ID A0A0D9S7F1_CHLSB Unreviewed; 1802 AA.
AC A0A0D9S7F1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=MAST2 {ECO:0000313|Ensembl:ENSCSAP00000016790.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000016790.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000016790.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000016790.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR EMBL; AQIB01144876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01144877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01144878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01144879; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01144880; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01144881; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01144882; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01144883; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01144884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007977120.1; XM_007978929.1.
DR STRING; 60711.ENSCSAP00000016790; -.
DR Ensembl; ENSCSAT00000017309.1; ENSCSAP00000016790.1; ENSCSAG00000001224.1.
DR GeneID; 103224901; -.
DR CTD; 23139; -.
DR eggNOG; KOG0606; Eukaryota.
DR GeneTree; ENSGT00940000155705; -.
DR OMA; PHNIPPG; -.
DR OrthoDB; 2915765at2759; -.
DR BioGRID-ORCS; 103224901; 1 hit in 9 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 20.
DR Bgee; ENSCSAG00000001224; Expressed in fibroblast and 7 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0019902; F:phosphatase binding; IEA:Ensembl.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd05609; STKc_MAST; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.20.1480.20; MAST3 pre-PK domain-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR037711; MAST.
DR InterPro; IPR015022; MAST_pre-PK_dom.
DR InterPro; IPR023142; MAST_pre-PK_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356:SF136; MICROTUBULE-ASSOCIATED SERINE_THREONINE-PROTEIN KINASE 2; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF08926; DUF1908; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF140482; MAST3 pre-PK domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 519..792
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 793..861
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1111..1199
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1074..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1202..1375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1388..1451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1465..1659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1686..1727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1741..1802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1098
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1224..1238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1368
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1596..1610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1632..1659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1690..1712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1782..1802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1802 AA; 196760 MW; BD42E48F6AA65E33 CRC64;
MKRSRCRDRP QPPLPDRRED GVQRAAELPQ SLPPRRRAPP GRQRLEERTC PVGPEGKEQD
VVTGLSPLLF RKLSNPDIFS STGKVKLQRQ LSQDDCKLWR GNLASSLSGK QLLPLSSSVH
SSVGQVTWQS SGEASNLVRM RNQSLGQSAP SLTAGLKELS LPRRGSFCRT SNRKSLIVTS
STSPTLPRPH SPLHGHTGNS PLDSPRNFSP NAPAHFSFVP ARSHSHRADR TDGRRWSLAS
LPSSGYGTNT PSSTVSSSCS SQEKLHQLPF QPTADELHFL TKHFSTESVP DEEGRQSPAM
RPRSRSLSPG RSPVSFDSEI IMMNHVYKER FPKATAQMEE RLAEFISSNT PDSVLPLADG
ALSFIHHQVI EMARDCLDKS RSGLITSQYF YELQENLEKL VQDAHERSES SEVAFVMQLV
KKLMIVIARP ARLLECLEFD PEEFYHLLEA AEGHAKEGQG IKCDIPRYIV SQLGLTRDPL
EEMAQLSSCD SPDTPETDDS IEGRGASLPS KKTPSEEDFE TIKLISNGAY GAVFLVRHKS
TRQRFAMKKI NKQNLILRNQ IQQAFVERDI LTFAENPFVV SMFCSFETKR HLCMVMEYVE
GGDCATLLKN IGALPVDMVR LYFAETVLAL EYLHNYGIVH RDLKPDNLLI TSMGHIKLTD
FGLSKIGLMS LTTNLYEGHI EKDAREFLDK QVCGTPEYIA PEVILRQGYG KPVDWWAMGI
ILYEFLVGCV PFFGDTPEEL FGQVISDEIV WPEGDDALPP DAQDLTSKLL HQNPLERLGT
GSAYEVKQHP FFTGLDWTGL LRQKAEFIPQ LESEDDTSYF DTRSERYHHM DSEDEEEVSE
DGCLEIRQFS SCSPRFSKVY SSMERLSLLE ERRTPPPTKR SLSEEKEDRS DGLAGLKGRD
RSWVIGSPEI LRKRLSVSES SHTESDSSPP MTVRRRCSGL LDAPRFPEGP EEASSALRRQ
PQEGIWVLTP PSGEGASGPV AERSGEQWPK LDEEAVGRSS GSSPAMETRG RGTPQLAEGA
TAKAISDLAV RRARHRLLSG DSTEKRTTRP VNKVIKSASA TALSLLIPSE HHTCSPLASP
MSPHSQSSNP SSRDSSPSRD FLPALGSVRP PIIIHRAGKK YGFTLRAIRV YMGDSDVYTV
HHMVWHVEDG GPASEAGLRQ GDLITHVNGE PVHGLVHTEV VELILKSGNK VAISTTPLEN
TSIKVGPARK GSYKAKMARR SKKGRGKDGQ ESRKRSSLFR KITKQVSLLH TSRSLSSLNR
SLSSGESGPG SPTHSHSLSP RSPTQGYRVT PDAVHSVGGN SSQSSSPSSS VPSSPAGSGH
TRPSSLHGLA PKLQRQYRSP RRKSAGSIPL SPLAHTPSPP PPAASPQRSP SPLSGHVAQA
FPAKLHLSPP LGRQLSRPKS AEPPRSPLLK RVQSAEKLAA ALAASEKKLA TSRKHSLDLP
HSELKKELPP REVSPLEVVG ARGVLSGKGA LPGKGVLQPA PSRALGTLRQ DRAERRESLQ
KQEAIREVDS SEDDTEEGPE NSQGAQELSL APHPAVSQCV APKGTGESGE EETFPSSDPR
SPGPVVPSLL TGITLGPPRM ESPSGPHRRL GSPQAVEEAA SSSSPGPNLG RSGATDPIPS
EGCWKAQHLH TQALAALSSS SSGLTPTSSC SPPSSTSGKL GMWSWKFHIE GPDRASPSRK
AIMAGGLVNL QDLETTTPAH PKNLSPREQG KTQPPSAHPP CEDPSQGWLW ESECAQAVKE
DPALSITQVP DASGDRRQDV PCQGCPLTQE SESSLLWRGQ EPGGHQKHRD LALVPDELLK
QT
//
