AAKB1_HUMAN - dbPTM
AAKB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AAKB1_HUMAN
UniProt AC Q9Y478
Protein Name 5'-AMP-activated protein kinase subunit beta-1
Gene Name PRKAB1
Organism Homo sapiens (Human).
Sequence Length 270
Subcellular Localization
Protein Description Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3)..
Protein Sequence MGNTSSERAALERHGGHKTPRRDSSGGTKDGDRPKILMDSPEDADLFHSEEIKAPEKEEFLAWQHDLEVNDKAPAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSHNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVKKTDFEVFDALMVDSQKCSDVSELSSSPPGPYHQEPYVCKPEERFRAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKPI
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Myristoylation------MGNTSSERA
------CCCCHHHHH		46.2321680840
2N-myristoyl glycine------MGNTSSERA
------CCCCHHHHH		46.23-
4Phosphorylation----MGNTSSERAAL
----CCCCHHHHHHH		28.0918088087
5Phosphorylation---MGNTSSERAALE
---CCCCHHHHHHHH		33.9118088087
6Phosphorylation--MGNTSSERAALER
--CCCCHHHHHHHHH		29.1218088087
19PhosphorylationERHGGHKTPRRDSSG
HHCCCCCCCCCCCCC		19.1617192257
24PhosphorylationHKTPRRDSSGGTKDG
CCCCCCCCCCCCCCC		29.1319376078
25PhosphorylationKTPRRDSSGGTKDGD
CCCCCCCCCCCCCCC		45.6028176443
28PhosphorylationRRDSSGGTKDGDRPK
CCCCCCCCCCCCCCC		29.5028176443
35UbiquitinationTKDGDRPKILMDSPE
CCCCCCCCCCCCCHH		49.74-
40PhosphorylationRPKILMDSPEDADLF
CCCCCCCCHHHHHCC		19.0730266825
49PhosphorylationEDADLFHSEEIKAPE
HHHHCCCCCCCCCCC		29.5954886891
53UbiquitinationLFHSEEIKAPEKEEF
CCCCCCCCCCCHHHH		62.26-
57UbiquitinationEEIKAPEKEEFLAWQ
CCCCCCCHHHHHHHC		62.5821890473
72UbiquitinationHDLEVNDKAPAQARP
CCCEECCCCCCCCCC		51.57-
80PhosphorylationAPAQARPTVFRWTGG
CCCCCCCEEEEECCC		27.0719376078
89UbiquitinationFRWTGGGKEVYLSGS
EEECCCCCEEEEECC		47.48-
92PhosphorylationTGGGKEVYLSGSFNN
CCCCCEEEEECCCCC		9.0230850111
94PhosphorylationGGKEVYLSGSFNNWS
CCCEEEEECCCCCCC		18.0726657352
96PhosphorylationKEVYLSGSFNNWSKL
CEEEEECCCCCCCCC		22.7925159151
101PhosphorylationSGSFNNWSKLPLTRS
ECCCCCCCCCCCCCC		26.8326657352
102UbiquitinationGSFNNWSKLPLTRSH
CCCCCCCCCCCCCCC		45.82-
106PhosphorylationNWSKLPLTRSHNNFV
CCCCCCCCCCCCCEE		28.3425159151
108PhosphorylationSKLPLTRSHNNFVAI
CCCCCCCCCCCEEEE		25.9025159151
125PhosphorylationLPEGEHQYKFFVDGQ
CCCCCCEEEEEECCE		16.2123927012
138PhosphorylationGQWTHDPSEPIVTSQ
CEECCCCCCCEEEEE		63.16113334293
144PhosphorylationPSEPIVTSQLGTVNN
CCCCEEEEECCCCCC		16.7146163111
148PhosphorylationIVTSQLGTVNNIIQV
EEEEECCCCCCEEEE		28.7526657352
157UbiquitinationNNIIQVKKTDFEVFD
CCEEEEECCCHHHCC		55.24-
158PhosphorylationNIIQVKKTDFEVFDA
CEEEEECCCHHHCCC		39.9615423663
170PhosphorylationFDALMVDSQKCSDVS
CCCEEECCCCCCCHH		21.8226074081
174PhosphorylationMVDSQKCSDVSELSS
EECCCCCCCHHHHCC		48.3523927012
177PhosphorylationSQKCSDVSELSSSPP
CCCCCCHHHHCCCCC		37.5022167270
180PhosphorylationCSDVSELSSSPPGPY
CCCHHHHCCCCCCCC		25.3922167270
181PhosphorylationSDVSELSSSPPGPYH
CCHHHHCCCCCCCCC		60.5322167270
182PhosphorylationDVSELSSSPPGPYHQ
CHHHHCCCCCCCCCC		31.5722167270
187PhosphorylationSSSPPGPYHQEPYVC
CCCCCCCCCCCCCCC		23.2722167270
192PhosphorylationGPYHQEPYVCKPEER
CCCCCCCCCCCHHHH		20.0922167270
195UbiquitinationHQEPYVCKPEERFRA
CCCCCCCCHHHHCCC		45.48-
252PhosphorylationKDGVMVLSATHRYKK
CCCEEEEEECCCCCC		21.5118691976
254PhosphorylationGVMVLSATHRYKKKY
CEEEEEECCCCCCCE		11.9620071362
261PhosphorylationTHRYKKKYVTTLLYK
CCCCCCCEEEEEEEC		16.3528152594
263PhosphorylationRYKKKYVTTLLYKPI
CCCCCEEEEEEECCC		14.5026074081
264PhosphorylationYKKKYVTTLLYKPI-
CCCCEEEEEEECCC-		12.5326074081
267PhosphorylationKYVTTLLYKPI----
CEEEEEEECCC----		20.1726074081
268UbiquitinationYVTTLLYKPI-----
EEEEEEECCC-----		35.88-
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
24SPhosphorylationKinasePRKAA1Q13131
GPS
24SPhosphorylationKinasePKACAP17612
PSP
80TPhosphorylationKinasePRKAA1Q13131
GPS
108SPhosphorylationKinasePRKAA1Q13131
GPS
148TPhosphorylationKinasePRKAA1Q13131
GPS
158TPhosphorylationKinasePRKAA1Q13131
GPS
174SPhosphorylationKinasePRKAA1Q13131
GPS
177SPhosphorylationKinasePRKAA1Q13131
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AAKB1_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 AAKB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AAKG1_HUMANPRKAG1physical
10698692
AAKG2_HUMANPRKAG2physical
10698692
GYS1_HUMANGYS1physical
17353931
DHX36_HUMANDHX36physical
17353931
EZRI_HUMANEZRphysical
17353931
ACLY_HUMANACLYphysical
17353931
AAKB2_HUMANPRKAB2physical
17353931
SYMC_HUMANMARSphysical
17353931
MYH10_HUMANMYH10physical
17353931
U520_HUMANSNRNP200physical
17353931
AAPK2_HUMANPRKAA2physical
20562859
AAPK1_HUMANPRKAA1physical
20562859
AAKG1_HUMANPRKAG1physical
20562859
AAKG2_HUMANPRKAG2physical
20562859
NSF_HUMANNSFphysical
20562859
CBR1_HUMANCBR1physical
20562859
TGM3_HUMANTGM3physical
20562859
AAKB2_HUMANPRKAB2physical
20562859
CASPE_HUMANCASP14physical
20562859
DSC1_HUMANDSC1physical
20562859
HDAC5_HUMANHDAC5physical
18184930
A4_HUMANAPPphysical
21832049
AAPK1_HUMANPRKAA1physical
22939629
AAKG1_HUMANPRKAG1physical
21988832
CIDEA_HUMANCIDEAphysical
18480843
AAKG1_HUMANPRKAG1physical
18480843
AAPK1_HUMANPRKAA1physical
18480843
ACACA_HUMANACACAphysical
18480843
AAKG1_HUMANPRKAG1physical
8621713
AAPK1_HUMANPRKAA1physical
8621713
SNF1_YEASTSNF1physical
8621713
AAKG_YEASTSNF4physical
8621713
AAKG1_HUMANPRKAG1physical
8663446
AAPK1_HUMANPRKAA1physical
8663446
AP1G1_HUMANAP1G1physical
26344197
AAPK1_HUMANPRKAA1physical
26344197
AAPK2_HUMANPRKAA2physical
26344197
AAPK2_HUMANPRKAA2physical
28514442
AAPK1_HUMANPRKAA1physical
28514442
AAKB2_HUMANPRKAB2physical
28514442
TBB1_HUMANTUBB1physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
NEK4_HUMANNEK4physical
28514442
TRM44_HUMANTRMT44physical
28514442
HEAT6_HUMANHEATR6physical
28514442
SYHM_HUMANHARS2physical
28514442
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
There are no disease associations of PTM sites.
Regulatory Network of AAKB1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-108, AND MASSSPECTROMETRY.
"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 THR-19; SER-24; SER-25;SER-40; SER-96; SER-101; SER-108; THR-148; SER-174; SER-177; SER-180;SER-181 AND SER-252, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-40 AND SER-108,AND MASS SPECTROMETRY.
"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 THR-4; SER-5; SER-6 ANDSER-108, AND MASS SPECTROMETRY.

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