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Reviewed, UniProtKB/Swiss-Prot P04627 (ARAF_MOUSE)

Last modified February 9, 2010. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    A-Raf proto-oncogene serine/threonine-protein kinase
    EC=2.7.11.1
Gene names
Name: Araf
Synonyms: A-raf, Araf1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length604 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Involved in the transduction of mitogenic signals from the cell membrane to the nucleus.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subunit structure

Interacts with TH1L/NELFD By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 604604A-Raf proto-oncogene serine/threonine-protein kinase
PRO_0000085623

Regions

Domain19 – 9173RBD
Domain308 – 568261Protein kinase
Zinc finger98 – 14447Phorbol-ester/DAG-type
Nucleotide binding314 – 3229ATP By similarity

Sites

Active site4271Proton acceptor By similarity
Metal binding991Zinc 1 By similarity
Metal binding1121Zinc 2 By similarity
Metal binding1151Zinc 2 By similarity
Metal binding1251Zinc 1 By similarity
Metal binding1281Zinc 1 By similarity
Metal binding1331Zinc 2 By similarity
Metal binding1361Zinc 2 By similarity
Metal binding1441Zinc 1 By similarity
Binding site3341ATP By similarity

Amino acid modifications

Modified residue1861Phosphoserine By similarity
Modified residue2131Phosphothreonine By similarity
Modified residue2151Phosphothreonine By similarity
Modified residue2551Phosphoserine By similarity
Modified residue3161Phosphothreonine By similarity
Modified residue5781Phosphoserine By similarity
Modified residue5801Phosphoserine By similarity

Experimental info

Sequence conflict1691E → K in BAA00018. Ref.4
Sequence conflict1861S → R in BAB23522. Ref.3
Sequence conflict1861S → R in BAB26674. Ref.3
Sequence conflict3261R → L in BAA00018. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P04627-1 [UniParc].

Last modified August 2, 2002. Version 2.
Checksum: 05F8262F99DDD087

FASTA60467,581
        10         20         30         40         50         60 
MEPPRGPPVS GAEPSRAVGT VKVYLPNKQR TVVTVREGMS VYDSLDKALK VRGLNQDCCV 

        70         80         90        100        110        120 
VYRLIKGRKT VTAWDTAIAP LDGEELIVEV LEDVPLTMHN FVRKTFFSLA FCDFCLKFLF 

       130        140        150        160        170        180 
HGFRCQTCGY KFHQHCSSKV PTVCVDMSTN RRQFYHSIQD LSGGSRQQEA PSNLSVNELL 

       190        200        210        220        230        240 
TPQGPSPFTQ QRDQEHFSFP APANPPLQRI RSTSTPNVHM VSTTAPMDSS LMQFTAQSFS 

       250        260        270        280        290        300 
TDAAGRGGDG APRGSPSPAS VSSGRKSPHS KLPSEQRERK SLADEKKKVK NLGYRDSGYY 

       310        320        330        340        350        360 
WEVPPSEVQL LKRIGTGSFG TVFRGRWHGD VAVKVLKVAQ PTAEQAQAFK NEMQVLRKTR 

       370        380        390        400        410        420 
HVNILLFMGF MTRPGFAIIT QWCEGSSLYH HLHVADTRFD MVQLIDVARQ TAQGMDYLHA 

       430        440        450        460        470        480 
KNIIHRDLKS NNIFLHEGLT VKIGDFGLAT VKTRWSGAQP LEQPSGSVLW MAAEVIRMQD 

       490        500        510        520        530        540 
PNPYSFQSDV YAYGVVLYEL MTGSLPYSHI GSRDQIIFMV GRGYLSPDLS KIFSNCPKAM 

       550        560        570        580        590        600 
RRLLTDCLKF QREERPLFPQ ILATIELLQR SLPKIERSAS EPSLHRTQAD ELPACLLSAA 


RLVP 

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6.
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary gland.
[3]"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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-283.
Strain: C57BL/6J.
Tissue: Lung, Tongue and Urinary bladder.
[4]"Characterization of murine A-raf, a new oncogene related to the v-raf oncogene."
Huleihel M., Goldsborough M., Cleveland J., Gunnell M., Bonner T., Rapp U.R.
Mol. Cell. Biol. 6:2655-2662(1986) [PubMed: 3491291] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 168-604.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL671885 Genomic DNA. Translation: CAM14589.1.
BC004757 mRNA. Translation: AAH04757.1.
AK004741 mRNA. Translation: BAB23522.1.
AK010060 mRNA. Translation: BAB26674.1.
AK020547 mRNA. Translation: BAB32131.3.
D00024 mRNA. Translation: BAA00018.1.
IPIIPI00320608.
PIRTVMSRF. A25382.
RefSeqNP_001153117.1.
NP_033833.1.
UniGeneMm.220946

3D structure databases

SMRP04627. Positions 20-91, 96-146, 301-574.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1070N.
IntActP04627. 2 interactions.
STRINGP04627.

PTM databases

PhosphoSiteP04627.

Proteomic databases

PRIDEP04627.

Genome annotation databases

EnsemblENSMUST00000001155; ENSMUSP00000001155; ENSMUSG00000001127; Mus musculus. [Genome view]
GeneID11836.
KEGGmmu:11836.
UCSCuc009stu.1. mouse.

Organism-specific databases

CTD11836.
MGIMGI:88065. Araf.

Phylogenomic databases

eggNOGroNOG10943.
HOGENOMHBG506535.
HOVERGENP04627.
InParanoidP04627.
OMAHVSETKF.
OrthoDBEOG9QC3QR.

Enzyme and pathway databases

BRENDA2.7.10.2. 244.
2.7.11.1. 244.

Gene expression databases

ArrayExpressP04627.
BgeeP04627.
CleanExMM_ARAF.
GenevestigatorP04627.
GermOnlineENSMUSG00000001127. Mus musculus.

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.
IPR008271. Ser/Thr_prot_kinase_AS.
[Graphical view]
PfamPF00130. C1_1. 1 hit.
PF02196. RBD. 1 hit.
[Graphical view]
PRINTSPR00008. DAGPEDOMAIN.
SMARTSM00109. C1. 1 hit.
SM00455. RBD. 1 hit.
[Graphical view]
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...

Other Resources

NextBio279767.
SOURCESearch...

Entry information

Entry nameARAF_MOUSE
AccessionPrimary (citable) accession number: P04627
Secondary accession number(s): B1AUN9 expand/collapse secondary AC list , Q99J44, Q9CTT5, Q9D6R6, Q9DBU7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 2, 2002
Last modified: February 9, 2010
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents