UniProt: H2TR73

Database: UniProt
Entry: H2TR73_TAKRU

LinkDB:  H2TR73_TAKRU 
Original site:  H2TR73_TAKRU

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Ontology (14)   
   GO (14)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (24)   
   InterPro (12)   
   Pfam (3)   
   PROSITE (6)   
   SMART (3)   
Literature (1)   
   PubMed (1)   
All databases (43)   

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ID   H2TR73_TAKRU            Unreviewed;      1350 AA.
AC   H2TR73;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 3.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=rock2 {ECO:0000313|Ensembl:ENSTRUP00000027180.3};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000027180.3, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000027180.3, ECO:0000313|Proteomes:UP000005226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA   Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu facilitates
RT   insights into distinct features of genome evolution in teleosts and
RT   mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000027180.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR   Ensembl; ENSTRUT00000027289.3; ENSTRUP00000027180.3; ENSTRUG00000010769.3.
DR   GeneTree; ENSGT01030000234517; -.
DR   Proteomes; UP000005226; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0048468; P:cell development; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0010825; P:positive regulation of centrosome duplication; IEA:InterPro.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0007266; P:Rho protein signal transduction; IEA:UniProtKB-UniRule.
DR   GO; GO:0006939; P:smooth muscle contraction; IEA:InterPro.
DR   CDD; cd20875; C1_ROCK2; 1.
DR   CDD; cd11638; HR1_ROCK2; 1.
DR   CDD; cd01242; PH_ROCK; 1.
DR   CDD; cd22250; ROCK_SBD; 1.
DR   CDD; cd05596; STKc_ROCK; 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); 1.
DR   Gene3D; 1.20.5.730; Single helix bin; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR020684; ROCK1/ROCK2.
DR   InterPro; IPR037311; ROCK2_HR1.
DR   InterPro; IPR015008; ROCK_Rho-bd_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR   PANTHER; PTHR22988:SF28; RHO-ASSOCIATED PROTEIN KINASE 2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   Pfam; PF08912; Rho_Binding; 1.
DR   PIRSF; PIRSF037568; Rho_kinase; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF103652; G protein-binding domain; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS51859; RHO_BD; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW   ProRule:PRU01206}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          68..330
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          331..401
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   DOMAIN          934..1002
FT                   /note="RhoBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51859"
FT   DOMAIN          1224..1276
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   REGION          999..1023
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1312..1350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          397..644
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          688..961
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1321..1350
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        190
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037568-1"
FT   BINDING         97
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037568-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1350 AA;  156658 MW;  918454B3BDB2E0A1 CRC64;
     MSLGAERRLE PRLRKLEDMI RDPRSAINLE SLLVSQNRCS NVHVFLALPA DEKVIEQTRD
     LQMKSEDFEK VKIIGRGAFG EVQLVRHRVS QKVYAMKLLS KFEMIKRSDS AFFWEERDIM
     AFSNSPWVVQ LCCAFQDEHY LYMVMEYMPG GDLVNLTSTY DVPEKWAKFY TAEVVMALDA
     IHSMGFIHRD VKPDNMLLDR NGHLKLADFG TCMKMNSTGM VHCDTAVGTP DYISPEVLKS
     QGGDGYYGRE CDWWSVGVFI FEMLVGDTPF YADSLVGTYS KIMDHKNSLN FPDDVDISKN
     ARNIICAFLT DREVRLGRNG VEEIKQHPFF KNDQWTFDTI RGTVAPVVPE LSSDIDTSNF
     DEIEDDKGDV ETFPTPKAFV GNQLPFVGFT YFKENQLKNQ KSSSAELQKK LQHLEVQLKN
     EKQHMGDLEH KYRYFIFAFL FQVGNRKSLE SSLRQLEREK ALLQHKSLES HRKAENEADR
     KRCLENEVNG LRDQLDDLKR RNQNSHISNE KNIHLQKQLE EANTLLRAES EAATRLRKTQ
     TESSKQLQQL EANVRELQDK CCLLERSKLS LEKECISLQA ALETERREHS QGSETISDLM
     GRISVLEEEA RQQRQALSKS ESEKRQLQEK LTDLEKEKSN KEIDLTYKLK VLQQELEQEE
     ASHKTTRGLL ADKSKIKVTI EGAKSESMKE MEQKLAEERA AKLRLENRIL ELEKHSSMMD
     CDYKQALQKL DELRRHKDQL TEEMKNMMLK IEQETQKRNL TQNDLKAQNQ QLSSLRTSEK
     QLKQELNHLL DIKRSLEKQN QELRKERQDA DGQMKELQDQ LEAEQYFSTL YKTQVRELKE
     ECEERNKLCK DAQQSLQEQQ EERDSLAAQL EITLTKADSE QLARSIAEEQ YSDLEKEKIM
     KELELKEMMA RHRQELAEKD ITISSLEEAN RTLTSDVANL ANEKEELNNK LKAAIEESQK
     SNDWEQQICQ MKQGFEKQLQ SERTLKTQAV NKLAEIMNRK EIRGGGSRRG NDTDMRRKEK
     ENRKLQLELR SEKEKLNSAI IKYQKEINEM QAQLSEESQM RIELQMALDS RDSDIEQLRN
     YLQSLSVPSL DSASVNSGPE FDTDDAYTGG GITFLHSLVS NIIGTIIMDL WPHGYYVVVS
     SKKILFYNNE QDKEQSIPYM VLDIDKLFHV RPVTQTDVYR ADAKEIPRIF QILYANEGES
     KKEPEFPVEP LPIGEKSSYI CHKGHEFIPT LYHFPTNCEA CTKPLWNMFK PPPALECRRC
     HIKCHKDHMD KKEDIIAPLN YDVSTAKNLL LLAVSQEEQQ KWVSRLVKKI PKKPPPAETF
     LRSSPRTSMK VQPSQSMRRP SRQLPTSKSR
//

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