dbPTM

AAPK1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AAPK1_HUMAN
UniProt AC	Q13131
Protein Name	5'-AMP-activated protein kinase catalytic subunit alpha-1
Gene Name	PRKAA1
Organism	Homo sapiens (Human).
Sequence Length	559
Subcellular Localization	Cytoplasm . Nucleus . In response to stress, recruited by p53/TP53 to specific promoters.
Protein Description	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. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1. In response to nutrient limitation, phosphorylates transcription factor FOXO3 promoting FOXO3 mitochontrial import (By similarity). AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1..
Protein Sequence	MRRLSSWRKMATAEKQKHDGRVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILNRQKIRSLDVVGKIRREIQNLKLFRHPHIIKLYQVISTPSDIFMVMEYVSGGELFDYICKNGRLDEKESRRLFQQILSGVDYCHRHMVVHRDLKPENVLLDAHMNAKIADFGLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALLCGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHMLQVDPMKRATIKDIREHEWFKQDLPKYLFPEDPSYSSTMIDDEALKEVCEKFECSEEEVLSCLYNRNHQDPLAVAYHLIIDNRRIMNEAKDFYLATSPPDSFLDDHHLTRPHPERVPFLVAETPRARHTLDELNPQKSKHQGVRKAKWHLGIRSQSRPNDIMAEVCRAIKQLDYEWKVVNPYYLRVRRKNPVTSTYSKMSLQLYQVDSRTYLLDFRSIDDEITEAKSGTATPQRSGSVSNYRSCQRSDSDAEAQGKSSEVSLTSSVTSLDSSPVDLTPRPGSHTIEFFEMCANLIKILAQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MRRLSSWRKMAT ---CCCHHHHHHHHH	26.50	28674151
6	Phosphorylation	--MRRLSSWRKMATA --CCCHHHHHHHHHH	35.18	46163063
22	Ubiquitination	KQKHDGRVKIGHYIL HHCCCCCEEEEEEEC	6.92	22817900
27	Ubiquitination	GRVKIGHYILGDTLG CCEEEEEEECCCCEE	7.82	22817900
32	Phosphorylation	GHYILGDTLGVGTFG EEEECCCCEECCCCC	24.50	28857561
37	Phosphorylation	GDTLGVGTFGKVKVG CCCEECCCCCEEEEC	27.15	28857561
40	Acetylation	LGVGTFGKVKVGKHE EECCCCCEEEECCEE	34.39	25953088
40	Ubiquitination	LGVGTFGKVKVGKHE EECCCCCEEEECCEE	34.39	19608861
40 (in isoform 2)	Ubiquitination	-	34.39	-
45	Ubiquitination	FGKVKVGKHELTGHK CCEEEECCEECCCCE	36.57	29967540
52	Acetylation	KHELTGHKVAVKILN CEECCCCEEHHHHHC	32.98	25953088
52	Ubiquitination	KHELTGHKVAVKILN CEECCCCEEHHHHHC	32.98	29967540
54	Ubiquitination	ELTGHKVAVKILNRQ ECCCCEEHHHHHCHH	11.16	24816145
56	Ubiquitination	TGHKVAVKILNRQKI CCCEEHHHHHCHHHC	31.57	29967540
56 (in isoform 2)	Ubiquitination	-	31.57	-
65	Phosphorylation	LNRQKIRSLDVVGKI HCHHHCCCCHHHHHH	32.18	28857561
71	Acetylation	RSLDVVGKIRREIQN CCCHHHHHHHHHHHC	22.79	25953088
71	Ubiquitination	RSLDVVGKIRREIQN CCCHHHHHHHHHHHC	22.79	33845483
80	Acetylation	RREIQNLKLFRHPHI HHHHHCCCCCCCHHH	53.80	22637185
80	Ubiquitination	RREIQNLKLFRHPHI HHHHHCCCCCCCHHH	53.80	24816145
80 (in isoform 2)	Malonylation	-	53.80	26320211
130	Ubiquitination	DEKESRRLFQQILSG CHHHHHHHHHHHHHC	4.40	29967540
138	Ubiquitination	FQQILSGVDYCHRHM HHHHHHCCHHHHHHC	4.21	21963094
139	Ubiquitination	QQILSGVDYCHRHMV HHHHHCCHHHHHHCE	43.82	21963094
140	Ubiquitination	QILSGVDYCHRHMVV HHHHCCHHHHHHCEE	6.43	22817900
152	Ubiquitination	MVVHRDLKPENVLLD CEECCCCCHHHEEEE	55.35	-
154	Ubiquitination	VHRDLKPENVLLDAH ECCCCCHHHEEEEHH	59.38	21963094
165	Ubiquitination	LDAHMNAKIADFGLS EEHHHCHHHHCCCHH	33.16	21963094
167 (in isoform 2)	Ubiquitination	-	12.84	-
172	Phosphorylation	KIADFGLSNMMSDGE HHHCCCHHHCCCCCC	24.06	22322096
174	Phosphorylation	ADFGLSNMMSDGEFL HCCCHHHCCCCCCHH	2.15	8910387
175	Phosphorylation	DFGLSNMMSDGEFLR CCCHHHCCCCCCHHH	3.75	18669648
176	Phosphorylation	FGLSNMMSDGEFLRT CCHHHCCCCCCHHHH	31.53	26657352
178	Phosphorylation	LSNMMSDGEFLRTSC HHHCCCCCCHHHHCC	21.90	18220336
180	Ubiquitination	NMMSDGEFLRTSCGS HCCCCCCHHHHCCCC	7.37	21963094
183	Phosphorylation	SDGEFLRTSCGSPNY CCCCHHHHCCCCCCC	30.43	22322096
184	Phosphorylation	DGEFLRTSCGSPNYA CCCHHHHCCCCCCCC	15.28	22322096
185	S-nitrosylation	GEFLRTSCGSPNYAA CCHHHHCCCCCCCCC	6.55	2212679
187	Phosphorylation	FLRTSCGSPNYAAPE HHHHCCCCCCCCCCH	17.82	22322096
190	Phosphorylation	TSCGSPNYAAPEVIS HCCCCCCCCCCHHHC	13.92	26552605
197	Phosphorylation	YAAPEVISGRLYAGP CCCCHHHCCCCCCCC	24.04	26552605
198	Phosphorylation	AAPEVISGRLYAGPE CCCHHHCCCCCCCCC	16.70	27251275
199	Ubiquitination	APEVISGRLYAGPEV CCHHHCCCCCCCCCC	20.10	21963094
227	Ubiquitination	CGTLPFDDDHVPTLF HCCCCCCCCCHHHHH	48.58	21963094
243	Phosphorylation	KICDGIFYTPQYLNP HHCCCCCCCHHHCCH	18.65	21406692
244	Phosphorylation	ICDGIFYTPQYLNPS HCCCCCCCHHHCCHH	7.99	21406692
247	Phosphorylation	GIFYTPQYLNPSVIS CCCCCHHHCCHHHHH	15.06	21406692
251	Phosphorylation	TPQYLNPSVISLLKH CHHHCCHHHHHHHHH	30.89	21406692
254	Phosphorylation	YLNPSVISLLKHMLQ HCCHHHHHHHHHHHC	26.03	24719451
254	Ubiquitination	YLNPSVISLLKHMLQ HCCHHHHHHHHHHHC	26.03	22817900
259	Ubiquitination	VISLLKHMLQVDPMK HHHHHHHHHCCCCCC	2.40	22817900
266	Ubiquitination	MLQVDPMKRATIKDI HHCCCCCCCCCHHHH	44.24	29967540
269	Phosphorylation	VDPMKRATIKDIREH CCCCCCCCHHHHHHC	32.37	-
269	Ubiquitination	VDPMKRATIKDIREH CCCCCCCCHHHHHHC	32.37	22817900
271	Ubiquitination	PMKRATIKDIREHEW CCCCCCHHHHHHCHH	42.63	29967540
274	Ubiquitination	RATIKDIREHEWFKQ CCCHHHHHHCHHHHC	49.72	22817900
276 (in isoform 1)	Ubiquitination	-	27.95	21906983
280	Ubiquitination	IREHEWFKQDLPKYL HHHCHHHHCCCCHHC	43.93	22817900
281	Ubiquitination	REHEWFKQDLPKYLF HHCHHHHCCCCHHCC	48.26	29967540
281 (in isoform 2)	Ubiquitination	-	48.26	-
285	Ubiquitination	WFKQDLPKYLFPEDP HHHCCCCHHCCCCCC	62.98	21906983
286	Phosphorylation	FKQDLPKYLFPEDPS HHCCCCHHCCCCCCC	16.19	28796482
286	Ubiquitination	FKQDLPKYLFPEDPS HHCCCCHHCCCCCCC	16.19	29967540
291 (in isoform 2)	Ubiquitination	-	37.37	21906983
293	Phosphorylation	YLFPEDPSYSSTMID HCCCCCCCCCCCCCC	50.39	28796482
294	Phosphorylation	LFPEDPSYSSTMIDD CCCCCCCCCCCCCCH	16.42	28796482
295	Phosphorylation	FPEDPSYSSTMIDDE CCCCCCCCCCCCCHH	24.54	28796482
295	Ubiquitination	FPEDPSYSSTMIDDE CCCCCCCCCCCCCHH	24.54	22817900
295 (in isoform 2)	Ubiquitination	-	24.54	-
296	Phosphorylation	PEDPSYSSTMIDDEA CCCCCCCCCCCCHHH	17.48	28796482
297	Phosphorylation	EDPSYSSTMIDDEAL CCCCCCCCCCCHHHH	16.53	28796482
300	Ubiquitination	SYSSTMIDDEALKEV CCCCCCCCHHHHHHH	36.55	22817900
309	Phosphorylation	EALKEVCEKFECSEE HHHHHHHHHCCCCHH	66.99	27642862
346	Phosphorylation	IDNRRIMNEAKDFYL HCCHHHHHHHHCEEE	43.64	18669648
347	Phosphorylation	DNRRIMNEAKDFYLA CCHHHHHHHHCEEEE	39.45	18669648
350	Phosphorylation	RIMNEAKDFYLATSP HHHHHHHCEEEECCC	44.46	27642862
352	Phosphorylation	MNEAKDFYLATSPPD HHHHHCEEEECCCCC	12.93	29255136
355	Phosphorylation	AKDFYLATSPPDSFL HHCEEEECCCCCCCC	38.89	29255136
356	Phosphorylation	KDFYLATSPPDSFLD HCEEEECCCCCCCCC	28.91	29255136
360	Phosphorylation	LATSPPDSFLDDHHL EECCCCCCCCCCCCC	33.22	29255136
367	Phosphorylation	SFLDDHHLTRPHPER CCCCCCCCCCCCCCC	3.79	27642862
368	Phosphorylation	FLDDHHLTRPHPERV CCCCCCCCCCCCCCC	37.49	23663014
370	Phosphorylation	DDHHLTRPHPERVPF CCCCCCCCCCCCCCE	41.99	24719451
370	Ubiquitination	DDHHLTRPHPERVPF CCCCCCCCCCCCCCE	41.99	21963094
372	Ubiquitination	HHLTRPHPERVPFLV CCCCCCCCCCCCEEE	33.50	22817900
373	Phosphorylation	HLTRPHPERVPFLVA CCCCCCCCCCCEEEE	64.38	18669648
375	Phosphorylation	TRPHPERVPFLVAET CCCCCCCCCEEEECC	3.61	27642862
382	Phosphorylation	VPFLVAETPRARHTL CCEEEECCHHHCCCH	14.34	29255136
385	Ubiquitination	LVAETPRARHTLDEL EEECCHHHCCCHHHH	14.60	21963094
387	Ubiquitination	AETPRARHTLDELNP ECCHHHCCCHHHHCC	29.78	22817900
387 (in isoform 1)	Ubiquitination	-	29.78	21906983
388	Phosphorylation	ETPRARHTLDELNPQ CCHHHCCCHHHHCCC	30.28	23663014
396	Ubiquitination	LDELNPQKSKHQGVR HHHHCCCCCCCCCCH	63.83	21906983
397	Phosphorylation	DELNPQKSKHQGVRK HHHCCCCCCCCCCHH	30.07	28857561
398	Ubiquitination	ELNPQKSKHQGVRKA HHCCCCCCCCCCHHH	47.16	22817900
402 (in isoform 2)	Ubiquitination	-	4.58	21906983
403	Phosphorylation	KSKHQGVRKAKWHLG CCCCCCCHHHHHCCC	39.79	27251275
406	Sumoylation	HQGVRKAKWHLGIRS CCCCHHHHHCCCCCC	37.88	-
406	Sumoylation	HQGVRKAKWHLGIRS CCCCHHHHHCCCCCC	37.88	-
406	Ubiquitination	HQGVRKAKWHLGIRS CCCCHHHHHCCCCCC	37.88	-
411	Ubiquitination	KAKWHLGIRSQSRPN HHHHCCCCCCCCCCC	4.88	21963094
411 (in isoform 2)	Ubiquitination	-	4.88	-
413	Ubiquitination	KWHLGIRSQSRPNDI HHCCCCCCCCCCCHH	30.50	22817900
421 (in isoform 2)	Malonylation	-	2.65	32601280
421 (in isoform 2)	Ubiquitination	-	2.65	-
429	Acetylation	AEVCRAIKQLDYEWK HHHHHHHHHCCCEEE	43.77	25953088
429	Ubiquitination	AEVCRAIKQLDYEWK HHHHHHHHHCCCEEE	43.77	29967540
431	Ubiquitination	VCRAIKQLDYEWKVV HHHHHHHCCCEEEEE	6.86	21963094
441	Phosphorylation	EWKVVNPYYLRVRRK EEEEECCEEEEEEEC	15.21	51241
442	Phosphorylation	WKVVNPYYLRVRRKN EEEECCEEEEEEECC	6.84	51247
444	Ubiquitination	VVNPYYLRVRRKNPV EECCEEEEEEECCCC	12.08	29967540
444 (in isoform 2)	Ubiquitination	-	12.08	-
446	Ubiquitination	NPYYLRVRRKNPVTS CCEEEEEEECCCCCC	37.10	21963094
448	Ubiquitination	YYLRVRRKNPVTSTY EEEEEEECCCCCCCC	55.85	29967540
457	Ubiquitination	PVTSTYSKMSLQLYQ CCCCCCEEEEEEEEE	23.30	21963094
459	Ubiquitination	TSTYSKMSLQLYQVD CCCCEEEEEEEEEEC	19.39	21963094
463	Phosphorylation	SKMSLQLYQVDSRTY EEEEEEEEEECCCEE	8.11	8391907
463	Ubiquitination	SKMSLQLYQVDSRTY EEEEEEEEEECCCEE	8.11	29967540
467	Phosphorylation	LQLYQVDSRTYLLDF EEEEEECCCEEEEEE	27.89	19060867
472	Ubiquitination	VDSRTYLLDFRSIDD ECCCEEEEEECCCCH	4.05	21963094
473	Phosphorylation	DSRTYLLDFRSIDDE CCCEEEEEECCCCHH	34.03	18669648
474	Ubiquitination	SRTYLLDFRSIDDEI CCEEEEEECCCCHHH	7.14	21963094
476	Phosphorylation	TYLLDFRSIDDEITE EEEEEECCCCHHHHC	30.29	28176443
476 (in isoform 1)	Ubiquitination	-	30.29	21906983
477	Phosphorylation	YLLDFRSIDDEITEA EEEEECCCCHHHHCC	7.25	18669648
479	Phosphorylation	LDFRSIDDEITEAKS EEECCCCHHHHCCCC	47.75	18669648
481	Phosphorylation	FRSIDDEITEAKSGT ECCCCHHHHCCCCCC	5.62	18669648
482	Phosphorylation	RSIDDEITEAKSGTA CCCCHHHHCCCCCCC	28.04	28176443
485	Ubiquitination	DDEITEAKSGTATPQ CHHHHCCCCCCCCCC	43.09	21906983
486	Phosphorylation	DEITEAKSGTATPQR HHHHCCCCCCCCCCC	48.72	22322096
487	Phosphorylation	EITEAKSGTATPQRS HHHCCCCCCCCCCCC	20.75	18669648
488	Phosphorylation	ITEAKSGTATPQRSG HHCCCCCCCCCCCCC	34.15	22322096
490	Phosphorylation	EAKSGTATPQRSGSV CCCCCCCCCCCCCCC	21.57	22322096
491 (in isoform 2)	Ubiquitination	-	25.73	21906983
494	Phosphorylation	GTATPQRSGSVSNYR CCCCCCCCCCCCCCC	30.12	25159151
496	Phosphorylation	ATPQRSGSVSNYRSC CCCCCCCCCCCCCCC	24.50	22322096
498	Phosphorylation	PQRSGSVSNYRSCQR CCCCCCCCCCCCCCC	29.82	21955146
500	Phosphorylation	RSGSVSNYRSCQRSD CCCCCCCCCCCCCCC	9.08	27362937
500	Ubiquitination	RSGSVSNYRSCQRSD CCCCCCCCCCCCCCC	9.08	21963094
500 (in isoform 2)	Ubiquitination	-	9.08	-
501	Phosphorylation	SGSVSNYRSCQRSDS CCCCCCCCCCCCCCC	34.90	27251275
502	Phosphorylation	GSVSNYRSCQRSDSD CCCCCCCCCCCCCCC	12.30	26552605
503	Phosphorylation	SVSNYRSCQRSDSDA CCCCCCCCCCCCCCH	2.63	27251275
506	Phosphorylation	NYRSCQRSDSDAEAQ CCCCCCCCCCCHHHC	18.65	8546373
508	Phosphorylation	RSCQRSDSDAEAQGK CCCCCCCCCHHHCCC	39.71	28102081
511	Phosphorylation	QRSDSDAEAQGKSSE CCCCCCHHHCCCCCE	46.66	24719451
515	Ubiquitination	SDAEAQGKSSEVSLT CCHHHCCCCCEEEEE	38.43	-
516	Phosphorylation	DAEAQGKSSEVSLTS CHHHCCCCCEEEEEE	38.26	23663014
517	Phosphorylation	AEAQGKSSEVSLTSS HHHCCCCCEEEEEEC	45.57	23663014
520	Phosphorylation	QGKSSEVSLTSSVTS CCCCCEEEEEECCEE	23.13	25072903
521	Phosphorylation	GKSSEVSLTSSVTSL CCCCEEEEEECCEEC	6.95	33259812
522	Phosphorylation	KSSEVSLTSSVTSLD CCCEEEEEECCEECC	16.08	25072903
523	Phosphorylation	SSEVSLTSSVTSLDS CCEEEEEECCEECCC	28.27	30631047
524	Phosphorylation	SEVSLTSSVTSLDSS CEEEEEECCEECCCC	24.95	30631047
526	Phosphorylation	VSLTSSVTSLDSSPV EEEEECCEECCCCCC	26.06	30631047
527	Phosphorylation	SLTSSVTSLDSSPVD EEEECCEECCCCCCC	28.20	30631047
530	Phosphorylation	SSVTSLDSSPVDLTP ECCEECCCCCCCCCC	41.66	25072903
531	Phosphorylation	SVTSLDSSPVDLTPR CCEECCCCCCCCCCC	28.71	23663014
536	Phosphorylation	DSSPVDLTPRPGSHT CCCCCCCCCCCCCCH	16.88	26074081
538	Phosphorylation	SPVDLTPRPGSHTIE CCCCCCCCCCCCHHH	42.87	27251275
541	Phosphorylation	DLTPRPGSHTIEFFE CCCCCCCCCHHHHHH	21.82	26074081
543	Phosphorylation	TPRPGSHTIEFFEMC CCCCCCCHHHHHHHH	24.73	26074081

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
174	T	Phosphorylation	Kinase	AMPK_GROUP	-	PhosphoELM
174	T	Phosphorylation	Kinase	STK11	Q15831	PhosphoELM
183	T	Phosphorylation	Kinase	CAMK2B	Q13554	PSP
183	T	Phosphorylation	Kinase	AMPK-FAMILY	-	GPS
183	T	Phosphorylation	Kinase	LKB1	Q9WTK7	PSP
183	T	Phosphorylation	Kinase	STK11	Q15831	GPS
183	T	Phosphorylation	Kinase	MAP3K11	Q16584	GPS
183	T	Phosphorylation	Kinase	CAMKK2	Q96RR4	Uniprot
183	T	Phosphorylation	Kinase	CAMKK1	Q8N5S9	PSP
183	T	Phosphorylation	Kinase	BRSK1	Q8TDC3-2	GPS
183	T	Phosphorylation	Kinase	BRSK2	Q8IWQ3	PSP
183	T	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
360	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
360	S	Phosphorylation	Kinase	ULK1	O75385	Uniprot
368	T	Phosphorylation	Kinase	ULK1	O75385	Uniprot
388	T	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
482	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
486	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
486	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
490	T	Phosphorylation	Kinase	GSK3A	P49840	PSP
490	T	Phosphorylation	Kinase	GSK3B	P49841	PSP
494	S	Phosphorylation	Kinase	AKT1	P31749	PSP
494	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
496	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
496	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
496	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
496	S	Phosphorylation	Kinase	PKCA	P04409	PSP
496	S	Phosphorylation	Kinase	AKT1	P31749	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM28	Q13263	PMID:25945414

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
183	T	Phosphorylation	14976552
Also phosphorylated at Thr-183 by CAMKK2; triggered by a rise in intracellular calcium ions, without detectable changes in the AMP/ATP ratio.
183	T	Phosphorylation	14976552
CAMKK1 can also phosphorylate Thr-183, but at a much lower level.
183	T	Phosphorylation	14976552
Phosphorylated at Thr-183 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39.

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 AAPK1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MTOR_HUMAN	MTOR	physical	14970221
TSC2_HUMAN	TSC2	physical	14651849
TSC2_HUMAN	TSC2	physical	15261145
FNIP1_HUMAN	FNIP1	physical	17028174
CFTR_HUMAN	CFTR	physical	10862786
IF2P_HUMAN	EIF5B	physical	20562859
AAKG1_HUMAN	PRKAG1	physical	20562859
SP16H_HUMAN	SUPT16H	physical	20562859
FXR2_HUMAN	FXR2	physical	20562859
PA2G4_HUMAN	PA2G4	physical	20562859
SND1_HUMAN	SND1	physical	20562859
G3BP1_HUMAN	G3BP1	physical	20562859
PARP1_HUMAN	PARP1	physical	20562859
FMR1_HUMAN	FMR1	physical	20562859
AAKB2_HUMAN	PRKAB2	physical	20562859
AAKB1_HUMAN	PRKAB1	physical	20562859
RL35_HUMAN	RPL35	physical	20562859
HS90A_HUMAN	HSP90AA1	physical	16306228
HSP74_HUMAN	HSPA4	physical	16306228
TBA1A_HUMAN	TUBA1A	physical	16306228
CDC37_HUMAN	CDC37	physical	16306228
AAKB1_HUMAN	PRKAB1	physical	16306228
AAKG1_HUMAN	PRKAG1	physical	16306228
AAKB2_HUMAN	PRKAB2	physical	16306228
SIK3_HUMAN	SIK3	physical	16306228
1433Z_HUMAN	YWHAZ	physical	16306228
1433E_HUMAN	YWHAE	physical	16306228
SIK1_HUMAN	SIK1	physical	16306228
SIK2_HUMAN	SIK2	physical	16306228
TERA_HUMAN	VCP	physical	16306228
2AAB_HUMAN	PPP2R1B	physical	16306228
PP2AA_HUMAN	PPP2CA	physical	16306228
UBP2_HUMAN	USP2	physical	16306228
NUAK1_HUMAN	NUAK1	physical	16306228
NUAK2_HUMAN	NUAK2	physical	16306228
BRSK1_HUMAN	BRSK1	physical	16306228
BRSK2_HUMAN	BRSK2	physical	16306228
MARK1_HUMAN	MARK1	physical	16306228
MARK2_HUMAN	MARK2	physical	16306228
MARK3_HUMAN	MARK3	physical	16306228
MARK4_HUMAN	MARK4	physical	16306228
SNRK_HUMAN	SNRK	physical	16306228
CFTR_HUMAN	CFTR	physical	20861072
PSD11_HUMAN	PSMD11	physical	19616115
CRBN_HUMAN	CRBN	physical	21232561
AAKB1_HUMAN	PRKAB1	physical	21232561
AAKG1_HUMAN	PRKAG1	physical	21232561
EPM2A_HUMAN	EPM2A	physical	21728993
RPTOR_HUMAN	RPTOR	physical	18439900
HDAC5_HUMAN	HDAC5	physical	22462548
CRTC2_HUMAN	CRTC2	physical	22462548
ABI1_HUMAN	ABI1	physical	20368287
SDE2_MOUSE	Sde2	physical	20368287
MTFR2_MOUSE	Mtfr2	physical	20368287
XRN2_MOUSE	Xrn2	physical	20368287
ABI1_MOUSE	Abi1	physical	20368287
AAKG1_MOUSE	Prkag1	physical	20368287
AAKG2_MOUSE	Prkag2	physical	20368287
CHERP_MOUSE	Cherp	physical	20368287
EMIL1_MOUSE	Emilin1	physical	20368287
RHG22_MOUSE	Arhgap22	physical	20368287
LZTS2_MOUSE	Lzts2	physical	20368287
MAGD1_MOUSE	Maged1	physical	20368287
NAB2_MOUSE	Nab2	physical	20368287
NRBF2_MOUSE	Nrbf2	physical	20368287
AAKB1_MOUSE	Prkab1	physical	20368287
RC3H1_MOUSE	Rc3h1	physical	20368287
SRBS1_MOUSE	Sorbs1	physical	20368287
TFPT_MOUSE	Tfpt	physical	20368287
THAP7_MOUSE	Thap7	physical	20368287
TRIP6_MOUSE	Trip6	physical	20368287
CBPE_HUMAN	CPE	physical	20368287
APT_MOUSE	Aprt	physical	20368287
BHE40_MOUSE	Bhlhe40	physical	20368287
CBPE_MOUSE	Cpe	physical	20368287
HSPB1_MOUSE	Hspb1	physical	20368287
KIF1C_MOUSE	Kif1c	physical	20368287
NEDD1_MOUSE	Nedd1	physical	20368287
AAKB2_HUMAN	PRKAB2	physical	21988832
MDM4_HUMAN	MDM4	physical	24190973
AAKB2_HUMAN	PRKAB2	physical	23455922
HS90A_HUMAN	HSP90AA1	physical	23455922
HS90B_HUMAN	HSP90AB1	physical	23455922
AAKG1_HUMAN	PRKAG1	physical	23455922
ACACA_HUMAN	ACACA	physical	23455922
FKBP5_HUMAN	FKBP5	physical	23455922
AAKG2_HUMAN	PRKAG2	physical	23455922
AAKB1_HUMAN	PRKAB1	physical	23455922
ACACA_HUMAN	ACACA	physical	18480843
P53_MOUSE	Trp53	physical	15866171
AAKB1_HUMAN	PRKAB1	physical	8621713
AAKG1_HUMAN	PRKAG1	physical	8621713
AAKB1_HUMAN	PRKAB1	physical	8663446
AAKG1_HUMAN	PRKAG1	physical	8663446
AAKB2_HUMAN	PRKAB2	physical	25416956
AAKG1_HUMAN	PRKAG1	physical	25416956
TRI27_HUMAN	TRIM27	physical	25416956
VPS52_HUMAN	VPS52	physical	25416956
TRIP6_HUMAN	TRIP6	physical	25416956
BHE40_HUMAN	BHLHE40	physical	25416956
ZBED1_HUMAN	ZBED1	physical	25416956
ABI2_HUMAN	ABI2	physical	25416956
RBPMS_HUMAN	RBPMS	physical	25416956
IKZF3_HUMAN	IKZF3	physical	25416956
MTUS2_HUMAN	MTUS2	physical	25416956
FSBP_HUMAN	RAD54B	physical	25416956
RA54B_HUMAN	RAD54B	physical	25416956
ROP1A_HUMAN	ROPN1	physical	25416956
THAP1_HUMAN	THAP1	physical	25416956
HOMEZ_HUMAN	HOMEZ	physical	25416956
HMBX1_HUMAN	HMBOX1	physical	25416956
VP37B_HUMAN	VPS37B	physical	25416956
T22D4_HUMAN	TSC22D4	physical	25416956
LMBL3_HUMAN	L3MBTL3	physical	25416956
RIM3A_HUMAN	RIMBP3	physical	25416956
UBX11_HUMAN	UBXN11	physical	25416956
PNMA5_HUMAN	PNMA5	physical	25416956
ADIP_HUMAN	SSX2IP	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
RFX6_HUMAN	RFX6	physical	25416956
IN80E_HUMAN	INO80E	physical	25416956
TXNIP_HUMAN	TXNIP	physical	23453806
EP300_HUMAN	EP300	physical	21567395
PPM1F_HUMAN	PPM1F	physical	20801214
FKBP5_HUMAN	FKBP5	physical	25852190
AAKB1_HUMAN	PRKAB1	physical	25852190
AAKB2_HUMAN	PRKAB2	physical	25852190
AAKG1_HUMAN	PRKAG1	physical	25852190
SUN2_HUMAN	SUN2	physical	25852190
UBP10_HUMAN	USP10	physical	26876938
FANCG_HUMAN	FANCG	physical	27449087
FANCA_HUMAN	FANCA	physical	27449087
GLI1_HUMAN	GLI1	physical	28562331
CYC_BOVIN	CYCS	physical	27758862

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
DB00945	Acetylsalicylic acid
DB00131	Adenosine monophosphate
DB00171	Adenosine triphosphate
DB00914	Phenformin

Regulatory Network of AAPK1_HUMAN

Related Literatures of Post-Translational Modification

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 THR-32; THR-183; SER-184;SER-187; THR-355; SER-356; SER-397; TYR-441; SER-467; SER-476;SER-486; THR-488; THR-490; SER-496; SER-502; SER-506; SER-508;SER-516; SER-520; THR-522; SER-523; SER-524 AND SER-527, AND MASSSPECTROMETRY.	19369195 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; THR-382; SER-486;THR-490 AND SER-496, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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 SER-356; SER-486; THR-490;SER-496; SER-508; SER-523 AND SER-527, AND MASS SPECTROMETRY.	18691976 [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-496, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496, AND MASSSPECTROMETRY.	16083285 [Abstract]
"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 THR-382 AND THR-490, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-382, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-442, AND MASSSPECTROMETRY.	18083107 [Abstract]

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