GRK1_HUMAN
ID GRK1_HUMAN Reviewed; 563 AA.
AC Q15835; Q53X14;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Rhodopsin kinase GRK1;
DE Short=RK;
DE EC=2.7.11.14 {ECO:0000269|PubMed:15946941};
DE AltName: Full=G protein-coupled receptor kinase 1 {ECO:0000312|HGNC:HGNC:10013};
DE Flags: Precursor;
GN Name=GRK1 {ECO:0000312|HGNC:HGNC:10013}; Synonyms=RHOK;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=9147475; DOI=10.1017/s0952523800011366;
RA Zhao X., Haeseleer F., Fariss R.N., Huang J., Baehr W., Milam A.H.,
RA Palczewski K.;
RT "Molecular cloning and localization of rhodopsin kinase in the mammalian
RT pineal.";
RL Vis. Neurosci. 14:225-232(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=8812493; DOI=10.1006/geno.1996.0399;
RA Khani S.C., Abitbol M., Yamamoto S., Maravic-Magovcevic I., Dryja T.P.;
RT "Characterization and chromosomal localization of the gene for human
RT rhodopsin kinase.";
RL Genomics 35:571-576(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Corpus callosum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=11717351; DOI=10.1523/jneurosci.21-23-09175.2001;
RA Weiss E.R., Ducceschi M.H., Horner T.J., Li A., Craft C.M., Osawa S.;
RT "Species-specific differences in expression of G-protein-coupled receptor
RT kinase (GRK) 7 and GRK1 in mammalian cone photoreceptor cells: implications
RT for cone cell phototransduction.";
RL J. Neurosci. 21:9175-9184(2001).
RN [6]
RP BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, FUNCTION IN
RP PHOSPHORYLATION OF RHO, PHOSPHORYLATION AT SER-21, ACTIVITY REGULATION,
RP AUTOPHOSPHORYLATION, AND MUTAGENESIS OF SER-21 AND LYS-219.
RX PubMed=15946941; DOI=10.1074/jbc.m505117200;
RA Horner T.J., Osawa S., Schaller M.D., Weiss E.R.;
RT "Phosphorylation of GRK1 and GRK7 by cAMP-dependent protein kinase
RT attenuates their enzymatic activities.";
RL J. Biol. Chem. 280:28241-28250(2005).
RN [7] {ECO:0007744|PDB:5AFP}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-25 IN COMPLEX WITH NCS1.
RX PubMed=25979333; DOI=10.1074/jbc.m114.627059;
RA Pandalaneni S., Karuppiah V., Saleem M., Haynes L.P., Burgoyne R.D.,
RA Mayans O., Derrick J.P., Lian L.Y.;
RT "Neuronal Calcium Sensor-1 Binds the D2 Dopamine Receptor and G-protein-
RT coupled Receptor Kinase 1 (GRK1) Peptides Using Different Modes of
RT Interactions.";
RL J. Biol. Chem. 290:18744-18756(2015).
RN [8]
RP VARIANTS GLN-136; MET-298; SER-330; HIS-438; SER-514; THR-522 AND LEU-536.
RX PubMed=9268593; DOI=10.1006/exer.1997.9998;
RA Yamamoto S., Khani S.C., Berson E.L., Dryja T.P.;
RT "Evaluation of the rhodopsin kinase gene in patients with retinitis
RT pigmentosa.";
RL Exp. Eye Res. 65:249-253(1997).
RN [9]
RP VARIANT CSNBO2 ASP-380.
RX PubMed=9020843; DOI=10.1038/ng0297-175;
RA Yamamoto S., Sippel K.C., Berson E.L., Dryja T.P.;
RT "Defects in the rhodopsin kinase gene in the Oguchi form of stationary
RT night blindness.";
RL Nat. Genet. 15:175-178(1997).
RN [10]
RP VARIANT CSNBO2 HIS-391.
RX PubMed=17070587; DOI=10.1016/j.ophtha.2006.05.069;
RA Hayashi T., Gekka T., Takeuchi T., Goto-Omoto S., Kitahara K.;
RT "A novel homozygous GRK1 mutation (P391H) in 2 siblings with Oguchi disease
RT with markedly reduced cone responses.";
RL Ophthalmology 114:134-141(2007).
CC -!- FUNCTION: Retina-specific kinase involved in the signal turnoff via
CC phosphorylation of rhodopsin (RHO), the G protein- coupled receptor
CC that initiates the phototransduction cascade (PubMed:15946941). This
CC rapid desensitization is essential for scotopic vision and permits
CC rapid adaptation to changes in illumination (By similarity). May play a
CC role in the maintenance of the outer nuclear layer in the retina (By
CC similarity). {ECO:0000250|UniProtKB:Q9WVL4,
CC ECO:0000269|PubMed:15946941}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[rhodopsin] = ADP + H(+) + O-phospho-L-
CC threonyl-[rhodopsin]; Xref=Rhea:RHEA:56552, Rhea:RHEA-COMP:14596,
CC Rhea:RHEA-COMP:14597, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.14; Evidence={ECO:0000269|PubMed:15946941};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[rhodopsin] = ADP + H(+) + O-phospho-L-seryl-
CC [rhodopsin]; Xref=Rhea:RHEA:23356, Rhea:RHEA-COMP:14594, Rhea:RHEA-
CC COMP:14595, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.14;
CC Evidence={ECO:0000269|PubMed:15946941};
CC -!- ACTIVITY REGULATION: Inhibited by RCVRN, which prevents the interaction
CC between GRK1 and RHO (By similarity). Inhibition is calcium-dependent
CC (By similarity). Inhibited by phosphorylation of Ser-21.
CC {ECO:0000250|UniProtKB:P28327, ECO:0000269|PubMed:15946941}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.5 uM for rhodopsin {ECO:0000269|PubMed:15946941};
CC KM=10.6 uM for ATP {ECO:0000269|PubMed:15946941};
CC Vmax=1132 nmol/min/mg enzyme {ECO:0000269|PubMed:15946941};
CC -!- SUBUNIT: Interacts (via N-terminus) with RCVRN (via C-terminus); the
CC interaction is Ca(2+)-dependent (By similarity). Interacts (when
CC prenylated) with PDE6D; this promotes release from membranes (By
CC similarity). May form a complex composed of RHO, GRK1 and RCVRN in a
CC Ca(2+)-dependent manner; RCVRN prevents the interaction between GRK1
CC and RHO (By similarity). {ECO:0000250|UniProtKB:P28327}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P28327}; Lipid-
CC anchor {ECO:0000250|UniProtKB:P28327}. Cell projection, cilium,
CC photoreceptor outer segment {ECO:0000250|UniProtKB:Q9WVL4}.
CC Note=Subcellular location is not affected by light or dark conditions.
CC {ECO:0000250|UniProtKB:Q9WVL4}.
CC -!- TISSUE SPECIFICITY: Retinal-specific. Expressed in rods and cones
CC cells. {ECO:0000269|PubMed:11717351}.
CC -!- PTM: Autophosphorylated, Ser-21 is a minor site of autophosphorylation
CC compared to Ser-491 and Thr-492 (By similarity). Phosphorylation at
CC Ser-21 is regulated by light and activated by cAMP. {ECO:0000250,
CC ECO:0000269|PubMed:15946941}.
CC -!- PTM: Farnesylation is required for full activity.
CC {ECO:0000250|UniProtKB:P28327}.
CC -!- DISEASE: Night blindness, congenital stationary, Oguchi type 2 (CSNBO2)
CC [MIM:613411]: A non-progressive retinal disorder characterized by
CC impaired night vision, often associated with nystagmus and myopia.
CC Congenital stationary night blindness Oguchi type is associated with
CC fundus discoloration and abnormally slow dark adaptation.
CC {ECO:0000269|PubMed:17070587, ECO:0000269|PubMed:9020843}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. GPRK subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Mutations of the RHOK gene; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/rkmut.htm";
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DR EMBL; U63973; AAB05929.1; -; mRNA.
DR EMBL; L77503; AAG50439.1; -; mRNA.
DR EMBL; L77502; AAT00534.2; -; Genomic_DNA.
DR EMBL; L77496; AAT00534.2; JOINED; Genomic_DNA.
DR EMBL; L77497; AAT00534.2; JOINED; Genomic_DNA.
DR EMBL; L77498; AAT00534.2; JOINED; Genomic_DNA.
DR EMBL; L77499; AAT00534.2; JOINED; Genomic_DNA.
DR EMBL; L77500; AAT00534.2; JOINED; Genomic_DNA.
DR EMBL; L77501; AAT00534.2; JOINED; Genomic_DNA.
DR EMBL; AC187648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK289912; BAF82601.1; -; mRNA.
DR CCDS; CCDS81785.1; -.
DR RefSeq; NP_002920.1; NM_002929.2.
DR PDB; 5AFP; X-ray; 2.30 A; C/D=1-25.
DR PDBsum; 5AFP; -.
DR AlphaFoldDB; Q15835; -.
DR SMR; Q15835; -.
DR BioGRID; 111943; 9.
DR IntAct; Q15835; 1.
DR STRING; 9606.ENSP00000334876; -.
DR BindingDB; Q15835; -.
DR ChEMBL; CHEMBL5607; -.
DR DrugCentral; Q15835; -.
DR GuidetoPHARMACOLOGY; 1465; -.
DR iPTMnet; Q15835; -.
DR PhosphoSitePlus; Q15835; -.
DR BioMuta; GRK1; -.
DR DMDM; 2833269; -.
DR MassIVE; Q15835; -.
DR MaxQB; Q15835; -.
DR PaxDb; Q15835; -.
DR PeptideAtlas; Q15835; -.
DR PRIDE; Q15835; -.
DR ProteomicsDB; 60785; -.
DR Antibodypedia; 25983; 343 antibodies from 34 providers.
DR DNASU; 6011; -.
DR Ensembl; ENST00000335678.7; ENSP00000334876.5; ENSG00000185974.7.
DR Ensembl; ENST00000672946.1; ENSP00000499886.1; ENSG00000288263.1.
DR GeneID; 6011; -.
DR KEGG; hsa:6011; -.
DR MANE-Select; ENST00000335678.7; ENSP00000334876.5; NM_002929.3; NP_002920.1.
DR UCSC; uc010tkf.3; human.
DR CTD; 6011; -.
DR DisGeNET; 6011; -.
DR GeneCards; GRK1; -.
DR HGNC; HGNC:10013; GRK1.
DR HPA; ENSG00000185974; Tissue enriched (retina).
DR MalaCards; GRK1; -.
DR MIM; 180381; gene.
DR MIM; 613411; phenotype.
DR neXtProt; NX_Q15835; -.
DR OpenTargets; ENSG00000185974; -.
DR Orphanet; 215; Congenital stationary night blindness.
DR Orphanet; 75382; Oguchi disease.
DR PharmGKB; PA34391; -.
DR VEuPathDB; HostDB:ENSG00000185974; -.
DR eggNOG; KOG0986; Eukaryota.
DR GeneTree; ENSGT00940000159927; -.
DR HOGENOM; CLU_000288_63_41_1; -.
DR InParanoid; Q15835; -.
DR OMA; PASKSGM; -.
DR OrthoDB; 1104340at2759; -.
DR PhylomeDB; Q15835; -.
DR TreeFam; TF313940; -.
DR BRENDA; 2.7.11.14; 2681.
DR PathwayCommons; Q15835; -.
DR Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR SABIO-RK; Q15835; -.
DR SignaLink; Q15835; -.
DR SIGNOR; Q15835; -.
DR BioGRID-ORCS; 6011; 10 hits in 270 CRISPR screens.
DR ChiTaRS; GRK1; human.
DR GenomeRNAi; 6011; -.
DR Pharos; Q15835; Tchem.
DR PRO; PR:Q15835; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q15835; protein.
DR Bgee; ENSG00000185974; Expressed in right lobe of thyroid gland and 42 other tissues.
DR Genevisible; Q15835; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004703; F:G protein-coupled receptor kinase activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0050254; F:rhodopsin kinase activity; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0022400; P:regulation of rhodopsin mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; TAS:ProtInc.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR CDD; cd05608; STKc_GRK1; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000239; GPCR_kinase.
DR InterPro; IPR032965; GRK1.
DR InterPro; IPR037716; GRK1_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24355:SF11; PTHR24355:SF11; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00615; RGS; 1.
DR PRINTS; PR00717; GPCRKINASE.
DR SMART; SM00315; RGS; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF56112; SSF56112; 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; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell projection;
KW Congenital stationary night blindness; Disease variant; Kinase;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Phosphoprotein;
KW Prenylation; Reference proteome; Sensory transduction;
KW Serine/threonine-protein kinase; Transferase; Vision.
FT CHAIN 1..560
FT /note="Rhodopsin kinase GRK1"
FT /id="PRO_0000024375"
FT PROPEP 561..563
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000024376"
FT DOMAIN 58..175
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 190..455
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 456..521
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..189
FT /note="N-terminal"
FT REGION 1..15
FT /note="Interaction with RCVRN"
FT /evidence="ECO:0000250|UniProtKB:P28327"
FT REGION 456..563
FT /note="C-terminal"
FT REGION 539..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 317
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 196..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28327"
FT MOD_RES 8
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P28327"
FT MOD_RES 21
FT /note="Phosphoserine; by PKA and autocatalysis"
FT /evidence="ECO:0000269|PubMed:15946941"
FT MOD_RES 491
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P28327"
FT MOD_RES 492
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P28327"
FT MOD_RES 560
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P28327"
FT LIPID 560
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P28327"
FT VARIANT 136
FT /note="E -> Q (in dbSNP:rs542688076)"
FT /evidence="ECO:0000269|PubMed:9268593"
FT /id="VAR_008283"
FT VARIANT 298
FT /note="T -> M (in dbSNP:rs572803634)"
FT /evidence="ECO:0000269|PubMed:9268593"
FT /id="VAR_008284"
FT VARIANT 330
FT /note="N -> S (in dbSNP:rs375409897)"
FT /evidence="ECO:0000269|PubMed:9268593"
FT /id="VAR_008285"
FT VARIANT 380
FT /note="V -> D (in CSNBO2; dbSNP:rs777094000)"
FT /evidence="ECO:0000269|PubMed:9020843"
FT /id="VAR_006215"
FT VARIANT 391
FT /note="P -> H (in CSNBO2; dbSNP:rs570621429)"
FT /evidence="ECO:0000269|PubMed:17070587"
FT /id="VAR_037904"
FT VARIANT 438
FT /note="R -> H (in dbSNP:rs750619057)"
FT /evidence="ECO:0000269|PubMed:9268593"
FT /id="VAR_008286"
FT VARIANT 514
FT /note="C -> S (in dbSNP:rs771561763)"
FT /evidence="ECO:0000269|PubMed:9268593"
FT /id="VAR_008287"
FT VARIANT 522
FT /note="M -> T (in dbSNP:rs779749742)"
FT /evidence="ECO:0000269|PubMed:9268593"
FT /id="VAR_008288"
FT VARIANT 536
FT /note="S -> L (in dbSNP:rs553969577)"
FT /evidence="ECO:0000269|PubMed:9268593"
FT /id="VAR_008289"
FT MUTAGEN 21
FT /note="S->E: Not phosphorylated by PKA."
FT /evidence="ECO:0000269|PubMed:15946941"
FT MUTAGEN 219
FT /note="K->A: Loss of autophosphorylation and RHO
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:15946941"
FT HELIX 7..14
FT /evidence="ECO:0007829|PDB:5AFP"
SQ SEQUENCE 563 AA; 63526 MW; 1244DCB97D40F53D CRC64;
MDFGSLETVV ANSAFIAARG SFDGSSSQPS RDKKYLAKLK LPPLSKCESL RDSLSLEFES
VCLEQPIGKK LFQQFLQSAE KHLPALELWK DIEDYDTADN DLQPQKAQTI LAQYLDPQAK
LFCSFLDEGI VAKFKEGPVE IQDGLFQPLL QATLAHLGQA PFQEYLGSLY FLRFLQWKWL
EAQPMGEDWF LDFRVLGKGG FGEVSACQMK ATGKLYACKK LNKKRLKKRK GYQGAMVEKK
ILMKVHSRFI VSLAYAFETK ADLCLVMTIM NGGDIRYHIY NVNEENPGFP EPRALFYTAQ
IICGLEHLHQ RRIVYRDLKP ENVLLDNDGN VRISDLGLAV ELLDGQSKTK GYAGTPGFMA
PELLQGEEYD FSVDYFALGV TLYEMIAARG PFRARGEKVE NKELKHRIIS EPVKYPDKFS
QASKDFCEAL LEKDPEKRLG FRDETCDKLR AHPLFKDLNW RQLEAGMLMP PFIPDSKTVY
AKDIQDVGAF STVKGVAFDK TDTEFFQEFA TGNCPIPWQE EMIETGIFGE LNVWRSDGQM
PDDMKGISGG SSSSSKSGMC LVS
