ID H2R2M9_PANTR Unreviewed; 1551 AA.
AC H2R2M9; A0A2J8QCI6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 84.
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=CDC42BPG {ECO:0000313|Ensembl:ENSPTRP00000044216.3,
GN ECO:0000313|VGNC:VGNC:6483};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000044216.3, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000044216.3, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000044216.3}
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. DMPK subfamily. {ECO:0000256|ARBA:ARBA00005719}.
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DR EMBL; AC161428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_001146567.2; XM_001146567.5.
DR PaxDb; 9598-ENSPTRP00000044216; -.
DR Ensembl; ENSPTRT00000046796.4; ENSPTRP00000044216.3; ENSPTRG00000003849.5.
DR GeneID; 742988; -.
DR KEGG; ptr:742988; -.
DR CTD; 55561; -.
DR VGNC; VGNC:6483; CDC42BPG.
DR eggNOG; KOG0612; Eukaryota.
DR GeneTree; ENSGT01030000234517; -.
DR HOGENOM; CLU_000288_140_3_1; -.
DR InParanoid; H2R2M9; -.
DR OMA; PWQHRIR; -.
DR OrthoDB; 988261at2759; -.
DR TreeFam; TF313551; -.
DR Proteomes; UP000002277; Chromosome 11.
DR Bgee; ENSPTRG00000003849; Expressed in cerebellar cortex and 9 other cell types or tissues.
DR GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
DR GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01243; PH_MRCK; 1.
DR CDD; cd05597; STKc_DMPK_like; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR014930; Myotonic_dystrophy_kinase_coil.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF22; SERINE_THREONINE-PROTEIN KINASE MRCK GAMMA; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF08826; DMPK_coil; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 71..337
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 338..408
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 878..927
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 947..1066
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1092..1366
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1437..1450
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 528..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1442..1551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 412..439
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 749..797
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 531..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1510..1537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1551 AA; 172581 MW; A99C2A28D136B2FF CRC64;
MERRLRALEQ LARGEAGGCP GLDGLLDLLL ALHHELSSGP LRRERSVAQF LSWASPFVSK
VKELRLQRDD FEILKVIGRG AFGEVTVVRQ RDTGQIFAMK MLHKWEMLKR AETACFREER
DVLVKGDSRW VTTLHYAFQD EEYLYLVMDY YAGGDLLTLL SRFEDRLPPE LAQFYLAEMV
LAIHSLHQLG YVHRDVKPDN VLLDVNGHIR LADFGSCLRL NTNGMVDSSV AVGTPDYISP
EILQAMEEGK GHYGPQCDWW SLGVCAYELL FGETPFYAES LVETYGKIMN HEDHLQFPPD
VPDVPASAQD LIRQLLCRQE ERLGRGGLDD FRNHPFFEGV DWERLASSTA PYIPELRGPM
DTSNFDVDDD TLNHPGTLPP PSHGAFSGHH LPFVGFTYTS GSHSPESRSE AWAALERKLQ
CLEQEKVELS RKHQEALHAP TDHRELEQLR KEVQTLWDRL PEMLRDKASL SQTDGPPAGS
PGQDSDLRQE LDRLHRELAE GRAGLQAQEQ ELCRAQGQQE ELLQRLQEAQ EREAATASQT
RALSSQLEEA RAAQRELEAQ VSSLSRQVTQ LQGQWEQRLE ESSQAKTIHT ASETNGMGPP
EGGPQEAQLR KEVAALREQL EQAHSHRPSG KEEALCQLQE ENRRLSREQE RLEAELAQEQ
ESKQRLEGER RETESNWEAQ LADILSWVND EKVSRGYLQA LATKMAEELE SLRNVGTQTL
PARPLDHQWK ARRLQKMEAS ARLELQSALE AEIRAKQGLQ ERLMQVQEAQ LQAERRLQEA
EKQSQALQQE LAMLREELRA RGPVDTKPSN SLIPFLSFRS SEKDSAKDPG ISGEATRHGG
EPDLRPEGQR SLRMGAVFPR APTANTASTE GLPAKPGSHT LRPRSFPSPT KCLRCTSLML
GLGRQGLGCD ACGYFCHTTC APQAPPCPVP PDLLCTALGV HPETGTGTAY EGFLSVPRPS
GVRRGWQRVF AALSDSRLLL FDAPDPRLSP PSRALLQVLD LRDPQFSATP VLASDVIHAQ
SRDLPRIFRV TTSQLAVPPT TCTVLLLAES EGERERWLQV LGELQRLLLD VRPRPRPVYT
LKEAYDNGLP LLPHTLCAAI LDQDRLALGT EEGLFVIHLR SNDIFQVGEC RRVQQLTLSP
SAGLLVVLCG RGPSVRLFAL AELENIEVAG AKIPESRGCQ ALAAGSILQA RTPVLCVAVK
RQVLCYQLGP GPGPWQRRIR ELQAPATVQS LGLLGDRLCV GAAGGFALYP LLNEAAPLAL
GAGLVPEELP PSRGGLGEAL GAVELSLSEF LLLFTTAGIY VDGAGRKSRG QELLWPAAPM
GWGYAAPYLT VFSENSIDVF DVRRAEWVQT VPLKKVRPLN PEGSLFLYGT EKVRLTYLRN
QLAEKDEFDI PDLTDNSRRQ LFRTKSKRRF FFRVSEEQQK QQRREMLKDP FVRSKLISPP
TNFNHLVHVG PANGRPGARD KSPAPEEKGR VARGSGPQRP HSFSEALRRP ASMGSEGLGG
DADPMKRKPW TSLSSESVSC PQGSLSPATS LMQVSERPRS LPLSPELESS P
//
