LOCUS       NP_001025210             450 aa            linear   ROD 17-OCT-2024
DEFINITION  tyrosine-protein kinase CSK [Rattus norvegicus].
ACCESSION   NP_001025210 XP_006243225 XP_236290
VERSION     NP_001025210.1
DBSOURCE    REFSEQ: accession NM_001030039.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 450)
  AUTHORS   Gonzalez-Sanchez,A., Jaraiz-Rodriguez,M., Dominguez-Prieto,M.,
            Herrero-Gonzalez,S., Medina,J.M. and Tabernero,A.
  TITLE     Connexin43 recruits PTEN and Csk to inhibit c-Src activity in
            glioma cells and astrocytes
  JOURNAL   Oncotarget 7 (31), 49819-49833 (2016)
   PUBMED   27391443
  REMARK    GeneRIF: recruitment of Csk and PTEN to the region between residues
            266 and 283 within the C-terminus of Cx43 leads to c-Src inhibition
            in glioma cells and astrocytes
REFERENCE   2  (residues 1 to 450)
  AUTHORS   Zhang,L., Ren,Z., Yang,Q. and Ding,G.
  TITLE     Csk regulates angiotensin II-induced podocyte apoptosis
  JOURNAL   Apoptosis 21 (7), 846-855 (2016)
   PUBMED   27225249
  REMARK    GeneRIF: Ang II increased Csk expression and induced podocyte
            apoptosis, stimulated Csk translocation and binding to Caveolin-1.
REFERENCE   3  (residues 1 to 450)
  AUTHORS   Senda,Y., Murata-Kamiya,N. and Hatakeyama,M.
  TITLE     C-terminal Src kinase-mediated EPIYA phosphorylation of Pragmin
            creates a feed-forward C-terminal Src kinase activation loop that
            promotes cell motility
  JOURNAL   Cancer Sci 107 (7), 972-980 (2016)
   PUBMED   27116701
REFERENCE   4  (residues 1 to 450)
  AUTHORS   Sarmiento,J., Wallis,R.H., Ning,T., Marandi,L., Chao,G.,
            Veillette,A., Lernmark,A., Paterson,A.D. and Poussier,P.
  TITLE     A functional polymorphism of Ptpn22 is associated with type 1
            diabetes in the BioBreeding rat
  JOURNAL   J Immunol 194 (2), 615-629 (2015)
   PUBMED   25505293
REFERENCE   5  (residues 1 to 450)
  AUTHORS   Tanaka,H., Akagi,K., Oneyama,C., Tanaka,M., Sasaki,Y., Kanou,T.,
            Lee,Y.H., Yokogawa,D., Dobenecker,M.W., Nakagawa,A., Okada,M. and
            Ikegami,T.
  TITLE     Identification of a new interaction mode between the Src homology 2
            domain of C-terminal Src kinase (Csk) and Csk-binding
            protein/phosphoprotein associated with glycosphingolipid
            microdomains
  JOURNAL   J Biol Chem 288 (21), 15240-15254 (2013)
   PUBMED   23548896
  REMARK    GeneRIF: an allosteric connection between Cbp binding and Csk
            activation that arises from residues in the betaB/betaC loop of the
            SH2 domain.
REFERENCE   6  (residues 1 to 450)
  AUTHORS   Cloutier,J.F. and Veillette,A.
  TITLE     Association of inhibitory tyrosine protein kinase p50csk with
            protein tyrosine phosphatase PEP in T cells and other hemopoietic
            cells
  JOURNAL   EMBO J 15 (18), 4909-4918 (1996)
   PUBMED   8890164
REFERENCE   7  (residues 1 to 450)
  AUTHORS   Inomata,M., Takayama,Y., Kiyama,H., Nada,S., Okada,M. and
            Nakagawa,H.
  TITLE     Regulation of Src family kinases in the developing rat brain:
            correlation with their regulator kinase, Csk
  JOURNAL   J Biochem 116 (2), 386-392 (1994)
   PUBMED   7529760
REFERENCE   8  (residues 1 to 450)
  AUTHORS   Bougeret,C., Rothhut,B., Jullien,P., Fischer,S. and Benarous,R.
  TITLE     Recombinant Csk expressed in Escherichia coli is autophosphorylated
            on tyrosine residue(s)
  JOURNAL   Oncogene 8 (5), 1241-1247 (1993)
   PUBMED   7683130
REFERENCE   9  (residues 1 to 450)
  AUTHORS   Okada,M., Nada,S., Yamanashi,Y., Yamamoto,T. and Nakagawa,H.
  TITLE     CSK: a protein-tyrosine kinase involved in regulation of src family
            kinases
  JOURNAL   J Biol Chem 266 (36), 24249-24252 (1991)
   PUBMED   1722201
REFERENCE   10 (residues 1 to 450)
  AUTHORS   Nada,S., Okada,M., MacAuley,A., Cooper,J.A. and Nakagawa,H.
  TITLE     Cloning of a complementary DNA for a protein-tyrosine kinase that
            specifically phosphorylates a negative regulatory site of p60c-src
  JOURNAL   Nature 351 (6321), 69-72 (1991)
   PUBMED   1709258
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000008.1.
            
            On or before Oct 7, 2024 this sequence version replaced
            XP_006243225.1, XP_236290.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR26643284.11296.1,
                                           SRR26360194.1653845.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760400,
                                           SAMEA5760476 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..450
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q24"
     Protein         1..450
                     /product="tyrosine-protein kinase CSK"
                     /EC_number="2.7.10.2"
                     /note="protein-tyrosine kinase (CSK); C-SRC kinase; c-src
                     tyrosine kinase; CSK, non-receptor tyrosine kinase"
                     /calculated_mol_wt=50615
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P41240; propagated from
                     UniProtKB/Swiss-Prot (P32577.1)"
     Region          9..70
                     /region_name="Interaction with PTPN22.
                     /evidence=ECO:0000250|UniProtKB:P41240"
                     /note="propagated from UniProtKB/Swiss-Prot (P32577.1)"
     Region          11..67
                     /region_name="SH3_CSK"
                     /note="Src Homology 3 domain of C-terminal Src kinase;
                     cd11769"
                     /db_xref="CDD:212703"
     Site            order(20,23..24,26,40..41,43..44,46..47,49,59,61..64)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212703"
     Region          78..175
                     /region_name="SH2_csk_like"
                     /note="Src homology 2 (SH2) domain found in
                     Carboxyl-Terminal Src Kinase (Csk); cd09937"
                     /db_xref="CDD:198190"
     Site            order(89,107,128,130)
                     /site_type="other"
                     /note="phosphotyrosine binding pocket [polypeptide
                     binding]"
                     /db_xref="CDD:198190"
     Site            order(129,156)
                     /site_type="other"
                     /note="hydrophobic binding pocket [polypeptide binding]"
                     /db_xref="CDD:198190"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P41240; propagated from
                     UniProtKB/Swiss-Prot (P32577.1)"
     Region          188..443
                     /region_name="PTKc_Csk"
                     /note="Catalytic domain of the Protein Tyrosine Kinase,
                     C-terminal Src kinase; cd05082"
                     /db_xref="CDD:133213"
     Site            order(201..203,209,220,222,249,266..269,272..273,314,
                     318..319,321,331..332,345..349,358,392)
                     /site_type="active"
                     /db_xref="CDD:133213"
     Site            order(201..203,209,220,222,249,266..269,272..273,318..319,
                     321,331..332)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:133213"
     Site            order(215,226,238,241..242,244,259)
                     /site_type="other"
                     /note="SH3/SH2 domain interface [polypeptide binding]"
                     /db_xref="CDD:133213"
     Site            order(279..283,351,384..385,388..390)
                     /site_type="other"
                     /note="c-Src interface [polypeptide binding]"
                     /db_xref="CDD:133213"
     Site            304
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P41240; propagated from
                     UniProtKB/Swiss-Prot (P32577.1)"
     Site            order(314,318,345..349,358,392)
                     /site_type="other"
                     /note="polypeptide substrate binding site [polypeptide
                     binding]"
                     /db_xref="CDD:133213"
     Site            331..351
                     /site_type="other"
                     /note="activation loop (A-loop)"
                     /db_xref="CDD:133213"
     Site            364
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PKA.
                     /evidence=ECO:0000250|UniProtKB:P41240; propagated from
                     UniProtKB/Swiss-Prot (P32577.1)"
     Site            416
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by autocatalysis.
                     /evidence=ECO:0000250|UniProtKB:P41240; propagated from
                     UniProtKB/Swiss-Prot (P32577.1)"
     CDS             1..450
                     /gene="Csk"
                     /coded_by="NM_001030039.2:680..2032"
                     /db_xref="GeneID:315707"
                     /db_xref="RGD:1308800"
ORIGIN      
        1 msaiqaswps gteciakynf hgtaeqdlpf ckgdvltiva vtkdpnwyka knkvgregii
       61 panyvqkreg vkagtklslm pwfhgkitre qaerllyppe tglflvrest nypgdytlcv
      121 scegkvehyr imyhasklsi deevyfenlm qlvehyttda dglctrlikp kvmegtvaaq
      181 defyrsgwal nmkelkllqt igkgefgdvm lgdyrgnkva vkcikndata qaflaeasvm
      241 tqlrhsnlvq llgviveekg glyivteyma kgslvdylrs rgrsvlggdc llkfsldvce
      301 ameylegnnf vhrdlaarnv lvsednvakv sdfgltkeas stqdtgklpv kwtapealre
      361 kkfstksdvw sfgillweiy sfgrvpypri plkdvvprve kgykmdapdg cppavydvmk
      421 ncwhldaatr ptflqlreql ehirthelhl
//
