ID D7RF68_HUMAN Unreviewed; 597 AA.
AC D7RF68;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:ADH51547.1};
RN [1] {ECO:0000313|EMBL:ADH51547.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20526349; DOI=10.1038/nm.2166;
RA Palanisamy N., Ateeq B., Kalyana-Sundaram S., Pflueger D., Ramnarayanan K.,
RA Shanker S., Han B., Cao Q., Cao X., Suleman K., Kumar-Sinha C.,
RA Dhanasekaran S.M., Chen Y.-B., Esgueva R., Banerjee S., LaFargue C.J.,
RA Siddiqui J., Demichelis F., Moeller P., Bismar T.A., Kuefer R.,
RA Fullen D.R., Johnson T.M., Greenson J.K., Giordano T.J., Tan P.,
RA Tomlins S.A., Varambally S., Rubin M.A., Maher C.A., Chinnaiyan A.M.;
RT "Rearrangements of the RAF kinase pathway in prostate cancer, gastric
RT cancer and melanoma.";
RL Nat. Med. 16:793-798(2010).
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};
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DR EMBL; HM053972; ADH51547.1; -; mRNA.
DR AlphaFoldDB; D7RF68; -.
DR PeptideAtlas; D7RF68; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0038166; P:angiotensin-activated signaling pathway; IEA:InterPro.
DR CDD; cd14062; STKc_Raf; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR009436; AGTRAP.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR44329:SF240; SERINE/THREONINE-PROTEIN KINASE B-RAF; 1.
DR PANTHER; PTHR44329; SERINE/THREONINE-PROTEIN KINASE TNNI3K-RELATED; 1.
DR Pfam; PF06396; AGTRAP; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00805; AGTRAP; 1.
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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 53..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 88..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 288..548
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 143..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 597 AA; 66206 MW; 96B530F719E9190D CRC64;
MELPAVNLKV ILLGHWLLTT WGCIVFSGSY AWANFTILAL GVWAVAQRDS IDAISMFLGG
LLATIFLDIV HISIFYPRVS LTDTGRFGVG MAILSLLLKP LSCCFVYHMY RERGGELLVH
TGFLGSSQDR SAYQTIDSAE APADPFAVPE GRSQDARGPQ ILTSPSPSKS IPIPQPFRPA
DEDHRNQFGQ RDRSSSAPNV HINTIEPVNI DDLIRDQGFR GDGGSTTGLS ATPPASLPGS
LTNVKALQKS PGPQRERKSS SSSEDRNRMK TLGRRDSSDD WEIPDGQITV GQRIGSGSFG
TVYKGKWHGD VAVKMLNVTA PTPQQLQAFK NEVGVLRKTR HVNILLFMGY STKPQLAIVT
QWCEGSSLYH HLHIIETKFE MIKLIDIARQ TAQGMDYLHA KSIIHRDLKS NNIFLHEDLT
VKIGDFGLAT VKSRWSGSHQ FEQLSGSILW MAPEVIRMQD KNPYSFQSDV YAFGIVLYEL
MTGQLPYSNI NNRDQIIFMV GRGYLSPDLS KVRSNCPKAM KRLMAECLKK KRDERPLFPQ
ILASIELLAR SLPKIHRSAS EPSLNRAGFQ TEDFSLYACA SPKTPIQAGG YGAFPVH
//