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P10398

- ARAF_HUMAN

UniProt

P10398 - ARAF_HUMAN

Protein

Serine/threonine-protein kinase A-Raf

Gene

ARAF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 175 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Involved in the transduction of mitogenic signals from the cell membrane to the nucleus. May also regulate the TOR signaling cascade.1 Publication
    Isoform 2: Serves as a positive regulator of myogenic differentiation by inducing cell cycle arrest, the expression of myogenin and other muscle-specific proteins, and myotube formation.1 Publication

    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 1By similarity
    Metal bindingi112 – 1121Zinc 2By similarity
    Metal bindingi115 – 1151Zinc 2By similarity
    Metal bindingi125 – 1251Zinc 1By similarity
    Metal bindingi128 – 1281Zinc 1By similarity
    Metal bindingi133 – 1331Zinc 2By similarity
    Metal bindingi136 – 1361Zinc 2By similarity
    Metal bindingi144 – 1441Zinc 1By similarity
    Binding sitei336 – 3361ATPPROSITE-ProRule annotation
    Active sitei429 – 4291Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri98 – 14447Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi316 – 3249ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

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

    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. 2681.
    SignaLinkiP10398.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase A-Raf (EC:2.7.11.1)
    Alternative name(s):
    Proto-oncogene A-Raf
    Proto-oncogene A-Raf-1
    Proto-oncogene Pks
    Gene namesi
    Name:ARAF
    Synonyms:ARAF1, PKS, PKS2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:646. ARAF.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: Ensembl

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA24928.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 606606Serine/threonine-protein kinase A-RafPRO_0000085622Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei186 – 1861Phosphoserine1 Publication
    Modified residuei257 – 2571Phosphoserine1 Publication
    Modified residuei318 – 3181Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP10398.
    PaxDbiP10398.
    PRIDEiP10398.

    PTM databases

    PhosphoSiteiP10398.

    Expressioni

    Tissue specificityi

    Predominantly in urogenital tissues.

    Gene expression databases

    ArrayExpressiP10398.
    BgeeiP10398.
    CleanExiHS_ARAF.
    GenevestigatoriP10398.

    Interactioni

    Subunit structurei

    Interacts with TH1L/NELFD.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ASS1P009664EBI-365961,EBI-536842
    BRAFP150562EBI-365961,EBI-365980
    COPS3Q9UNS23EBI-365961,EBI-350590
    CPS1P313273EBI-365961,EBI-536811
    EFEMP1Q128053EBI-365961,EBI-536772
    HSP90AB1P082386EBI-365961,EBI-352572
    IRAK2O431872EBI-365961,EBI-447733
    IRF7Q929852EBI-365961,EBI-968267
    MAP2K2P365074EBI-365961,EBI-1056930
    NELFCDQ8IXH75EBI-365961,EBI-536725
    NUDT14O958483EBI-365961,EBI-536866
    PBKQ96KB53EBI-365961,EBI-536853
    PKMP146182EBI-365961,EBI-353408
    PRPF6O949064EBI-365961,EBI-536755
    RABGGTBP536113EBI-365961,EBI-536715
    RRAS2P620703EBI-365961,EBI-491037
    TIMM44O436153EBI-365961,EBI-861737
    TIMM50Q3ZCQ83EBI-365961,EBI-355175
    TIRAPP587532EBI-365961,EBI-528644
    YWHAZP631043EBI-365961,EBI-347088

    Protein-protein interaction databases

    BioGridi106864. 43 interactions.
    DIPiDIP-31374N.
    IntActiP10398. 38 interactions.
    MINTiMINT-88835.
    STRINGi9606.ENSP00000366244.

    Structurei

    Secondary structure

    1
    606
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi19 – 246
    Beta strandi26 – 283
    Beta strandi30 – 345
    Helixi42 – 509
    Beta strandi56 – 6712
    Beta strandi69 – 724
    Beta strandi74 – 785
    Beta strandi85 – 906

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WXMNMR-A19-91[»]
    ProteinModelPortaliP10398.
    SMRiP10398. Positions 20-91, 96-146, 273-576.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10398.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini19 – 9173RBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini310 – 570261Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri98 – 14447Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000252972.
    HOVERGENiHBG001886.
    KOiK08845.
    OMAiLFHTTRL.
    OrthoDBiEOG7F5128.
    PhylomeDBiP10398.
    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.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P10398-1) [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

    MEPPRGPPAN GAEPSRAVGT VKVYLPNKQR TVVTVRDGMS VYDSLDKALK    50
    VRGLNQDCCV VYRLIKGRKT VTAWDTAIAP LDGEELIVEV LEDVPLTMHN 100
    FVRKTFFSLA FCDFCLKFLF HGFRCQTCGY KFHQHCSSKV PTVCVDMSTN 150
    RQQFYHSVQD LSGGSRQHEA PSNRPLNELL TPQGPSPRTQ HCDPEHFPFP 200
    APANAPLQRI RSTSTPNVHM VSTTAPMDSN LIQLTGQSFS TDAAGSRGGS 250
    DGTPRGSPSP ASVSSGRKSP HSKSPAEQRE RKSLADDKKK VKNLGYRDSG 300
    YYWEVPPSEV QLLKRIGTGS FGTVFRGRWH GDVAVKVLKV SQPTAEQAQA 350
    FKNEMQVLRK TRHVNILLFM GFMTRPGFAI ITQWCEGSSL YHHLHVADTR 400
    FDMVQLIDVA RQTAQGMDYL HAKNIIHRDL KSNNIFLHEG LTVKIGDFGL 450
    ATVKTRWSGA QPLEQPSGSV LWMAAEVIRM QDPNPYSFQS DVYAYGVVLY 500
    ELMTGSLPYS HIGCRDQIIF MVGRGYLSPD LSKISSNCPK AMRRLLSDCL 550
    KFQREERPLF PQILATIELL QRSLPKIERS ASEPSLHRTQ ADELPACLLS 600
    AARLVP 606
    Length:606
    Mass (Da):67,585
    Last modified:October 1, 1996 - v2
    Checksum:iD23E5711304AA468
    GO
    Isoform 2 (identifier: P10398-2) [UniParc]FASTAAdd to Basket

    Also known as: DA-Raf1

    The sequence of this isoform differs from the canonical sequence as follows:
         186-186: S → R
         187-606: Missing.

    Note: Has a wider tissue distribution than isoform 1, and acts as dominant-negative antagonist.

    Show »
    Length:186
    Mass (Da):20,904
    Checksum:i22710574E5D8A1B3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti368 – 3681L → P in AAB08754. (PubMed:3529082)Curated
    Sequence conflicti378 – 3781F → V in AAB08754. (PubMed:3529082)Curated
    Sequence conflicti469 – 4691S → P in AAB08754. (PubMed:3529082)Curated
    Sequence conflicti478 – 4781I → T in AAB08754. (PubMed:3529082)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti98 – 981M → T.1 Publication
    Corresponds to variant rs56197559 [ dbSNP | Ensembl ].
    VAR_040375
    Natural varianti331 – 3311G → C in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_040376
    Natural varianti578 – 5781E → D.1 Publication
    Corresponds to variant rs55852926 [ dbSNP | Ensembl ].
    VAR_040377

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei186 – 1861S → R in isoform 2. 2 PublicationsVSP_045609
    Alternative sequencei187 – 606420Missing in isoform 2. 2 PublicationsVSP_045610Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04790 mRNA. Translation: CAA28476.1.
    L24038 Genomic DNA. Translation: AAA65219.1.
    U01337 Genomic DNA. Translation: AAB03517.1.
    AB158254 mRNA. Translation: BAE66645.1.
    BT019864 mRNA. Translation: AAV38667.1.
    AL542736 mRNA. No translation available.
    Z84466 Genomic DNA. Translation: CAI42468.1.
    Z84466 Genomic DNA. Translation: CAI42469.1.
    BC002466 mRNA. Translation: AAH02466.1.
    M13829 mRNA. Translation: AAB08754.1.
    CCDSiCCDS35232.1. [P10398-1]
    CCDS59164.1. [P10398-2]
    PIRiA53026. TVHUAF.
    RefSeqiNP_001243125.1. NM_001256196.1.
    NP_001243126.1. NM_001256197.1. [P10398-2]
    NP_001645.1. NM_001654.4. [P10398-1]
    UniGeneiHs.446641.

    Genome annotation databases

    EnsembliENST00000377039; ENSP00000366238; ENSG00000078061. [P10398-2]
    ENST00000377045; ENSP00000366244; ENSG00000078061. [P10398-1]
    GeneIDi369.
    KEGGihsa:369.
    UCSCiuc011mlp.3. human. [P10398-1]
    uc031tjj.1. human.

    Polymorphism databases

    DMDMi1730068.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04790 mRNA. Translation: CAA28476.1 .
    L24038 Genomic DNA. Translation: AAA65219.1 .
    U01337 Genomic DNA. Translation: AAB03517.1 .
    AB158254 mRNA. Translation: BAE66645.1 .
    BT019864 mRNA. Translation: AAV38667.1 .
    AL542736 mRNA. No translation available.
    Z84466 Genomic DNA. Translation: CAI42468.1 .
    Z84466 Genomic DNA. Translation: CAI42469.1 .
    BC002466 mRNA. Translation: AAH02466.1 .
    M13829 mRNA. Translation: AAB08754.1 .
    CCDSi CCDS35232.1. [P10398-1 ]
    CCDS59164.1. [P10398-2 ]
    PIRi A53026. TVHUAF.
    RefSeqi NP_001243125.1. NM_001256196.1.
    NP_001243126.1. NM_001256197.1. [P10398-2 ]
    NP_001645.1. NM_001654.4. [P10398-1 ]
    UniGenei Hs.446641.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WXM NMR - A 19-91 [» ]
    ProteinModelPortali P10398.
    SMRi P10398. Positions 20-91, 96-146, 273-576.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106864. 43 interactions.
    DIPi DIP-31374N.
    IntActi P10398. 38 interactions.
    MINTi MINT-88835.
    STRINGi 9606.ENSP00000366244.

    Chemistry

    ChEMBLi CHEMBL1169596.
    DrugBanki DB00171. Adenosine triphosphate.
    GuidetoPHARMACOLOGYi 1933.

    PTM databases

    PhosphoSitei P10398.

    Polymorphism databases

    DMDMi 1730068.

    Proteomic databases

    MaxQBi P10398.
    PaxDbi P10398.
    PRIDEi P10398.

    Protocols and materials databases

    DNASUi 369.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000377039 ; ENSP00000366238 ; ENSG00000078061 . [P10398-2 ]
    ENST00000377045 ; ENSP00000366244 ; ENSG00000078061 . [P10398-1 ]
    GeneIDi 369.
    KEGGi hsa:369.
    UCSCi uc011mlp.3. human. [P10398-1 ]
    uc031tjj.1. human.

    Organism-specific databases

    CTDi 369.
    GeneCardsi GC0XP047429.
    HGNCi HGNC:646. ARAF.
    MIMi 311010. gene.
    neXtProti NX_P10398.
    PharmGKBi PA24928.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000252972.
    HOVERGENi HBG001886.
    KOi K08845.
    OMAi LFHTTRL.
    OrthoDBi EOG7F5128.
    PhylomeDBi P10398.
    TreeFami TF317006.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 2681.
    SignaLinki P10398.

    Miscellaneous databases

    EvolutionaryTracei P10398.
    GeneWikii ARAF.
    GenomeRNAii 369.
    NextBioi 1545.
    PROi P10398.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10398.
    Bgeei P10398.
    CleanExi HS_ARAF.
    Genevestigatori P10398.

    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 complete coding sequence of the human A-raf-1 oncogene and transforming activity of a human A-raf carrying retrovirus."
      Beck T.W., Huleihel M., Gunnell M., Bonner T.I., Rapp U.R.
      Nucleic Acids Res. 15:595-609(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "The complete sequence and promoter activity of the human A-raf-1 gene (ARAF1)."
      Lee J.-E., Beck T.W., Brennscheidt U., DeGennaro L.J., Rapp U.R.
      Genomics 20:43-55(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Placenta.
    3. "DA-Raf1, a competent intrinsic dominant-negative antagonist of the Ras-ERK pathway, is required for myogenic differentiation."
      Yokoyama T., Takano K., Yoshida A., Katada F., Sun P., Takenawa T., Andoh T., Endo T.
      J. Cell Biol. 177:781-793(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2), ALTERNATIVE SPLICING.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Placenta.
    6. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Kidney.
    8. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 292-589 (ISOFORM 1).
    9. "Identification of TH1 as an interaction partner of A-Raf kinase."
      Yin X.L., Chen S., Gu J.X.
      Mol. Cell. Biochem. 231:69-74(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NELFD.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "PRR5L degradation promotes mTORC2-mediated PKC-delta phosphorylation and cell migration downstream of Galpha12."
      Gan X., Wang J., Wang C., Sommer E., Kozasa T., Srinivasula S., Alessi D., Offermanns S., Simon M.I., Wu D.
      Nat. Cell Biol. 14:686-696(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TOR SIGNALING.
    20. "Solution structure of the N-terminal RAS-binding domain (RBD) in human A-RAF kinase."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUL-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 19-91.
    21. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-98; CYS-331 AND ASP-578.

    Entry informationi

    Entry nameiARAF_HUMAN
    AccessioniPrimary (citable) accession number: P10398
    Secondary accession number(s): P07557, Q5H9B2, Q5H9B3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 175 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3