P23443
Gene name |
RPS6KB1 (STK14A) |
Protein name |
Ribosomal protein S6 kinase beta-1 |
Names |
S6K-beta-1, S6K1, 70 kDa ribosomal protein S6 kinase 1, P70S6K1, p70-S6K 1, Ribosomal protein S6 kinase I, Serine/threonine-protein kinase 14A, p70 ribosomal S6 kinase alpha, p70 S6 kinase alpha, p70 S6K-alpha, p70 S6KA |
Species |
Homo sapiens (Human) |
KEGG Pathway |
hsa:6198 |
EC number |
2.7.11.1: Protein-serine/threonine kinases |
Protein Class |
RIBOSOMAL PROTEIN S6 KINASE (PTHR24351) |

Descriptions
Ribosomal protein S6 kinases are proteins playing a crucial role in regulating cellular growth and metabolism through its involvement in the mTOR signaling pathway. S6Ks are activated by a wide variety of growth factor receptors, including receptor tyrosine kinases, G-protein-coupled receptors, and the interleukin-2 receptor.
The activity of S6K protein is regulated by autoinhibitory domains. Phosphorylation of specific serine residues within the N-terminal autoinhibitory domain of S6K by cyclin-dependent kinase 5 (Cdk5) is required for dendritic spine morphogenesis in the neuron. In S6K, the N-terminal region also contains an autoinhibitory domain and its deletion activates S6K.
Autoinhibitory domains (AIDs)
Target domain |
91-352 (Protein kinase domain) |
Relief mechanism |
Partner binding |
Assay |
Deletion assay |
Target domain |
91-352 (Protein kinase domain) |
Relief mechanism |
PTM |
Assay |
|
Accessory elements
235-258 (Activation loop from InterPro)
Target domain |
91-352 (Protein kinase domain) |
Relief mechanism |
|
Assay |
|
References
- Lai KO et al. (2015) "Cyclin-dependent Kinase 5 (Cdk5)-dependent Phosphorylation of p70 Ribosomal S6 Kinase 1 (S6K) Is Required for Dendritic Spine Morphogenesis", The Journal of biological chemistry, 290, 14637-46
- Dennis PB et al. (1998) "Phosphorylation sites in the autoinhibitory domain participate in p70(s6k) activation loop phosphorylation", The Journal of biological chemistry, 273, 14845-52
- Mahalingam M et al. (1996) "Constitutive activation of S6 kinase by deletion of amino-terminal autoinhibitory and rapamycin sensitivity domains", Molecular and cellular biology, 16, 405-13
Autoinhibited structure

Activated structure

23 structures for P23443
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
3A60 | X-ray | 280 A | A/B | 75-399 | PDB |
3A61 | X-ray | 343 A | A | 75-399 | PDB |
3A62 | X-ray | 235 A | A | 75-399 | PDB |
3WE4 | X-ray | 200 A | A | 78-399 | PDB |
3WF5 | X-ray | 210 A | A | 78-399 | PDB |
3WF6 | X-ray | 203 A | A | 78-399 | PDB |
3WF7 | X-ray | 185 A | A | 78-399 | PDB |
3WF8 | X-ray | 198 A | A | 78-399 | PDB |
3WF9 | X-ray | 204 A | A | 78-399 | PDB |
4L3J | X-ray | 210 A | A | 75-375 | PDB |
4L3L | X-ray | 210 A | A | 75-375 | PDB |
4L42 | X-ray | 280 A | A | 75-417 | PDB |
4L43 | X-ray | 300 A | A | 75-417 | PDB |
4L44 | X-ray | 290 A | A | 75-417 | PDB |
4L45 | X-ray | 290 A | A | 75-417 | PDB |
4L46 | X-ray | 301 A | A | 75-417 | PDB |
4RLO | X-ray | 253 A | A/B | 85-372 | PDB |
4RLP | X-ray | 279 A | A | 85-372 | PDB |
5WBH | X-ray | 175 A | W | 412-437 | PDB |
5WBK | X-ray | 311 A | T | 24-37 | PDB |
7N91 | X-ray | 300 A | A/B | 82-421 | PDB |
7N93 | X-ray | 274 A | A/B | 82-421 | PDB |
AF-P23443-F1 | Predicted | AlphaFoldDB |
179 variants for P23443
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
rs769786318 CA8682731 |
2 | R>K | No |
ClinGen ExAC TOPMed gnomAD |
|
rs1456168166 CA400435358 |
2 | R>W | No |
ClinGen gnomAD |
|
CA292159075 rs1007996112 |
5 | R>K | No |
ClinGen Ensembl |
|
rs773013562 CA8682732 |
5 | R>S | No |
ClinGen ExAC gnomAD |
|
CA8682733 rs762843401 |
7 | R>G | No |
ClinGen ExAC gnomAD |
|
rs762843401 CA400435400 |
7 | R>W | No |
ClinGen ExAC gnomAD |
|
CA8682735 rs139530428 |
9 | G>S | No |
ClinGen ESP ExAC TOPMed gnomAD |
|
rs201606773 CA292159097 |
10 | F>Y | No |
ClinGen Ensembl |
|
CA400435445 rs1598604302 |
11 | Y>S | No |
ClinGen Ensembl |
|
CA400435458 rs1421811183 |
12 | P>S | No |
ClinGen TOPMed gnomAD |
|
CA400435464 rs1465279456 |
13 | A>T | No |
ClinGen gnomAD |
|
CA400435489 rs1404397597 |
15 | D>A | No |
ClinGen gnomAD |
|
CA8682736 rs759865603 |
16 | F>C | No |
ClinGen ExAC TOPMed gnomAD |
|
rs1231145816 CA400435512 |
17 | R>* | No |
ClinGen TOPMed |
|
CA8682738 rs767780996 |
17 | R>P | No |
ClinGen ExAC gnomAD |
|
rs767780996 CA8682737 |
17 | R>Q | No |
ClinGen ExAC gnomAD |
|
rs756132794 CA8682739 |
18 | D>N | No |
ClinGen ExAC gnomAD |
|
CA8682741 rs754270633 |
20 | E>K | No |
ClinGen ExAC gnomAD |
|
rs757691849 CA8682742 |
21 | A>V | No |
ClinGen ExAC TOPMed gnomAD |
|
CA400435579 rs1443518745 |
23 | D>N | No |
ClinGen TOPMed |
|
CA400435610 rs1226172830 |
25 | A>V | No |
ClinGen gnomAD |
|
rs1483907789 CA400435625 |
27 | V>G | No |
ClinGen gnomAD |
|
rs1488886621 CA400435699 |
33 | D>A | No |
ClinGen gnomAD |
|
rs376390460 CA292159142 |
37 | D>E | No |
ClinGen ESP TOPMed gnomAD |
|
rs1446143670 CA400435751 |
37 | D>G | No |
ClinGen TOPMed |
|
rs142855919 CA8682746 |
37 | D>N | No |
ClinGen ESP ExAC TOPMed gnomAD |
|
rs1167359257 CA400435771 |
39 | G>A | No |
ClinGen TOPMed |
|
CA8682748 rs769152306 |
39 | G>C | No |
ClinGen ExAC gnomAD |
|
rs1464661498 CA400435787 |
41 | E>* | No |
ClinGen gnomAD |
|
CA8682749 rs763484257 |
41 | E>D | No |
ClinGen ExAC TOPMed gnomAD |
|
CA400435796 rs1374813056 |
42 | D>N | No |
ClinGen gnomAD |
|
CA400435818 rs1158964070 |
43 | E>D | No |
ClinGen TOPMed |
|
CA400435857 rs1231119934 |
46 | E>D | No |
ClinGen TOPMed |
|
CA400435855 rs1231119934 |
46 | E>D | No |
ClinGen TOPMed |
|
CA8682769 rs771005046 |
48 | G>C | No |
ClinGen ExAC gnomAD |
|
CA400437097 rs1445839180 |
50 | L>F | No |
ClinGen TOPMed |
|
CA400437154 rs1238870402 |
54 | M>R | No |
ClinGen gnomAD |
|
CA400437173 rs1339950914 |
55 | D>Y | No |
ClinGen TOPMed |
|
CA8682770 rs774417798 |
56 | H>D | No |
ClinGen ExAC gnomAD |
|
rs1411844093 CA400437192 |
56 | H>R | No |
ClinGen TOPMed |
|
CA8682772 rs771959807 |
57 | G>A | No |
ClinGen ExAC gnomAD |
|
CA8682771 rs745723563 |
57 | G>R | No |
ClinGen ExAC gnomAD |
|
rs775831949 CA8682773 |
58 | G>A | No |
ClinGen ExAC gnomAD |
|
rs930082055 CA292170233 |
58 | G>R | No |
ClinGen TOPMed gnomAD |
|
CA292170243 rs1047107646 |
61 | P>S | No |
ClinGen TOPMed gnomAD |
|
rs1047107646 CA400437238 |
61 | P>T | No |
ClinGen TOPMed gnomAD |
|
CA292170245 rs967994179 |
64 | L>I | No |
ClinGen TOPMed |
|
rs200282847 CA8682784 |
65 | G>S | No |
ClinGen 1000Genomes ExAC TOPMed gnomAD |
|
CA400437416 rs1353369885 |
66 | M>V | No |
ClinGen gnomAD |
|
rs369352640 CA8682785 |
67 | E>Q | No |
ClinGen ESP ExAC TOPMed gnomAD |
|
rs1377606156 CA400437475 |
72 | F>Y | No |
ClinGen gnomAD |
|
rs1323291838 CA400437528 |
78 | S>G | No |
ClinGen TOPMed |
|
rs756820769 CA8682787 |
78 | S>N | No |
ClinGen ExAC gnomAD |
|
rs1320301030 CA400437561 |
80 | N>K | No |
ClinGen TOPMed gnomAD |
|
CA292171513 rs758392709 |
83 | P>S | No |
ClinGen Ensembl |
|
CA292171519 rs201788760 |
85 | K>N | No |
ClinGen Ensembl |
|
rs1160966767 CA400437615 |
85 | K>Q | No |
ClinGen TOPMed |
|
rs779032288 CA8682788 |
86 | I>T | No |
ClinGen ExAC gnomAD |
|
rs1212484580 CA400437641 |
87 | R>G | No |
ClinGen Ensembl |
|
COSM1384928 CA292171534 rs951553081 |
95 | R>W | large_intestine breast [Cosmic] | No |
ClinGen cosmic curated Ensembl |
CA400437833 rs1312790624 |
102 | Y>F | No |
ClinGen gnomAD |
|
rs1304242590 CA400438106 |
109 | R>Q | No |
ClinGen TOPMed |
|
CA400438113 rs1236587996 |
110 | K>R | No |
ClinGen TOPMed |
|
CA8682812 rs768495617 |
114 | A>G | No |
ClinGen ExAC TOPMed gnomAD |
|
rs377332462 CA8682813 |
116 | T>I | No |
ClinGen ESP ExAC TOPMed gnomAD |
|
CA400438178 rs1159721037 |
120 | F>Y | No |
ClinGen gnomAD |
|
CA8682830 rs781068987 |
129 | M>I | No |
ClinGen ExAC gnomAD |
|
rs1236732025 CA400439483 |
131 | V>I | No |
ClinGen gnomAD |
|
rs747867363 CA8682831 |
134 | A>D | No |
ClinGen ExAC gnomAD |
|
CA400439570 rs1256976213 |
137 | T>I | No |
ClinGen TOPMed |
|
rs1356718539 CA400439657 |
144 | R>Q | No |
ClinGen gnomAD |
|
CA8682833 rs183590386 |
145 | N>S | No |
ClinGen 1000Genomes ExAC TOPMed gnomAD |
|
rs1467731056 CA400439726 |
149 | E>D | No |
ClinGen gnomAD |
|
CA8682834 rs749435991 |
156 | V>A | No |
ClinGen ExAC gnomAD |
|
rs1310960425 CA400439815 |
157 | D>N | No |
ClinGen TOPMed |
|
CA8682837 rs746408016 |
163 | Q>* | No |
ClinGen ExAC gnomAD |
|
rs367762054 CA292179639 |
166 | G>R | No |
ClinGen ESP TOPMed gnomAD |
|
rs371239209 CA8682848 |
189 | I>V | No |
ClinGen ESP ExAC TOPMed gnomAD |
|
CA400426318 rs1355015141 |
207 | G>R | No |
ClinGen gnomAD |
|
rs1259284409 CA400426544 |
218 | D>N | No |
ClinGen gnomAD |
|
CA8682865 rs773920494 |
229 | Q>E | No |
ClinGen ExAC gnomAD |
|
CA292150005 rs944521053 |
240 | C>G | No |
ClinGen TOPMed |
|
CA400427840 rs1222867548 |
244 | I>V | No |
ClinGen TOPMed |
|
rs745629253 CA292150014 |
248 | T>I | No |
ClinGen Ensembl |
|
CA400428136 rs1295474347 |
257 | I>V | No |
ClinGen TOPMed gnomAD |
|
CA400428331 rs1306881654 |
264 | I>M | No |
ClinGen gnomAD |
|
rs1011153223 CA292150107 |
268 | S>G | No |
ClinGen TOPMed |
|
rs766645749 CA8682913 VAR_040640 |
272 | R>C | No |
ClinGen UniProt ExAC TOPMed dbSNP gnomAD |
|
rs201582805 CA292150131 |
276 | W>* | No |
ClinGen 1000Genomes |
|
CA8682916 rs147955400 |
281 | A>V | No |
ClinGen ESP ExAC gnomAD |
|
rs1418112814 CA400428748 |
283 | M>T | No |
ClinGen gnomAD |
|
rs756594255 CA400428781 |
284 | Y>C | No |
ClinGen ExAC gnomAD |
|
CA8682918 rs756594255 |
284 | Y>S | No |
ClinGen ExAC gnomAD |
|
CA400430270 rs1212126307 |
293 | F>L | No |
ClinGen TOPMed |
|
rs769735104 CA8682929 |
299 | K>R | No |
ClinGen ExAC gnomAD |
|
CA400430395 rs1568484527 |
302 | I>T | No |
ClinGen Ensembl |
|
rs762824413 CA8682931 |
302 | I>V | No |
ClinGen ExAC gnomAD |
|
rs1351800084 CA400430427 |
304 | K>N | No |
ClinGen TOPMed gnomAD |
|
rs766770547 CA8682932 |
304 | K>R | No |
ClinGen ExAC gnomAD |
|
CA8682933 rs774681501 |
305 | I>V | No |
ClinGen ExAC gnomAD |
|
rs752780303 CA8682936 |
307 | K>R | No |
ClinGen ExAC TOPMed gnomAD |
|
rs752780303 CA8682937 |
307 | K>T | No |
ClinGen ExAC TOPMed gnomAD |
|
CA8682940 rs200443093 |
311 | N>S | No |
ClinGen 1000Genomes ESP ExAC TOPMed gnomAD |
|
CA400430562 rs1232388015 |
314 | P>L | No |
ClinGen gnomAD |
|
CA400430674 rs1228058375 |
320 | A>S | No |
ClinGen TOPMed |
|
CA8682942 rs746643734 |
322 | D>V | No |
ClinGen ExAC gnomAD |
|
CA400430734 rs1331453119 |
323 | L>V | No |
ClinGen TOPMed |
|
rs373201580 CA8682951 |
328 | L>M | No |
ClinGen ESP ExAC TOPMed gnomAD |
|
CA8682952 rs745681533 |
331 | N>H | No |
ClinGen ExAC TOPMed gnomAD |
|
rs1223791841 CA400431026 |
334 | S>T | No |
ClinGen TOPMed |
|
CA400431050 rs1332846171 |
335 | R>H | No |
ClinGen TOPMed |
|
rs1598806787 CA400431093 |
341 | G>A | No |
ClinGen Ensembl |
|
CA8682955 rs764576299 |
343 | A>T | No |
ClinGen ExAC gnomAD |
|
rs1436560081 CA400431110 |
344 | G>E | No |
ClinGen gnomAD |
|
CA400431115 rs1568487397 |
345 | E>* | No |
ClinGen Ensembl |
|
rs754312922 CA8682956 |
346 | V>I | No |
ClinGen ExAC TOPMed gnomAD |
|
CA400431163 rs1189222736 |
348 | A>S | No |
ClinGen TOPMed |
|
CA8682977 rs762342327 |
349 | H>Y | No |
ClinGen ExAC gnomAD |
|
rs975291099 COSM1384933 CA292151455 |
351 | F>L | large_intestine [Cosmic] | No |
ClinGen cosmic curated TOPMed |
CA400431219 rs1259908500 |
355 | I>F | No |
ClinGen TOPMed |
|
rs527883108 CA8682979 |
363 | R>* | No |
ClinGen 1000Genomes ExAC gnomAD |
|
CA8682980 rs763367511 |
363 | R>Q | No |
ClinGen ExAC TOPMed gnomAD |
|
CA400431390 rs1598808033 |
365 | V>G | No |
ClinGen Ensembl |
|
rs767111740 CA8682981 |
367 | P>T | No |
ClinGen ExAC gnomAD |
|
CA400431468 rs1310819944 |
370 | K>R | No |
ClinGen gnomAD |
|
rs1181565268 CA400432487 |
388 | R>H | No |
ClinGen TOPMed |
|
rs760407176 CA8683002 |
399 | T>S | No |
ClinGen ExAC TOPMed gnomAD |
|
rs1328723452 CA400432663 |
400 | L>I | No |
ClinGen gnomAD |
|
CA400432676 rs1220336638 |
401 | S>G | No |
ClinGen TOPMed |
|
rs774803147 CA8683022 |
424 | E>G | No |
ClinGen ExAC gnomAD |
|
CA400433509 rs1419564659 |
433 | R>Q | No |
ClinGen gnomAD |
|
CA400433540 rs1342376918 |
438 | F>S | No |
ClinGen Ensembl |
|
CA400433546 rs1307279204 |
439 | I>F | No |
ClinGen TOPMed |
|
CA400433559 rs1355645776 |
441 | S>C | No |
ClinGen gnomAD |
|
rs776419041 CA8683025 |
441 | S>N | No |
ClinGen ExAC gnomAD |
|
CA400433563 rs1598844554 |
441 | S>R | No |
ClinGen Ensembl |
|
rs761466990 CA8683026 |
443 | R>* | No |
ClinGen ExAC gnomAD |
|
rs1415771859 CA400433571 |
443 | R>Q | No |
ClinGen gnomAD |
|
rs201316437 CA8683027 |
445 | P>S | No |
ClinGen ESP ExAC TOPMed gnomAD |
|
rs146927684 CA8683028 |
446 | V>F | No |
ClinGen ESP ExAC TOPMed gnomAD |
|
rs146927684 CA292155680 |
446 | V>L | No |
ClinGen ESP ExAC TOPMed gnomAD |
|
rs1295366485 CA400433721 |
450 | K>R | No |
ClinGen gnomAD |
|
CA8683046 rs535213123 |
453 | P>R | No |
ClinGen 1000Genomes ExAC gnomAD |
|
rs932504496 CA292156209 |
453 | P>S | No |
ClinGen TOPMed |
|
rs1234773348 CA400433796 |
454 | G>E | No |
ClinGen gnomAD |
|
rs1341855672 CA400433810 |
455 | D>G | No |
ClinGen TOPMed |
|
CA8683048 rs769289034 |
456 | F>S | No |
ClinGen ExAC gnomAD |
|
CA8683049 rs772798588 |
458 | G>R | No |
ClinGen ExAC gnomAD |
|
CA400433930 rs1242329117 |
461 | A>T | No |
ClinGen gnomAD |
|
rs762344908 CA8683050 |
461 | A>V | No |
ClinGen ExAC gnomAD |
|
CA8683052 rs751489954 |
462 | S>L | No |
ClinGen ExAC gnomAD |
|
CA8683053 rs759415083 |
472 | V>G | No |
ClinGen ExAC gnomAD |
|
rs1423417423 CA400434204 |
475 | P>L | No |
ClinGen gnomAD |
|
CA400434216 rs1278779632 |
476 | M>T | No |
ClinGen TOPMed gnomAD |
|
rs1414134583 CA400434209 |
476 | M>V | No |
ClinGen gnomAD |
|
rs137873345 CA292156248 |
484 | M>V | No |
ClinGen ESP TOPMed gnomAD |
|
CA8683057 rs201664077 |
488 | M>V | No |
ClinGen ExAC TOPMed gnomAD |
|
CA400434321 rs1598848397 |
489 | S>R | No |
ClinGen Ensembl |
|
COSM192063 rs1410557496 CA400434348 |
494 | A>T | large_intestine [Cosmic] | No |
ClinGen cosmic curated TOPMed |
CA400434378 rs1568519206 |
498 | I>M | No |
ClinGen Ensembl |
|
rs149039467 CA292156277 |
499 | R>* | No |
ClinGen ESP TOPMed |
|
CA292156279 rs774592527 |
499 | R>Q | No |
ClinGen gnomAD |
|
CA292156280 rs561028562 |
500 | Q>P | No |
ClinGen gnomAD |
|
CA8683060 rs779532384 |
501 | P>L | No |
ClinGen ExAC gnomAD |
|
CA8683062 rs578242191 |
502 | N>H | No |
ClinGen 1000Genomes ExAC gnomAD |
|
rs760585468 CA8683064 |
503 | S>C | No |
ClinGen ExAC gnomAD |
|
CA8683063 rs780595729 |
503 | S>P | No |
ClinGen ExAC gnomAD |
|
CA292156311 rs1040429813 |
504 | G>A | No |
ClinGen TOPMed |
|
CA8683068 rs770364465 |
507 | K>I | No |
ClinGen ExAC gnomAD |
|
rs770364465 CA8683069 |
507 | K>R | No |
ClinGen ExAC gnomAD |
|
rs796087301 CA292156319 |
512 | P>S | No |
ClinGen Ensembl |
|
rs1482169997 CA400434466 |
513 | M>V | No |
ClinGen TOPMed |
|
CA8683070 rs759504757 |
516 | K>R | No |
ClinGen ExAC TOPMed gnomAD |
|
rs1455802572 CA400434495 |
517 | R>Q | No |
ClinGen gnomAD |
|
CA292156359 rs1033258409 |
517 | R>W | No |
ClinGen TOPMed |
|
rs1395231513 CA400434528 |
522 | R>H | No |
ClinGen gnomAD |
|
CA400434538 rs1463062966 |
523 | M>I | No |
ClinGen gnomAD |
|
CA400434542 rs1255679788 |
524 | N>H | No |
ClinGen TOPMed |
|
CA400434551 rs1346438176 |
525 | L>P | No |
ClinGen gnomAD |
No associated diseases with P23443
5 regional properties for P23443
Type | Name | Position | InterPro Accession |
---|---|---|---|
domain | Protein kinase domain | 91 - 352 | IPR000719 |
domain | AGC-kinase, C-terminal | 353 - 423 | IPR000961 |
active_site | Serine/threonine-protein kinase, active site | 214 - 226 | IPR008271 |
binding_site | Protein kinase, ATP binding site | 97 - 123 | IPR017441 |
domain | Protein kinase, C-terminal | 374 - 413 | IPR017892 |
Functions
Description | ||
---|---|---|
EC Number | 2.7.11.1 | Protein-serine/threonine kinases |
Subcellular Localization |
|
|
PANTHER Family | PTHR24351 | RIBOSOMAL PROTEIN S6 KINASE |
PANTHER Subfamily | PTHR24351:SF48 | RIBOSOMAL PROTEIN S6 KINASE BETA-1 |
PANTHER Protein Class | protein modifying enzyme | |
PANTHER Pathway Category |
CCKR signaling map p70S6K1 p53 pathway by glucose deprivation S6K PI3 kinase pathway S6K Insulin/IGF pathway-mitogen activated protein kinase kinase/MAP kinase cascade P90 RSK PDGF signaling pathway p90RSK |
10 GO annotations of cellular component
Name | Definition |
---|---|
cell surface | The external part of the cell wall and/or plasma membrane. |
cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
mitochondrial outer membrane | The outer, i.e. cytoplasm-facing, lipid bilayer of the mitochondrial envelope. |
mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
neuron projection | A prolongation or process extending from a nerve cell, e.g. an axon or dendrite. |
nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
perinuclear region of cytoplasm | Cytoplasm situated near, or occurring around, the nucleus. |
synapse | The junction between an axon of one neuron and a dendrite of another neuron, a muscle fiber or a glial cell. As the axon approaches the synapse it enlarges into a specialized structure, the presynaptic terminal bouton, which contains mitochondria and synaptic vesicles. At the tip of the terminal bouton is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic terminal bouton secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane. |
10 GO annotations of molecular function
Name | Definition |
---|---|
ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
identical protein binding | Binding to an identical protein or proteins. |
PDZ domain binding | Binding to a PDZ domain of a protein, a domain found in diverse signaling proteins. |
peptide binding | Binding to a peptide, an organic compound comprising two or more amino acids linked by peptide bonds. |
protein kinase activity | Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP. |
protein phosphatase 2A binding | Binding to protein phosphatase 2A. |
protein serine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. |
protein serine/threonine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate. |
protein serine/threonine/tyrosine kinase activity | Catalysis of the reactions: ATP + a protein serine = ADP + protein serine phosphate; ATP + a protein threonine = ADP + protein threonine phosphate; and ATP + a protein tyrosine = ADP + protein tyrosine phosphate. |
ribosomal protein S6 kinase activity | Catalysis of the reaction: ribosomal protein S6 + ATP = ribosomal protein S6 phosphate + ATP. |
44 GO annotations of biological process
Name | Definition |
---|---|
aging | A developmental process that is a deterioration and loss of function over time. Aging includes loss of functions such as resistance to disease, homeostasis, and fertility, as well as wear and tear. Aging includes cellular senescence, but is more inclusive. May precede death and may succeed developmental maturation (GO:0021700). |
apoptotic process | A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died. |
behavioral fear response | An acute behavioral change resulting from a perceived external threat. |
cell migration | The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues. Cell migration is a central process in the development and maintenance of multicellular organisms. |
cellular response to dexamethasone stimulus | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a dexamethasone stimulus. |
cellular response to growth factor stimulus | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a growth factor stimulus. |
cellular response to insulin stimulus | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an insulin stimulus. Insulin is a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms. |
cellular response to interferon-gamma | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interferon-gamma stimulus. Interferon gamma is the only member of the type II interferon found so far. |
G1/S transition of mitotic cell cycle | The mitotic cell cycle transition by which a cell in G1 commits to S phase. The process begins with the build up of G1 cyclin-dependent kinase (G1 CDK), resulting in the activation of transcription of G1 cyclins. The process ends with the positive feedback of the G1 cyclins on the G1 CDK which commits the cell to S phase, in which DNA replication is initiated. |
germ cell development | The process whose specific outcome is the progression of an immature germ cell over time, from its formation to the mature structure (gamete). A germ cell is any reproductive cell in a multicellular organism. |
long-chain fatty acid import into cell | The directed movement of a long-chain fatty acid from outside of a cell into a cell. This may occur via transport across the plasma membrane or via endocytosis. A long-chain fatty acid is a fatty acid with a chain length between C13 and C22. |
long-term memory | The memory process that deals with the storage, retrieval and modification of information a long time (typically weeks, months or years) after receiving that information. This type of memory is typically dependent on gene transcription regulated by second messenger activation. |
negative regulation of apoptotic process | Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process. |
negative regulation of extrinsic apoptotic signaling pathway | Any process that stops, prevents or reduces the frequency, rate or extent of extrinsic apoptotic signaling pathway. |
negative regulation of insulin receptor signaling pathway | Any process that stops, prevents, or reduces the frequency, rate or extent of insulin receptor signaling. |
peptidyl-serine phosphorylation | The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine. |
phosphatidylinositol-mediated signaling | The series of molecular signals in which a cell uses a phosphatidylinositol-mediated signaling to convert a signal into a response. Phosphatidylinositols include phosphatidylinositol (PtdIns) and its phosphorylated derivatives. |
positive regulation of mitotic cell cycle | Any process that activates or increases the rate or extent of progression through the mitotic cell cycle. |
positive regulation of skeletal muscle tissue growth | Any process that activates, maintains or increases the rate of skeletal muscle growth. |
positive regulation of smooth muscle cell migration | Any process that activates, maintains or increases the frequency, rate or extent of smooth muscle cell migration. |
positive regulation of smooth muscle cell proliferation | Any process that activates or increases the rate or extent of smooth muscle cell proliferation. |
positive regulation of translation | Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA. |
positive regulation of translational initiation | Any process that activates or increases the frequency, rate or extent of translational initiation. |
protein kinase B signaling | A series of reactions, mediated by the intracellular serine/threonine kinase protein kinase B (also called AKT), which occurs as a result of a single trigger reaction or compound. |
regulation of glucose import | Any process that modulates the frequency, rate or extent of the import of the hexose monosaccharide glucose into a cell or organelle. |
response to electrical stimulus involved in regulation of muscle adaptation | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an electrical stimulus. This process occurs as part of the regulation of muscle adaptation. |
response to ethanol | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ethanol stimulus. |
response to glucagon | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a glucagon stimulus. |
response to glucose | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a glucose stimulus. |
response to heat | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism. |
response to leucine | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a leucine stimulus. |
response to lipopolysaccharide | Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lipopolysaccharide stimulus; lipopolysaccharide is a major component of the cell wall of gram-negative bacteria. |
response to mechanical stimulus | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a mechanical stimulus. |
response to nutrient | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a nutrient stimulus. |
response to nutrient levels | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus reflecting the presence, absence, or concentration of nutrients. |
response to testosterone | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a testosterone stimulus. |
response to toxic substance | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a toxic stimulus. |
response to tumor necrosis factor | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a tumor necrosis factor stimulus. |
response to wounding | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to the organism. |
response to xenobiotic stimulus | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a xenobiotic, a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical. |
signal transduction | The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell. |
skeletal muscle atrophy | A process, occurring in skeletal muscle, that is characterized by a decrease in protein content, fiber diameter, force production and fatigue resistance in response to different conditions such as starvation, aging and disuse. |
skeletal muscle contraction | A process in which force is generated within skeletal muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. In the skeletal muscle, the muscle contraction takes advantage of an ordered sarcomeric structure and in most cases it is under voluntary control. |
TOR signaling | The series of molecular signals mediated by TOR (Target of rapamycin) proteins, members of the phosphoinositide (PI) 3-kinase related kinase (PIKK) family that act as serine/threonine kinases in response to nutrient availability or growth factors. |
17 homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
Q6TJY3 | RPS6KB1 | Ribosomal protein S6 kinase beta-1 | Bos taurus (Bovine) | SS |
Q9HBY8 | SGK2 | Serine/threonine-protein kinase Sgk2 | Homo sapiens (Human) | SS |
O00141 | SGK1 | Serine/threonine-protein kinase Sgk1 | Homo sapiens (Human) | PR |
Q96BR1 | SGK3 | Serine/threonine-protein kinase Sgk3 | Homo sapiens (Human) | SS |
Q15349 | RPS6KA2 | Ribosomal protein S6 kinase alpha-2 | Homo sapiens (Human) | SS |
Q15418 | RPS6KA1 | Ribosomal protein S6 kinase alpha-1 | Homo sapiens (Human) | EV |
Q9UK32 | RPS6KA6 | Ribosomal protein S6 kinase alpha-6 | Homo sapiens (Human) | SS |
P51812 | RPS6KA3 | Ribosomal protein S6 kinase alpha-3 | Homo sapiens (Human) | EV |
O75676 | RPS6KA4 | Ribosomal protein S6 kinase alpha-4 | Homo sapiens (Human) | SS |
O75582 | RPS6KA5 | Ribosomal protein S6 kinase alpha-5 | Homo sapiens (Human) | SS |
Q9UBS0 | RPS6KB2 | Ribosomal protein S6 kinase beta-2 | Homo sapiens (Human) | PR |
Q8QZV4 | Stk32c | Serine/threonine-protein kinase 32C | Mus musculus (Mouse) | PR |
Q9Z1M4 | Rps6kb2 | Ribosomal protein S6 kinase beta-2 | Mus musculus (Mouse) | SS |
Q9ERE3 | Sgk3 | Serine/threonine-protein kinase Sgk3 | Mus musculus (Mouse) | PR |
Q8BSK8 | Rps6kb1 | Ribosomal protein S6 kinase beta-1 | Mus musculus (Mouse) | SS |
P67999 | Rps6kb1 | Ribosomal protein S6 kinase beta-1 | Rattus norvegicus (Rat) | EV SS |
Q5BKK4 | sgk1 | Serine/threonine-protein kinase Sgk1 | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | PR |
10 | 20 | 30 | 40 | 50 | 60 |
MRRRRRRDGF | YPAPDFRDRE | AEDMAGVFDI | DLDQPEDAGS | EDELEEGGQL | NESMDHGGVG |
70 | 80 | 90 | 100 | 110 | 120 |
PYELGMEHCE | KFEISETSVN | RGPEKIRPEC | FELLRVLGKG | GYGKVFQVRK | VTGANTGKIF |
130 | 140 | 150 | 160 | 170 | 180 |
AMKVLKKAMI | VRNAKDTAHT | KAERNILEEV | KHPFIVDLIY | AFQTGGKLYL | ILEYLSGGEL |
190 | 200 | 210 | 220 | 230 | 240 |
FMQLEREGIF | MEDTACFYLA | EISMALGHLH | QKGIIYRDLK | PENIMLNHQG | HVKLTDFGLC |
250 | 260 | 270 | 280 | 290 | 300 |
KESIHDGTVT | HTFCGTIEYM | APEILMRSGH | NRAVDWWSLG | ALMYDMLTGA | PPFTGENRKK |
310 | 320 | 330 | 340 | 350 | 360 |
TIDKILKCKL | NLPPYLTQEA | RDLLKKLLKR | NAASRLGAGP | GDAGEVQAHP | FFRHINWEEL |
370 | 380 | 390 | 400 | 410 | 420 |
LARKVEPPFK | PLLQSEEDVS | QFDSKFTRQT | PVDSPDDSTL | SESANQVFLG | FTYVAPSVLE |
430 | 440 | 450 | 460 | 470 | 480 |
SVKEKFSFEP | KIRSPRRFIG | SPRTPVSPVK | FSPGDFWGRG | ASASTANPQT | PVEYPMETSG |
490 | 500 | 510 | 520 | ||
IEQMDVTMSG | EASAPLPIRQ | PNSGPYKKQA | FPMISKRPEH | LRMNL |