESD DYSQPSTSSS IVYSSQESGK ELKEDTQDKE ESMESSFSLN
410 420 430 440 450
AIEPCVICQG RPKNGCIVHG KTGHLMSCFT CAKKLKKRNK PCPVCRQPIQ

MIVLTYFN
Length:458
Mass (Da):51,051
Last modified:April 20, 2010 - v1
Checksum:iA521BF918BA6E926
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06049829 Genomic DNA. No translation available.
CH473960 Genomic DNA. Translation: EDM16616.1.
CH473960 Genomic DNA. Translation: EDM16617.1.
RefSeqiNP_001101569.1. NM_001108099.1.
UniGeneiRn.91829.

Genome annotation databases

EnsembliENSRNOT00000066767; ENSRNOP00000063449; ENSRNOG00000006304.
GeneIDi314856.
KEGGirno:314856.
UCSCiRGD:1305332. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06049829 Genomic DNA. No translation available.
CH473960 Genomic DNA. Translation: EDM16616.1.
CH473960 Genomic DNA. Translation: EDM16617.1.
RefSeqiNP_001101569.1. NM_001108099.1.
UniGeneiRn.91829.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000066767; ENSRNOP00000063449; ENSRNOG00000006304.
GeneIDi314856.
KEGGirno:314856.
UCSCiRGD:1305332. rat.

Organism-specific databases

CTDi4193.
RGDi1305332. Mdm2.

Phylogenomic databases

GeneTreeiENSGT00530000063539.
KOiK06643.
OMAiFEREETQ.
OrthoDBiEOG7RRF7T.

Enzyme and pathway databases

ReactomeiREACT_198729. Constitutive PI3K/AKT Signaling in Cancer.
REACT_203770. Oxidative Stress Induced Senescence.
REACT_207379. Stabilization of p53.
REACT_215142. Oncogene Induced Senescence.
REACT_252972. AKT phosphorylates targets in the cytosol.
REACT_258022. Trafficking of AMPA receptors.

Miscellaneous databases

NextBioi668312.

Family and domain databases

Gene3Di1.10.245.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR015459. 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]
PANTHERiPTHR10360:SF11. PTHR10360:SF11. 1 hit.
PfamiPF02201. SWIB. 1 hit.
PF00641. zf-RanBP. 1 hit.
[Graphical view]
PIRSFiPIRSF006748. p53_MDM_2/4. 1 hit.
SMARTiSM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF47592. SSF47592. 2 hits.
PROSITEiPS01358. ZF_RANBP2_1. 1 hit.
PS50199. ZF_RANBP2_2. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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 NorwayImported.
  2. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  4. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiD3ZVH5_RAT
AccessioniPrimary (citable) accession number: D3ZVH5
Entry historyi
Integrated into UniProtKB/TrEMBL: April 20, 2010
Last sequence update: April 20, 2010
Last modified: February 4, 2015
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.