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Q04982 (BRAF_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase B-raf
EC=2.7.11.1
Alternative name(s):
Proto-oncogene B-Raf
Proto-oncogene c-Rmil
Serine/threonine-protein kinase Rmil
Gene names
Name:BRAF
Synonyms:RMIL
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length806 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in transducing specific signals in neural cells.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Binds 2 zinc ions per subunit Potential.

Subcellular location

Nucleus. Cytoplasm By similarity. Cell membrane By similarity.

Tissue specificity

Expressed preferentially in neural tissue.

Sequence similarities

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. RAF subfamily.

Contains 1 phorbol-ester/DAG-type zinc finger.

Contains 1 protein kinase domain.

Contains 1 RBD (Ras-binding) domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q04982-1)

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.
Isoform Short (identifier: Q04982-2)

The sequence of this isoform differs from the canonical sequence as follows:
     393-432: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 806806Serine/threonine-protein kinase B-raf
PRO_0000085667

Regions

Domain155 – 22773RBD
Domain497 – 757261Protein kinase
Zinc finger234 – 28047Phorbol-ester/DAG-type
Nucleotide binding503 – 5119ATP By similarity
Compositional bias122 – 1298Poly-Ser
Compositional bias248 – 28033Cys-rich

Sites

Active site6161Proton acceptor By similarity
Metal binding2351Zinc 1 By similarity
Metal binding2481Zinc 2 By similarity
Metal binding2511Zinc 2 By similarity
Metal binding2611Zinc 1 By similarity
Metal binding2641Zinc 1 By similarity
Metal binding2691Zinc 2 By similarity
Metal binding2721Zinc 2 By similarity
Metal binding2801Zinc 1 By similarity
Binding site5231ATP By similarity

Amino acid modifications

Modified residue7901Phosphoserine; by MAPK1 Ref.3
Modified residue7931Phosphothreonine; by MAPK1 Ref.3

Natural variations

Alternative sequence393 – 43240Missing in isoform Short.
VSP_004798

Experimental info

Mutagenesis7901S → A: Lack of phosphorylation; when associated with T-793. Ref.3
Mutagenesis7931T → A: Lack of phosphorylation; when associated with S-790. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 8F3FA4D5274FB75C

FASTA80689,366
        10         20         30         40         50         60 
MAALSSGSSA EGASLFNGDM EPEPPPPVLG ACYAGSGGGD PAIPEEVWNI KQMIKLTQEH 

        70         80         90        100        110        120 
IEALLDKFGG EHNPPSIYLE AYEEYTSKLD ALQQREQQLL ESMGNGTDFS VSSSASTDTV 

       130        140        150        160        170        180 
ASSSSSSLSV APSSLSVYQN PTDMSRNNPK SPQKPIVRVF LPNKQRTVVP ARCGVTVRDS 

       190        200        210        220        230        240 
LKKALMMRGL IPECCAVYRI QDGEKKPIGW DTDISWLTGE ELHVEVLENV PLTTHNFVRK 

       250        260        270        280        290        300 
TFFTLAFCDF CRKLLFQGFR CQTCGYKFHQ RCSTEVPLMC VNYDQLDLLF VSKFFEHHPI 

       310        320        330        340        350        360 
SQEETTLGET TPASGSYPSV PPSDSVGPPI LPSPSPSKSI PIPQPFRPAD EDHRNQFGQR 

       370        380        390        400        410        420 
DRSSSAPNVH INTIEPVNID DLIRDQGVRG EGAPLNQLMR CLRKYQSRTP SPLLHSVPSE 

       430        440        450        460        470        480 
IVFDFEPGPV FRGSTAGLSA TPPASLPGSL TNVKALQKSP GPQRERKSSS SSEDRNRMKT 

       490        500        510        520        530        540 
LGRRDSSDDW EIPDGQITVG QRIGSGSFGT VYKGKWHGDV AVKMLNVTAP TPQQLQAFKN 

       550        560        570        580        590        600 
EVGVLRKTRH VNILLFMGYS TKPQLAIVTQ WCEGSSLYHH LHIIETKFEM IKLIDIARQT 

       610        620        630        640        650        660 
AQGMDYLHAK SIIHRDLKSN NIFLHEDLTV KIGDFGLATV KSRWSGSHQF EQLSGSILWM 

       670        680        690        700        710        720 
APEVIRMQDK NPYSFQSDVY AFGIVLYELM TGQLPYSNIN NRDQIIFMVG RGYLSPDLSK 

       730        740        750        760        770        780 
VRSNCPKAMK RLMAECLKKK RDERPLFPQI LASIELLARS LPKIHRSASE PSLNRAGFQT 

       790        800 
EDFSLYACAS PKTPIQAGGY GGFPVH

« Hide

Isoform Short [UniParc].

Checksum: C9495CE014444A13
Show »

FASTA76684,756

References

[1]"Genomic organization and nucleotide sequence of the coding region of the chicken c-Rmil(B-raf-1) proto-oncogene."
Calogeraki I., Barnier J.V., Eychene A., Felder M.-P., Calothy G., Marx M.
Biochem. Biophys. Res. Commun. 193:1324-1331(1993) [PubMed: 8323553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
Tissue: Fibroblast and Lymphocyte.
[2]"Feedback phosphorylation of B-Raf by ERK in activated B cells."
Brummer T., Naegele H., Reth M., Misawa Y.
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 55-806 (ISOFORM SHORT).
Tissue: Bursa of Fabricius.
[3]"Identification of novel ERK-mediated feedback phosphorylation sites at the C-terminus of B-Raf."
Brummer T., Naegele H., Reth M., Misawa Y.
Oncogene 22:8823-8834(2003) [PubMed: 14654779] [Abstract]
Cited for: PHOSPHORYLATION AT SER-790 AND THR-793, MUTAGENESIS OF SER-790 AND THR-793.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X67052 mRNA. Translation: CAA47436.1.
AF449458 mRNA. Translation: AAO13358.1.
IPIIPI00573649.
IPI00586394.
PIRJN0612.
RefSeqNP_990633.1. NM_205302.1.
UniGeneGga.719.

3D structure databases

ProteinModelPortalQ04982.
SMRQ04982. Positions 157-227, 232-283.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ04982.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396239.
KEGGgga:396239.

Organism-specific databases

CTD673.

Phylogenomic databases

eggNOGveNOG07162.
GeneTreeENSGT00600000084194.
HOGENOMHBG506535.
HOVERGENHBG001886.
InParanoidQ04982.

Enzyme and pathway databases

BRENDA2.7.11.1. 1306.

Family and domain databases

InterProIPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR003116. Raf-like_ras-bd.
IPR001245. Ser-Thr/Tyr_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
KOK04365.
PfamPF00130. C1_1. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF02196. RBD. 1 hit.
[Graphical view]
PRINTSPR00008. DAGPEDOMAIN.
SMARTSM00109. C1. 1 hit.
SM00455. RBD. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
PROSITEPS00107. 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]
ProtoNetSearch...

Entry information

Entry nameBRAF_CHICK
AccessionPrimary (citable) accession number: Q04982
Secondary accession number(s): Q8AV85
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: November 16, 2011
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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