SWISS-PROT: P25098
ID   ARK1_HUMAN     STANDARD;      PRT;   689 AA.
AC   P25098; Q13837;
DT   01-MAY-1992 (REL. 22, CREATED)
DT   01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE)
DT   01-FEB-1998 (REL. 36, LAST ANNOTATION UPDATE)
DE   BETA-ADRENERGIC RECEPTOR KINASE 1 (EC 2.7.1.126) (BETA-ARK-1) (G-
DE   PROTEIN COUPLED RECEPTOR KINASE 2).
GN   ADRBK1 OR GRK2 OR BARK1 OR BARK.
OS   HOMO SAPIENS (HUMAN).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 91243858. [NCBI, ExPASy, Japan]
RA   BENOVIC J.L., STONE W.C., HUEBNER K., CROCE C., CARON M.G.,
RA   LEFKOWITZ R.J.;
RL   FEBS LETT. 283:122-126(1991).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   TISSUE=BLOOD;
RX   MEDLINE; 92202245. [NCBI, ExPASy, Japan]
RA   CHUANG T.T., SALLESE M., AMBROSINI G., PARRUTI G., DE BLASI A.;
RL   J. BIOL. CHEM. 267:6886-6892(1992).
RN   [3]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 94253044. [NCBI, ExPASy, Japan]
RA   PENN R.B., BENOVIC J.L.;
RL   J. BIOL. CHEM. 269:14924-14930(1994).
RN   [4]
RP   STRUCTURE BY NMR OF 552-670.
RX   MEDLINE; 98112832. [NCBI, ExPASy, Japan]
RA   FUSHMAN D., NAJMABADI-HASKE T., CAHILL S., ZHENG J., LEVINE H. III,
RA   COWBURN D.;
RL   J. BIOL. CHEM. 273:2835-2843(1998).
CC   -!- FUNCTION: SPECIFICALLY PHOSPHORYLATES THE AGONIST-OCCUPIED FORM
CC       OF THE BETA-ADRENERGIC AND CLOSELY RELATED RECEPTORS, PROBABLY
CC       INDUCING A DESENSITIZATION OF THEM.
CC   -!- CATALYTIC ACTIVITY: ATP + [BETA-ADRENERGIC RECEPTOR] = ADP +
CC       [BETA-ADRENERGIC RECEPTOR] PHOSPHATE.
CC   -!- SIMILARITY: TO THE CATALYTIC DOMAINS OF OTHER SERINE/THREONINE
CC       KINASES. STRONG, TO OTHER KINASES THAT PHOSPHORYLATES G-COUPLED
CC       RECEPTORS.
CC   -!- SIMILARITY: CONTAINS A PH DOMAIN.
DR   EMBL; X61157; G288308; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; M80776; G179335; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; U08438; G531122; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; U08435; G531122; JOINED. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; U08436; G531122; JOINED. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   EMBL; U08437; G531122; JOINED. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   PIR; S15781; S15781.
DR   PDB; 1BAK; 25-FEB-98. [ExPASy / Brookhaven]
DR   SWISS-3DIMAGE; ARK1_HUMAN.
DR   GeneCard; ADRBK1.
DR   MIM; 109635; -.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   DOMO; P25098.
DR   PRODOM [Domain structure / List of seq. sharing at least 1 domain]
DR   PROTOMAP; P25098.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   TRANSFERASE; SERINE/THREONINE-PROTEIN KINASE; ATP-BINDING;
KW   MULTIGENE FAMILY; 3D-STRUCTURE.
FT   DOMAIN        1    190       N-TERMINAL.
FT   DOMAIN      191    453       PROTEIN KINASE.
FT   DOMAIN      454    689       C-TERMINAL.
FT   DOMAIN      558    652       PH.
FT   NP_BIND     197    205       ATP (BY SIMILARITY).
FT   BINDING     220    220       ATP (BY SIMILARITY).
FT   ACT_SITE    317    317       BY SIMILARITY.
FT   CONFLICT    168    185       SDKFTRFCQWKNVELNIH -> RISSHGFASGRMWSSTST
FT                                (IN REF. 3).
FT   CONFLICT    211    211       R -> A (IN REF. 2).
FT   CONFLICT    422    422       H -> R (IN REF. 2).
FT   CONFLICT    465    465       R -> K (IN REF. 2 AND 3).
SQ   SEQUENCE   689 AA;  79667 MW;  C21DCA82 CRC32;
     MADLEAVLAD VSYLMAMEKS KATPAARASK KILLPEPSIR SVMQKYLEDR GEVTFEKIFS
     QKLGYLLFRD FCLNHLEEAR PLVEFYEEIK KYEKLETEEE RVARSREIFD SYIMKELLAC
     SHPFSKSATE HVQGHLGKKQ VPPDLFQPYI EEICQNLRGD VFQKFIESDK FTRFCQWKNV
     ELNIHLTMND FSVHRIIGRG GFGEVYGCRK RDTGKMYAMK CLDKKRIKMK QGETLALNER
     IMLSLVSTGD CPFIVCMSYA FHTPDKLSFI LDLMNGGDLH YHLSQHGVFS EADMRFYAAE
     IILGLEHMHN RFVVYRDLKP ANILLDEHGH VRISDLGLAC DFSKKKPHAS VGTHGYMAPE
     VLQKGVAYDS SADWFSLGCM LFKLLRGHSP FRQHKTKDKH EIDRMTLTMA VELPDSFSPE
     LHSLLEGLLQ RDVNRRLGCL GRGAQEVKES PFFRSLDWQM VFLQRYPPPL IPPRGEVNAA
     DAFDIGSFDE EDTKGIKLLD SDQELYRNFP LTISERWQQE VAETVFDTIN AETDRLEARK
     KAKNKQLGHE EDYALGKDCI MHGYMSKMGN PFLTQWQRRY FYLFPNRLEW RGEGEAPQSL
     LTMEEIQSVE ETQIKERKCL LLKIRGGKQF ILQCDSDPEL VQWKKELRDA YREAQQLVQR
     VPKMKNKPRS PVVELSKVPL VQRGSANGL
//

Direct WU-BLAST submission at EMBNet-CH (Lausanne, Switzerland)

Direct BLAST submission at NCBI (Bethesda, USA)

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Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass