dbPTM

ARBK1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ARBK1_HUMAN
UniProt AC	P25098
Protein Name	Beta-adrenergic receptor kinase 1
Gene Name	GRK2 {ECO:0000312\|HGNC:HGNC:289}
Organism	Homo sapiens (Human).
Sequence Length	689
Subcellular Localization	Cytoplasm . Cell membrane .
Protein Description	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. [PubMed: 19306925]
Protein Sequence	MADLEAVLADVSYLMAMEKSKATPAARASKKILLPEPSIRSVMQKYLEDRGEVTFEKIFSQKLGYLLFRDFCLNHLEEARPLVEFYEEIKKYEKLETEEERVARSREIFDSYIMKELLACSHPFSKSATEHVQGHLGKKQVPPDLFQPYIEEICQNLRGDVFQKFIESDKFTRFCQWKNVELNIHLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTGDCPFIVCMSYAFHTPDKLSFILDLMNGGDLHYHLSQHGVFSEADMRFYAAEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHASVGTHGYMAPEVLQKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAVELPDSFSPELRSLLEGLLQRDVNRRLGCLGRGAQEVKESPFFRSLDWQMVFLQKYPPPLIPPRGEVNAADAFDIGSFDEEDTKGIKLLDSDQELYRNFPLTISERWQQEVAETVFDTINAETDRLEARKKAKNKQLGHEEDYALGKDCIMHGYMSKMGNPFLTQWQRRYFYLFPNRLEWRGEGEAPQSLLTMEEIQSVEETQIKERKCLLLKIRGGKQFILQCDSDPELVQWKKELRDAYREAQQLVQRVPKMKNKPRSPVVELSKVPLVQRGSANGL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADLEAVLA ------CCHHHHHHH	30.05	-
13	Phosphorylation	AVLADVSYLMAMEKS HHHHHHHHHHHHHHC	10.59	16725308
19	Ubiquitination	SYLMAMEKSKATPAA HHHHHHHHCCCCHHH	44.14	17006543
21	Ubiquitination	LMAMEKSKATPAARA HHHHHHCCCCHHHHH	68.31	17006543
29	Phosphorylation	ATPAARASKKILLPE CCHHHHHCCHHHCCC	29.00	22817900
30	Ubiquitination	TPAARASKKILLPEP CHHHHHCCHHHCCCH	42.73	17006543
31	Ubiquitination	PAARASKKILLPEPS HHHHHCCHHHCCCHH	35.77	17006543
38	Phosphorylation	KILLPEPSIRSVMQK HHHCCCHHHHHHHHH	29.04	28450419
41	Phosphorylation	LPEPSIRSVMQKYLE CCCHHHHHHHHHHHH	21.92	23090842
45	Ubiquitination	SIRSVMQKYLEDRGE HHHHHHHHHHHHCCC	33.44	-
50	Methylation	MQKYLEDRGEVTFEK HHHHHHHCCCCCHHH	33.52	-
54	Phosphorylation	LEDRGEVTFEKIFSQ HHHCCCCCHHHHHHH	23.06	23090842
57	Ubiquitination	RGEVTFEKIFSQKLG CCCCCHHHHHHHHHH	44.88	21890473
62	Ubiquitination	FEKIFSQKLGYLLFR HHHHHHHHHHHHHHH	42.56	21890473
86	Phosphorylation	ARPLVEFYEEIKKYE HHHHHHHHHHHHHHH	10.11	16725308
92	Phosphorylation	FYEEIKKYEKLETEE HHHHHHHHHCCCCHH	17.19	16725308
94	Ubiquitination	EEIKKYEKLETEEER HHHHHHHCCCCHHHH	48.83	-
115	Ubiquitination	IFDSYIMKELLACSH HHHHHHHHHHHHCCC	35.33	-
126	Ubiquitination	ACSHPFSKSATEHVQ HCCCCCCHHHHHHHH	44.48	-
138	Ubiquitination	HVQGHLGKKQVPPDL HHHHCCCCCCCCHHH	46.52	-
139	Ubiquitination	VQGHLGKKQVPPDLF HHHCCCCCCCCHHHH	55.52	-
164	Ubiquitination	LRGDVFQKFIESDKF CCCCHHHHHHHCCCC	36.52	-
164	Acetylation	LRGDVFQKFIESDKF CCCCHHHHHHHCCCC	36.52	26822725
170	Ubiquitination	QKFIESDKFTRFCQW HHHHHCCCCCEECCC	58.89	21890473
206	Phosphorylation	RGGFGEVYGCRKADT CCCCCCCCCCCCCCC	13.25	-
213	Phosphorylation	YGCRKADTGKMYAMK CCCCCCCCCCEEEEH	43.49	22964224
215	Ubiquitination	CRKADTGKMYAMKCL CCCCCCCCEEEEHHH	30.72	-
220	Ubiquitination	TGKMYAMKCLDKKRI CCCEEEEHHHCHHHC	24.39	-
230	Ubiquitination	DKKRIKMKQGETLAL CHHHCCCCCCCEEEE	50.58	-
247	Phosphorylation	RIMLSLVSTGDCPFI HHHHHHHCCCCCCEE	31.78	22817900
248	Phosphorylation	IMLSLVSTGDCPFIV HHHHHHCCCCCCEEE	29.56	22817900
263	Phosphorylation	CMSYAFHTPDKLSFI EEEHHCCCCCHHHHH	27.08	22817900
319	Ubiquitination	FVVYRDLKPANILLD EEEEECCCHHCEEEC	46.50	-
344	Acetylation	GLACDFSKKKPHASV CEECCCCCCCCCCCC	65.88	25953088
344	Ubiquitination	GLACDFSKKKPHASV CEECCCCCCCCCCCC	65.88	-
345	Ubiquitination	LACDFSKKKPHASVG EECCCCCCCCCCCCC	71.04	-
346	Ubiquitination	ACDFSKKKPHASVGT ECCCCCCCCCCCCCC	45.85	-
350	Phosphorylation	SKKKPHASVGTHGYM CCCCCCCCCCCCCCC	20.32	19369195
353	Phosphorylation	KPHASVGTHGYMAPE CCCCCCCCCCCCCHH	15.24	22817900
356	Phosphorylation	ASVGTHGYMAPEVLQ CCCCCCCCCCHHHHH	5.19	-
389	Phosphorylation	FKLLRGHSPFRQHKT HHHHHCCCHHHHCCC	28.67	27067055
416	Phosphorylation	MAVELPDSFSPELRS EEEECCCCCCHHHHH	26.19	-
423	Phosphorylation	SFSPELRSLLEGLLQ CCCHHHHHHHHHHHH	50.35	21712546
448	Ubiquitination	GRGAQEVKESPFFRS CCCCHHHHHCCCHHC	52.28	-
487	Phosphorylation	ADAFDIGSFDEEDTK HHCCCCCCCCCCCCC	29.83	29978859
493	Phosphorylation	GSFDEEDTKGIKLLD CCCCCCCCCCEEEEC	34.15	27732954
494	Ubiquitination	SFDEEDTKGIKLLDS CCCCCCCCCEEEECC	71.59	-
497	Ubiquitination	EEDTKGIKLLDSDQE CCCCCCEEEECCCHH	52.22	-
501	Phosphorylation	KGIKLLDSDQELYRN CCEEEECCCHHHHHH	40.96	27067055
506	Phosphorylation	LDSDQELYRNFPLTI ECCCHHHHHHCCCCC	11.62	29978859
545	Ubiquitination	ARKKAKNKQLGHEED HHHHHHHHCCCCHHH	46.31	-
557	Ubiquitination	EEDYALGKDCIMHGY HHHHHCCHHHHHHHH	50.72	-
628	Ubiquitination	LLKIRGGKQFILQCD EEEEECCCEEEEECC	44.88	-
644	Ubiquitination	DPELVQWKKELRDAY CHHHHHHHHHHHHHH	21.19	-
644	Acetylation	DPELVQWKKELRDAY CHHHHHHHHHHHHHH	21.19	25953088
670	Phosphorylation	KMKNKPRSPVVELSK HHCCCCCCCCEEHHC	30.49	29255136
676	Phosphorylation	RSPVVELSKVPLVQR CCCCEEHHCCCCEEC	20.36	23927012
677	Ubiquitination	SPVVELSKVPLVQRG CCCEEHHCCCCEECC	61.57	21890473
683	Methylation	SKVPLVQRGSANGL- HCCCCEECCCCCCC-	33.29	-
685	Phosphorylation	VPLVQRGSANGL--- CCCEECCCCCCC---	22.28	28355574

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
13	Y	Phosphorylation	Kinase	SRC	P12931	PSP
29	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
29	S	Phosphorylation	Kinase	PKCA	P05696	PSP
29	S	Phosphorylation	Kinase	PRKCD	P09215	GPS
29	S	Phosphorylation	Kinase	PRKCG	P05129	GPS
86	Y	Phosphorylation	Kinase	SRC	P12931	PSP
92	Y	Phosphorylation	Kinase	SRC	P12931	PSP
670	S	Phosphorylation	Kinase	CDK2	P24941	PSP
670	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
670	S	Phosphorylation	Kinase	MAPK_GROUP	-	PhosphoELM
685	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
685	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:17006543

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ARBK1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of ARBK1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GNAQ_HUMAN	GNAQ	physical	12885252
GNA15_HUMAN	GNA15	physical	12885252
KPCB_HUMAN	PRKCB	physical	12679936
CNRG_HUMAN	PDE6G	physical	12624098
SRC_HUMAN	SRC	physical	12624098
PHLP_HUMAN	PDCL	physical	10884381
PHOS_HUMAN	PDC	physical	10884381
OPSD_HUMAN	RHO	physical	10722682
FSHR_HUMAN	FSHR	physical	10379886
HDAC6_HUMAN	HDAC6	physical	22193721
MDM2_HUMAN	MDM2	physical	21081496
ARRB1_HUMAN	ARRB1	physical	21081496
GBB1_HUMAN	GNB1	physical	17548351
GBB1_HUMAN	GNB1	physical	10744734
CSEN_HUMAN	KCNIP3	physical	17102134
ADRB2_HUMAN	ADRB2	physical	14654844
PEBP1_HUMAN	PEBP1	physical	14654844
EPHA2_HUMAN	EPHA2	physical	21988832
RGRF1_HUMAN	RASGRF1	physical	21988832
GNAQ_HUMAN	GNAQ	physical	21940795
RPGF3_MOUSE	Rapgef3	physical	20861385
HS90A_HUMAN	HSP90AA1	physical	23455922
HS90B_HUMAN	HSP90AB1	physical	23455922
ARBK2_HUMAN	ADRBK2	physical	23455922
ACACA_HUMAN	ACACA	physical	23455922
SYNM_HUMAN	NARS2	physical	26344197
ARBK2_HUMAN	ADRBK2	physical	28514442
GNAQ_HUMAN	GNAQ	physical	10727532

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00171	Adenosine triphosphate

Regulatory Network of ARBK1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350 AND THR-353, ANDMASS SPECTROMETRY.	19369195 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-670, AND MASSSPECTROMETRY.	18088087 [Abstract]