ID A5X3G4_MOUSE Unreviewed; 947 AA.
AC A5X3G4;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Kinase suppressor of ras 2 {ECO:0000313|EMBL:ABF74604.1};
GN Name=Ksr2 {ECO:0000313|EMBL:ABF74604.1, ECO:0000313|MGI:MGI:3610315};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:ABF74604.1};
RN [1] {ECO:0000313|EMBL:ABF74604.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Dba/1lac.j {ECO:0000313|EMBL:ABF74604.1};
RA Costanzo D.L., Pfluger P., Stock J.L., Schreiner A., Volle D.J., Treece T.,
RA Wu M.-H., Shaw A.S., McNeish J., Kim J.K., Tschoep M.H., Lewis R.E.;
RT "The Molecular Scaffold KSR2 Regulates Energy Expenditure.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DQ531035; ABF74604.1; -; mRNA.
DR AlphaFoldDB; A5X3G4; -.
DR PeptideAtlas; A5X3G4; -.
DR AGR; MGI:3610315; -.
DR MGI; MGI:3610315; Ksr2.
DR ChiTaRS; Ksr2; mouse.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20873; C1_KSR2; 1.
DR CDD; cd14153; PK_KSR2; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 6.10.140.1120; -; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR025561; KSR_SAM-like_dom.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR046861; SAM_KSR1_N.
DR InterPro; IPR046933; SAM_KSR1_N_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR23257:SF775; KINASE SUPPRESSOR OF RAS 2; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF13543; SAM_KSR1; 1.
DR Pfam; PF20406; SAM_KSR1_N; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 2: Evidence at transcript level;
KW Kinase {ECO:0000313|EMBL:ABF74604.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 409..453
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 663..928
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 265..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..291
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..547
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 947 AA; 107204 MW; 567470BCEA4B8B20 CRC64;
MDEENMTKSE EQQPLSLQKA LQQCELVQNM IDLSISNLEG LRTKCAASND LTQKEIRTLE
SKLVKYFSRQ LSCKKKVALQ ERNAELDGFP QLRHWFRIVD VRKEVLEEIS PDQLSLEDLL
EMTDEQVCET VEKYGANQEE CARLNASLSC LRNVHKSGGN LSKQDWIIQW PTTEPGQESN
PVCPPEPSPW IRTHLSQSPR VQTKCPQHFC PTSPTPGTPV YTQVDRLTVD AYPNLCPPPP
PLESGHRSLP PSPRQRHVVR TPNIVTTVTP PGTPPMRRKN KLKPPGTPPP SSRKLIHLIP
GFTALHRSKS HEFQLGNRVD EANTPKAKKK SKPLNLKIHS GVGSCENIPA QQRSPLLSER
SLRSFFVGHG PFLPSTPPVH TEANFSANTL SVPRWSPQIP RRDLGNSIKH RFSTKYWMSQ
TCTVCGKGML FGLKCKNCKL KCHNKCTKEA PPCHLLIIHR GDPARLVRTE SVPCDINNPV
RKPARYSDLH ISQTLPKTNK INKDHIPVPY QPDSSSNPSS TTSSTPSSPA PPLPPSATPP
SPLHPSPQCP RQKKNFNLPA SHYYKYKQQF IFPDVVPVPE TPTRAPQVIL HPVTSNTILE
GNPLLQIEVE PTSENEESHN EAEESEDEFE EMNLSLLSAR SFPRKASQTS IFLQEWDIPF
EQLEIGELIG KGRFGQVYHG RWHGEVAIRL IDIERDNEDQ LKAFKREVMA YRQTRHENVV
LFMGACMSPP HLAIITSLCK GRTLYSVVRD AKIVLDVNKT RQIAQEIVKG MGYLHAKGIL
HKDLKSKNVF YDNGKVVITD FGLFSISGVL QAGRRDDKLR IQNGWLCHLA PEIIRQLSPD
TEEDKLPFSK HSDVFALGTI WYELHAREWP FKTQPAEAII WQMGTGMKPN LSQIGMGKEI
SDILLFCWAF EQEERPTFTK LMDMLEKLPK RNRRLSHPGH FWKSAEL
//
