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P04627

- ARAF_MOUSE

UniProt

P04627 - ARAF_MOUSE

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Protein

Serine/threonine-protein kinase A-Raf

Gene
Araf, A-raf, Araf1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May also regulate the TOR signaling cascade By similarity.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Binds 2 zinc ions per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi99 – 991Zinc 1 By similarity
Metal bindingi112 – 1121Zinc 2 By similarity
Metal bindingi115 – 1151Zinc 2 By similarity
Metal bindingi125 – 1251Zinc 1 By similarity
Metal bindingi128 – 1281Zinc 1 By similarity
Metal bindingi133 – 1331Zinc 2 By similarity
Metal bindingi136 – 1361Zinc 2 By similarity
Metal bindingi144 – 1441Zinc 1 By similarity
Binding sitei334 – 3341ATP By similarity
Active sitei427 – 4271Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri98 – 14447Phorbol-ester/DAG-typeAdd
BLAST
Nucleotide bindingi314 – 3229ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. protein binding Source: MGI
  4. protein serine/threonine kinase activity Source: UniProtKB-KW
  5. receptor signaling protein activity Source: InterPro

GO - Biological processi

  1. negative regulation of apoptotic process Source: Ensembl
  2. positive regulation of peptidyl-serine phosphorylation Source: Ensembl
  3. regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  4. regulation of TOR signaling Source: UniProtKB
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

BRENDAi2.7.10.2. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase A-Raf (EC:2.7.11.1)
Alternative name(s):
Proto-oncogene A-Raf
Gene namesi
Name:Araf
Synonyms:A-raf, Araf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:88065. Araf.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: MGI
Complete GO annotation...

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 604604Serine/threonine-protein kinase A-RafPRO_0000085623Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei186 – 1861Phosphoserine By similarity
Modified residuei255 – 2551Phosphoserine By similarity
Modified residuei316 – 3161Phosphothreonine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP04627.
PaxDbiP04627.
PRIDEiP04627.

PTM databases

PhosphoSiteiP04627.

Expressioni

Gene expression databases

ArrayExpressiP04627.
BgeeiP04627.
CleanExiMM_ARAF.
GenevestigatoriP04627.

Interactioni

Subunit structurei

Interacts with TH1L/NELFD By similarity.

Protein-protein interaction databases

DIPiDIP-1070N.
IntActiP04627. 5 interactions.
MINTiMINT-1582260.

Structurei

3D structure databases

ProteinModelPortaliP04627.
SMRiP04627. Positions 20-91, 96-146, 275-604.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 9173RBDAdd
BLAST
Domaini308 – 568261Protein kinaseAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00750000117324.
HOGENOMiHOG000252972.
HOVERGENiHBG001886.
InParanoidiB1AUN9.
KOiK08845.
OMAiLFHTTRL.
OrthoDBiEOG7F5128.
PhylomeDBiP04627.
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]

Sequencei

Sequence statusi: Complete.

P04627-1 [UniParc]FASTAAdd to Basket

« Hide

MEPPRGPPVS GAEPSRAVGT VKVYLPNKQR TVVTVREGMS VYDSLDKALK    50
VRGLNQDCCV VYRLIKGRKT VTAWDTAIAP LDGEELIVEV LEDVPLTMHN 100
FVRKTFFSLA FCDFCLKFLF HGFRCQTCGY KFHQHCSSKV PTVCVDMSTN 150
RRQFYHSIQD LSGGSRQQEA PSNLSVNELL TPQGPSPFTQ QRDQEHFSFP 200
APANPPLQRI RSTSTPNVHM VSTTAPMDSS LMQFTAQSFS TDAAGRGGDG 250
APRGSPSPAS VSSGRKSPHS KLPSEQRERK SLADEKKKVK NLGYRDSGYY 300
WEVPPSEVQL LKRIGTGSFG TVFRGRWHGD VAVKVLKVAQ PTAEQAQAFK 350
NEMQVLRKTR HVNILLFMGF MTRPGFAIIT QWCEGSSLYH HLHVADTRFD 400
MVQLIDVARQ TAQGMDYLHA KNIIHRDLKS NNIFLHEGLT VKIGDFGLAT 450
VKTRWSGAQP LEQPSGSVLW MAAEVIRMQD PNPYSFQSDV YAYGVVLYEL 500
MTGSLPYSHI GSRDQIIFMV GRGYLSPDLS KIFSNCPKAM RRLLTDCLKF 550
QREERPLFPQ ILATIELLQR SLPKIERSAS EPSLHRTQAD ELPACLLSAA 600
RLVP 604
Length:604
Mass (Da):67,581
Last modified:August 2, 2002 - v2
Checksum:i05F8262F99DDD087
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti169 – 1691E → K in BAA00018. 1 Publication
Sequence conflicti186 – 1861S → R in BAB23522. 1 Publication
Sequence conflicti186 – 1861S → R in BAB26674. 1 Publication
Sequence conflicti326 – 3261R → L in BAA00018. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS40886.1.
PIRiA25382. TVMSRF.
RefSeqiNP_001153117.1. NM_001159645.1.
NP_033833.1. NM_009703.2.
XP_006527619.1. XM_006527556.1.
XP_006527620.1. XM_006527557.1.
UniGeneiMm.220946.

Genome annotation databases

EnsembliENSMUST00000001155; ENSMUSP00000001155; ENSMUSG00000001127.
GeneIDi11836.
KEGGimmu:11836.
UCSCiuc009stt.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS40886.1.
PIRi A25382. TVMSRF.
RefSeqi NP_001153117.1. NM_001159645.1.
NP_033833.1. NM_009703.2.
XP_006527619.1. XM_006527556.1.
XP_006527620.1. XM_006527557.1.
UniGenei Mm.220946.

3D structure databases

ProteinModelPortali P04627.
SMRi P04627. Positions 20-91, 96-146, 275-604.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-1070N.
IntActi P04627. 5 interactions.
MINTi MINT-1582260.

PTM databases

PhosphoSitei P04627.

Proteomic databases

MaxQBi P04627.
PaxDbi P04627.
PRIDEi P04627.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000001155 ; ENSMUSP00000001155 ; ENSMUSG00000001127 .
GeneIDi 11836.
KEGGi mmu:11836.
UCSCi uc009stt.2. mouse.

Organism-specific databases

CTDi 369.
MGIi MGI:88065. Araf.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00750000117324.
HOGENOMi HOG000252972.
HOVERGENi HBG001886.
InParanoidi B1AUN9.
KOi K08845.
OMAi LFHTTRL.
OrthoDBi EOG7F5128.
PhylomeDBi P04627.
TreeFami TF317006.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 3474.

Miscellaneous databases

ChiTaRSi ARAF. mouse.
NextBioi 279767.
PROi P04627.
SOURCEi Search...

Gene expression databases

ArrayExpressi P04627.
Bgeei P04627.
CleanExi MM_ARAF.
Genevestigatori P04627.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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] [Europe PMC] [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.
    , 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] 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 168-604.

Entry informationi

Entry nameiARAF_MOUSE
AccessioniPrimary (citable) accession number: P04627
Secondary accession number(s): B1AUN9
, Q99J44, Q9CTT5, Q9D6R6, Q9DBU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 2, 2002
Last modified: July 9, 2014
This is version 164 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. 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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