KS6A2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KS6A2_MOUSE
• UniProt AC: Q9WUT3
• Protein Name: Ribosomal protein S6 kinase alpha-2
• Gene Name: Rps6ka2
• Organism: Mus musculus (Mouse).
• Sequence Length: 733
• 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 transcription factors, regulates translation, and mediates cellular proliferation, survival, and differentiation. May function as tumor suppressor in epithelial ovarian cancer cells (By similarity)..
• Protein Sequence: MELSMKKFTVRRFFSVYLRKKSRSKSSSLSRLEEEGIVKEIDISNHVKEGFEKADPSQFELLKVLGQGSYGKVFLVRKVTGSDAGQLYAMKVLKKATLKVRDRVRSKMERDILAEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHGLGIIYRDLKPENILLDEEGHIKITDFGLSKEATDHDKRAYSFCGTIEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMALILKAKLGMPQFLSAEAQSLLRALFKRNPCNRLGAGVDGVEEIKRHPFFVTIDWNKLYRKEIKPPFKPAVGRPEDTFHFDPEFTARTPTDSPGVPPSANAHHLFRGFSFVASSLVQEPSQQDVPKAPIHPIVQQLHGNNIHFTDGYEIKEDIGVGSYSVCKRCVHKATDAEYAVKIIDKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKYVYLVMELMRGGELLDRILRQRCFSEREASDVLYTIARTMDYLHSQGVVHRDLKPSNILYMDESGNPESIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDVWSLGILLYTMLAGFTPFANGPDDTPEEILARIGSGKYALSGGNWDSISDAAKDVVSKMLHVDPQQRLTAVQVLKHPWIVNREYLSQNQLSRQDVHLVKGAMAATYFALNRTPQAPRLEPVLSSSLAQRRGMKRLTSTRL

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
21	Acetylation	FSVYLRKKSRSKSSS HHHHHHHHCCCCCCC	44.67	19862095
25	Acetylation	LRKKSRSKSSSLSRL HHHHCCCCCCCCHHH	53.93	19862105
39	Acetylation	LEEEGIVKEIDISNH HHHCCCEEEEECCHH	47.21	19862115
88	Phosphorylation	GSDAGQLYAMKVLKK CCCHHHHHHHHHHHH	9.21	23140645
183	Methylation	HGLGIIYRDLKPENI CCCCEEECCCCHHHE	32.17	30989271
217	Phosphorylation	TDHDKRAYSFCGTIE CCCCHHHHHHHHHHH	13.30	22322096
218	Phosphorylation	DHDKRAYSFCGTIEY CCCHHHHHHHHHHHH	17.05	26643407
222	Phosphorylation	RAYSFCGTIEYMAPE HHHHHHHHHHHHCHH	16.30	22322096
239	Phosphorylation	NRRGHTQSADWWSFG CCCCCCCCCCHHHHH	29.38	21183079
254	Phosphorylation	VLMFEMLTGSLPFQG HHHHHHHHCCCCCCC	24.34	21183079
288	Phosphorylation	FLSAEAQSLLRALFK HHCHHHHHHHHHHHH	36.10	28059163
356	Phosphorylation	DPEFTARTPTDSPGV CHHHCCCCCCCCCCC	28.24	19060867
360	Phosphorylation	TARTPTDSPGVPPSA CCCCCCCCCCCCCCC	26.49	19060867
377	Phosphorylation	HHLFRGFSFVASSLV HHHHHCHHHHHHHHC	22.95	25521595
381	Phosphorylation	RGFSFVASSLVQEPS HCHHHHHHHHCCCCC	20.92	29899451
382	Phosphorylation	GFSFVASSLVQEPSQ CHHHHHHHHCCCCCC	23.87	18779572
463	Phosphorylation	EIEILLRYGQHPNII HHHHHHHHCCCCCEE	22.55	21454597
471	Phosphorylation	GQHPNIITLKDVYDD CCCCCEEEEEECCCC	24.77	21454597
476	Phosphorylation	IITLKDVYDDGKYVY EEEEEECCCCCCEEE	20.60	25168779
481	Phosphorylation	DVYDDGKYVYLVMEL ECCCCCCEEEEEEHH	10.39	25168779
483	Phosphorylation	YDDGKYVYLVMELMR CCCCCEEEEEEHHHH	7.18	25168779
559	Ubiquitination	ICDFGFAKQLRAENG ECCHHHHHHHHHHCC	47.83	-
570	Phosphorylation	AENGLLMTPCYTANF HHCCCEECCCEECCC	15.35	26824392
573	Phosphorylation	GLLMTPCYTANFVAP CCEECCCEECCCCCH	15.30	25266776
574	Phosphorylation	LLMTPCYTANFVAPE CEECCCEECCCCCHH	23.11	25777480
677	Phosphorylation	PWIVNREYLSQNQLS HHHHCHHHHCCCCCC	14.39	29514104
698	Phosphorylation	VKGAMAATYFALNRT HHHHHHHHHHHHCCC	15.05	-
699	Phosphorylation	KGAMAATYFALNRTP HHHHHHHHHHHCCCC	5.11	29514104
705	Phosphorylation	TYFALNRTPQAPRLE HHHHHCCCCCCCCCH	20.76	-
716	Phosphorylation	PRLEPVLSSSLAQRR CCCHHHHCHHHHHHH	20.36	28066266
717	Phosphorylation	RLEPVLSSSLAQRRG CCHHHHCHHHHHHHC	25.80	28066266
718	Phosphorylation	LEPVLSSSLAQRRGM CHHHHCHHHHHHHCH	25.09	28066266

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
218	S	Phosphorylation	Kinase	PDPK1	Q9Z2A0	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
218	S	Phosphorylation	Activated by phosphorylation at Ser-218 by PDPK1.	-
356	T	Phosphorylation	May be phosphorylated at Thr-356 and Ser-360 by MAPK1/ERK2 and MAPK3/ERK1 (By similarity).	-
360	S	Phosphorylation	May be phosphorylated at Thr-356 and Ser-360 by MAPK1/ERK2 and MAPK3/ERK1 (By similarity).	-
377	S	Phosphorylation	Autophosphorylated on Ser-377, as part of the activation process.	15345747

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of KS6A2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of KS6A2_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.