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Reviewed, UniProtKB/Swiss-Prot P35626 (ARBK2_HUMAN)

Last modified July 22, 2008. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Beta-adrenergic receptor kinase 2
      Short name=Beta-ARK-2
    EC=2.7.11.15
Alternative name(s):
    G-protein-coupled receptor kinase 3
Gene names
Name: ADRBK2
Synonyms: BARK2, GRK3
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length688 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors.

Catalytic activity

ATP + [beta-adrenergic receptor] = ADP + [beta-adrenergic receptor] phosphate.

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. GPRK subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 PH domain.

Contains 1 protein kinase domain.

Contains 1 RGS domain.

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Ontologies

Keywords

   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase

Gene Ontology (GO)

   Biological processsignal transduction Ref.1

Traceable author statement. Source: ProtInc

   Molecular functionprotein kinase activity Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 688688Beta-adrenergic receptor kinase 2

Regions

Domain54 – 175122RGS
Domain191 – 453263Protein kinase
Domain454 – 52168AGC-kinase C-terminal
Domain558 – 65295PH
Nucleotide binding197 – 2059ATP By similarity
Region1 – 190190N-terminal

Sites

Active site3171Proton acceptor By similarity
Binding site2201ATP By similarity

Natural variations

Natural variant501R → S
Natural variant601N → S
Natural variant1041R → K in a lung bronchoalveolar carcinoma sample; somatic mutation.
Natural variant4091V → M: dbSNP rs2272859.

Experimental info

Sequence conflict3081M → V in CAA48870. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P35626-1 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 50844236A01C1423

FASTA68879,710
        10         20         30         40         50         60 
MADLEAVLAD VSYLMAMEKS KATPAARASK RIVLPEPSIR SVMQKYLAER NEITFDKIFN 

        70         80         90        100        110        120 
QKIGFLLFKD FCLNEINEAV PQVKFYEEIK EYEKLDNEED RLCRSRQIYD AYIMKELLSC 

       130        140        150        160        170        180 
SHPFSKQAVE HVQSHLSKKQ VTSTLFQPYI EEICESLRGD IFQKFMESDK FTRFCQWKNV 

       190        200        210        220        230        240 
ELNIHLTMNE FSVHRIIGRG GFGEVYGCRK ADTGKMYAMK CLDKKRIKMK QGETLALNER 

       250        260        270        280        290        300 
IMLSLVSTGD CPFIVCMTYA FHTPDKLCFI LDLMNGGDLH YHLSQHGVFS EKEMRFYATE 

       310        320        330        340        350        360 
IILGLEHMHN RFVVYRDLKP ANILLDEHGH ARISDLGLAC DFSKKKPHAS VGTHGYMAPE 

       370        380        390        400        410        420 
VLQKGTAYDS SADWFSLGCM LFKLLRGHSP FRQHKTKDKH EIDRMTLTVN VELPDTFSPE 

       430        440        450        460        470        480 
LKSLLEGLLQ RDVSKRLGCH GGGSQEVKEH SFFKGVDWQH VYLQKYPPPL IPPRGEVNAA 

       490        500        510        520        530        540 
DAFDIGSFDE EDTKGIKLLD CDQELYKNFP LVISERWQQE VTETVYEAVN ADTDKIEARK 

       550        560        570        580        590        600 
RAKNKQLGHE EDYALGKDCI MHGYMLKLGN PFLTQWQRRY FYLFPNRLEW RGEGESRQNL 

       610        620        630        640        650        660 
LTMEQILSVE ETQIKDKKCI LFRIKGGKQF VLQCESDPEF VQWKKELNET FKEAQRLLRR 

       670        680 
APKFLNKPRS GTVELPKPSL CHRNSNGL

« Hide

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References

« Hide 'large scale' references
[1]"Molecular cloning, functional expression and mRNA analysis of human beta-adrenergic receptor kinase 2."
Parruti G., Ambrosini G., Sallese M., de Blasi A.
Biochem. Biophys. Res. Commun. 190:475-481(1993) [PubMed: 8427589] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed: 10591208] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-50; SER-60 AND LYS-104.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X69117 mRNA. Translation: CAA48870.1.
AL022329 Genomic DNA. Translation: CAB45657.1.
PIRJC1469.
RefSeqNP_005151.2.
UniGeneHs.657494

3D structure databases

HSSPHSSP built from PDB template 1OMW based on UniProtKB P21146.
SMRP35626. Positions 29-668.
ModBaseSearch...

PTM databases

PhosphoSiteP35626.

Genome annotation databases

EnsemblENSG00000100077. Homo sapiens. [Contig view]
GeneID157.
KEGGhsa:157.

Organism-specific databases

H-InvDBHIX0016319.
HGNCHGNC:290. ADRBK2.
HPAHPA000804.
MIM109636. gene.
PharmGKBPA41.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMP35626.
HOVERGENP35626.

Gene expression databases

ArrayExpressP35626.
CleanExHS_ADRBK2.
GermOnlineENSG00000100077. Homo sapiens.

Family and domain databases

InterProIPR015743. BARK.
IPR000239. GPCR_kinase.
IPR001849. PH.
IPR011993. PH_type.
IPR000961. Pkinase_C.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_bd_CS.
IPR000342. Regulat_G_prot_signal.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]
Gene3DG3DSA:2.30.29.30. PH_type. 1 hit.
PANTHERPTHR22985:SF5. BARK. 1 hit.
PfamPF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSPR00717. GPCRKINASE.
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00233. PH. 1 hit.
SM00315. RGS. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS50003. PH_DOMAIN. 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]
BLOCKSSearch...

Other Resources

DrugBankDB00171. Adenosine triphosphate.
LinkHubP35626.
SOURCESearch...
ProtoNetSearch...

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Entry information

Entry nameARBK2_HUMAN
AccessionPrimary (citable) accession number: P35626
Secondary accession number(s): Q9UGW9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: October 17, 2006
Last modified: July 22, 2008
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents