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Protein

Beta-adrenergic receptor kinase 2

Gene

ADRBK2

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

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei220 – 2201ATPPROSITE-ProRule annotation
Active sitei317 – 3171Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi197 – 2059ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • receptor internalization Source: UniProtKB
  • signal transduction Source: ProtInc
  • termination of G-protein coupled receptor signaling pathway Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.15. 2681.
SignaLinkiP35626.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-adrenergic receptor kinase 2 (EC:2.7.11.15)
Short name:
Beta-ARK-2
Alternative name(s):
G-protein-coupled receptor kinase 3
Gene namesi
Name:ADRBK2
Synonyms:BARK2, GRK3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:290. ADRBK2.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA41.

Chemistry

DrugBankiDB00171. Adenosine triphosphate.

Polymorphism and mutation databases

BioMutaiADRBK2.
DMDMi116241253.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 688688Beta-adrenergic receptor kinase 2PRO_0000085632Add
BLAST

Post-translational modificationi

Ubiquitinated.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiP35626.
PaxDbiP35626.
PRIDEiP35626.

PTM databases

PhosphoSiteiP35626.

Expressioni

Gene expression databases

BgeeiP35626.
CleanExiHS_ADRBK2.
ExpressionAtlasiP35626. baseline and differential.
GenevisibleiP35626. HS.

Organism-specific databases

HPAiHPA000804.

Interactioni

Protein-protein interaction databases

BioGridi106666. 6 interactions.
IntActiP35626. 4 interactions.
STRINGi9606.ENSP00000317578.

Structurei

3D structure databases

ProteinModelPortaliP35626.
SMRiP35626. Positions 30-668.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 175122RGSPROSITE-ProRule annotationAdd
BLAST
Domaini191 – 453263Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini454 – 52168AGC-kinase C-terminalAdd
BLAST
Domaini558 – 65295PHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 190190N-terminalAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00770000120493.
HOGENOMiHOG000006742.
HOVERGENiHBG050559.
InParanoidiP35626.
KOiK00910.
OMAiDHVQTHL.
OrthoDBiEOG7FV3PP.
PhylomeDBiP35626.
TreeFamiTF313940.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR000239. GPCR_kinase.
IPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_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]
PfamiPF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSiPR00717. GPCRKINASE.
SMARTiSM00233. PH. 1 hit.
SM00315. 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.
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]

Sequencei

Sequence statusi: Complete.

P35626-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADLEAVLAD VSYLMAMEKS KATPAARASK RIVLPEPSIR SVMQKYLAER
60 70 80 90 100
NEITFDKIFN QKIGFLLFKD FCLNEINEAV PQVKFYEEIK EYEKLDNEED
110 120 130 140 150
RLCRSRQIYD AYIMKELLSC SHPFSKQAVE HVQSHLSKKQ VTSTLFQPYI
160 170 180 190 200
EEICESLRGD IFQKFMESDK FTRFCQWKNV ELNIHLTMNE FSVHRIIGRG
210 220 230 240 250
GFGEVYGCRK ADTGKMYAMK CLDKKRIKMK QGETLALNER IMLSLVSTGD
260 270 280 290 300
CPFIVCMTYA FHTPDKLCFI LDLMNGGDLH YHLSQHGVFS EKEMRFYATE
310 320 330 340 350
IILGLEHMHN RFVVYRDLKP ANILLDEHGH ARISDLGLAC DFSKKKPHAS
360 370 380 390 400
VGTHGYMAPE VLQKGTAYDS SADWFSLGCM LFKLLRGHSP FRQHKTKDKH
410 420 430 440 450
EIDRMTLTVN VELPDTFSPE LKSLLEGLLQ RDVSKRLGCH GGGSQEVKEH
460 470 480 490 500
SFFKGVDWQH VYLQKYPPPL IPPRGEVNAA DAFDIGSFDE EDTKGIKLLD
510 520 530 540 550
CDQELYKNFP LVISERWQQE VTETVYEAVN ADTDKIEARK RAKNKQLGHE
560 570 580 590 600
EDYALGKDCI MHGYMLKLGN PFLTQWQRRY FYLFPNRLEW RGEGESRQNL
610 620 630 640 650
LTMEQILSVE ETQIKDKKCI LFRIKGGKQF VLQCESDPEF VQWKKELNET
660 670 680
FKEAQRLLRR APKFLNKPRS GTVELPKPSL CHRNSNGL
Length:688
Mass (Da):79,710
Last modified:October 17, 2006 - v2
Checksum:i50844236A01C1423
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti308 – 3081M → V in CAA48870 (PubMed:8427589).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti50 – 501R → S.1 Publication
Corresponds to variant rs55700971 [ dbSNP | Ensembl ].
VAR_040380
Natural varianti60 – 601N → S.1 Publication
Corresponds to variant rs55740593 [ dbSNP | Ensembl ].
VAR_040381
Natural varianti104 – 1041R → K in a lung bronchoalveolar carcinoma sample; somatic mutation. 1 Publication
VAR_040382
Natural varianti409 – 4091V → M.
Corresponds to variant rs2272859 [ dbSNP | Ensembl ].
VAR_028005

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69117 mRNA. Translation: CAA48870.1.
AL022329 Genomic DNA. Translation: CAB45657.1.
CCDSiCCDS13832.1.
PIRiJC1469.
RefSeqiNP_005151.2. NM_005160.3.
UniGeneiHs.657494.

Genome annotation databases

EnsembliENST00000324198; ENSP00000317578; ENSG00000100077.
GeneIDi157.
KEGGihsa:157.
UCSCiuc003abw.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69117 mRNA. Translation: CAA48870.1.
AL022329 Genomic DNA. Translation: CAB45657.1.
CCDSiCCDS13832.1.
PIRiJC1469.
RefSeqiNP_005151.2. NM_005160.3.
UniGeneiHs.657494.

3D structure databases

ProteinModelPortaliP35626.
SMRiP35626. Positions 30-668.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106666. 6 interactions.
IntActiP35626. 4 interactions.
STRINGi9606.ENSP00000317578.

Chemistry

BindingDBiP35626.
ChEMBLiCHEMBL1075166.
DrugBankiDB00171. Adenosine triphosphate.
GuidetoPHARMACOLOGYi1467.

PTM databases

PhosphoSiteiP35626.

Polymorphism and mutation databases

BioMutaiADRBK2.
DMDMi116241253.

Proteomic databases

MaxQBiP35626.
PaxDbiP35626.
PRIDEiP35626.

Protocols and materials databases

DNASUi157.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000324198; ENSP00000317578; ENSG00000100077.
GeneIDi157.
KEGGihsa:157.
UCSCiuc003abw.2. human.

Organism-specific databases

CTDi157.
GeneCardsiGC22P025960.
H-InvDBHIX0041309.
HGNCiHGNC:290. ADRBK2.
HPAiHPA000804.
MIMi109636. gene.
neXtProtiNX_P35626.
PharmGKBiPA41.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00770000120493.
HOGENOMiHOG000006742.
HOVERGENiHBG050559.
InParanoidiP35626.
KOiK00910.
OMAiDHVQTHL.
OrthoDBiEOG7FV3PP.
PhylomeDBiP35626.
TreeFamiTF313940.

Enzyme and pathway databases

BRENDAi2.7.11.15. 2681.
SignaLinkiP35626.

Miscellaneous databases

ChiTaRSiADRBK2. human.
GeneWikiiBeta_adrenergic_receptor_kinase-2.
GenomeRNAii157.
NextBioi625.
PROiP35626.
SOURCEiSearch...

Gene expression databases

BgeeiP35626.
CleanExiHS_ADRBK2.
ExpressionAtlasiP35626. baseline and differential.
GenevisibleiP35626. HS.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR000239. GPCR_kinase.
IPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_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]
PfamiPF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00615. RGS. 1 hit.
[Graphical view]
PRINTSiPR00717. GPCRKINASE.
SMARTiSM00233. PH. 1 hit.
SM00315. 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.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Development and validation of a method for profiling post-translational modification activities using protein microarrays."
    Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B., Spruck C.
    PLoS ONE 5:E11332-E11332(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  4. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-50; SER-60 AND LYS-104.

Entry informationi

Entry nameiARBK2_HUMAN
AccessioniPrimary (citable) accession number: P35626
Secondary accession number(s): Q9UGW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: October 17, 2006
Last modified: June 24, 2015
This is version 152 of the entry and version 2 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 22
    Human chromosome 22: 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

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.