KS6A6_HUMAN - dbPTM
KS6A6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KS6A6_HUMAN
UniProt AC Q9UK32
Protein Name Ribosomal protein S6 kinase alpha-6
Gene Name RPS6KA6
Organism Homo sapiens (Human).
Sequence Length 745
Subcellular Localization Cytoplasm, cytosol . Nucleus . Predominantly cytosolic.
Protein Description Constitutively active serine/threonine-protein kinase that exhibits growth-factor-independent kinase activity and that may participate in p53/TP53-dependent cell growth arrest signaling and play an inhibitory role during embryogenesis..
Protein Sequence MLPFAPQDEPWDREMEVFSGGGASSGEVNGLKMVDEPMEEGEADSCHDEGVVKEIPITHHVKEGYEKADPAQFELLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPANRLGSEGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDSPGLPASANAHQLFKGFSFVATSIAEEYKITPITSANVLPIVQINGNAAQFGEVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTPEEILLRIGNGKFSLSGGNWDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWITHRDQLPNDQPKRNDVSHVVKGAMVATYSALTHKTFQPVLEPVAASSLAQRRSMKKRTSTGL
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
77UbiquitinationPAQFELLKVLGQGSF
HHHHHHHHHHCCCCC		48.3022817900
83PhosphorylationLKVLGQGSFGKVFLV
HHHHCCCCCCEEEEE		23.9620873877
86UbiquitinationLGQGSFGKVFLVRKK
HCCCCCCEEEEEEEC		28.01-
86AcetylationLGQGSFGKVFLVRKK
HCCCCCCEEEEEEEC		28.0188651
86UbiquitinationLGQGSFGKVFLVRKK
HCCCCCCEEEEEEEC		28.0122817900
94UbiquitinationVFLVRKKTGPDAGQL
EEEEEECCCCCHHHH		57.9122817900
94PhosphorylationVFLVRKKTGPDAGQL
EEEEEECCCCCHHHH		57.91-
103UbiquitinationPDAGQLYAMKVLKKA
CCHHHHHHHHHHHHC		10.4221890473
105AcetylationAGQLYAMKVLKKASL
HHHHHHHHHHHHCCC		35.927987889
108AcetylationLYAMKVLKKASLKVR
HHHHHHHHHCCCHHH		49.647987899
149PhosphorylationFQTEGKLYLILDFLR
EECCCEEEEEEHHHC		8.6530576142
162PhosphorylationLRGGDVFTRLSKEVL
HCCCCHHHHHCCHHC		30.4630576142
215PhosphorylationEIGHIKLTDFGLSKE
CCCCEEECCCCCCHH		25.0421082442
220PhosphorylationKLTDFGLSKESVDQE
EECCCCCCHHHCCCH		34.4521082442
231PhosphorylationVDQEKKAYSFCGTVE
CCCHHHHHHCCCCHH		15.9122322096
232PhosphorylationDQEKKAYSFCGTVEY
CCHHHHHHCCCCHHH		20.9422322096
236PhosphorylationKAYSFCGTVEYMAPE
HHHHCCCCHHHHCHH		16.0222322096
239PhosphorylationSFCGTVEYMAPEVVN
HCCCCHHHHCHHHHC		8.3423927012
302PhosphorylationFLSAEAQSLLRMLFK
HHCHHHHHHHHHHHH		36.1024719451
331UbiquitinationIKRHLFFANIDWDKL
HHHHHHEEECCHHHH		12.5321963094
348AcetylationREVQPPFKPASGKPD
CCCCCCCCCCCCCCC		45.5120167786
367AcetylationFDPEFTAKTPKDSPG
ECHHHCCCCCCCCCC		63.4028736149
368PhosphorylationDPEFTAKTPKDSPGL
CHHHCCCCCCCCCCC		32.8622496350
372PhosphorylationTAKTPKDSPGLPASA
CCCCCCCCCCCCCCC		27.3029514088
378PhosphorylationDSPGLPASANAHQLF
CCCCCCCCCCHHHHH		21.8127732954
386AcetylationANAHQLFKGFSFVAT
CCHHHHHHHCEEEEE		68.5820167786
389PhosphorylationHQLFKGFSFVATSIA
HHHHHHCEEEEEHHH		27.7215632195
393PhosphorylationKGFSFVATSIAEEYK
HHCEEEEEHHHHHHC		18.5027251275
394PhosphorylationGFSFVATSIAEEYKI
HCEEEEEHHHHHHCC		15.2927251275
437PhosphorylationEDIGVGSYSVCKRCI
CCCCCCCHHHHHHHH		10.13-
441UbiquitinationVGSYSVCKRCIHATT
CCCHHHHHHHHHCCC		48.4232015554
449UbiquitinationRCIHATTNMEFAVKI
HHHHCCCCCHHHHHH		24.5121963094
467UbiquitinationSKRDPSEEIEILMRY
HCCCHHHHHHHHHHH		50.7021963094
474PhosphorylationEIEILMRYGQHPNII
HHHHHHHHCCCCCEE		13.7420071362
482PhosphorylationGQHPNIITLKDVFDD
CCCCCEEEEEECCCC		24.7720071362
521PhosphorylationCFSEREASDILYVIS
CCCHHHHHHHHHHHH		22.04-
525PhosphorylationREASDILYVISKTVD
HHHHHHHHHHHHHCC		8.96-
547PhosphorylationVHRDLKPSNILYMDE
ECCCCCHHHEEEEEC		34.61-
555PhosphorylationNILYMDESASADSIR
HEEEEECCCCCCEEE		24.22-
570UbiquitinationICDFGFAKQLRGENG
ECCHHHHHHHCCCCC		47.8321963094
570UbiquitinationICDFGFAKQLRGENG
ECCHHHHHHHCCCCC		47.83-
581PhosphorylationGENGLLLTPCYTANF
CCCCEEECCCCCCCC		15.9822817900
587UbiquitinationLTPCYTANFVAPEVL
ECCCCCCCCCCHHHH		24.9121963094
710PhosphorylationVKGAMVATYSALTHK
HHHHHHHHHHHHHCC		13.4421214269
711PhosphorylationKGAMVATYSALTHKT
HHHHHHHHHHHHCCC		5.1321214269
715PhosphorylationVATYSALTHKTFQPV
HHHHHHHHCCCCHHC		22.5021214269
718PhosphorylationYSALTHKTFQPVLEP
HHHHHCCCCHHCCHH		21.65-
730PhosphorylationLEPVAASSLAQRRSM
CHHHHHHHHHHHHHH		24.01-
736PhosphorylationSSLAQRRSMKKRTST
HHHHHHHHHHHHCCC		36.82-
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

Oops, there are no upstream regulatory protein records of KS6A6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
232SPhosphorylation

15632195
372SPhosphorylation

15632195
389SPhosphorylation

15632195
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 KS6A6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NR4A1_HUMANNR4A1physical
16169070
MICA1_HUMANMICAL1physical
21900206
EM55_HUMANMPP1physical
21900206
RXRA_HUMANRXRAphysical
21900206
DHX34_HUMANDHX34physical
21900206
CENPB_HUMANCENPBphysical
21900206
ADIRF_HUMANADIRFphysical
21900206
ZN227_HUMANZNF227physical
21900206
SYNE4_HUMANSYNE4physical
21900206
UFM1_HUMANUFM1physical
21900206
SPTN4_HUMANSPTBN4physical
21900206
S30BP_HUMANSAP30BPphysical
21900206
FBN3_HUMANFBN3physical
21900206
DJC13_HUMANDNAJC13physical
21900206
ERG28_HUMANC14orf1physical
21900206
LMO4_HUMANLMO4physical
21900206
CEBPZ_HUMANCEBPZphysical
21900206
ZN746_HUMANZNF746physical
21900206
RLA1_HUMANRPLP1physical
21900206
MED24_HUMANMED24physical
21900206
SUH_HUMANRBPJphysical
21900206
DNMT1_HUMANDNMT1physical
21900206
TETN_HUMANCLEC3Bphysical
21900206
MASP1_HUMANMASP1physical
21900206
FZD5_HUMANFZD5physical
21900206
A4_HUMANAPPphysical
21832049
NFYA_HUMANNFYAphysical
22939629
PQBP1_HUMANPQBP1physical
22939629
UBAC1_HUMANUBAC1physical
22939629
SL9A1_HUMANSLC9A1physical
22939629
MBP_HUMANMBPphysical
22939629
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 KS6A6_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-232, AND MASSSPECTROMETRY.
"Functional characterization of human RSK4, a new 90-kDa ribosomal S6kinase, reveals constitutive activation in most cell types.";
Duemmler B.A., Hauge C., Silber J., Yntema H.G., Kruse L.S.,Kofoed B., Hemmings B.A., Alessi D.R., Froedin M.;
J. Biol. Chem. 280:13304-13314(2005).
Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH MAPK3, SUBCELLULARLOCATION, PHOSPHORYLATION AT SER-232; SER-372; SER-389 AND THR-581,AND MUTAGENESIS OF SER-372; SER-389 AND THR-581.

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