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Database: UniProt
Entry: B4DRJ9_HUMAN
LinkDB: B4DRJ9_HUMAN
Original site: B4DRJ9_HUMAN 
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
//
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