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P42685

- FRK_HUMAN

UniProt

P42685 - FRK_HUMAN

Protein

Tyrosine-protein kinase FRK

Gene

FRK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Non-receptor tyrosine-protein kinase that negatively regulates cell proliferation. Positively regulates PTEN protein stability through phosphorylation of PTEN on 'Tyr-336', which in turn prevents its ubiquitination and degradation, possibly by reducing its binding to NEDD4. May function as a tumor suppressor.1 Publication

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei262 – 2621ATPPROSITE-ProRule annotation
    Active sitei354 – 3541Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi240 – 2489ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. non-membrane spanning protein tyrosine kinase activity Source: ProtInc
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell differentiation Source: Ensembl
    2. negative regulation of cell proliferation Source: ProtInc
    3. peptidyl-tyrosine phosphorylation Source: GOC
    4. protein phosphorylation Source: ProtInc

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 2681.
    SignaLinkiP42685.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase FRK (EC:2.7.10.2)
    Alternative name(s):
    FYN-related kinase
    Nuclear tyrosine protein kinase RAK
    Protein-tyrosine kinase 5
    Gene namesi
    Name:FRK
    Synonyms:PTK5, RAK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:3955. FRK.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Predominantly found in the nucleus, with a small fraction found in the cell periphery.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. intracellular Source: ProtInc
    4. nucleus Source: ProtInc
    5. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi262 – 2621K → R: Loss of ability to phosphorylate PTEN. 1 Publication

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA28373.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 505505Tyrosine-protein kinase FRKPRO_0000088097Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei37 – 371Phosphoserine1 Publication
    Modified residuei387 – 3871Phosphotyrosine; by autocatalysisBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP42685.
    PaxDbiP42685.
    PRIDEiP42685.

    PTM databases

    PhosphoSiteiP42685.

    Expressioni

    Tissue specificityi

    Predominantly expressed in epithelial derived cell lines and tissues, especially normal liver, kidney, breast and colon.1 Publication

    Gene expression databases

    ArrayExpressiP42685.
    BgeeiP42685.
    CleanExiHS_FRK.
    GenevestigatoriP42685.

    Organism-specific databases

    HPAiCAB025217.

    Interactioni

    Subunit structurei

    Interacts (via the SH3-domain) with PTEN. Interacts with RB1.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PTENP604847EBI-1383583,EBI-696162
    RB1P064003EBI-1383583,EBI-491274

    Protein-protein interaction databases

    BioGridi108726. 6 interactions.
    IntActiP42685. 9 interactions.
    MINTiMINT-3015573.
    STRINGi9606.ENSP00000357615.

    Structurei

    3D structure databases

    ProteinModelPortaliP42685.
    SMRiP42685. Positions 17-499.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini42 – 11069SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini116 – 20893SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini234 – 491258Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH2 domain, SH3 domain

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233858.
    HOVERGENiHBG008761.
    InParanoidiP42685.
    KOiK08892.
    OMAiVSHYTKT.
    OrthoDBiEOG7GTT2V.
    PhylomeDBiP42685.
    TreeFamiTF351634.

    Family and domain databases

    Gene3Di3.30.505.10. 1 hit.
    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR001452. SH3_domain.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view]
    PfamiPF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    PR00109. TYRKINASE.
    SMARTiSM00252. SH2. 1 hit.
    SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P42685-1) [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

    MSNICQRLWE YLEPYLPCLS TEADKSTVIE NPGALCSPQS QRHGHYFVAL    50
    FDYQARTAED LSFRAGDKLQ VLDTLHEGWW FARHLEKRRD GSSQQLQGYI 100
    PSNYVAEDRS LQAEPWFFGA IGRSDAEKQL LYSENKTGSF LIRESESQKG 150
    EFSLSVLDGA VVKHYRIKRL DEGGFFLTRR RIFSTLNEFV SHYTKTSDGL 200
    CVKLGKPCLK IQVPAPFDLS YKTVDQWEID RNSIQLLKRL GSGQFGEVWE 250
    GLWNNTTPVA VKTLKPGSMD PNDFLREAQI MKNLRHPKLI QLYAVCTLED 300
    PIYIITELMR HGSLQEYLQN DTGSKIHLTQ QVDMAAQVAS GMAYLESRNY 350
    IHRDLAARNV LVGEHNIYKV ADFGLARVFK VDNEDIYESR HEIKLPVKWT 400
    APEAIRSNKF SIKSDVWSFG ILLYEIITYG KMPYSGMTGA QVIQMLAQNY 450
    RLPQPSNCPQ QFYNIMLECW NAEPKERPTF ETLRWKLEDY FETDSSYSDA 500
    NNFIR 505
    Length:505
    Mass (Da):58,254
    Last modified:November 1, 1995 - v1
    Checksum:i06EC050DDBCD930B
    GO
    Isoform 2 (identifier: P42685-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-13: MSNICQRLWEYLE → MDSTSLLPNPWIR
         14-155: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:363
    Mass (Da):41,980
    Checksum:iE1A26410F13F6232
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti115 – 1151P → A in AAC50116. (PubMed:7696183)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti100 – 1001I → V.1 Publication
    Corresponds to variant rs34704018 [ dbSNP | Ensembl ].
    VAR_041702
    Natural varianti122 – 1221G → R.1 Publication
    Corresponds to variant rs3756772 [ dbSNP | Ensembl ].
    VAR_006283
    Natural varianti133 – 1331S → L.1 Publication
    Corresponds to variant rs34064900 [ dbSNP | Ensembl ].
    VAR_041703

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1313MSNIC…WEYLE → MDSTSLLPNPWIR in isoform 2. 1 PublicationVSP_056496Add
    BLAST
    Alternative sequencei14 – 155142Missing in isoform 2. 1 PublicationVSP_056497Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U22322 mRNA. Translation: AAC50116.1.
    U00803 mRNA. Translation: AAA18284.1.
    AK302264 mRNA. Translation: BAG63611.1.
    AL021451 Genomic DNA. No translation available.
    AL121963, AL357141 Genomic DNA. Translation: CAB87592.2.
    AL357141, AL121963 Genomic DNA. Translation: CAI16469.1.
    CH471051 Genomic DNA. Translation: EAW48241.1.
    BC012916 mRNA. Translation: AAH12916.1.
    CCDSiCCDS5103.1.
    PIRiI38396.
    RefSeqiNP_002022.1. NM_002031.2.
    XP_005266937.1. XM_005266880.2.
    XP_005266938.1. XM_005266881.1.
    XP_005266939.1. XM_005266882.2.
    UniGeneiHs.89426.

    Genome annotation databases

    EnsembliENST00000538210; ENSP00000443075; ENSG00000111816.
    ENST00000606080; ENSP00000476145; ENSG00000111816.
    GeneIDi2444.
    KEGGihsa:2444.
    UCSCiuc003pwi.1. human.

    Polymorphism databases

    DMDMi1169745.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U22322 mRNA. Translation: AAC50116.1 .
    U00803 mRNA. Translation: AAA18284.1 .
    AK302264 mRNA. Translation: BAG63611.1 .
    AL021451 Genomic DNA. No translation available.
    AL121963 , AL357141 Genomic DNA. Translation: CAB87592.2 .
    AL357141 , AL121963 Genomic DNA. Translation: CAI16469.1 .
    CH471051 Genomic DNA. Translation: EAW48241.1 .
    BC012916 mRNA. Translation: AAH12916.1 .
    CCDSi CCDS5103.1.
    PIRi I38396.
    RefSeqi NP_002022.1. NM_002031.2.
    XP_005266937.1. XM_005266880.2.
    XP_005266938.1. XM_005266881.1.
    XP_005266939.1. XM_005266882.2.
    UniGenei Hs.89426.

    3D structure databases

    ProteinModelPortali P42685.
    SMRi P42685. Positions 17-499.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108726. 6 interactions.
    IntActi P42685. 9 interactions.
    MINTi MINT-3015573.
    STRINGi 9606.ENSP00000357615.

    Chemistry

    BindingDBi P42685.
    ChEMBLi CHEMBL2363074.
    GuidetoPHARMACOLOGYi 2025.

    PTM databases

    PhosphoSitei P42685.

    Polymorphism databases

    DMDMi 1169745.

    Proteomic databases

    MaxQBi P42685.
    PaxDbi P42685.
    PRIDEi P42685.

    Protocols and materials databases

    DNASUi 2444.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000538210 ; ENSP00000443075 ; ENSG00000111816 .
    ENST00000606080 ; ENSP00000476145 ; ENSG00000111816 .
    GeneIDi 2444.
    KEGGi hsa:2444.
    UCSCi uc003pwi.1. human.

    Organism-specific databases

    CTDi 2444.
    GeneCardsi GC06M116308.
    HGNCi HGNC:3955. FRK.
    HPAi CAB025217.
    MIMi 606573. gene.
    neXtProti NX_P42685.
    PharmGKBi PA28373.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233858.
    HOVERGENi HBG008761.
    InParanoidi P42685.
    KOi K08892.
    OMAi VSHYTKT.
    OrthoDBi EOG7GTT2V.
    PhylomeDBi P42685.
    TreeFami TF351634.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 2681.
    SignaLinki P42685.

    Miscellaneous databases

    GeneWikii Fyn-related_kinase.
    GenomeRNAii 2444.
    NextBioi 9741.
    PROi P42685.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P42685.
    Bgeei P42685.
    CleanExi HS_FRK.
    Genevestigatori P42685.

    Family and domain databases

    Gene3Di 3.30.505.10. 1 hit.
    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR001452. SH3_domain.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view ]
    Pfami PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    PR00109. TYRKINASE.
    SMARTi SM00252. SH2. 1 hit.
    SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Rak, a novel nuclear tyrosine kinase expressed in epithelial cells."
      Cance W.G., Craven R.J., Bergman M., Xu L.H., Alitalo K., Liu E.T.
      Cell Growth Differ. 5:1347-1355(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    2. "Cloning of FRK, a novel human intracellular SRC-like tyrosine kinase-encoding gene."
      Lee J., Wang Z., Luoh S.-M., Wood W.I., Scadden D.T.
      Gene 138:247-251(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Lymphoid tissue.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Testis.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Urinary bladder.
    7. "Novel protein kinases expressed in human breast cancer."
      Cance W.G., Craven R.J., Weiner T.M., Liu E.T.
      Int. J. Cancer 54:571-577(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
    8. "The nuclear tyrosine kinase Rak associates with the retinoblastoma protein pRb."
      Craven R.J., Cance W.G., Liu E.T.
      Cancer Res. 55:3969-3972(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RB1.
    9. "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-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Rak functions as a tumor suppressor by regulating PTEN protein stability and function."
      Yim E.-K., Peng G., Dai H., Hu R., Li K., Lu Y., Mills G.B., Meric-Bernstam F., Hennessy B.T., Craven R.J., Lin S.-Y.
      Cancer Cell 15:304-314(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PTEN, MUTAGENESIS OF LYS-262.
    11. "RAKing in AKT: a tumor suppressor function for the intracellular tyrosine kinase FRK."
      Brauer P.M., Tyner A.L.
      Cell Cycle 8:2728-2732(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    12. "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] VAL-100; ARG-122 AND LEU-133.

    Entry informationi

    Entry nameiFRK_HUMAN
    AccessioniPrimary (citable) accession number: P42685
    Secondary accession number(s): B4DY49, Q13128, Q9NTR5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 150 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3