ID B4DRJ9_HUMAN Unreviewed; 746 AA.
AC B4DRJ9;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 94.
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:BAG61311.1};
RN [1] {ECO:0000313|EMBL:BAG61311.1}
RP NUCLEOTIDE SEQUENCE.
RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA Sugano S., Nomura N., Isogai T.;
RT "NEDO human cDNA sequencing project focused on splicing variants.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00009903}.
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DR EMBL; AK299296; BAG61311.1; -; mRNA.
DR AlphaFoldDB; B4DRJ9; -.
DR PeptideAtlas; B4DRJ9; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:UniProtKB-UniRule.
DR CDD; cd20875; C1_ROCK2; 1.
DR CDD; cd01242; PH_ROCK; 1.
DR CDD; cd22250; ROCK_SBD; 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); 2.
DR Gene3D; 1.20.5.730; Single helix bin; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR015008; ROCK_Rho-bd_dom.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF28; RHO-ASSOCIATED PROTEIN KINASE 2; 1.
DR Pfam; PF08912; Rho_Binding; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF103652; G protein-binding domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51859; RHO_BD; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01206, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kinase {ECO:0000313|EMBL:BAG61311.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000313|EMBL:BAG61311.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 337..405
FT /note="RhoBD"
FT /evidence="ECO:0000259|PROSITE:PS51859"
FT DOMAIN 508..707
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 618..673
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 703..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 13..367
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 414..459
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 721..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 746 AA; 87257 MW; 1E04A9429063A77D CRC64;
MIYKVECGLE EDLKNGKILL AKVELEKRQL QERFTDLEKE KSNMEIDMTY QLKVIQQSLE
QEEAEHKATK ARLADKNKIY ESIEEAKSEA MKEMEKKLLE ERTLKQKVEN LLLEAEKRCS
LLDCDLKQSQ QKINELLKQK DVLNEDVRNL TLKIEQETQK RCLTQNDLKM QTQQVNTLKM
SEKQLKQENN HLMEMKMNLE KQNAELRKER QDADGQMKEL QDQLEAEQYF STLYKTQVRE
LKEECEEKTK LGKELQQKKQ ELQDERDSLA AQLEITLTKA DSEQLARSIA EEQYSDLEKE
KIMKELEIKE MMARHKQELT EKDATIASLE ETNRTLTSDV ANLANEKEEL NNKLKDVQEQ
LSRLKDEEIS AAAIKAQFEK QLLTERTLKT QAVNKLAEIM NRKEPVKRGN DTDVRRKEKE
NRKLHMELKS EREKLTQQMI KYQKELNEMQ AQIAEESQIR IELQMTLDSK DSDIEQLRSQ
LQALHIGLDS SSIGSGPGDA EADDGFPESR LEGWLSLPVR NNTKKFGWVK KYVIVSSKKI
LFYDSEQDKE QCNPYMVLDI DKLFHVRPVT QTDVYRADAK EIPRIFQILY ANEGESKKEQ
EFPVEPVGEK SNYICHKGHE FIPTLYHFPT NCEACMKPLW HMFKPPPALE CRRCHIKCHK
DHMDKKEEII APCKVYYDIS TAKNLLLLAN STEEQQKWVS RLVKKIPKKP PAPDPFARSS
PRTSMKIQQN QSIRRPSRQL APNKPS
//