dbPTM

KS6A1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KS6A1_HUMAN
UniProt AC	Q15418
Protein Name	Ribosomal protein S6 kinase alpha-1
Gene Name	RPS6KA1
Organism	Homo sapiens (Human).
Sequence Length	735
Subcellular Localization	Nucleus. Cytoplasm.
Protein Description	Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1, which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the pre-initiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4). Mediates induction of hepatocyte prolifration by TGFA through phosphorylation of CEBPB (By similarity). Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression. Phosphorylates EPHA2 at 'Ser-897', the RPS6KA-EPHA2 signaling pathway controls cell migration. [PubMed: 26158630]
Protein Sequence	MPLAQLKEPWPLMELVPLDPENGQTSGEEAGLQPSKDEGVLKEISITHHVKAGSEKADPSHFELLKVLGQGSFGKVFLVRKVTRPDSGHLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFVVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALGLDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEAIDHEKKAYSFCGTVEYMAPEVVNRQGHSHSADWWSYGVLMFEMLTGSLPFQGKDRKETMTLILKAKLGMPQFLSTEAQSLLRALFKRNPANRLGSGPDGAEEIKRHVFYSTIDWNKLYRREIKPPFKPAVAQPDDTFYFDTEFTSRTPKDSPGIPPSAGAHQLFRGFSFVATGLMEDDGKPRAPQAPLHSVVQQLHGKNLVFSDGYVVKETIGVGSYSECKRCVHKATNMEYAVKVIDKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKHVYLVTELMRGGELLDKILRQKFFSEREASFVLHTIGKTVEYLHSQGVVHRDLKPSNILYVDESGNPECLRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANGPSDTPEEILTRIGSGKFTLSGGNWNTVSETAKDLVSKMLHVDPHQRLTAKQVLQHPWVTQKDKLPQSQLSHQDLQLVKGAMAATYSALNSSKPTPQLKPIESSILAQRRVRKLPSTTL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
21	Methylation	ELVPLDPENGQTSGE EEEECCCCCCCCCCC	73.91	-
25	Phosphorylation	LDPENGQTSGEEAGL CCCCCCCCCCCCCCC	39.85	18691976
26	Phosphorylation	DPENGQTSGEEAGLQ CCCCCCCCCCCCCCC	36.00	28102081
28	Phosphorylation	ENGQTSGEEAGLQPS CCCCCCCCCCCCCCC	44.43	-
28 (in isoform 2)	Phosphorylation	-	44.43	28450419
30	Phosphorylation	GQTSGEEAGLQPSKD CCCCCCCCCCCCCCC	21.50	-
30 (in isoform 2)	Phosphorylation	-	21.50	28450419
31	Phosphorylation	QTSGEEAGLQPSKDE CCCCCCCCCCCCCCC	28.29	-
31 (in isoform 2)	Phosphorylation	-	28.29	28450419
35	Ubiquitination	EEAGLQPSKDEGVLK CCCCCCCCCCCCCCE	39.52	29967540
40	Ubiquitination	QPSKDEGVLKEISIT CCCCCCCCCEEEEEE	6.94	29967540
45	Phosphorylation	EGVLKEISITHHVKA CCCCEEEEEEEEEEC	23.64	26657352
47	Phosphorylation	VLKEISITHHVKAGS CCEEEEEEEEEECCC	10.11	29514088
50	Ubiquitination	EISITHHVKAGSEKA EEEEEEEEECCCCCC	3.36	21890473
51	Ubiquitination	ISITHHVKAGSEKAD EEEEEEEECCCCCCC	42.55	29967540
54	Phosphorylation	THHVKAGSEKADPSH EEEEECCCCCCCHHH	40.56	28450419
56	Acetylation	HVKAGSEKADPSHFE EEECCCCCCCHHHHH	60.84	25953088
56	Ubiquitination	HVKAGSEKADPSHFE EEECCCCCCCHHHHH	60.84	29967540
59	Ubiquitination	AGSEKADPSHFELLK CCCCCCCHHHHHHHH	34.27	21890473
60	Phosphorylation	GSEKADPSHFELLKV CCCCCCHHHHHHHHH	41.16	20873877
60 (in isoform 2)	Ubiquitination	-	41.16	-
65	Ubiquitination	DPSHFELLKVLGQGS CHHHHHHHHHHCCCC	2.58	29967540
65 (in isoform 2)	Ubiquitination	-	2.58	-
66	Ubiquitination	PSHFELLKVLGQGSF HHHHHHHHHHCCCCC	48.30	22817900
72	Phosphorylation	LKVLGQGSFGKVFLV HHHHCCCCCCEEEEE	23.96	20873877
75	Ubiquitination	LGQGSFGKVFLVRKV HCCCCCCEEEEEEEE	28.01	21890473
75	Ubiquitination	LGQGSFGKVFLVRKV HCCCCCCEEEEEEEE	28.01	21890473
75	Acetylation	LGQGSFGKVFLVRKV HCCCCCCEEEEEEEE	28.01	88639
75	Ubiquitination	LGQGSFGKVFLVRKV HCCCCCCEEEEEEEE	28.01	22817900
75 (in isoform 2)	Ubiquitination	-	28.01	-
78	Ubiquitination	GSFGKVFLVRKVTRP CCCCEEEEEEEEECC	4.00	29967540
81	Phosphorylation	GKVFLVRKVTRPDSG CEEEEEEEEECCCCC	40.24	24719451
81	Ubiquitination	GKVFLVRKVTRPDSG CEEEEEEEEECCCCC	40.24	29967540
83	Phosphorylation	VFLVRKVTRPDSGHL EEEEEEEECCCCCCE	39.25	25954137
84	Ubiquitination	FLVRKVTRPDSGHLY EEEEEEECCCCCCEE	35.70	21890473
84	Ubiquitination	FLVRKVTRPDSGHLY EEEEEEECCCCCCEE	35.70	21890473
84	Ubiquitination	FLVRKVTRPDSGHLY EEEEEEECCCCCCEE	35.70	21890473
84 (in isoform 2)	Ubiquitination	-	35.70	-
87	Phosphorylation	RKVTRPDSGHLYAMK EEEECCCCCCEEEHH	30.69	22210691
90	Ubiquitination	TRPDSGHLYAMKVLK ECCCCCCEEEHHHHH	3.13	29967540
91	Phosphorylation	RPDSGHLYAMKVLKK CCCCCCEEEHHHHHH	10.04	25954137
94	Ubiquitination	SGHLYAMKVLKKATL CCCEEEHHHHHHCCC	35.92	29967540
103	Ubiquitination	LKKATLKVRDRVRTK HHHCCCHHHHHHHHH	9.65	29967540
138	Phosphorylation	FQTEGKLYLILDFLR EECCCEEEEEEHHHH	8.65	-
154	Phosphorylation	GDLFTRLSKEVMFTE CCHHHHHCCCCCCCH	24.39	12618428
160	Phosphorylation	LSKEVMFTEEDVKFY HCCCCCCCHHHHHHH	21.99	22210691
163	Phosphorylation	EVMFTEEDVKFYLAE CCCCCHHHHHHHHHH	42.55	-
186	Ubiquitination	HSLGIIYRDLKPENI HHCCEEECCCCHHHE	32.17	21890473
189	Ubiquitination	GIIYRDLKPENILLD CEEECCCCHHHEEEC	55.35	-
194	Ubiquitination	DLKPENILLDEEGHI CCCHHHEEECCCCCE	8.11	29967540
204	Phosphorylation	EEGHIKLTDFGLSKE CCCCEEECCCCCCHH	25.04	23312004
205	Phosphorylation	EGHIKLTDFGLSKEA CCCEEECCCCCCHHH	46.16	32142685
209	Phosphorylation	KLTDFGLSKEAIDHE EECCCCCCHHHHCCC	28.91	23312004
210	Ubiquitination	LTDFGLSKEAIDHEK ECCCCCCHHHHCCCH	57.09	29967540
219	Ubiquitination	AIDHEKKAYSFCGTV HHCCCHHHHHCCCCC	19.10	29967540
220	Phosphorylation	IDHEKKAYSFCGTVE HCCCHHHHHCCCCCC	15.91	22322096
221	Phosphorylation	DHEKKAYSFCGTVEY CCCHHHHHCCCCCCC	20.94	22322096
225	Phosphorylation	KAYSFCGTVEYMAPE HHHHCCCCCCCCCHH	16.02	22322096
228	Phosphorylation	SFCGTVEYMAPEVVN HCCCCCCCCCHHHHC	8.34	23927012
229	Phosphorylation	FCGTVEYMAPEVVNR CCCCCCCCCHHHHCC	2.95	-
230	Phosphorylation	CGTVEYMAPEVVNRQ CCCCCCCCHHHHCCC	9.01	24719451
234	Phosphorylation	EYMAPEVVNRQGHSH CCCCHHHHCCCCCCC	4.69	32645325
237	Phosphorylation	APEVVNRQGHSHSAD CHHHHCCCCCCCCCC	49.07	-
260	Ubiquitination	FEMLTGSLPFQGKDR HHHHHCCCCCCCCCH	5.36	22817900
262	Ubiquitination	MLTGSLPFQGKDRKE HHHCCCCCCCCCHHH	21.23	21890473
272	O-linked_Glycosylation	KDRKETMTLILKAKL CCHHHHHHHHHHHHH	20.33	30379171
276	Ubiquitination	ETMTLILKAKLGMPQ HHHHHHHHHHHCCCH	36.16	22817900
278	Ubiquitination	MTLILKAKLGMPQFL HHHHHHHHHCCCHHH	43.94	21890473
285	Ubiquitination	KLGMPQFLSTEAQSL HHCCCHHHCHHHHHH	5.36	22817900
287	Ubiquitination	GMPQFLSTEAQSLLR CCCHHHCHHHHHHHH	37.17	21890473
287	Ubiquitination	GMPQFLSTEAQSLLR CCCHHHCHHHHHHHH	37.17	21890473
287	Ubiquitination	GMPQFLSTEAQSLLR CCCHHHCHHHHHHHH	37.17	21890473
287 (in isoform 2)	Ubiquitination	-	37.17	-
291	Phosphorylation	FLSTEAQSLLRALFK HHCHHHHHHHHHHHH	36.10	24719451
300	Ubiquitination	LRALFKRNPANRLGS HHHHHHHCHHHCCCC	40.40	21906983
300	Ubiquitination	LRALFKRNPANRLGS HHHHHHHCHHHCCCC	40.40	27667366
307	Phosphorylation	NPANRLGSGPDGAEE CHHHCCCCCCCCHHH	52.31	28857561
316	Phosphorylation	PDGAEEIKRHVFYST CCCHHHHHHHHEEEE	39.47	24719451
316	Ubiquitination	PDGAEEIKRHVFYST CCCHHHHHHHHEEEE	39.47	27667366
319	Ubiquitination	AEEIKRHVFYSTIDW HHHHHHHHEEEECCH	5.82	29967540
321	Phosphorylation	EIKRHVFYSTIDWNK HHHHHHEEEECCHHH	12.10	26074081
322	Phosphorylation	IKRHVFYSTIDWNKL HHHHHEEEECCHHHH	13.86	26074081
323	Phosphorylation	KRHVFYSTIDWNKLY HHHHEEEECCHHHHH	16.15	26074081
323	Ubiquitination	KRHVFYSTIDWNKLY HHHHEEEECCHHHHH	16.15	29967540
325	Ubiquitination	HVFYSTIDWNKLYRR HHEEEECCHHHHHHC	42.88	27667366
325 (in isoform 2)	Ubiquitination	-	42.88	-
330	Phosphorylation	TIDWNKLYRREIKPP ECCHHHHHHCCCCCC	14.83	26074081
335	Ubiquitination	KLYRREIKPPFKPAV HHHHCCCCCCCCCCC	41.71	29967540
339	Ubiquitination	REIKPPFKPAVAQPD CCCCCCCCCCCCCCC	37.53	29967540
344	Ubiquitination	PFKPAVAQPDDTFYF CCCCCCCCCCCCEEE	35.04	29967540
347	Phosphorylation	PAVAQPDDTFYFDTE CCCCCCCCCEEECCC	45.45	32645325
348	Phosphorylation	AVAQPDDTFYFDTEF CCCCCCCCEEECCCC	27.84	19060867
348	Ubiquitination	AVAQPDDTFYFDTEF CCCCCCCCEEECCCC	27.84	29967540
353	Phosphorylation	DDTFYFDTEFTSRTP CCCEEECCCCCCCCC	24.09	33259812
356	Phosphorylation	FYFDTEFTSRTPKDS EEECCCCCCCCCCCC	15.86	26074081
357	Phosphorylation	YFDTEFTSRTPKDSP EECCCCCCCCCCCCC	39.20	26074081
359	Phosphorylation	DTEFTSRTPKDSPGI CCCCCCCCCCCCCCC	34.16	22167270
363	Phosphorylation	TSRTPKDSPGIPPSA CCCCCCCCCCCCCCC	31.02	22167270
368	Phosphorylation	KDSPGIPPSAGAHQL CCCCCCCCCCCHHHH	34.59	24719451
369	Phosphorylation	DSPGIPPSAGAHQLF CCCCCCCCCCHHHHH	33.70	23927012
372	Phosphorylation	GIPPSAGAHQLFRGF CCCCCCCHHHHHCCC	6.23	32645325
378	Phosphorylation	GAHQLFRGFSFVATG CHHHHHCCCEEEEEC	18.40	33259812
380	Phosphorylation	HQLFRGFSFVATGLM HHHHCCCEEEEECCC	22.95	22322096
384	Phosphorylation	RGFSFVATGLMEDDG CCCEEEEECCCCCCC	26.08	30266825
389	Phosphorylation	VATGLMEDDGKPRAP EEECCCCCCCCCCCC	56.87	27251275
392	Ubiquitination	GLMEDDGKPRAPQAP CCCCCCCCCCCCCCC	38.02	-
401 (in isoform 2)	Ubiquitination	-	19.93	-
402	Phosphorylation	APQAPLHSVVQQLHG CCCCCHHHHHHHHCC	31.50	28857561
405	Ubiquitination	APLHSVVQQLHGKNL CCHHHHHHHHCCCCC	37.65	29967540
408	Ubiquitination	HSVVQQLHGKNLVFS HHHHHHHCCCCCEEC	40.62	21890473
410	Ubiquitination	VVQQLHGKNLVFSDG HHHHHCCCCCEECCC	36.04	-
415	Phosphorylation	HGKNLVFSDGYVVKE CCCCCEECCCEEEEE	23.73	20068231
417	Ubiquitination	KNLVFSDGYVVKETI CCCEECCCEEEEEEE	18.88	29967540
419 (in isoform 2)	Ubiquitination	-	6.40	-
421	Ubiquitination	FSDGYVVKETIGVGS ECCCEEEEEEECCCC	38.81	29967540
422	Ubiquitination	SDGYVVKETIGVGSY CCCEEEEEEECCCCH	33.76	29967540
430	Ubiquitination	TIGVGSYSECKRCVH EECCCCHHHHHHHHH	37.91	29967540
433	Acetylation	VGSYSECKRCVHKAT CCCHHHHHHHHHHHC	44.79	26051181
433	Ubiquitination	VGSYSECKRCVHKAT CCCHHHHHHHHHHHC	44.79	29967540
438	Ubiquitination	ECKRCVHKATNMEYA HHHHHHHHHCCHHHH	36.19	29967540
442	Ubiquitination	CVHKATNMEYAVKVI HHHHHCCHHHHHEEH	3.46	29967540
442 (in isoform 2)	Ubiquitination	-	3.46	-
447	Ubiquitination	TNMEYAVKVIDKSKR CCHHHHHEEHHHHCC	25.87	29967540
453	Ubiquitination	VKVIDKSKRDPSEEI HEEHHHHCCCHHHHH	67.57	-
460	Ubiquitination	KRDPSEEIEILLRYG CCCHHHHHHHHHHHC	3.33	29967540
462 (in isoform 2)	Ubiquitination	-	5.58	-
466	Phosphorylation	EIEILLRYGQHPNII HHHHHHHHCCCCCEE	22.55	20071362
474	Phosphorylation	GQHPNIITLKDVYDD CCCCCEEEEEECCCC	24.77	20071362
476	Ubiquitination	HPNIITLKDVYDDGK CCCEEEEEECCCCCC	36.18	29967540
484	Ubiquitination	DVYDDGKHVYLVTEL ECCCCCCEEEEEEEH	20.98	21890473
485	Ubiquitination	VYDDGKHVYLVTELM CCCCCCEEEEEEEHH	4.50	29967540
486	Phosphorylation	YDDGKHVYLVTELMR CCCCCEEEEEEEHHH	8.65	20860994
489	Phosphorylation	GKHVYLVTELMRGGE CCEEEEEEEHHHCHH	22.32	20860994
489	Ubiquitination	GKHVYLVTELMRGGE CCEEEEEEEHHHCHH	22.32	22817900
500	Ubiquitination	RGGELLDKILRQKFF HCHHHHHHHHHHHCC	43.54	21906983
505	Ubiquitination	LDKILRQKFFSEREA HHHHHHHHCCCHHHH	41.78	22817900
509	Ubiquitination	LRQKFFSEREASFVL HHHHCCCHHHHHHHH	49.75	21890473
509	Ubiquitination	LRQKFFSEREASFVL HHHHCCCHHHHHHHH	49.75	21890473
509	Ubiquitination	LRQKFFSEREASFVL HHHHCCCHHHHHHHH	49.75	21890473
513	Phosphorylation	FFSEREASFVLHTIG CCCHHHHHHHHHHHH	15.90	20873877
514	Ubiquitination	FSEREASFVLHTIGK CCHHHHHHHHHHHHH	9.75	22817900
521	Ubiquitination	FVLHTIGKTVEYLHS HHHHHHHHHHHHHHH	45.61	29967540
522	Phosphorylation	VLHTIGKTVEYLHSQ HHHHHHHHHHHHHHC	17.23	27251275
537	Ubiquitination	GVVHRDLKPSNILYV CCCCCCCCHHHEEEE	51.17	29967540
546	Ubiquitination	SNILYVDESGNPECL HHEEEECCCCCHHHE	50.96	32015554
546 (in isoform 2)	Ubiquitination	-	50.96	-
562	Ubiquitination	ICDFGFAKQLRAENG ECCHHHHHHHHHHCC	47.83	21890473
562	Ubiquitination	ICDFGFAKQLRAENG ECCHHHHHHHHHHCC	47.83	24816145
571	Ubiquitination	LRAENGLLMTPCYTA HHHHCCCEECCCEEC	3.68	21963094
573	Phosphorylation	AENGLLMTPCYTANF HHCCCEECCCEECCC	15.35	21945579
576	Phosphorylation	GLLMTPCYTANFVAP CCEECCCEECCCCCH	15.30	21945579
577	Phosphorylation	LLMTPCYTANFVAPE CEECCCEECCCCCHH	23.11	21945579
582	Phosphorylation	CYTANFVAPEVLKRQ CEECCCCCHHHHHHC	7.15	27251275
585	Phosphorylation	ANFVAPEVLKRQGYD CCCCCHHHHHHCCCC	8.11	-
586	Phosphorylation	NFVAPEVLKRQGYDE CCCCHHHHHHCCCCC	3.45	-
587	Acetylation	FVAPEVLKRQGYDEG CCCHHHHHHCCCCCC	48.10	26051181
587	Ubiquitination	FVAPEVLKRQGYDEG CCCHHHHHHCCCCCC	48.10	21963094
591	Phosphorylation	EVLKRQGYDEGCDIW HHHHHCCCCCCCCHH	11.50	22468782
596	Ubiquitination	QGYDEGCDIWSLGIL CCCCCCCCHHHHHHH	57.14	21963094
619	Phosphorylation	TPFANGPSDTPEEIL CCCCCCCCCCHHHHH	56.36	26657352
621	Phosphorylation	FANGPSDTPEEILTR CCCCCCCCHHHHHHH	36.62	20071362
631	Phosphorylation	EILTRIGSGKFTLSG HHHHHHHCCEEEECC	36.12	28857561
633	Ubiquitination	LTRIGSGKFTLSGGN HHHHHCCEEEECCCC	36.55	22817900
635	Phosphorylation	RIGSGKFTLSGGNWN HHHCCEEEECCCCCH	24.41	28450419
637	Phosphorylation	GSGKFTLSGGNWNTV HCCEEEECCCCCHHH	41.41	28450419
638	Ubiquitination	SGKFTLSGGNWNTVS CCEEEECCCCCHHHH	36.24	21890473
642 (in isoform 2)	Ubiquitination	-	34.30	-
643	Phosphorylation	LSGGNWNTVSETAKD ECCCCCHHHHHHHHH	19.61	28857561
646	Phosphorylation	GNWNTVSETAKDLVS CCCHHHHHHHHHHHH	48.74	27251275
647	Phosphorylation	NWNTVSETAKDLVSK CCHHHHHHHHHHHHH	31.34	20071362
649	Ubiquitination	NTVSETAKDLVSKML HHHHHHHHHHHHHHC	60.04	22817900
651	Ubiquitination	VSETAKDLVSKMLHV HHHHHHHHHHHHCCC	4.64	32015554
654	Ubiquitination	TAKDLVSKMLHVDPH HHHHHHHHHCCCCHH	37.69	21906983
658	Ubiquitination	LVSKMLHVDPHQRLT HHHHHCCCCHHHCCC	12.32	22817900
658 (in isoform 2)	Ubiquitination	-	12.32	-
662	Ubiquitination	MLHVDPHQRLTAKQV HCCCCHHHCCCHHHH	47.68	29967540
663	Ubiquitination	LHVDPHQRLTAKQVL CCCCHHHCCCHHHHH	30.85	21890473
663	Ubiquitination	LHVDPHQRLTAKQVL CCCCHHHCCCHHHHH	30.85	21890473
663	Ubiquitination	LHVDPHQRLTAKQVL CCCCHHHCCCHHHHH	30.85	21890473
663 (in isoform 2)	Ubiquitination	-	30.85	-
664	Ubiquitination	HVDPHQRLTAKQVLQ CCCHHHCCCHHHHHC	4.37	29967540
667	Ubiquitination	PHQRLTAKQVLQHPW HHHCCCHHHHHCCCC	35.39	32015554
676	Ubiquitination	VLQHPWVTQKDKLPQ HHCCCCCCCCCCCCH	26.49	32015554
676 (in isoform 2)	Ubiquitination	-	26.49	-
678	Ubiquitination	QHPWVTQKDKLPQSQ CCCCCCCCCCCCHHH	47.68	29967540
680	Ubiquitination	PWVTQKDKLPQSQLS CCCCCCCCCCHHHCC	69.93	29967540
684	Phosphorylation	QKDKLPQSQLSHQDL CCCCCCHHHCCHHHH	31.02	25159151
687	Phosphorylation	KLPQSQLSHQDLQLV CCCHHHCCHHHHHHH	16.09	26657352
687	Ubiquitination	KLPQSQLSHQDLQLV CCCHHHCCHHHHHHH	16.09	29967540
689	Ubiquitination	PQSQLSHQDLQLVKG CHHHCCHHHHHHHHH	50.13	29967540
693	Ubiquitination	LSHQDLQLVKGAMAA CCHHHHHHHHHHHHH	5.82	29967540
696	Phosphorylation	QDLQLVKGAMAATYS HHHHHHHHHHHHHHH	17.07	24719451
701	Phosphorylation	VKGAMAATYSALNSS HHHHHHHHHHHHHCC	14.42	28796482
702	Phosphorylation	KGAMAATYSALNSSK HHHHHHHHHHHHCCC	6.29	28796482
703	Phosphorylation	GAMAATYSALNSSKP HHHHHHHHHHHCCCC	23.17	28796482
707	Phosphorylation	ATYSALNSSKPTPQL HHHHHHHCCCCCCCC	40.36	29978859
708	Phosphorylation	TYSALNSSKPTPQLK HHHHHHCCCCCCCCC	41.40	29978859
709	Ubiquitination	YSALNSSKPTPQLKP HHHHHCCCCCCCCCC	53.37	29967540
711	Phosphorylation	ALNSSKPTPQLKPIE HHHCCCCCCCCCCCC	27.66	24719451
715	Acetylation	SKPTPQLKPIESSIL CCCCCCCCCCCHHHH	38.41	26051181
718	Ubiquitination	TPQLKPIESSILAQR CCCCCCCCHHHHHHH	47.13	29967540
719	Phosphorylation	PQLKPIESSILAQRR CCCCCCCHHHHHHHH	24.33	28857561
720	Phosphorylation	QLKPIESSILAQRRV CCCCCCHHHHHHHHH	14.61	28857561
732	Phosphorylation	RRVRKLPSTTL---- HHHHCCCCCCC----	44.45	23401153
733	Phosphorylation	RVRKLPSTTL----- HHHCCCCCCC-----	30.12	30266825
734	O-linked_Glycosylation	VRKLPSTTL------ HHCCCCCCC------	34.50	30379171
734	Phosphorylation	VRKLPSTTL------ HHCCCCCCC------	34.50	30266825
741	Phosphorylation	TL------------- CC-------------		-
742	Phosphorylation	L-------------- C--------------		-
743	Phosphorylation	--------------- ---------------		24719451

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
221	S	Phosphorylation	Kinase	PDK1	Q15118	GPS
221	S	Phosphorylation	Kinase	PDK1	O15530	PSP
221	S	Phosphorylation	Kinase	RSK-SUBFAMILY	-	GPS
221	S	Phosphorylation	Kinase	RSK_GROUP	-	PhosphoELM
359	T	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
359	T	Phosphorylation	Kinase	MAPK_GROUP	-	PhosphoELM
363	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
363	S	Phosphorylation	Kinase	MAPK_GROUP	-	PhosphoELM
380	S	Phosphorylation	Kinase	MAP3K8	P41279	GPS
573	T	Phosphorylation	Kinase	ERK2	P28482	PSP
573	T	Phosphorylation	Kinase	MAPK1	P63086	GPS
573	T	Phosphorylation	Kinase	MAPK3	P21708	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
221	S	Phosphorylation	9430688
Activated by phosphorylation at Ser-221 by PDPK1.
359	T	Phosphorylation	9430688
May be phosphorylated at Thr-359 and Ser-363 by MAPK1/ERK2 and MAPK3/ERK1.
363	S	Phosphorylation	9430688
May be phosphorylated at Thr-359 and Ser-363 by MAPK1/ERK2 and MAPK3/ERK1.
380	S	Phosphorylation	9430688
Autophosphorylated on Ser-380, as part of the activation process.

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 KS6A1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MK03_HUMAN	MAPK3	physical	12832467
MK01_HUMAN	MAPK1	physical	12832467
1433B_HUMAN	YWHAB	physical	12618428
BAD_HUMAN	BAD	physical	11500364
TSC2_HUMAN	TSC2	physical	15757502
TSC2_HUMAN	TSC2	physical	15342917
CHSP1_HUMAN	CARHSP1	physical	15910284
EF2K_HUMAN	EEF2K	physical	11500364
MK01_HUMAN	MAPK1	physical	9915826
IKBA_HUMAN	NFKBIA	physical	9214631
TOB1_HUMAN	TOB1	physical	11260258
ESR1_HUMAN	ESR1	physical	9528769
IKBA_HUMAN	NFKBIA	physical	9261139
DDAH2_HUMAN	DDAH2	physical	21900206
ATX3_HUMAN	ATXN3	physical	21900206
EM55_HUMAN	MPP1	physical	21900206
PPM1G_HUMAN	PPM1G	physical	21900206
TTK_HUMAN	TTK	physical	21900206
GBP2_HUMAN	GBP2	physical	21900206
SRSF5_HUMAN	SRSF5	physical	21900206
PHAX_HUMAN	PHAX	physical	21900206
TERA_HUMAN	VCP	physical	21900206
COF1_HUMAN	CFL1	physical	21900206
TCPD_HUMAN	CCT4	physical	21900206
MAD1_HUMAN	MXD1	physical	18451027
YBOX1_HUMAN	YBX1	physical	19036157
PDCD4_HUMAN	PDCD4	physical	22586265
IKBA_HUMAN	NFKBIA	physical	9914500
RPTOR_HUMAN	RPTOR	physical	18722121
TAU_HUMAN	MAPT	physical	17512525
GSK3B_HUMAN	GSK3B	physical	19470470
CDN1B_HUMAN	CDKN1B	physical	19470470
CREB1_HUMAN	CREB1	physical	21832046
IF4H_HUMAN	EIF4H	physical	22863883
PSF2_HUMAN	GINS2	physical	22863883
HS90A_HUMAN	HSP90AA1	physical	23455922
HS90B_HUMAN	HSP90AB1	physical	23455922
MK01_HUMAN	MAPK1	physical	23455922
GRN_HUMAN	GRN	physical	23455922
KS6A3_HUMAN	RPS6KA3	physical	23455922
CSK2B_HUMAN	CSNK2B	physical	23455922
ACACA_HUMAN	ACACA	physical	23455922
KS6A2_HUMAN	RPS6KA2	physical	23455922
TLK2_HUMAN	TLK2	physical	23455922
GWL_HUMAN	MASTL	physical	23455922
PDIP3_HUMAN	POLDIP3	physical	25049393
RHG07_HUMAN	DLC1	physical	16338927
ILKAP_HUMAN	ILKAP	physical	26344197
DPTOR_HUMAN	DEPTOR	physical	22017876
MK01_HUMAN	MAPK1	physical	10922375
FGFR1_HUMAN	FGFR1	physical	15117958
UBE2T_HUMAN	UBE2T	physical	28162934

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 KS6A1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-380, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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-25; SER-26; SER-54;SER-72; THR-204; SER-209; TYR-220; SER-221; SER-307; THR-359; SER-363;SER-369; SER-380; THR-573; TYR-576; THR-635; SER-637; SER-684 ANDSER-732, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-31(ISOFORM 2), AND MASS SPECTROMETRY.	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 THR-359; SER-363; SER-369;SER-380 AND THR-573, 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 THR-359; SER-363; SER-369;SER-380 AND THR-573, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry."; Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.; Mol. Cell. Proteomics 6:537-547(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221; THR-225; THR-359;SER-363; SER-369 AND SER-380, AND MASS SPECTROMETRY.	17192257 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359 AND SER-363, ANDMASS SPECTROMETRY.	17081983 [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-732, AND MASSSPECTROMETRY.	16083285 [Abstract]
"Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90rskthat are inducible by MAPK."; Dalby K.N., Morrice N., Caudwell F.B., Avruch J., Cohen P.; J. Biol. Chem. 273:1496-1505(1998). Cited for: FUNCTION, ENZYME REGULATION, AND PHOSPHORYLATION AT SER-221; THR-359;SER-363; SER-380; THR-573 AND SER-732.	9430688 [Abstract]

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