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P13405

- RB_MOUSE

UniProt

P13405 - RB_MOUSE

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Protein

Retinoblastoma-associated protein

Gene

Rb1

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

Functioni

Key regulator of entry into cell division that acts as a tumor suppressor. Promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, SUV420H1 and SUV420H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex (By similarity).By similarity

GO - Molecular functioni

  1. core promoter binding Source: Ensembl
  2. enzyme binding Source: UniProtKB
  3. kinase binding Source: UniProtKB
  4. RNA polymerase II activating transcription factor binding Source: BHF-UCL
  5. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. cell cycle arrest Source: MGI
  2. cell division Source: MGI
  3. cell morphogenesis involved in neuron differentiation Source: MGI
  4. chromatin modification Source: UniProtKB-KW
  5. digestive tract development Source: MGI
  6. enucleate erythrocyte differentiation Source: MGI
  7. G1/S transition of mitotic cell cycle Source: MGI
  8. glial cell apoptotic process Source: MGI
  9. hepatocyte apoptotic process Source: MGI
  10. maintenance of mitotic sister chromatid cohesion Source: Ensembl
  11. myoblast differentiation Source: UniProtKB
  12. negative regulation of cell cycle Source: MGI
  13. negative regulation of cell proliferation Source: MGI
  14. negative regulation of epithelial cell proliferation Source: MGI
  15. negative regulation of G1/S transition of mitotic cell cycle Source: MGI
  16. negative regulation of mitotic cell cycle Source: MGI
  17. negative regulation of protein kinase activity Source: UniProtKB
  18. negative regulation of smoothened signaling pathway Source: MGI
  19. negative regulation of transcription, DNA-templated Source: MGI
  20. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  21. negative regulation of transcription involved in G1/S transition of mitotic cell cycle Source: BHF-UCL
  22. neuron apoptotic process Source: MGI
  23. neuron differentiation Source: MGI
  24. neuron maturation Source: MGI
  25. neuron projection development Source: MGI
  26. positive regulation of macrophage differentiation Source: MGI
  27. positive regulation of mitotic metaphase/anaphase transition Source: Ensembl
  28. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  29. protein localization to chromosome, centromeric region Source: Ensembl
  30. Ras protein signal transduction Source: Ensembl
  31. regulation of cell cycle Source: MGI
  32. regulation of cohesin localization to chromatin Source: Ensembl
  33. regulation of lipid kinase activity Source: UniProtKB
  34. sister chromatid biorientation Source: Ensembl
  35. skeletal muscle cell differentiation Source: MGI
  36. striated muscle cell differentiation Source: MGI
  37. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_196580. Condensation of Prophase Chromosomes.
REACT_208887. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_209428. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
REACT_219010. Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
REACT_223647. Cyclin A:Cdk2-associated events at S phase entry.
REACT_245230. Orc1 removal from chromatin.
REACT_258573. Cyclin D associated events in G1.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinoblastoma-associated protein
Alternative name(s):
pRb
Short name:
Rb
pp105
Gene namesi
Name:Rb1
Synonyms:Rb-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:97874. Rb1.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: UniProtKB
  2. PML body Source: UniProtKB
  3. Rb-E2F complex Source: BHF-UCL
  4. spindle Source: MGI
  5. transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi746 – 7461I → A: Abolishes the interaction with many chromatin regulators but not that with SUV420H1 and SUV420H2; when associated with A-750 and A-754. 1 Publication
Mutagenesisi750 – 7501N → A: Abolishes the interaction with many chromatin regulators but not that with SUV420H1 and SUV420H2; when associated with A-746 and A-754. 1 Publication
Mutagenesisi754 – 7541M → A: Abolishes the interaction with many chromatin regulators but not that with SUV420H1 and SUV420H2; when associated with A-746 and A-750. 1 Publication

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 921920Retinoblastoma-associated proteinPRO_0000167837Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N,N-dimethylproline; by NTM11 Publication
Modified residuei31 – 311PhosphoserineBy similarity
Modified residuei243 – 2431Phosphoserine; by CDK1By similarity
Modified residuei246 – 2461Phosphothreonine; by CDK1By similarity
Modified residuei350 – 3501PhosphothreonineBy similarity
Modified residuei367 – 3671Phosphothreonine; by CDK1By similarity
Modified residuei561 – 5611Phosphoserine; by CDK2By similarity
Modified residuei605 – 6051Phosphoserine; by CHEK2 and CHEK1By similarity
Modified residuei788 – 7881PhosphoserineBy similarity
Modified residuei800 – 8001Phosphoserine; by CDK1 and CDK3By similarity
Modified residuei803 – 8031N6-methyllysine; by SMYD2By similarity
Modified residuei804 – 8041Phosphoserine; by CDK1 and CDK3By similarity
Modified residuei814 – 8141Phosphothreonine; by CDK6By similarity
Modified residuei816 – 8161PhosphothreonineBy similarity
Modified residuei819 – 8191Phosphothreonine; by CDK4
Modified residuei834 – 8341PhosphothreonineBy similarity
Modified residuei853 – 8531N6-methyllysine; by SMYD2By similarity
Modified residuei866 – 8661N6-acetyllysine; by PCAFBy similarity
Modified residuei867 – 8671N6-acetyllysine; by PCAFBy similarity

Post-translational modificationi

Phosphorylated by CDK6 and CDK4, and subsequently by CDK2 at Ser-561 in G1, thereby releasing E2F1 which is then able to activate cell growth. Dephosphorylated at the late M phase. Phosphorylation of threonine residues in domain C promotes interaction between the C-terminal domain C and the Pocket domain, and thereby inhibits interactions with heterodimeric E2F/DP transcription factor complexes. Dephosphorylated at Ser-788 by calcineruin upon calcium stimulation. CDK3/cyclin-C-mediated phosphorylation at Ser-800 and Ser-804 is required for G0-G1 transition (By similarity). Phosphorylated by CDK1 and CDK2 upon TGFB1-mediated apoptosis (By similarity).By similarity
Monomethylation at Lys-803 by SMYD2 enhances phosphorylation at Ser-800 and Ser-804, and promotes cell cycle progression. Monomethylation at Lys-853 by SMYD2 promotes interaction with L3MBTL1 (By similarity). N-terminus is methylated by METTL11A/NTM1.By similarity1 Publication
Acetylation at Lys-866 and Lys-867 regulates subcellular localization, at least during keratinocytes differentiation.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP13405.
PaxDbiP13405.
PRIDEiP13405.

PTM databases

PhosphoSiteiP13405.

Expressioni

Tissue specificityi

Expressed in the cell nuclei of renal tubules, hepathocytes and skeletal muscles. Colocalizes with RB1CC1 in various tissues.1 Publication

Gene expression databases

BgeeiP13405.
CleanExiMM_RB1.
ExpressionAtlasiP13405. baseline and differential.
GenevestigatoriP13405.

Interactioni

Subunit structurei

The hypophosphorylated form interacts with and sequesters the E2F1 transcription factor. Interacts with heterodimeric E2F/DP transcription factor complexes containing TFDP1 and either E2F1, E2F3, E2F4 or E2F5, or TFDP2 and E2F4. The unphosphorylated form interacts with EID1, ARID3B, KDM5A, SUV39H1, MJD2A/JHDM3A and THOC1. Interacts with the N-terminal domain of TAF1. Interacts with SNW1, ATAD5, AATF, DNMT1, LIN9, LMNA, SUV420H1, SUV420H2, PELP1, UHRF2, TMPO-alpha and USP4. May interact with NDC80. Interacts with GRIP1 and UBR4. Interacts with ARID4A and KDM5B. Interacts with E4F1 and LIMD1. Interacts with SMARCA4/BRG1 and HDAC1. Interacts with USP4. Interacts (when methylated at Lys-853) with L3MBTL1. Binds to CDK1 and CDK2. Interacts with CHEK2; phosphorylates RB1 (By similarity). Interacts with PRMT2.By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CenpfQ155P74EBI-971782,EBI-2211248
DgkzQ80UP32EBI-971782,EBI-971774
Ifi202Q9R0027EBI-971782,EBI-3043899
Pax3P246103EBI-971782,EBI-1208116
Pdx1P529462EBI-971782,EBI-7128945
Smarca4Q3TKT43EBI-971782,EBI-1210244
Vsx2Q614122EBI-971782,EBI-1208174

Protein-protein interaction databases

BioGridi202815. 37 interactions.
DIPiDIP-37637N.
IntActiP13405. 16 interactions.
MINTiMINT-225292.

Structurei

3D structure databases

ProteinModelPortaliP13405.
SMRiP13405. Positions 47-779, 822-865.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni367 – 764398Pocket; binds T and E1ABy similarityAdd
BLAST
Regioni367 – 573207Domain ABy similarityAdd
BLAST
Regioni574 – 63259SpacerBy similarityAdd
BLAST
Regioni633 – 764132Domain BBy similarityAdd
BLAST
Regioni756 – 921166Interaction with LIMD1By similarityAdd
BLAST
Regioni764 – 921158Domain; mediates interaction with E4F1By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi863 – 8697Nuclear localization signalBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi9 – 124Poly-Ala
Compositional biasi14 – 229Poly-Pro

Sequence similaritiesi

Belongs to the retinoblastoma protein (RB) family.Curated

Phylogenomic databases

eggNOGiNOG296920.
GeneTreeiENSGT00530000063235.
HOGENOMiHOG000136539.
HOVERGENiHBG008967.
InParanoidiP13405.
KOiK06618.
OMAiTNILQYA.
OrthoDBiEOG7P5T04.
TreeFamiTF105568.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR002720. RB_A.
IPR002719. RB_B.
IPR015030. RB_C.
IPR028309. RB_fam.
IPR024599. RB_N.
[Graphical view]
PANTHERiPTHR13742. PTHR13742. 1 hit.
PfamiPF11934. DUF3452. 1 hit.
PF01858. RB_A. 1 hit.
PF01857. RB_B. 1 hit.
PF08934. Rb_C. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.

Sequencei

Sequence statusi: Complete.

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

P13405-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPPKAPRRAA AAEPPPPPPP PPREDDPAQD SGPEELPLAR LEFEEIEEPE
60 70 80 90 100
FIALCQKLKV PDHVRERAWL TWEKVSSVDG ILEGYIQKKK ELWGICIFIA
110 120 130 140 150
AVDLDEMPFT FTELQKSIET SVYKFFDLLK EIDTSTKVDN AMSRLLKKYN
160 170 180 190 200
VLCALYSKLE RTCELIYLTQ PSSALSTEIN SMLVLKISWI TFLLAKGEVL
210 220 230 240 250
QMEDDLVISF QLMLCVVDYF IKFSPPALLR EPYKTAAIPI NGSPRTPRRG
260 270 280 290 300
QNRSARIAKQ LENDTRIIEV LCKEHECNID EVKNVYFKNF IPFINSLGIV
310 320 330 340 350
SSNGLPEVES LSKRYEEVYL KNKDLDARLF LDHDKTLQTD PIDSFETERT
360 370 380 390 400
PRKNNPDEEA NVVTPHTPVR TVMNTIQQLM VILNSASDQP SENLISYFNN
410 420 430 440 450
CTVNPKENIL KRVKDVGHIF KEKFANAVGQ GCVDIGVQRY KLGVRLYYRV
460 470 480 490 500
MESMLKSEEE RLSIQNFSKL LNDNIFHMSL LACALEVVMA TYSRSTLQHL
510 520 530 540 550
DSGTDLSFPW ILNVLNLKAF DFYKVIESFI KVEANLTREM IKHLERCEHR
560 570 580 590 600
IMESLAWLSD SPLFDLIKQS KDGEGPDNLE PACPLSLPLQ GNHTAADMYL
610 620 630 640 650
SPLRSPKKRT STTRVNSAAN TETQAASAFH TQKPLKSTSL ALFYKKVYRL
660 670 680 690 700
AYLRLNTLCA RLLSDHPELE HIIWTLFQHT LQNEYELMRD RHLDQIMMCS
710 720 730 740 750
MYGICKVKNI DLKFKIIVTA YKDLPHAAQE TFKRVLIREE EFDSIIVFYN
760 770 780 790 800
SVFMQRLKTN ILQYASTRPP TLSPIPHIPR SPYKFSSSPL RIPGGNIYIS
810 820 830 840 850
PLKSPYKISE GLPTPTKMTP RSRILVSIGE SFGTSEKFQK INQMVCNSDR
860 870 880 890 900
VLKRSAEGGN PPKPLKKLRF DIEGADEADG SKHLPAESKF QQKLAEMTST
910 920
RTRMQKQRMN ESKDVSNKEE K
Length:921
Mass (Da):105,367
Last modified:July 27, 2011 - v2
Checksum:iAE81D35A07ADB493
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti867 – 8682KL → NV in AAA39964. (PubMed:2671991)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26391 mRNA. Translation: AAA39964.1.
DQ400415 mRNA. Translation: ABD72475.1.
BC096525 mRNA. Translation: AAH96525.1.
CCDSiCCDS27267.1.
PIRiA33718.
RefSeqiNP_033055.2. NM_009029.2.
UniGeneiMm.273862.

Genome annotation databases

EnsembliENSMUST00000022701; ENSMUSP00000022701; ENSMUSG00000022105.
GeneIDi19645.
KEGGimmu:19645.
UCSCiuc007upp.2. mouse.

Cross-referencesi

Web resourcesi

Wikipedia

Retinoblastoma protein entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26391 mRNA. Translation: AAA39964.1 .
DQ400415 mRNA. Translation: ABD72475.1 .
BC096525 mRNA. Translation: AAH96525.1 .
CCDSi CCDS27267.1.
PIRi A33718.
RefSeqi NP_033055.2. NM_009029.2.
UniGenei Mm.273862.

3D structure databases

ProteinModelPortali P13405.
SMRi P13405. Positions 47-779, 822-865.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202815. 37 interactions.
DIPi DIP-37637N.
IntActi P13405. 16 interactions.
MINTi MINT-225292.

PTM databases

PhosphoSitei P13405.

Proteomic databases

MaxQBi P13405.
PaxDbi P13405.
PRIDEi P13405.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022701 ; ENSMUSP00000022701 ; ENSMUSG00000022105 .
GeneIDi 19645.
KEGGi mmu:19645.
UCSCi uc007upp.2. mouse.

Organism-specific databases

CTDi 5925.
MGIi MGI:97874. Rb1.

Phylogenomic databases

eggNOGi NOG296920.
GeneTreei ENSGT00530000063235.
HOGENOMi HOG000136539.
HOVERGENi HBG008967.
InParanoidi P13405.
KOi K06618.
OMAi TNILQYA.
OrthoDBi EOG7P5T04.
TreeFami TF105568.

Enzyme and pathway databases

Reactomei REACT_196580. Condensation of Prophase Chromosomes.
REACT_208887. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_209428. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
REACT_219010. Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes.
REACT_223647. Cyclin A:Cdk2-associated events at S phase entry.
REACT_245230. Orc1 removal from chromatin.
REACT_258573. Cyclin D associated events in G1.

Miscellaneous databases

NextBioi 296890.
PROi P13405.
SOURCEi Search...

Gene expression databases

Bgeei P13405.
CleanExi MM_RB1.
ExpressionAtlasi P13405. baseline and differential.
Genevestigatori P13405.

Family and domain databases

Gene3Di 1.10.472.10. 2 hits.
InterProi IPR013763. Cyclin-like.
IPR002720. RB_A.
IPR002719. RB_B.
IPR015030. RB_C.
IPR028309. RB_fam.
IPR024599. RB_N.
[Graphical view ]
PANTHERi PTHR13742. PTHR13742. 1 hit.
Pfami PF11934. DUF3452. 1 hit.
PF01858. RB_A. 1 hit.
PF01857. RB_B. 1 hit.
PF08934. Rb_C. 1 hit.
[Graphical view ]
SMARTi SM00385. CYCLIN. 1 hit.
[Graphical view ]
SUPFAMi SSF47954. SSF47954. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and expression of the murine retinoblastoma gene and characterization of its encoded protein."
    Bernards R., Schackleford G.M., Gerber M.R., Horowitz J.M., Friend S.H., Schartl M., Bogenmann E., Rapaport J., McGee T., Dryja T.P., Weinberg R.A.
    Proc. Natl. Acad. Sci. U.S.A. 86:6474-6478(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequencing of the full-length cDNA sequence of the murine retinoblastoma gene."
    Wu J., Liao J.D.
    Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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/6.
    Tissue: Brain.
  4. "DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters."
    Robertson K.D., Ait-Si-Ali S., Yokochi T., Wade P.A., Jones P.L., Wolffe A.P.
    Nat. Genet. 25:338-342(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DNMT1.
  5. "pRB binds to and modulates the transrepressing activity of the E1A-regulated transcription factor p120E4F."
    Fajas L., Paul C., Zugasti O., Le Cam L., Polanowska J., Fabbrizio E., Medema R., Vignais M.-L., Sardet C.
    Proc. Natl. Acad. Sci. U.S.A. 97:7738-7743(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH E4F1.
  6. "Association of UNP, a ubiquitin-specific protease, with the pocket proteins pRb, p107 and p130."
    Blanchette P., Gilchrist C.A., Baker R.T., Gray D.A.
    Oncogene 20:5533-5537(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH USP4.
  7. "Isolation, characterization and mapping of the mouse and human RB1CC1 genes."
    Chano T., Ikegawa S., Saito-Ohara F., Inazawa J., Mabuchi A., Saeki Y., Okabe H.
    Gene 291:29-34(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, COLOCALIZATION WITH RB1CC1.
    Strain: C57BL/6.
    Tissue: Skeletal muscle.
  8. "Role of the RB1 family in stabilizing histone methylation at constitutive heterochromatin."
    Gonzalo S., Garcia-Cao M., Fraga M.F., Schotta G., Peters A.H.F.M., Cotter S.E., Eguia R., Dean D.C., Esteller M., Jenuwein T., Blasco M.A.
    Nat. Cell Biol. 7:420-428(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SUV420H1 AND SUV420H2.
  9. "Frag1, a homolog of alternative replication factor C subunits, links replication stress surveillance with apoptosis."
    Ishii H., Inageta T., Mimori K., Saito T., Sasaki H., Isobe M., Mori M., Croce C.M., Huebner K., Ozawa K., Furukawa Y.
    Proc. Natl. Acad. Sci. U.S.A. 102:9655-9660(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATAD5.
  10. "The arginine methyltransferase PRMT2 binds RB and regulates E2F function."
    Yoshimoto T., Boehm M., Olive M., Crook M.F., San H., Langenickel T., Nabel E.G.
    Exp. Cell Res. 312:2040-2053(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRMT2.
  11. Cited for: FUNCTION, INTERACTION WITH SUV420H1 AND SUV420H2, MUTAGENESIS OF ILE-746; ASN-750 AND MET-754.
  12. "NRMT is an alpha-N-methyltransferase that methylates RCC1 and retinoblastoma protein."
    Tooley C.E., Petkowski J.J., Muratore-Schroeder T.L., Balsbaugh J.L., Shabanowitz J., Sabat M., Minor W., Hunt D.F., Macara I.G.
    Nature 466:1125-1128(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE OF INITIATOR METHIONINE, METHYLATION AT PRO-2.

Entry informationi

Entry nameiRB_MOUSE
AccessioniPrimary (citable) accession number: P13405
Secondary accession number(s): Q4VA62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 159 of the entry and version 2 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