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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
26 | Phosphorylation | RRKSRSKSSSLSRLE HHHCCCCCCCCHHHH | 26.80 | - | |
27 | Phosphorylation | RKSRSKSSSLSRLEE HHCCCCCCCCHHHHH | 38.75 | - | |
28 | Phosphorylation | KSRSKSSSLSRLEEE HCCCCCCCCHHHHHC | 37.14 | - | |
30 | Phosphorylation | RSKSSSLSRLEEEGV CCCCCCCHHHHHCCC | 36.45 | - | |
88 | Phosphorylation | GSDAGQLYAMKVLKK CCCHHHHHHHHHHHH | 9.21 | 27811184 | |
91 | Acetylation | AGQLYAMKVLKKATL HHHHHHHHHHHHHCH | 35.92 | 7987797 | |
94 | Acetylation | LYAMKVLKKATLKVR HHHHHHHHHHCHHHH | 43.26 | 7987809 | |
106 | Phosphorylation | KVRDRVRSKMERDIL HHHHHHHHHHHHHHH | 33.23 | 20068231 | |
135 | Phosphorylation | FQTEGKLYLILDFLR EECCCEEEEEEHHHH | 8.65 | - | |
151 | Phosphorylation | GDLFTRLSKEVMFTE CCHHHHHCCCCCCCH | 24.39 | 12618428 | |
157 | Phosphorylation | LSKEVMFTEEDVKFY HCCCCCCCHHHHHHH | 21.99 | 22210691 | |
186 | Ubiquitination | GIIYRDLKPENILLD CCEECCCCHHHEEEC | 55.35 | - | |
206 | Phosphorylation | KITDFGLSKEAIDHD EECCCCCCHHHHCCC | 28.91 | 21815630 | |
217 | Phosphorylation | IDHDKRAYSFCGTIE HCCCHHHHHHCHHHH | 13.30 | 26657352 | |
218 | Phosphorylation | DHDKRAYSFCGTIEY CCCHHHHHHCHHHHH | 17.05 | 17192257 | |
222 | Phosphorylation | RAYSFCGTIEYMAPE HHHHHCHHHHHHCHH | 16.30 | 26657352 | |
225 | Phosphorylation | SFCGTIEYMAPEVVN HHCHHHHHHCHHHHC | 8.50 | 26657352 | |
230 | Phosphorylation | IEYMAPEVVNRRGHT HHHHCHHHHCCCCCC | 4.50 | 27251275 | |
288 | Phosphorylation | FLSGEAQSLLRALFK HHCHHHHHHHHHHHH | 36.10 | 24719451 | |
295 | Acetylation | SLLRALFKRNPCNRL HHHHHHHHHCCCCCC | 52.71 | 12437829 | |
377 | Phosphorylation | HHLFRGFSFVASSLI HHHHHCHHHHHHHHC | 22.95 | 15345747 | |
381 | Phosphorylation | RGFSFVASSLIQEPS HCHHHHHHHHCCCCC | 22.00 | - | |
385 | Phosphorylation | FVASSLIQEPSQQDL HHHHHHCCCCCCCCH | 62.94 | 27251275 | |
388 | Phosphorylation | SSLIQEPSQQDLHKV HHHCCCCCCCCHHCC | 39.46 | - | |
426 | Phosphorylation | EDIGVGSYSVCKRCV CCCCCCCHHHHHHHH | 10.13 | - | |
430 | Ubiquitination | VGSYSVCKRCVHKAT CCCHHHHHHHHHCCC | 46.83 | - | |
450 | Ubiquitination | VKIIDKSKRDPSEEI HHHHHHHCCCHHHHH | 67.57 | - | |
463 | Phosphorylation | EIEILLRYGQHPNII HHHHHHHHCCCCCEE | 22.55 | 20071362 | |
471 | Phosphorylation | GQHPNIITLKDVYDD CCCCCEEEEEEECCC | 24.77 | 20071362 | |
473 | Ubiquitination | HPNIITLKDVYDDGK CCCEEEEEEECCCCC | 36.18 | - | |
540 | Phosphorylation | LKPSNILYRDESGSP CCHHHCEEECCCCCC | 16.54 | 18083107 | |
544 | Phosphorylation | NILYRDESGSPESIR HCEEECCCCCCCCEE | 49.19 | 22210691 | |
546 | Phosphorylation | LYRDESGSPESIRVC EEECCCCCCCCEEEC | 34.47 | 25850435 | |
570 | Phosphorylation | AGNGLLMTPCYTANF CCCCEEECCCEECCC | 15.35 | 18691976 | |
573 | Phosphorylation | GLLMTPCYTANFVAP CEEECCCEECCCCCH | 15.30 | 18691976 | |
574 | Phosphorylation | LLMTPCYTANFVAPE EEECCCEECCCCCHH | 23.11 | 17192257 | |
582 | Phosphorylation | ANFVAPEVLKRQGYD CCCCCHHHHHHCCCC | 8.11 | 27251275 | |
618 | Phosphorylation | FANGPDDTPEEILAR CCCCCCCCHHHHHHH | 39.72 | - | |
628 | Phosphorylation | EILARIGSGKYALSG HHHHHHCCCCEECCC | 29.73 | 25278378 | |
630 | Ubiquitination | LARIGSGKYALSGGN HHHHCCCCEECCCCC | 29.10 | 17370265 | |
631 | Phosphorylation | ARIGSGKYALSGGNW HHHCCCCEECCCCCC | 19.12 | 25278378 | |
634 | Phosphorylation | GSGKYALSGGNWDSI CCCCEECCCCCCHHH | 36.16 | 21082442 | |
640 | Phosphorylation | LSGGNWDSISDAAKD CCCCCCHHHHHHHHH | 18.66 | 25278378 | |
642 | Phosphorylation | GGNWDSISDAAKDVV CCCCHHHHHHHHHHH | 25.75 | 25278378 | |
650 | Phosphorylation | DAAKDVVSKMLHVDP HHHHHHHHHHCCCCH | 16.52 | 25278378 | |
662 | Phosphorylation | VDPHQRLTAMQVLKH CCHHHHHHHHHHHCC | 23.44 | - | |
677 | Phosphorylation | PWVVNREYLSPNQLS CCEECHHHCCHHHCC | 14.83 | 29978859 | |
679 | Phosphorylation | VVNREYLSPNQLSRQ EECHHHCCHHHCCHH | 22.39 | 27499020 | |
684 | Phosphorylation | YLSPNQLSRQDVHLV HCCHHHCCHHHHHHH | 20.38 | 29978859 | |
729 | Phosphorylation | RRGMKRLTSTRL--- HHCCHHHHCCCC--- | 31.89 | 29514088 | |
730 | Phosphorylation | RGMKRLTSTRL---- HCCHHHHCCCC---- | 19.00 | 29514088 | |
731 | Phosphorylation | GMKRLTSTRL----- CCHHHHCCCC----- | 30.65 | 29514088 |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
MK03_HUMAN | MAPK3 | physical | 12832467 | |
MK01_HUMAN | MAPK1 | physical | 12832467 | |
MK03_HUMAN | MAPK3 | physical | 8939914 | |
MK01_HUMAN | MAPK1 | physical | 8939914 | |
KS6A2_HUMAN | RPS6KA2 | physical | 7623830 | |
JUN_HUMAN | JUN | physical | 7623830 | |
FOS_HUMAN | FOS | physical | 7623830 | |
NQO2_HUMAN | NQO2 | physical | 22939629 | |
STXB2_HUMAN | STXBP2 | physical | 22939629 | |
FAT1_HUMAN | FAT1 | physical | 25852190 | |
GRSF1_HUMAN | GRSF1 | physical | 25852190 | |
MK01_HUMAN | MAPK1 | physical | 25852190 | |
SHRM3_HUMAN | SHROOM3 | physical | 25852190 |
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. |
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Phosphorylation | |
Reference | PubMed |
"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 | |
Reference | PubMed |
"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. |