Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P28028

- BRAF_MOUSE

UniProt

P28028 - BRAF_MOUSE

Protein

Serine/threonine-protein kinase B-raf

Gene

Braf

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May play a role in the postsynaptic responses of hippocampal neuron By similarity.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Binds 2 zinc ions per subunit.Curated

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi219 – 2191Zinc 1By similarity
    Metal bindingi232 – 2321Zinc 2By similarity
    Metal bindingi235 – 2351Zinc 2By similarity
    Metal bindingi245 – 2451Zinc 1By similarity
    Metal bindingi248 – 2481Zinc 1By similarity
    Metal bindingi253 – 2531Zinc 2By similarity
    Metal bindingi256 – 2561Zinc 2By similarity
    Metal bindingi264 – 2641Zinc 1By similarity
    Binding sitei520 – 5201ATPPROSITE-ProRule annotation
    Active sitei613 – 6131Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi500 – 5089ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calcium ion binding Source: Ensembl
    3. MAP kinase kinase kinase activity Source: Ensembl
    4. protein binding Source: IntAct
    5. protein kinase activity Source: BHF-UCL

    GO - Biological processi

    1. alpha-beta T cell differentiation Source: MGI
    2. CD4-positive, alpha-beta T cell differentiation Source: MGI
    3. cell differentiation Source: MGI
    4. cellular response to calcium ion Source: Ensembl
    5. cellular response to drug Source: MGI
    6. long-term synaptic potentiation Source: MGI
    7. myeloid progenitor cell differentiation Source: MGI
    8. negative regulation of endothelial cell apoptotic process Source: MGI
    9. negative regulation of fibroblast migration Source: MGI
    10. negative regulation of neuron apoptotic process Source: MGI
    11. negative regulation of synaptic vesicle exocytosis Source: MGI
    12. positive regulation of ERK1 and ERK2 cascade Source: MGI
    13. positive regulation of gene expression Source: Ensembl
    14. positive regulation of peptidyl-serine phosphorylation Source: Ensembl
    15. positive regulation of stress fiber assembly Source: MGI
    16. positive regulation of substrate adhesion-dependent cell spreading Source: MGI
    17. positive T cell selection Source: MGI
    18. protein heterooligomerization Source: Ensembl
    19. protein phosphorylation Source: BHF-UCL
    20. regulation of cell proliferation Source: MGI
    21. response to cAMP Source: Ensembl
    22. response to epidermal growth factor Source: Ensembl
    23. response to peptide hormone Source: Ensembl
    24. somatic stem cell maintenance Source: MGI
    25. visual learning Source: MGI

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_198246. CREB phosphorylation through the activation of Ras.
    REACT_198526. Spry regulation of FGF signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase B-raf (EC:2.7.11.1)
    Alternative name(s):
    Proto-oncogene B-Raf
    Gene namesi
    Name:Braf
    Synonyms:B-raf
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:88190. Braf.

    Subcellular locationi

    Nucleus By similarity. Cytoplasm By similarity. Cell membrane By similarity
    Note: Colocalizes with RGS14 and RAF1 in both the cytoplasm and membranes.By similarity

    GO - Cellular componenti

    1. cell body Source: MGI
    2. cytoplasm Source: MGI
    3. mitochondrion Source: MGI
    4. neuron projection Source: MGI
    5. nucleus Source: UniProtKB-SubCell
    6. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Participates in a chromosomal translocation that produces a Tif1a-BRAF (T18) oncogene originally isolated from a furfural-induced hepatoma.

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 804803Serine/threonine-protein kinase B-rafPRO_0000085666Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei348 – 3481Phosphoserine; by SGK1By similarity
    Modified residuei356 – 3561Phosphothreonine; by autocatalysisBy similarity
    Modified residuei431 – 4311PhosphothreonineBy similarity
    Modified residuei434 – 4341PhosphoserineBy similarity
    Modified residuei436 – 4361PhosphothreonineBy similarity
    Modified residuei483 – 4831Phosphoserine1 Publication
    Modified residuei484 – 4841PhosphoserineBy similarity
    Cross-linki615 – 615Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei708 – 7081Omega-N-methylarginine; by PRMT5By similarity
    Modified residuei766 – 7661PhosphoserineBy similarity
    Modified residuei790 – 7901Phosphothreonine; by MAPK1By similarity

    Post-translational modificationi

    Phosphorylation at Ser-348 by SGK1 inhibits its activity.By similarity
    Methylation by PRMT5 decreases stability and kinase activity.1 Publication
    Ubiquitinated by RNF149; which leads to proteasomal degradation. Polyubiquitinated at Lys-615 in response to EGF By similarity.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP28028.
    PaxDbiP28028.
    PRIDEiP28028.

    PTM databases

    PhosphoSiteiP28028.

    Expressioni

    Gene expression databases

    ArrayExpressiP28028.
    BgeeiP28028.
    CleanExiMM_BRAF.
    GenevestigatoriP28028.

    Interactioni

    Subunit structurei

    Monomer. Homodimer. Heterodimerizes with RAF1, and the heterodimer possesses a highly increased kinase activity compared to the respective homodimers or monomers. Heterodimerization is mitogen-regulated and enhanced by 14-3-3 proteins. MAPK1/ERK2 activation can induce a negative feedback that promotes the dissociation of the heterodimer by phosphorylating BRAF at Thr-790. Found in a complex with at least BRAF, HRAS, MAP2K1, MAPK3 and RGS14. Interacts with RIT1. Interacts (via N-terminus) with RGS14 (via RBD domains); the interaction mediates the formation of a ternary complex with RAF1, a ternary complex inhibited by GNAI1 By similarity. Interacts with DGKH By similarity. Interacts with PRMT5 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Raf1Q99N572EBI-2584830,EBI-397757

    Protein-protein interaction databases

    BioGridi225124. 3 interactions.
    DIPiDIP-57050N.
    IntActiP28028. 8 interactions.
    MINTiMINT-1518176.

    Structurei

    3D structure databases

    ProteinModelPortaliP28028.
    SMRiP28028. Positions 133-267, 485-760.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini139 – 21173RBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini494 – 754261Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi6 – 3025Poly-GlyAdd
    BLAST
    Compositional biasi465 – 4695Poly-Ser

    Sequence similaritiesi

    Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 RBD (Ras-binding) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00750000117324.
    HOGENOMiHOG000252972.
    HOVERGENiHBG001886.
    InParanoidiP28028.
    KOiK04365.
    OMAiHRTRTSS.
    OrthoDBiEOG7F5128.
    TreeFamiTF317006.

    Family and domain databases

    InterProiIPR020454. DAG/PE-bd.
    IPR011009. Kinase-like_dom.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR003116. Raf-like_ras-bd.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF00130. C1_1. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF02196. RBD. 1 hit.
    [Graphical view]
    PRINTSiPR00008. DAGPEDOMAIN.
    SMARTiSM00109. C1. 1 hit.
    SM00455. RBD. 1 hit.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50898. RBD. 1 hit.
    PS00479. ZF_DAG_PE_1. 1 hit.
    PS50081. ZF_DAG_PE_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P28028-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAALSGGGGS SSGGGGGGGG GGGGGDGGGG AEQGQALFNG DMEPEAGAGA    50
    AASSAADPAI PEEVWNIKQM IKLTQEHIEA LLDKFGGEHN PPSIYLEAYE 100
    EYTSKLDALQ QREQQLLESL VFQTPTDASR NNPKSPQKPI VRVFLPNKQR 150
    TVVPARCGVT VRDSLKKALM MRGLIPECCA VYRIQDGEKK PIGWDTDISW 200
    LTGEELHVEV LENVPLTTHN FVRKTFFTLA FCDFCRKLLF QGFRCQTCGY 250
    KFHQRCSTEV PLMCVNYDQL DLLFVSKFFE HHPVPQEEAS FPETALPSGS 300
    SSAPPSDSTG PQILTSPSPS KSIPIPQPFR PADEDHRNQF GQRDRSSSAP 350
    NVHINTIEPV NIDEKFPEVE LQDQRDLIRD QGFRGDGAPL NQLMRCLRKY 400
    QSRTPSPLLH SVPSEIVFDF EPGPVFRGST TGLSATPPAS LPGSLTNVKA 450
    LQKSPGPQRE RKSSSSSSSE DRSRMKTLGR RDSSDDWEIP DGQITVGQRI 500
    GSGSFGTVYK GKWHGDVAVK MLNVTAPTPQ QLQAFKNEVG VLRKTRHVNI 550
    LLFMGYSTKP QLAIVTQWCE GSSLYHHLHI IETKFEMIKL IDIARQTAQG 600
    MDYLHAKSII HRDLKSNNIF LHEDLTVKIG DFGLATVKSR WSGSHQFEQL 650
    SGSILWMAPE VIRMQDKNPY SFQSDVYAFG IVLYELMTGQ LPYSNINNRD 700
    QIIFMVGRGY LSPDLSKVRS NCPKAMKRLM AECLKKKRDE RPLFPQILAS 750
    IELLARSLPK IHRSASEPSL NRAGFQTEDF SLYACASPKT PIQAGGYGEF 800
    AAFK 804
    Length:804
    Mass (Da):88,780
    Last modified:July 27, 2011 - v3
    Checksum:i4C6CC16A2C660A17
    GO
    Isoform 2 (identifier: P28028-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-474: Missing.
         799-804: EFAAFK → GFPVH

    Note: No experimental confirmation available.

    Show »
    Length:330
    Mass (Da):37,249
    Checksum:i89D505AD29A47209
    GO

    Sequence cautioni

    The sequence AAA37320.1 differs from that shown. Reason: Chimeric cDNA.
    The sequence AAA37320.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 112SS → RR in BAE24384. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 474473Missing in isoform 2. 1 PublicationVSP_022169Add
    BLAST
    Alternative sequencei799 – 8046EFAAFK → GFPVH in isoform 2. 1 PublicationVSP_022170

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK140431 mRNA. Translation: BAE24384.1.
    AC122345 Genomic DNA. No translation available.
    AC163109 Genomic DNA. No translation available.
    M64429 mRNA. Translation: AAA37320.1. Sequence problems.
    CCDSiCCDS39463.1. [P28028-1]
    PIRiA40951. TVMSBF.
    RefSeqiNP_647455.3. NM_139294.5. [P28028-1]
    UniGeneiMm.245513.
    Mm.489691.

    Genome annotation databases

    EnsembliENSMUST00000002487; ENSMUSP00000002487; ENSMUSG00000002413. [P28028-1]
    GeneIDi109880.
    KEGGimmu:109880.
    UCSCiuc009bme.2. mouse. [P28028-1]
    uc009bmf.1. mouse. [P28028-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK140431 mRNA. Translation: BAE24384.1 .
    AC122345 Genomic DNA. No translation available.
    AC163109 Genomic DNA. No translation available.
    M64429 mRNA. Translation: AAA37320.1 . Sequence problems.
    CCDSi CCDS39463.1. [P28028-1 ]
    PIRi A40951. TVMSBF.
    RefSeqi NP_647455.3. NM_139294.5. [P28028-1 ]
    UniGenei Mm.245513.
    Mm.489691.

    3D structure databases

    ProteinModelPortali P28028.
    SMRi P28028. Positions 133-267, 485-760.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 225124. 3 interactions.
    DIPi DIP-57050N.
    IntActi P28028. 8 interactions.
    MINTi MINT-1518176.

    Chemistry

    ChEMBLi CHEMBL2331061.

    PTM databases

    PhosphoSitei P28028.

    Proteomic databases

    MaxQBi P28028.
    PaxDbi P28028.
    PRIDEi P28028.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000002487 ; ENSMUSP00000002487 ; ENSMUSG00000002413 . [P28028-1 ]
    GeneIDi 109880.
    KEGGi mmu:109880.
    UCSCi uc009bme.2. mouse. [P28028-1 ]
    uc009bmf.1. mouse. [P28028-2 ]

    Organism-specific databases

    CTDi 673.
    MGIi MGI:88190. Braf.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117324.
    HOGENOMi HOG000252972.
    HOVERGENi HBG001886.
    InParanoidi P28028.
    KOi K04365.
    OMAi HRTRTSS.
    OrthoDBi EOG7F5128.
    TreeFami TF317006.

    Enzyme and pathway databases

    Reactomei REACT_198246. CREB phosphorylation through the activation of Ras.
    REACT_198526. Spry regulation of FGF signaling.

    Miscellaneous databases

    ChiTaRSi BRAF. mouse.
    NextBioi 362941.
    PROi P28028.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P28028.
    Bgeei P28028.
    CleanExi MM_BRAF.
    Genevestigatori P28028.

    Family and domain databases

    InterProi IPR020454. DAG/PE-bd.
    IPR011009. Kinase-like_dom.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR003116. Raf-like_ras-bd.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF00130. C1_1. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF02196. RBD. 1 hit.
    [Graphical view ]
    PRINTSi PR00008. DAGPEDOMAIN.
    SMARTi SM00109. C1. 1 hit.
    SM00455. RBD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50898. RBD. 1 hit.
    PS00479. ZF_DAG_PE_1. 1 hit.
    PS50081. ZF_DAG_PE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Medulla oblongata.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "Development of a highly efficient expression cDNA cloning system: application to oncogene isolation."
      Miki T., Fleming T.P., Crescenzi M., Molloy C.J., Blam S.B., Reynolds S.H., Aaronson S.A.
      Proc. Natl. Acad. Sci. U.S.A. 88:5167-5171(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 476-804 (ISOFORM 2).
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    5. "Protein arginine methyltransferase 5 regulates ERK1/2 signal transduction amplitude and cell fate through CRAF."
      Andreu-Perez P., Esteve-Puig R., de Torre-Minguela C., Lopez-Fauqued M., Bech-Serra J.J., Tenbaum S., Garcia-Trevijano E.R., Canals F., Merlino G., Avila M.A., Recio J.A.
      Sci. Signal. 4:RA58-RA58(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION.

    Entry informationi

    Entry nameiBRAF_MOUSE
    AccessioniPrimary (citable) accession number: P28028
    Secondary accession number(s): E9QNG9, Q3USE9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 145 of the entry and version 3 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3