Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P25098

- ARBK1_HUMAN

UniProt

P25098 - ARBK1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Beta-adrenergic receptor kinase 1

Gene

ADRBK1

Organism
Homo sapiens (Human)
Status
Reviewed - 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, probably inducing a desensitization of them. Key regulator of LPAR1 signaling. Competes with RALA for binding to LPAR1 thus affecting the signaling properties of the receptor. Desensitizes LPAR1 and LPAR2 in a phosphorylation-independent manner.1 Publication

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. alpha-2A adrenergic receptor binding Source: BHF-UCL
  2. ATP binding Source: UniProtKB-KW
  3. beta-adrenergic receptor kinase activity Source: UniProtKB-EC
  4. Edg-2 lysophosphatidic acid receptor binding Source: UniProtKB
  5. G-protein coupled receptor kinase activity Source: BHF-UCL
  6. protein kinase activity Source: BHF-UCL

GO - Biological processi

  1. activation of phospholipase C activity Source: Reactome
  2. cardiac muscle contraction Source: BHF-UCL
  3. desensitization of G-protein coupled receptor protein signaling pathway Source: BHF-UCL
  4. epidermal growth factor receptor signaling pathway Source: Reactome
  5. fibroblast growth factor receptor signaling pathway Source: Reactome
  6. G-protein coupled acetylcholine receptor signaling pathway Source: BHF-UCL
  7. heart development Source: Ensembl
  8. innate immune response Source: Reactome
  9. negative regulation of striated muscle contraction Source: BHF-UCL
  10. negative regulation of the force of heart contraction by chemical signal Source: BHF-UCL
  11. neurotrophin TRK receptor signaling pathway Source: Reactome
  12. peptidyl-serine phosphorylation Source: BHF-UCL
  13. peptidyl-threonine phosphorylation Source: Ensembl
  14. positive regulation of catecholamine secretion Source: BHF-UCL
  15. receptor internalization Source: UniProtKB
  16. signal transduction Source: Reactome
  17. tachykinin receptor signaling pathway Source: BHF-UCL
  18. 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.
ReactomeiREACT_18283. G alpha (q) signalling events.
REACT_9000. Calmodulin induced events.
SignaLinkiP25098.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-adrenergic receptor kinase 1 (EC:2.7.11.15)
Short name:
Beta-ARK-1
Alternative name(s):
G-protein coupled receptor kinase 2
Gene namesi
Name:ADRBK1
Synonyms:BARK, BARK1, GRK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:289. ADRBK1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. cytosol Source: Reactome
  3. membrane Source: UniProtKB
  4. plasma membrane Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA40.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 689689Beta-adrenergic receptor kinase 1PRO_0000085627Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei670 – 6701Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP25098.
PaxDbiP25098.
PRIDEiP25098.

PTM databases

PhosphoSiteiP25098.

Expressioni

Tissue specificityi

Expressed in peripheral blood leukocytes.1 Publication

Gene expression databases

BgeeiP25098.
CleanExiHS_ADRBK1.
ExpressionAtlasiP25098. baseline and differential.
GenevestigatoriP25098.

Organism-specific databases

HPAiCAB005021.
CAB037248.
HPA048330.

Interactioni

Subunit structurei

Interacts with GIT1 (By similarity). Interacts with, and phosphorylates chemokine-stimulated CCR5. Interacts with ARRB1. Interacts with LPAR1 and LPAR2. Interacts with RALA in response to LPAR1 activation. ADRBK1 and RALA mutually inhibit each other's binding to LPAR1.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FPR1P214623EBI-3904795,EBI-2869495
GIT1Q9Y2X75EBI-3904795,EBI-466061
MDM2Q009874EBI-3904795,EBI-389668
UBCP0CG483EBI-3904795,EBI-3390054

Protein-protein interaction databases

BioGridi106665. 38 interactions.
DIPiDIP-42429N.
IntActiP25098. 15 interactions.
MINTiMINT-1214643.
STRINGi9606.ENSP00000312262.

Structurei

Secondary structure

1
689
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi39 – 4911Combined sources
Helixi55 – 595Combined sources
Helixi62 – 7514Combined sources
Helixi77 – 793Combined sources
Helixi80 – 9314Combined sources
Helixi98 – 10912Combined sources
Helixi112 – 1187Combined sources
Beta strandi119 – 1224Combined sources
Helixi126 – 13712Combined sources
Turni143 – 1464Combined sources
Helixi147 – 15711Combined sources
Helixi160 – 1678Combined sources
Helixi169 – 18113Combined sources
Helixi188 – 1903Combined sources
Beta strandi191 – 1999Combined sources
Beta strandi201 – 21010Combined sources
Turni211 – 2133Combined sources
Beta strandi216 – 2238Combined sources
Helixi224 – 2296Combined sources
Helixi233 – 24614Combined sources
Beta strandi247 – 2493Combined sources
Beta strandi252 – 2543Combined sources
Beta strandi257 – 2626Combined sources
Beta strandi264 – 2718Combined sources
Helixi279 – 2868Combined sources
Helixi291 – 30919Combined sources
Turni310 – 3123Combined sources
Helixi320 – 3223Combined sources
Beta strandi323 – 3253Combined sources
Beta strandi331 – 3333Combined sources
Helixi336 – 3383Combined sources
Beta strandi343 – 3453Combined sources
Helixi354 – 3563Combined sources
Helixi359 – 3624Combined sources
Helixi371 – 38616Combined sources
Helixi393 – 3953Combined sources
Helixi399 – 40810Combined sources
Beta strandi415 – 4173Combined sources
Helixi419 – 42810Combined sources
Helixi433 – 4353Combined sources
Beta strandi440 – 4423Combined sources
Helixi444 – 4474Combined sources
Helixi451 – 4533Combined sources
Helixi458 – 4625Combined sources
Helixi500 – 5034Combined sources
Turni504 – 5085Combined sources
Helixi514 – 5229Combined sources
Turni523 – 5253Combined sources
Helixi526 – 54621Combined sources
Beta strandi555 – 5573Combined sources
Beta strandi561 – 5688Combined sources
Helixi571 – 5733Combined sources
Beta strandi577 – 5848Combined sources
Beta strandi587 – 5915Combined sources
Beta strandi593 – 5953Combined sources
Beta strandi599 – 6024Combined sources
Helixi603 – 6053Combined sources
Beta strandi606 – 61611Combined sources
Beta strandi618 – 6247Combined sources
Turni625 – 6273Combined sources
Beta strandi628 – 6336Combined sources
Helixi637 – 65822Combined sources
Turni662 – 6643Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BAKNMR-A556-670[»]
3CIKX-ray2.75A1-689[»]
3KRWX-ray2.90A2-689[»]
3KRXX-ray3.10A2-689[»]
3V5WX-ray2.07A1-689[»]
4MK0X-ray2.40A30-668[»]
4PNKX-ray2.56A1-689[»]
ProteinModelPortaliP25098.
SMRiP25098. Positions 30-670.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25098.

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.
InParanoidiP25098.
KOiK00910.
OMAiDFCLKHL.
OrthoDBiEOG7FV3PP.
PhylomeDBiP25098.
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.
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.

P25098-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MADLEAVLAD VSYLMAMEKS KATPAARASK KILLPEPSIR SVMQKYLEDR
60 70 80 90 100
GEVTFEKIFS QKLGYLLFRD FCLNHLEEAR PLVEFYEEIK KYEKLETEEE
110 120 130 140 150
RVARSREIFD SYIMKELLAC SHPFSKSATE HVQGHLGKKQ VPPDLFQPYI
160 170 180 190 200
EEICQNLRGD VFQKFIESDK FTRFCQWKNV ELNIHLTMND FSVHRIIGRG
210 220 230 240 250
GFGEVYGCRK ADTGKMYAMK CLDKKRIKMK QGETLALNER IMLSLVSTGD
260 270 280 290 300
CPFIVCMSYA FHTPDKLSFI LDLMNGGDLH YHLSQHGVFS EADMRFYAAE
310 320 330 340 350
IILGLEHMHN RFVVYRDLKP ANILLDEHGH VRISDLGLAC DFSKKKPHAS
360 370 380 390 400
VGTHGYMAPE VLQKGVAYDS SADWFSLGCM LFKLLRGHSP FRQHKTKDKH
410 420 430 440 450
EIDRMTLTMA VELPDSFSPE LRSLLEGLLQ RDVNRRLGCL GRGAQEVKES
460 470 480 490 500
PFFRSLDWQM VFLQKYPPPL IPPRGEVNAA DAFDIGSFDE EDTKGIKLLD
510 520 530 540 550
SDQELYRNFP LTISERWQQE VAETVFDTIN AETDRLEARK KAKNKQLGHE
560 570 580 590 600
EDYALGKDCI MHGYMSKMGN PFLTQWQRRY FYLFPNRLEW RGEGEAPQSL
610 620 630 640 650
LTMEEIQSVE ETQIKERKCL LLKIRGGKQF ILQCDSDPEL VQWKKELRDA
660 670 680
YREAQQLVQR VPKMKNKPRS PVVELSKVPL VQRGSANGL
Length:689
Mass (Da):79,574
Last modified:February 20, 2007 - v2
Checksum:i4DB68F62841AFA7D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti168 – 18518SDKFT…ELNIH → RISSHGFASGRMWSSTST in AAB60689. (PubMed:8195124)CuratedAdd
BLAST
Sequence conflicti211 – 2111A → R in CAA43470. (PubMed:2037065)Curated
Sequence conflicti211 – 2111A → R in AAB60689. (PubMed:8195124)Curated
Sequence conflicti422 – 4221R → H in CAA43470. (PubMed:2037065)Curated
Sequence conflicti422 – 4221R → H in AAB60689. (PubMed:8195124)Curated
Sequence conflicti465 – 4651K → R in CAA43470. (PubMed:2037065)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti184 – 1841I → T.1 Publication
Corresponds to variant rs55696045 [ dbSNP | Ensembl ].
VAR_040378
Natural varianti578 – 5781R → Q in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_040379

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61157 mRNA. Translation: CAA43470.1.
M80776 mRNA. Translation: AAA58391.1.
U08438
, U08435, U08436, U08437 Genomic DNA. Translation: AAB60689.1.
EU326303 Genomic DNA. Translation: ACA05909.1.
BC037963 mRNA. Translation: AAH37963.1.
BC090863 mRNA. Translation: AAH90863.1.
CCDSiCCDS8156.1.
PIRiA53791.
RefSeqiNP_001610.2. NM_001619.3.
UniGeneiHs.83636.

Genome annotation databases

EnsembliENST00000308595; ENSP00000312262; ENSG00000173020.
GeneIDi156.
KEGGihsa:156.
UCSCiuc009yrn.1. human.

Polymorphism databases

DMDMi126302521.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Beta adrenergic receptor kinase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61157 mRNA. Translation: CAA43470.1 .
M80776 mRNA. Translation: AAA58391.1 .
U08438
, U08435 , U08436 , U08437 Genomic DNA. Translation: AAB60689.1 .
EU326303 Genomic DNA. Translation: ACA05909.1 .
BC037963 mRNA. Translation: AAH37963.1 .
BC090863 mRNA. Translation: AAH90863.1 .
CCDSi CCDS8156.1.
PIRi A53791.
RefSeqi NP_001610.2. NM_001619.3.
UniGenei Hs.83636.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BAK NMR - A 556-670 [» ]
3CIK X-ray 2.75 A 1-689 [» ]
3KRW X-ray 2.90 A 2-689 [» ]
3KRX X-ray 3.10 A 2-689 [» ]
3V5W X-ray 2.07 A 1-689 [» ]
4MK0 X-ray 2.40 A 30-668 [» ]
4PNK X-ray 2.56 A 1-689 [» ]
ProteinModelPortali P25098.
SMRi P25098. Positions 30-670.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106665. 38 interactions.
DIPi DIP-42429N.
IntActi P25098. 15 interactions.
MINTi MINT-1214643.
STRINGi 9606.ENSP00000312262.

Chemistry

BindingDBi P25098.
ChEMBLi CHEMBL4079.
DrugBanki DB00171. Adenosine triphosphate.
GuidetoPHARMACOLOGYi 1466.

PTM databases

PhosphoSitei P25098.

Polymorphism databases

DMDMi 126302521.

Proteomic databases

MaxQBi P25098.
PaxDbi P25098.
PRIDEi P25098.

Protocols and materials databases

DNASUi 156.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000308595 ; ENSP00000312262 ; ENSG00000173020 .
GeneIDi 156.
KEGGi hsa:156.
UCSCi uc009yrn.1. human.

Organism-specific databases

CTDi 156.
GeneCardsi GC11P067033.
HGNCi HGNC:289. ADRBK1.
HPAi CAB005021.
CAB037248.
HPA048330.
MIMi 109635. gene.
neXtProti NX_P25098.
PharmGKBi PA40.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00770000120493.
HOGENOMi HOG000006742.
HOVERGENi HBG050559.
InParanoidi P25098.
KOi K00910.
OMAi DFCLKHL.
OrthoDBi EOG7FV3PP.
PhylomeDBi P25098.
TreeFami TF313940.

Enzyme and pathway databases

BRENDAi 2.7.11.15. 2681.
Reactomei REACT_18283. G alpha (q) signalling events.
REACT_9000. Calmodulin induced events.
SignaLinki P25098.

Miscellaneous databases

ChiTaRSi ADRBK1. human.
EvolutionaryTracei P25098.
GeneWikii Beta_adrenergic_receptor_kinase.
GenomeRNAii 156.
NextBioi 621.
PROi P25098.
SOURCEi Search...

Gene expression databases

Bgeei P25098.
CleanExi HS_ADRBK1.
ExpressionAtlasi P25098. baseline and differential.
Genevestigatori P25098.

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.
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

« Hide 'large scale' publications
  1. "cDNA cloning and chromosomal localization of the human beta-adrenergic receptor kinase."
    Benovic J.L., Stone W.C., Huebner K., Croce C., Caron M.G., Lefkowitz R.J.
    FEBS Lett. 283:122-126(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "High expression of beta-adrenergic receptor kinase in human peripheral blood leukocytes. Isoproterenol and platelet activating factor can induce kinase translocation."
    Chuang T.T., Sallese M., Ambrosini G., Parruti G., de Blasi A.
    J. Biol. Chem. 267:6886-6892(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Blood.
  3. "Structure of the human gene encoding the beta-adrenergic receptor kinase."
    Penn R.B., Benovic J.L.
    J. Biol. Chem. 269:14924-14930(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. NHLBI resequencing and genotyping service (RS&G)
    Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: PNS and Testis.
  6. "Monocyte chemoattractant protein-1-induced CCR2B receptor desensitization mediated by the G protein-coupled receptor kinase 2."
    Aragay A.M., Mellado M., Frade J.M., Martin A.M., Jimenez-Sainz M.C., Martinez-A C., Mayor F. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 95:2985-2990(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARRB1.
  7. "Differential effects of CC chemokines on CC chemokine receptor 5 (CCR5) phosphorylation and identification of phosphorylation sites on the CCR5 carboxyl terminus."
    Oppermann M., Mack M., Proudfoot A.E., Olbrich H.
    J. Biol. Chem. 274:8875-8885(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCR5, TISSUE SPECIFICITY.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-670, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  9. "Dual regulation of lysophosphatidic acid (LPA1) receptor signalling by Ral and GRK."
    Aziziyeh A.I., Li T.T., Pape C., Pampillo M., Chidiac P., Possmayer F., Babwah A.V., Bhattacharya M.
    Cell. Signal. 21:1207-1217(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LPAR1; LPAR2 AND RALA.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "The solution structure and dynamics of the pleckstrin homology domain of G protein-coupled receptor kinase 2 (beta-adrenergic receptor kinase 1). A binding partner of Gbetagamma subunits."
    Fushman D., Najmabadi-Haske T., Cahill S., Zheng J., Levine H. III, Cowburn D.
    J. Biol. Chem. 273:2835-2843(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 552-670.
  12. "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] THR-184 AND GLN-578.

Entry informationi

Entry nameiARBK1_HUMAN
AccessioniPrimary (citable) accession number: P25098
Secondary accession number(s): B0ZBE1, Q13837, Q6GTT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: February 20, 2007
Last modified: November 26, 2014
This is version 168 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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