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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei219 – 2191ATPPROSITE-ProRule annotation
Active sitei317 – 3171Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi196 – 2049ATPPROSITE-ProRule annotation

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

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

BRENDAi2.7.11.14. 2681.
ReactomeiREACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.
SignaLinkiQ15835.

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 1
Gene namesi
Name:GRK1
Synonyms:RHOK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti380 – 3801V → D in CSNBO2. 1 Publication
VAR_006215
Natural varianti391 – 3911P → H in CSNBO2. 1 Publication
VAR_037904

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi21 – 211S → E: Not phosphorylated by PKA. 1 Publication
Mutagenesisi219 – 2191K → A: Loss of autophosphorylation and RHO phosphorylation. 1 Publication

Keywords - Diseasei

Congenital stationary night blindness, Disease mutation

Organism-specific databases

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

Polymorphism and mutation databases

BioMutaiGRK1.
DMDMi2833269.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 560560Rhodopsin kinasePRO_0000024375Add
BLAST
Propeptidei561 – 5633Removed in mature formBy similarityPRO_0000024376

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51PhosphoserineBy similarity
Modified residuei8 – 81PhosphothreonineBy similarity
Modified residuei21 – 211Phosphoserine; by PKA and autocatalysis1 Publication
Modified residuei491 – 4911Phosphoserine; by autocatalysisBy similarity
Modified residuei492 – 4921Phosphothreonine; by autocatalysisBy similarity
Modified residuei560 – 5601Cysteine methyl esterBy similarity
Lipidationi560 – 5601S-farnesyl cysteineBy similarity

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

PaxDbiQ15835.
PRIDEiQ15835.

PTM databases

PhosphoSiteiQ15835.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ15835.
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 interactions.
IntActiQ15835. 1 interaction.
STRINGi9606.ENSP00000334876.

Structurei

Secondary structure

1
563
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 148Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5AFPX-ray2.30C/D1-25[»]
ProteinModelPortaliQ15835.
SMRiQ15835. Positions 30-535.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 175118RGSPROSITE-ProRule annotationAdd
BLAST
Domaini190 – 455266Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini456 – 52166AGC-kinase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 189189N-terminalAdd
BLAST
Regioni456 – 563108C-terminalAdd
BLAST

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

eggNOGiCOG0515.
GeneTreeiENSGT00770000120493.
HOGENOMiHOG000006742.
HOVERGENiHBG004532.
InParanoidiQ15835.
KOiK00909.
OMAiFRDGTCD.
OrthoDBiEOG7TF78J.
PhylomeDBiQ15835.
TreeFamiTF313940.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR000239. GPCR_kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016137. RGS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti136 – 1361E → Q.1 Publication
VAR_008283
Natural varianti298 – 2981T → M.1 Publication
VAR_008284
Natural varianti330 – 3301N → S.1 Publication
VAR_008285
Natural varianti380 – 3801V → D in CSNBO2. 1 Publication
VAR_006215
Natural varianti391 – 3911P → H in CSNBO2. 1 Publication
VAR_037904
Natural varianti438 – 4381R → H.1 Publication
VAR_008286
Natural varianti514 – 5141C → S.1 Publication
VAR_008287
Natural varianti522 – 5221M → T.1 Publication
VAR_008288
Natural varianti536 – 5361S → L.1 Publication
VAR_008289

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.
RefSeqiNP_002920.1. NM_002929.2.
UniGeneiHs.103501.
Hs.721727.

Genome annotation databases

EnsembliENST00000335678; ENSP00000334876; ENSG00000185974.
GeneIDi6011.
KEGGihsa:6011.
UCSCiuc010tkf.2. 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.
RefSeqiNP_002920.1. NM_002929.2.
UniGeneiHs.103501.
Hs.721727.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5AFPX-ray2.30C/D1-25[»]
ProteinModelPortaliQ15835.
SMRiQ15835. Positions 30-535.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111943. 8 interactions.
IntActiQ15835. 1 interaction.
STRINGi9606.ENSP00000334876.

Chemistry

BindingDBiQ15835.
ChEMBLiCHEMBL5607.
GuidetoPHARMACOLOGYi1465.

PTM databases

PhosphoSiteiQ15835.

Polymorphism and mutation databases

BioMutaiGRK1.
DMDMi2833269.

Proteomic databases

PaxDbiQ15835.
PRIDEiQ15835.

Protocols and materials databases

DNASUi6011.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000335678; ENSP00000334876; ENSG00000185974.
GeneIDi6011.
KEGGihsa:6011.
UCSCiuc010tkf.2. human.

Organism-specific databases

CTDi6011.
GeneCardsiGC13P114321.
HGNCiHGNC:10013. GRK1.
MIMi180381. gene.
613411. phenotype.
neXtProtiNX_Q15835.
Orphaneti215. Congenital stationary night blindness.
75382. Oguchi disease.
PharmGKBiPA34391.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00770000120493.
HOGENOMiHOG000006742.
HOVERGENiHBG004532.
InParanoidiQ15835.
KOiK00909.
OMAiFRDGTCD.
OrthoDBiEOG7TF78J.
PhylomeDBiQ15835.
TreeFamiTF313940.

Enzyme and pathway databases

BRENDAi2.7.11.14. 2681.
ReactomeiREACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.
SignaLinkiQ15835.

Miscellaneous databases

GenomeRNAii6011.
NextBioi23453.
PROiQ15835.
SOURCEiSearch...

Gene expression databases

BgeeiQ15835.
CleanExiHS_GRK1.
GenevisibleiQ15835. HS.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR000239. GPCR_kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016137. RGS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
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...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and localization of rhodopsin kinase in the mammalian pineal."
    Zhao X., Haeseleer F., Fariss R.N., Huang J., Baehr W., Milam A.H., Palczewski K.
    Vis. Neurosci. 14:225-232(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  2. "Characterization and chromosomal localization of the gene for human rhodopsin kinase."
    Khani S.C., Abitbol M., Yamamoto S., Maravic-Magovcevic I., Dryja T.P.
    Genomics 35:571-576(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Corpus callosum.
  4. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Species-specific differences in expression of G-protein-coupled receptor kinase (GRK) 7 and GRK1 in mammalian cone photoreceptor cells: implications for cone cell phototransduction."
    Weiss E.R., Ducceschi M.H., Horner T.J., Li A., Craft C.M., Osawa S.
    J. Neurosci. 21:9175-9184(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "Phosphorylation of GRK1 and GRK7 by cAMP-dependent protein kinase attenuates their enzymatic activities."
    Horner T.J., Osawa S., Schaller M.D., Weiss E.R.
    J. Biol. Chem. 280:28241-28250(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, FUNCTION IN PHOSPHORYLATION OF RHO, PHOSPHORYLATION AT SER-21, ENZYME REGULATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF SER-21 AND LYS-219.
  7. "Evaluation of the rhodopsin kinase gene in patients with retinitis pigmentosa."
    Yamamoto S., Khani S.C., Berson E.L., Dryja T.P.
    Exp. Eye Res. 65:249-253(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GLN-136; MET-298; SER-330; HIS-438; SER-514; THR-522 AND LEU-536.
  8. "Defects in the rhodopsin kinase gene in the Oguchi form of stationary night blindness."
    Yamamoto S., Sippel K.C., Berson E.L., Dryja T.P.
    Nat. Genet. 15:175-178(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CSNBO2 ASP-380.
  9. "A novel homozygous GRK1 mutation (P391H) in 2 siblings with Oguchi disease with markedly reduced cone responses."
    Hayashi T., Gekka T., Takeuchi T., Goto-Omoto S., Kitahara K.
    Ophthalmology 114:134-141(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CSNBO2 HIS-391.

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: June 24, 2015
This is version 155 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

External Data

Dasty 3

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 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.