KS6A2_HUMAN - dbPTM
KS6A2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KS6A2_HUMAN
UniProt AC Q15349
Protein Name Ribosomal protein S6 kinase alpha-2
Gene Name RPS6KA2
Organism Homo sapiens (Human).
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..
Protein Sequence MDLSMKKFAVRRFFSVYLRRKSRSKSSSLSRLEEEGVVKEIDISHHVKEGFEKADPSQFELLKVLGQGSYGKVFLVRKVKGSDAGQLYAMKVLKKATLKVRDRVRSKMERDILAEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKITDFGLSKEAIDHDKRAYSFCGTIEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMALILKAKLGMPQFLSGEAQSLLRALFKRNPCNRLGAGIDGVEEIKRHPFFVTIDWNTLYRKEIKPPFKPAVGRPEDTFHFDPEFTARTPTDSPGVPPSANAHHLFRGFSFVASSLIQEPSQQDLHKVPVHPIVQQLHGNNIHFTDGYEIKEDIGVGSYSVCKRCVHKATDTEYAVKIIDKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKFVYLVMELMRGGELLDRILRQRYFSEREASDVLCTITKTMDYLHSQGVVHRDLKPSNILYRDESGSPESIRVCDFGFAKQLRAGNGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFANGPDDTPEEILARIGSGKYALSGGNWDSISDAAKDVVSKMLHVDPHQRLTAMQVLKHPWVVNREYLSPNQLSRQDVHLVKGAMAATYFALNRTPQAPRLEPVLSSNLAQRRGMKRLTSTRL
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
26PhosphorylationRRKSRSKSSSLSRLE
HHHCCCCCCCCHHHH		26.80-
27PhosphorylationRKSRSKSSSLSRLEE
HHCCCCCCCCHHHHH		38.75-
28PhosphorylationKSRSKSSSLSRLEEE
HCCCCCCCCHHHHHC		37.14-
30PhosphorylationRSKSSSLSRLEEEGV
CCCCCCCHHHHHCCC		36.45-
88PhosphorylationGSDAGQLYAMKVLKK
CCCHHHHHHHHHHHH		9.2127811184
91AcetylationAGQLYAMKVLKKATL
HHHHHHHHHHHHHCH		35.927987797
94AcetylationLYAMKVLKKATLKVR
HHHHHHHHHHCHHHH		43.267987809
106PhosphorylationKVRDRVRSKMERDIL
HHHHHHHHHHHHHHH		33.2320068231
135PhosphorylationFQTEGKLYLILDFLR
EECCCEEEEEEHHHH		8.65-
151PhosphorylationGDLFTRLSKEVMFTE
CCHHHHHCCCCCCCH		24.3912618428
157PhosphorylationLSKEVMFTEEDVKFY
HCCCCCCCHHHHHHH		21.9922210691
186UbiquitinationGIIYRDLKPENILLD
CCEECCCCHHHEEEC		55.35-
206PhosphorylationKITDFGLSKEAIDHD
EECCCCCCHHHHCCC		28.9121815630
217PhosphorylationIDHDKRAYSFCGTIE
HCCCHHHHHHCHHHH		13.3026657352
218PhosphorylationDHDKRAYSFCGTIEY
CCCHHHHHHCHHHHH		17.0517192257
222PhosphorylationRAYSFCGTIEYMAPE
HHHHHCHHHHHHCHH		16.3026657352
225PhosphorylationSFCGTIEYMAPEVVN
HHCHHHHHHCHHHHC		8.5026657352
230PhosphorylationIEYMAPEVVNRRGHT
HHHHCHHHHCCCCCC		4.5027251275
288PhosphorylationFLSGEAQSLLRALFK
HHCHHHHHHHHHHHH		36.1024719451
295AcetylationSLLRALFKRNPCNRL
HHHHHHHHHCCCCCC		52.7112437829
377PhosphorylationHHLFRGFSFVASSLI
HHHHHCHHHHHHHHC		22.9515345747
381PhosphorylationRGFSFVASSLIQEPS
HCHHHHHHHHCCCCC		22.00-
385PhosphorylationFVASSLIQEPSQQDL
HHHHHHCCCCCCCCH		62.9427251275
388PhosphorylationSSLIQEPSQQDLHKV
HHHCCCCCCCCHHCC		39.46-
426PhosphorylationEDIGVGSYSVCKRCV
CCCCCCCHHHHHHHH		10.13-
430UbiquitinationVGSYSVCKRCVHKAT
CCCHHHHHHHHHCCC		46.83-
450UbiquitinationVKIIDKSKRDPSEEI
HHHHHHHCCCHHHHH		67.57-
463PhosphorylationEIEILLRYGQHPNII
HHHHHHHHCCCCCEE		22.5520071362
471PhosphorylationGQHPNIITLKDVYDD
CCCCCEEEEEEECCC		24.7720071362
473UbiquitinationHPNIITLKDVYDDGK
CCCEEEEEEECCCCC		36.18-
540PhosphorylationLKPSNILYRDESGSP
CCHHHCEEECCCCCC		16.5418083107
544PhosphorylationNILYRDESGSPESIR
HCEEECCCCCCCCEE		49.1922210691
546PhosphorylationLYRDESGSPESIRVC
EEECCCCCCCCEEEC		34.4725850435
570PhosphorylationAGNGLLMTPCYTANF
CCCCEEECCCEECCC		15.3518691976
573PhosphorylationGLLMTPCYTANFVAP
CEEECCCEECCCCCH		15.3018691976
574PhosphorylationLLMTPCYTANFVAPE
EEECCCEECCCCCHH		23.1117192257
582PhosphorylationANFVAPEVLKRQGYD
CCCCCHHHHHHCCCC		8.1127251275
618PhosphorylationFANGPDDTPEEILAR
CCCCCCCCHHHHHHH		39.72-
628PhosphorylationEILARIGSGKYALSG
HHHHHHCCCCEECCC		29.7325278378
630UbiquitinationLARIGSGKYALSGGN
HHHHCCCCEECCCCC		29.1017370265
631PhosphorylationARIGSGKYALSGGNW
HHHCCCCEECCCCCC		19.1225278378
634PhosphorylationGSGKYALSGGNWDSI
CCCCEECCCCCCHHH		36.1621082442
640PhosphorylationLSGGNWDSISDAAKD
CCCCCCHHHHHHHHH		18.6625278378
642PhosphorylationGGNWDSISDAAKDVV
CCCCHHHHHHHHHHH		25.7525278378
650PhosphorylationDAAKDVVSKMLHVDP
HHHHHHHHHHCCCCH		16.5225278378
662PhosphorylationVDPHQRLTAMQVLKH
CCHHHHHHHHHHHCC		23.44-
677PhosphorylationPWVVNREYLSPNQLS
CCEECHHHCCHHHCC		14.8329978859
679PhosphorylationVVNREYLSPNQLSRQ
EECHHHCCHHHCCHH		22.3927499020
684PhosphorylationYLSPNQLSRQDVHLV
HCCHHHCCHHHHHHH		20.3829978859
729PhosphorylationRRGMKRLTSTRL---
HHCCHHHHCCCC---		31.8929514088
730PhosphorylationRGMKRLTSTRL----
HCCHHHHCCCC----		19.0029514088
731PhosphorylationGMKRLTSTRL-----
CCHHHHCCCC-----		30.6529514088
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
218SPhosphorylationKinaseRPS6KA2Q15349
GPS
218SPhosphorylationKinasePDPK1O15530
Uniprot
570TPhosphorylationKinaseRPS6KA2Q15349
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
218SPhosphorylation

10480933
356TPhosphorylation

-
360SPhosphorylation

-
377SPhosphorylation

19369195
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 KS6A2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MK03_HUMANMAPK3physical
12832467
MK01_HUMANMAPK1physical
12832467
MK03_HUMANMAPK3physical
8939914
MK01_HUMANMAPK1physical
8939914
KS6A2_HUMANRPS6KA2physical
7623830
JUN_HUMANJUNphysical
7623830
FOS_HUMANFOSphysical
7623830
NQO2_HUMANNQO2physical
22939629
STXB2_HUMANSTXBP2physical
22939629
FAT1_HUMANFAT1physical
25852190
GRSF1_HUMANGRSF1physical
25852190
MK01_HUMANMAPK1physical
25852190
SHRM3_HUMANSHROOM3physical
25852190
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 KS6A2_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 TYR-217; SER-218; SER-377AND SER-546, AND MASS SPECTROMETRY.
"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-218, AND MASSSPECTROMETRY.
"90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-phosphoinositide-dependent protein kinase-1.";
Jensen C.J., Buch M.-B., Krag T.O., Hemmings B.A., Gammeltoft S.,Froedin M.;
J. Biol. Chem. 274:27168-27176(1999).
Cited for: ENZYME REGULATION, AND PHOSPHORYLATION AT SER-218.
Ubiquitylation
ReferencePubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry.";
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
Proteomics 7:868-874(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-630, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory