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P35626

- ARBK2_HUMAN

UniProt

P35626 - ARBK2_HUMAN

Protein

Beta-adrenergic receptor kinase 2

Gene

ADRBK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    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

    1. ATP binding Source: UniProtKB-KW
    2. beta-adrenergic receptor kinase activity Source: UniProtKB-EC
    3. G-protein coupled receptor kinase activity Source: Ensembl
    4. protein kinase activity Source: ProtInc

    GO - Biological processi

    1. receptor internalization Source: UniProtKB
    2. signal transduction Source: ProtInc
    3. termination of G-protein coupled receptor signaling pathway Source: InterPro

    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: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:290. ADRBK2.

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA41.

    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

    ArrayExpressiP35626.
    BgeeiP35626.
    CleanExiHS_ADRBK2.
    GenevestigatoriP35626.

    Organism-specific databases

    HPAiHPA000804.

    Interactioni

    Protein-protein interaction databases

    BioGridi106666. 6 interactions.
    IntActiP35626. 3 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.
    HOGENOMiHOG000006742.
    HOVERGENiHBG050559.
    InParanoidiP35626.
    KOiK00910.
    OMAiQTHLAKK.
    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. Regulat_G_prot_signal_superfam.
    IPR000342. RGS_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    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

    MADLEAVLAD VSYLMAMEKS KATPAARASK RIVLPEPSIR SVMQKYLAER    50
    NEITFDKIFN QKIGFLLFKD FCLNEINEAV PQVKFYEEIK EYEKLDNEED 100
    RLCRSRQIYD AYIMKELLSC SHPFSKQAVE HVQSHLSKKQ VTSTLFQPYI 150
    EEICESLRGD IFQKFMESDK FTRFCQWKNV ELNIHLTMNE FSVHRIIGRG 200
    GFGEVYGCRK ADTGKMYAMK CLDKKRIKMK QGETLALNER IMLSLVSTGD 250
    CPFIVCMTYA FHTPDKLCFI LDLMNGGDLH YHLSQHGVFS EKEMRFYATE 300
    IILGLEHMHN RFVVYRDLKP ANILLDEHGH ARISDLGLAC DFSKKKPHAS 350
    VGTHGYMAPE VLQKGTAYDS SADWFSLGCM LFKLLRGHSP FRQHKTKDKH 400
    EIDRMTLTVN VELPDTFSPE LKSLLEGLLQ RDVSKRLGCH GGGSQEVKEH 450
    SFFKGVDWQH VYLQKYPPPL IPPRGEVNAA DAFDIGSFDE EDTKGIKLLD 500
    CDQELYKNFP LVISERWQQE VTETVYEAVN ADTDKIEARK RAKNKQLGHE 550
    EDYALGKDCI MHGYMLKLGN PFLTQWQRRY FYLFPNRLEW RGEGESRQNL 600
    LTMEQILSVE ETQIKDKKCI LFRIKGGKQF VLQCESDPEF VQWKKELNET 650
    FKEAQRLLRR APKFLNKPRS GTVELPKPSL CHRNSNGL 688
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi116241253.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X69117 mRNA. Translation: CAA48870.1 .
    AL022329 Genomic DNA. Translation: CAB45657.1 .
    CCDSi CCDS13832.1.
    PIRi JC1469.
    RefSeqi NP_005151.2. NM_005160.3.
    UniGenei Hs.657494.

    3D structure databases

    ProteinModelPortali P35626.
    SMRi P35626. Positions 30-668.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106666. 6 interactions.
    IntActi P35626. 3 interactions.
    STRINGi 9606.ENSP00000317578.

    Chemistry

    BindingDBi P35626.
    ChEMBLi CHEMBL1075166.
    DrugBanki DB00171. Adenosine triphosphate.
    GuidetoPHARMACOLOGYi 1467.

    PTM databases

    PhosphoSitei P35626.

    Polymorphism databases

    DMDMi 116241253.

    Proteomic databases

    MaxQBi P35626.
    PaxDbi P35626.
    PRIDEi P35626.

    Protocols and materials databases

    DNASUi 157.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000324198 ; ENSP00000317578 ; ENSG00000100077 .
    GeneIDi 157.
    KEGGi hsa:157.
    UCSCi uc003abw.2. human.

    Organism-specific databases

    CTDi 157.
    GeneCardsi GC22P025960.
    H-InvDB HIX0041309.
    HGNCi HGNC:290. ADRBK2.
    HPAi HPA000804.
    MIMi 109636. gene.
    neXtProti NX_P35626.
    PharmGKBi PA41.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000006742.
    HOVERGENi HBG050559.
    InParanoidi P35626.
    KOi K00910.
    OMAi QTHLAKK.
    OrthoDBi EOG7FV3PP.
    PhylomeDBi P35626.
    TreeFami TF313940.

    Enzyme and pathway databases

    BRENDAi 2.7.11.15. 2681.
    SignaLinki P35626.

    Miscellaneous databases

    GeneWikii Beta_adrenergic_receptor_kinase-2.
    GenomeRNAii 157.
    NextBioi 625.
    PROi P35626.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35626.
    Bgeei P35626.
    CleanExi HS_ADRBK2.
    Genevestigatori P35626.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR000961. 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. Regulat_G_prot_signal_superfam.
    IPR000342. RGS_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00169. PH. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00615. RGS. 1 hit.
    [Graphical view ]
    PRINTSi PR00717. GPCRKINASE.
    SMARTi SM00233. PH. 1 hit.
    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.
    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 ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 147 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