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Database: UniProt
Entry: D7RF68_HUMAN
LinkDB: D7RF68_HUMAN
Original site: D7RF68_HUMAN 
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
//
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