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

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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.

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