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P28028

- BRAF_MOUSE

UniProt

P28028 - BRAF_MOUSE

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Protein
Serine/threonine-protein kinase B-raf
Gene
Braf, B-raf
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Binds 2 zinc ions per subunit Reviewed prediction.

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi500 – 5089ATP By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. CD4-positive, alpha-beta T cell differentiation Source: MGI
  2. 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 T cell selection Source: MGI
  13. positive regulation of ERK1 and ERK2 cascade Source: MGI
  14. positive regulation of gene expression Source: Ensembl
  15. positive regulation of peptidyl-serine phosphorylation Source: Ensembl
  16. positive regulation of stress fiber assembly Source: MGI
  17. positive regulation of substrate adhesion-dependent cell spreading 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: BHF-UCL
  23. response to peptide hormone Source: Ensembl
  24. somatic stem cell maintenance Source: MGI
  25. visual learning Source: MGI
Complete GO annotation...

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
Complete GO annotation...

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 – 11Removed By similarity
Chaini2 – 804803Serine/threonine-protein kinase B-raf
PRO_0000085666Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei348 – 3481Phosphoserine; by SGK1 By similarity
Modified residuei356 – 3561Phosphothreonine; by autocatalysis By similarity
Modified residuei431 – 4311Phosphothreonine By similarity
Modified residuei434 – 4341Phosphoserine By similarity
Modified residuei436 – 4361Phosphothreonine By similarity
Modified residuei483 – 4831Phosphoserine1 Publication
Modified residuei484 – 4841Phosphoserine By similarity
Cross-linki615 – 615Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Modified residuei708 – 7081Omega-N-methylarginine; by PRMT5 By similarity
Modified residuei766 – 7661Phosphoserine By similarity
Modified residuei790 – 7901Phosphothreonine; by MAPK1 By 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.

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.

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini139 – 21173RBD
Add
BLAST
Domaini494 – 754261Protein kinase
Add
BLAST

Compositional bias

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

Sequence similaritiesi

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 474473Missing in isoform 2.
VSP_022169Add
BLAST
Alternative sequencei799 – 8046EFAAFK → GFPVH in isoform 2.
VSP_022170

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 112SS → RR in BAE24384. 1 Publication

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 144 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

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