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Protein

Rhodopsin kinase

Gene

GRK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Retina-specific kinase involved in the signal turnoff via phosphorylation of rhodopsin (RHO), the G protein- coupled receptor that initiates the phototransduction cascade. This rapid desensitization is essential for scotopic vision and permits rapid adaptation to changes in illumination.1 Publication

Catalytic activityi

ATP + [rhodopsin] = ADP + [rhodopsin] phosphate.1 Publication

Enzyme regulationi

Inhibited by phosphorylation of Ser-21.1 Publication

Kineticsi

  1. KM=3.5 µM for rhodopsin1 Publication
  2. KM=10.6 µM for ATP1 Publication
  1. Vmax=1132 nmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei219ATPPROSITE-ProRule annotation1
Active sitei317Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi196 – 204ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • G-protein coupled receptor kinase activity Source: InterPro
  • protein kinase activity Source: ProtInc
  • rhodopsin kinase activity Source: UniProtKB

GO - Biological processi

  • protein autophosphorylation Source: UniProtKB
  • regulation of G-protein coupled receptor protein signaling pathway Source: ProtInc
  • regulation of rhodopsin mediated signaling pathway Source: UniProtKB
  • rhodopsin mediated signaling pathway Source: ProtInc
  • visual perception Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS00048-MONOMER.
BRENDAi2.7.11.14. 2681.
ReactomeiR-HSA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
SignaLinkiQ15835.
SIGNORiQ15835.

Names & Taxonomyi

Protein namesi
Recommended name:
Rhodopsin kinase (EC:2.7.11.141 Publication)
Short name:
RK
Alternative name(s):
G protein-coupled receptor kinase 1Imported
Gene namesi
Name:GRK1Imported
Synonyms:RHOK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:10013. GRK1.

Subcellular locationi

  • Membrane By similarity; Lipid-anchor By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Night blindness, congenital stationary, Oguchi type 2 (CSNBO2)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA non-progressive retinal disorder characterized by impaired night vision, often associated with nystagmus and myopia. Congenital stationary night blindness Oguchi type is associated with fundus discoloration and abnormally slow dark adaptation.
See also OMIM:613411
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_006215380V → D in CSNBO2. 1 PublicationCorresponds to variant rs777094000dbSNPEnsembl.1
Natural variantiVAR_037904391P → H in CSNBO2. 1 PublicationCorresponds to variant rs570621429dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi21S → E: Not phosphorylated by PKA. 1 Publication1
Mutagenesisi219K → A: Loss of autophosphorylation and RHO phosphorylation. 1 Publication1

Keywords - Diseasei

Congenital stationary night blindness, Disease mutation

Organism-specific databases

DisGeNETi6011.
MalaCardsiGRK1.
MIMi613411. phenotype.
OpenTargetsiENSG00000185974.
Orphaneti215. Congenital stationary night blindness.
75382. Oguchi disease.
PharmGKBiPA34391.

Chemistry databases

ChEMBLiCHEMBL5607.
GuidetoPHARMACOLOGYi1465.

Polymorphism and mutation databases

BioMutaiGRK1.
DMDMi2833269.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000243751 – 560Rhodopsin kinaseAdd BLAST560
PropeptideiPRO_0000024376561 – 563Removed in mature formBy similarity3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei5PhosphoserineBy similarity1
Modified residuei8PhosphothreonineBy similarity1
Modified residuei21Phosphoserine; by PKA and autocatalysis1 Publication1
Modified residuei491Phosphoserine; by autocatalysisBy similarity1
Modified residuei492Phosphothreonine; by autocatalysisBy similarity1
Modified residuei560Cysteine methyl esterBy similarity1
Lipidationi560S-farnesyl cysteineBy similarity1

Post-translational modificationi

Autophosphorylated, Ser-21 is a minor site of autophosphorylation compared to Ser-491 and Thr-492 (By similarity). Phosphorylation at Ser-21 is regulated by light and activated by cAMP.By similarity1 Publication
Farnesylation is required for full activity.By similarity

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

EPDiQ15835.
MaxQBiQ15835.
PaxDbiQ15835.
PeptideAtlasiQ15835.
PRIDEiQ15835.

PTM databases

iPTMnetiQ15835.
PhosphoSitePlusiQ15835.

Expressioni

Tissue specificityi

Retinal-specific. Expressed in rods and cones cells.1 Publication

Gene expression databases

BgeeiENSG00000185974.
CleanExiHS_GRK1.
GenevisibleiQ15835. HS.

Interactioni

Subunit structurei

Interacts (when prenylated) with PDE6D; this promotes release from membranes.By similarity

Protein-protein interaction databases

BioGridi111943. 8 interactors.
IntActiQ15835. 1 interactor.
STRINGi9606.ENSP00000334876.

Chemistry databases

BindingDBiQ15835.

Structurei

Secondary structure

1563
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 14Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5AFPX-ray2.30C/D1-25[»]
ProteinModelPortaliQ15835.
SMRiQ15835.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini58 – 175RGSPROSITE-ProRule annotationAdd BLAST118
Domaini190 – 455Protein kinasePROSITE-ProRule annotationAdd BLAST266
Domaini456 – 521AGC-kinase C-terminalAdd BLAST66

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 189N-terminalAdd BLAST189
Regioni456 – 563C-terminalAdd BLAST108

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 RGS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0986. Eukaryota.
ENOG410YRQZ. LUCA.
GeneTreeiENSGT00860000133699.
HOGENOMiHOG000006742.
HOVERGENiHBG004532.
InParanoidiQ15835.
KOiK00909.
OMAiKSGMCLV.
OrthoDBiEOG091G062G.
PhylomeDBiQ15835.
TreeFamiTF313940.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR000239. GPCR_kinase.
IPR032965. GRK1.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016137. RGS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24355:SF11. PTHR24355:SF11. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSiPR00717. GPCRKINASE.
SMARTiSM00315. RGS. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q15835-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDFGSLETVV ANSAFIAARG SFDGSSSQPS RDKKYLAKLK LPPLSKCESL
60 70 80 90 100
RDSLSLEFES VCLEQPIGKK LFQQFLQSAE KHLPALELWK DIEDYDTADN
110 120 130 140 150
DLQPQKAQTI LAQYLDPQAK LFCSFLDEGI VAKFKEGPVE IQDGLFQPLL
160 170 180 190 200
QATLAHLGQA PFQEYLGSLY FLRFLQWKWL EAQPMGEDWF LDFRVLGKGG
210 220 230 240 250
FGEVSACQMK ATGKLYACKK LNKKRLKKRK GYQGAMVEKK ILMKVHSRFI
260 270 280 290 300
VSLAYAFETK ADLCLVMTIM NGGDIRYHIY NVNEENPGFP EPRALFYTAQ
310 320 330 340 350
IICGLEHLHQ RRIVYRDLKP ENVLLDNDGN VRISDLGLAV ELLDGQSKTK
360 370 380 390 400
GYAGTPGFMA PELLQGEEYD FSVDYFALGV TLYEMIAARG PFRARGEKVE
410 420 430 440 450
NKELKHRIIS EPVKYPDKFS QASKDFCEAL LEKDPEKRLG FRDETCDKLR
460 470 480 490 500
AHPLFKDLNW RQLEAGMLMP PFIPDSKTVY AKDIQDVGAF STVKGVAFDK
510 520 530 540 550
TDTEFFQEFA TGNCPIPWQE EMIETGIFGE LNVWRSDGQM PDDMKGISGG
560
SSSSSKSGMC LVS
Length:563
Mass (Da):63,526
Last modified:November 1, 1996 - v1
Checksum:i1244DCB97D40F53D
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_008283136E → Q.1 PublicationCorresponds to variant rs542688076dbSNPEnsembl.1
Natural variantiVAR_008284298T → M.1 PublicationCorresponds to variant rs572803634dbSNPEnsembl.1
Natural variantiVAR_008285330N → S.1 PublicationCorresponds to variant rs375409897dbSNPEnsembl.1
Natural variantiVAR_006215380V → D in CSNBO2. 1 PublicationCorresponds to variant rs777094000dbSNPEnsembl.1
Natural variantiVAR_037904391P → H in CSNBO2. 1 PublicationCorresponds to variant rs570621429dbSNPEnsembl.1
Natural variantiVAR_008286438R → H.1 PublicationCorresponds to variant rs750619057dbSNPEnsembl.1
Natural variantiVAR_008287514C → S.1 PublicationCorresponds to variant rs771561763dbSNPEnsembl.1
Natural variantiVAR_008288522M → T.1 PublicationCorresponds to variant rs779749742dbSNPEnsembl.1
Natural variantiVAR_008289536S → L.1 PublicationCorresponds to variant rs553969577dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63973 mRNA. Translation: AAB05929.1.
L77503 mRNA. Translation: AAG50439.1.
L77502
, L77496, L77497, L77498, L77499, L77500, L77501 Genomic DNA. Translation: AAT00534.2.
AC187648 Genomic DNA. No translation available.
AK289912 mRNA. Translation: BAF82601.1.
CCDSiCCDS81785.1.
RefSeqiNP_002920.1. NM_002929.2.
UniGeneiHs.103501.
Hs.721727.

Genome annotation databases

EnsembliENST00000335678; ENSP00000334876; ENSG00000185974.
GeneIDi6011.
KEGGihsa:6011.
UCSCiuc010tkf.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Mutations of the RHOK gene

Retina International's Scientific Newsletter

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63973 mRNA. Translation: AAB05929.1.
L77503 mRNA. Translation: AAG50439.1.
L77502
, L77496, L77497, L77498, L77499, L77500, L77501 Genomic DNA. Translation: AAT00534.2.
AC187648 Genomic DNA. No translation available.
AK289912 mRNA. Translation: BAF82601.1.
CCDSiCCDS81785.1.
RefSeqiNP_002920.1. NM_002929.2.
UniGeneiHs.103501.
Hs.721727.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5AFPX-ray2.30C/D1-25[»]
ProteinModelPortaliQ15835.
SMRiQ15835.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111943. 8 interactors.
IntActiQ15835. 1 interactor.
STRINGi9606.ENSP00000334876.

Chemistry databases

BindingDBiQ15835.
ChEMBLiCHEMBL5607.
GuidetoPHARMACOLOGYi1465.

PTM databases

iPTMnetiQ15835.
PhosphoSitePlusiQ15835.

Polymorphism and mutation databases

BioMutaiGRK1.
DMDMi2833269.

Proteomic databases

EPDiQ15835.
MaxQBiQ15835.
PaxDbiQ15835.
PeptideAtlasiQ15835.
PRIDEiQ15835.

Protocols and materials databases

DNASUi6011.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000335678; ENSP00000334876; ENSG00000185974.
GeneIDi6011.
KEGGihsa:6011.
UCSCiuc010tkf.3. human.

Organism-specific databases

CTDi6011.
DisGeNETi6011.
GeneCardsiGRK1.
HGNCiHGNC:10013. GRK1.
MalaCardsiGRK1.
MIMi180381. gene.
613411. phenotype.
neXtProtiNX_Q15835.
OpenTargetsiENSG00000185974.
Orphaneti215. Congenital stationary night blindness.
75382. Oguchi disease.
PharmGKBiPA34391.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0986. Eukaryota.
ENOG410YRQZ. LUCA.
GeneTreeiENSGT00860000133699.
HOGENOMiHOG000006742.
HOVERGENiHBG004532.
InParanoidiQ15835.
KOiK00909.
OMAiKSGMCLV.
OrthoDBiEOG091G062G.
PhylomeDBiQ15835.
TreeFamiTF313940.

Enzyme and pathway databases

BioCyciZFISH:HS00048-MONOMER.
BRENDAi2.7.11.14. 2681.
ReactomeiR-HSA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
SignaLinkiQ15835.
SIGNORiQ15835.

Miscellaneous databases

GenomeRNAii6011.
PROiQ15835.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000185974.
CleanExiHS_GRK1.
GenevisibleiQ15835. HS.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR000239. GPCR_kinase.
IPR032965. GRK1.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016137. RGS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24355:SF11. PTHR24355:SF11. 1 hit.
PfamiPF00069. Pkinase. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSiPR00717. GPCRKINASE.
SMARTiSM00315. RGS. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF48097. SSF48097. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50132. RGS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRK_HUMAN
AccessioniPrimary (citable) accession number: Q15835
Secondary accession number(s): Q53X14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 169 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.