ID A0A0P6JE79_HETGA Unreviewed; 716 AA.
AC A0A0P6JE79;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Mitogen-activated protein kinase 6 {ECO:0000256|ARBA:ARBA00039551};
DE EC=2.7.11.24 {ECO:0000256|ARBA:ARBA00012411};
GN Name=MAPK6 {ECO:0000313|EMBL:JAO01777.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:JAO01777.1};
RN [1] {ECO:0000313|EMBL:JAO01777.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Liver {ECO:0000313|EMBL:JAO01777.1};
RA Bens M., Sahm A., Jahn N., Morhart M., Holtze S., Hildebrandt T.B.,
RA Platzer M., Szafranski K.;
RT "FRAMA: From RNA-seq data to annotated mRNA assemblies.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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=2.7.11.24;
CC Evidence={ECO:0000256|ARBA:ARBA00000494};
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=2.7.11.24; Evidence={ECO:0000256|ARBA:ARBA00000088};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily.
CC {ECO:0000256|ARBA:ARBA00008832}.
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DR EMBL; GEBF01001856; JAO01777.1; -; Transcribed_RNA.
DR RefSeq; XP_004835451.1; XM_004835394.2.
DR RefSeq; XP_004835452.1; XM_004835395.2.
DR RefSeq; XP_004835453.1; XM_004835396.1.
DR RefSeq; XP_012929800.1; XM_013074346.1.
DR RefSeq; XP_012929803.1; XM_013074349.1.
DR AlphaFoldDB; A0A0P6JE79; -.
DR Ensembl; ENSHGLT00100015028; ENSHGLP00100014865; ENSHGLG00100011007.
DR GeneID; 101700449; -.
DR KEGG; hgl:101700449; -.
DR CTD; 5597; -.
DR OrthoDB; 5344491at2759; -.
DR Bgee; ENSHGLG00000018577; Expressed in cerebellum and 10 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0032156; C:septin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IEA:Ensembl.
DR CDD; cd07854; STKc_MAPK4_6; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR008350; MAPK_ERK3/4.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1.
DR PANTHER; PTHR24055:SF171; MITOGEN-ACTIVATED PROTEIN KINASE 6; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01771; ERK3ERK4MAPK.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 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, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:JAO01777.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 20..316
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 684..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 716 AA; 81948 MW; DDC0BD757E0216A3 CRC64;
MAEKFESLMN IHGFDLGSRY MDLKPLGCGG NGLVFSAVDN DCDKRVAIKK IVLTDPQSVK
HALREIKIIR RLDHDNIVKV FEILGPSGSR LADDVGSLTE LSSVYIVQEY METDLASVLE
QGPLLEEHAR LFMYQLLRGL KYIHSANVLH RDLKPANLFI NTEDLVLKIG DFGLARIMDP
HYSHKGHLSE GLVTKWYRSP RLLLSPNNYT KAIDMWAAGC IFAEMLTGKT LFAGAHELEQ
MQLILESIPV VHEEDRQELL SVIPVYIRSD MTEPHRPLTQ LLPEIGREAL DFLEQILTFS
PMDRLTAEEA LSHPYMSMYA FPTDEPISSH PFHIEDEVDD ILLMDETHSH IYNWERYHDC
QFSEHDWPIH NNFDIDEVQL DPRALSDITD EEEGQVDPRK YLDGDREKYL EDPAFDASYS
AEPCWQSPDH HENKYCELEC GHTCNYKARS ASYLDSLVWR ESEVNHYYEP KLIIDLSNWK
EQSREKPDKK GKSKCERNGL VKAQIALEEA SQQRAEKERE KNQGFDFDSF IAGTIQLSSQ
HEPTDVVDKL NDLNSSVSQL ELKGLIPKSV SREKQEKGMA NLAQLEALYQ SSWDSQFGGG
GEERFLIDQF CCEVRKDEQV EKEHTYTSYL DRFFSRREEA ELLEAEPGED RPRVERGGGE
GFLNHSGELL LNKQLECMGL PQLHSPVGSP RKSVPAVKAS PRVPPRTYSS ILRHLN
//
