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Q15835

- RK_HUMAN

UniProt

Q15835 - RK_HUMAN

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Protein

Rhodopsin kinase

Gene
GRK1, RHOK
Organism
Homo sapiens (Human)
Status
Reviewed - 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 By similarity.1 Publication

Kineticsi

  1. KM=3.5 µM for rhodopsin1 Publication
  2. KM=10.6 µM for ATP

Vmax=1132 nmol/min/mg enzyme

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei219 – 2191ATP By similarity
Active sitei317 – 3171Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi196 – 2049ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. G-protein coupled receptor kinase activity Source: InterPro
  3. protein kinase activity Source: ProtInc
  4. rhodopsin kinase activity Source: UniProtKB

GO - Biological processi

  1. negative regulation of apoptotic process Source: Ensembl
  2. photoreceptor cell morphogenesis Source: Ensembl
  3. phototransduction, visible light Source: Reactome
  4. positive regulation of phosphorylation Source: Ensembl
  5. post-embryonic retina morphogenesis in camera-type eye Source: Ensembl
  6. protein autophosphorylation Source: UniProtKB
  7. regulation of G-protein coupled receptor protein signaling pathway Source: ProtInc
  8. regulation of rhodopsin mediated signaling pathway Source: UniProtKB
  9. rhodopsin mediated signaling pathway Source: Reactome
  10. termination of G-protein coupled receptor signaling pathway Source: InterPro
  11. 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

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:2.7.11.14)
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: Chromosome 13

Organism-specific databases

HGNCiHGNC:10013. GRK1.

Subcellular locationi

GO - Cellular componenti

  1. photoreceptor disc membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Night blindness, congenital stationary, Oguchi type 2 (CSNBO2) [MIM:613411]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51Phosphoserine By similarity
Modified residuei8 – 81Phosphothreonine By similarity
Modified residuei21 – 211Phosphoserine; by PKA and autocatalysis1 Publication
Modified residuei491 – 4911Phosphoserine; by autocatalysis By similarity
Modified residuei492 – 4921Phosphothreonine; by autocatalysis By similarity
Modified residuei560 – 5601Cysteine methyl ester By similarity
Lipidationi560 – 5601S-farnesyl cysteine By 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.1 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

ArrayExpressiQ15835.
BgeeiQ15835.
CleanExiHS_GRK1.
GenevestigatoriQ15835.

Interactioni

Protein-protein interaction databases

BioGridi111943. 7 interactions.
STRINGi9606.ENSP00000334876.

Structurei

3D structure databases

ProteinModelPortaliQ15835.
SMRiQ15835. Positions 30-535.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 175118RGSAdd
BLAST
Domaini190 – 455266Protein kinaseAdd
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 RGS domain.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000006742.
HOVERGENiHBG004532.
InParanoidiQ15835.
KOiK00909.
OMAiMPDDMKG.
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. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
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

MDFGSLETVV ANSAFIAARG SFDGSSSQPS RDKKYLAKLK LPPLSKCESL    50
RDSLSLEFES VCLEQPIGKK LFQQFLQSAE KHLPALELWK DIEDYDTADN 100
DLQPQKAQTI LAQYLDPQAK LFCSFLDEGI VAKFKEGPVE IQDGLFQPLL 150
QATLAHLGQA PFQEYLGSLY FLRFLQWKWL EAQPMGEDWF LDFRVLGKGG 200
FGEVSACQMK ATGKLYACKK LNKKRLKKRK GYQGAMVEKK ILMKVHSRFI 250
VSLAYAFETK ADLCLVMTIM NGGDIRYHIY NVNEENPGFP EPRALFYTAQ 300
IICGLEHLHQ RRIVYRDLKP ENVLLDNDGN VRISDLGLAV ELLDGQSKTK 350
GYAGTPGFMA PELLQGEEYD FSVDYFALGV TLYEMIAARG PFRARGEKVE 400
NKELKHRIIS EPVKYPDKFS QASKDFCEAL LEKDPEKRLG FRDETCDKLR 450
AHPLFKDLNW RQLEAGMLMP PFIPDSKTVY AKDIQDVGAF STVKGVAFDK 500
TDTEFFQEFA TGNCPIPWQE EMIETGIFGE LNVWRSDGQM PDDMKGISGG 550
SSSSSKSGMC LVS 563
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:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi2833269.

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:
EMBL
GenBank
DDBJ
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 .
RefSeqi NP_002920.1. NM_002929.2.
UniGenei Hs.103501.
Hs.721727.

3D structure databases

ProteinModelPortali Q15835.
SMRi Q15835. Positions 30-535.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111943. 7 interactions.
STRINGi 9606.ENSP00000334876.

Chemistry

BindingDBi Q15835.
ChEMBLi CHEMBL5607.
GuidetoPHARMACOLOGYi 1465.

PTM databases

PhosphoSitei Q15835.

Polymorphism databases

DMDMi 2833269.

Proteomic databases

PaxDbi Q15835.
PRIDEi Q15835.

Protocols and materials databases

DNASUi 6011.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000335678 ; ENSP00000334876 ; ENSG00000185974 .
GeneIDi 6011.
KEGGi hsa:6011.
UCSCi uc010tkf.2. human.

Organism-specific databases

CTDi 6011.
GeneCardsi GC13P114321.
HGNCi HGNC:10013. GRK1.
MIMi 180381. gene.
613411. phenotype.
neXtProti NX_Q15835.
Orphaneti 215. Congenital stationary night blindness.
75382. Oguchi disease.
PharmGKBi PA34391.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000006742.
HOVERGENi HBG004532.
InParanoidi Q15835.
KOi K00909.
OMAi MPDDMKG.
OrthoDBi EOG7TF78J.
PhylomeDBi Q15835.
TreeFami TF313940.

Enzyme and pathway databases

BRENDAi 2.7.11.14. 2681.
Reactomei REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.
SignaLinki Q15835.

Miscellaneous databases

GenomeRNAii 6011.
NextBioi 23453.
PROi Q15835.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q15835.
Bgeei Q15835.
CleanExi HS_GRK1.
Genevestigatori Q15835.

Family and domain databases

InterProi IPR000961. AGC-kinase_C.
IPR000239. GPCR_kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016137. Regulat_G_prot_signal_superfam.
IPR000342. RGS_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view ]
PRINTSi PR00717. GPCRKINASE.
SMARTi SM00315. RGS. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF48097. SSF48097. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS51285. 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 ]
ProtoNeti Search...

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: September 3, 2014
This is version 146 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

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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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