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Q15418

- KS6A1_HUMAN

UniProt

Q15418 - KS6A1_HUMAN

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Protein

Ribosomal protein S6 kinase alpha-1

Gene

RPS6KA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1, which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4). Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression.11 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Enzyme regulationi

Upon extracellular signal or mitogen stimulation, phosphorylated at Thr-573 in the C-terminal kinase domain (CTKD) by MAPK1/ERK2 and MAPK3/ERK1. The activated CTKD then autophosphorylates Ser-380, allowing binding of PDPK1, which in turn phosphorylates Ser-221 in the N-terminal kinase domain (NTDK) leading to the full activation of the protein and subsequent phosphorylation of the substrates by the NTKD.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei94 – 941ATPPROSITE-ProRule annotation
Active sitei187 – 1871Proton acceptorBy similarity
Binding sitei447 – 4471ATPPROSITE-ProRule annotation
Active sitei535 – 5351Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi68 – 769ATPPROSITE-ProRule annotation
Nucleotide bindingi424 – 4329ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: UniProtKB
  3. magnesium ion binding Source: InterPro
  4. protein serine/threonine/tyrosine kinase activity Source: MGI
  5. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. axon guidance Source: Reactome
  2. cell cycle Source: UniProtKB-KW
  3. innate immune response Source: Reactome
  4. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  5. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  6. negative regulation of apoptotic process Source: UniProtKB
  7. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  8. neurotrophin TRK receptor signaling pathway Source: Reactome
  9. positive regulation of cell differentiation Source: UniProtKB
  10. positive regulation of cell growth Source: UniProtKB
  11. positive regulation of hepatic stellate cell activation Source: UniProtKB
  12. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  13. regulation of DNA-templated transcription in response to stress Source: UniProtKB
  14. regulation of translation in response to stress Source: UniProtKB
  15. signal transduction Source: ProtInc
  16. stress-activated MAPK cascade Source: Reactome
  17. synaptic transmission Source: Reactome
  18. toll-like receptor 10 signaling pathway Source: Reactome
  19. toll-like receptor 2 signaling pathway Source: Reactome
  20. toll-like receptor 3 signaling pathway Source: Reactome
  21. toll-like receptor 4 signaling pathway Source: Reactome
  22. toll-like receptor 5 signaling pathway Source: Reactome
  23. toll-like receptor 9 signaling pathway Source: Reactome
  24. toll-like receptor signaling pathway Source: Reactome
  25. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  26. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  27. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Stress response

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiREACT_120966. Gastrin-CREB signalling pathway via PKC and MAPK.
REACT_12524. CREB phosphorylation.
REACT_12599. ERK/MAPK targets.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_20510. RSK activation.
REACT_20568. CREB phosphorylation through the activation of Ras.
REACT_22365. Recycling pathway of L1.
SignaLinkiQ15418.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosomal protein S6 kinase alpha-1 (EC:2.7.11.1)
Short name:
S6K-alpha-1
Alternative name(s):
90 kDa ribosomal protein S6 kinase 1
Short name:
p90-RSK 1
Short name:
p90RSK1
Short name:
p90S6K
MAP kinase-activated protein kinase 1a
Short name:
MAPK-activated protein kinase 1a
Short name:
MAPKAP kinase 1a
Short name:
MAPKAPK-1a
Ribosomal S6 kinase 1
Short name:
RSK-1
Gene namesi
Name:RPS6KA1
Synonyms:MAPKAPK1A, RSK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:10430. RPS6KA1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. nucleoplasm Source: Reactome
  4. nucleus Source: HPA
  5. spindle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34845.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 735735Ribosomal protein S6 kinase alpha-1PRO_0000086198Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541Phosphoserine1 Publication
Modified residuei221 – 2211Phosphoserine; by PDPK11 Publication
Modified residuei307 – 3071Phosphoserine1 Publication
Modified residuei348 – 3481Phosphothreonine
Modified residuei359 – 3591Phosphothreonine5 Publications
Modified residuei363 – 3631Phosphoserine5 Publications
Modified residuei369 – 3691Phosphoserine2 Publications
Modified residuei380 – 3801Phosphoserine; by autocatalysis5 Publications
Modified residuei573 – 5731Phosphothreonine1 Publication
Modified residuei732 – 7321Phosphoserine1 Publication

Post-translational modificationi

Activated by phosphorylation at Ser-221 by PDPK1. Autophosphorylated on Ser-380, as part of the activation process. May be phosphorylated at Thr-359 and Ser-363 by MAPK1/ERK2 and MAPK3/ERK1.6 Publications
N-terminal myristoylation results in an activated kinase in the absence of added growth factors.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ15418.
PaxDbiQ15418.
PRIDEiQ15418.

2D gel databases

UCD-2DPAGEQ15418.

PTM databases

PhosphoSiteiQ15418.

Expressioni

Gene expression databases

BgeeiQ15418.
CleanExiHS_RPS6KA1.
ExpressionAtlasiQ15418. baseline and differential.
GenevestigatoriQ15418.

Organism-specific databases

HPAiCAB003852.
HPA007981.

Interactioni

Subunit structurei

Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in quiescent cells. Transiently dissociates following mitogenic stimulation. Interacts with ETV1/ER81 and FGFR1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSP90AB1P082382EBI-963034,EBI-352572
VASPP505524EBI-963034,EBI-748201

Protein-protein interaction databases

BioGridi112109. 57 interactions.
DIPiDIP-29987N.
IntActiQ15418. 28 interactions.
MINTiMINT-207205.
STRINGi9606.ENSP00000363277.

Structurei

Secondary structure

1
735
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi59 – 613Combined sources
Beta strandi62 – 7110Combined sources
Beta strandi74 – 818Combined sources
Beta strandi83 – 864Combined sources
Beta strandi90 – 967Combined sources
Beta strandi127 – 1337Combined sources
Beta strandi136 – 1416Combined sources
Helixi149 – 1568Combined sources
Helixi161 – 18020Combined sources
Helixi190 – 1923Combined sources
Beta strandi193 – 1953Combined sources
Beta strandi197 – 1993Combined sources
Beta strandi201 – 2033Combined sources
Helixi226 – 2283Combined sources
Helixi231 – 2344Combined sources
Helixi241 – 25717Combined sources
Helixi267 – 27610Combined sources
Helixi287 – 29610Combined sources
Turni301 – 3033Combined sources
Beta strandi307 – 3104Combined sources
Helixi312 – 3165Combined sources
Helixi319 – 3213Combined sources
Helixi326 – 3305Combined sources
Beta strandi418 – 42710Combined sources
Beta strandi430 – 4378Combined sources
Turni438 – 4403Combined sources
Beta strandi443 – 4508Combined sources
Helixi457 – 46610Combined sources
Beta strandi475 – 4806Combined sources
Beta strandi482 – 4898Combined sources
Helixi497 – 5026Combined sources
Beta strandi503 – 5053Combined sources
Helixi509 – 52820Combined sources
Helixi538 – 5403Combined sources
Beta strandi541 – 5455Combined sources
Helixi550 – 5523Combined sources
Beta strandi553 – 5553Combined sources
Turni574 – 5763Combined sources
Helixi588 – 60922Combined sources
Helixi622 – 63110Combined sources
Helixi639 – 6435Combined sources
Helixi646 – 65510Combined sources
Helixi660 – 6623Combined sources
Helixi666 – 6705Combined sources
Helixi673 – 6764Combined sources
Helixi678 – 6803Combined sources
Helixi691 – 70717Combined sources
Helixi717 – 7193Combined sources
Helixi721 – 7244Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WNTX-ray2.40A/B413-719[»]
2Z7QX-ray2.00A33-353[»]
2Z7RX-ray2.00A33-353[»]
2Z7SX-ray2.10A33-353[»]
3RNYX-ray2.70A/B411-735[»]
3TEIX-ray2.40B712-735[»]
4H3PX-ray2.30B/E712-735[»]
ProteinModelPortaliQ15418.
SMRiQ15418. Positions 10-709.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15418.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini62 – 321260Protein kinase 1PROSITE-ProRule annotationAdd
BLAST
Domaini322 – 39170AGC-kinase C-terminalAdd
BLAST
Domaini418 – 675258Protein kinase 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 2 protein kinase domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00770000120454.
HOVERGENiHBG108317.
InParanoidiQ15418.
KOiK04373.
OMAiPWITQKD.
OrthoDBiEOG7B8S38.
PhylomeDBiQ15418.
TreeFamiTF313438.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016239. Ribosomal_S6_kinase_II.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 2 hits.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000606. Ribsml_S6_kin_2. 1 hit.
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 2 hits.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 2 hits.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00108. PROTEIN_KINASE_ST. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15418-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPLAQLKEPW PLMELVPLDP ENGQTSGEEA GLQPSKDEGV LKEISITHHV
60 70 80 90 100
KAGSEKADPS HFELLKVLGQ GSFGKVFLVR KVTRPDSGHL YAMKVLKKAT
110 120 130 140 150
LKVRDRVRTK MERDILADVN HPFVVKLHYA FQTEGKLYLI LDFLRGGDLF
160 170 180 190 200
TRLSKEVMFT EEDVKFYLAE LALGLDHLHS LGIIYRDLKP ENILLDEEGH
210 220 230 240 250
IKLTDFGLSK EAIDHEKKAY SFCGTVEYMA PEVVNRQGHS HSADWWSYGV
260 270 280 290 300
LMFEMLTGSL PFQGKDRKET MTLILKAKLG MPQFLSTEAQ SLLRALFKRN
310 320 330 340 350
PANRLGSGPD GAEEIKRHVF YSTIDWNKLY RREIKPPFKP AVAQPDDTFY
360 370 380 390 400
FDTEFTSRTP KDSPGIPPSA GAHQLFRGFS FVATGLMEDD GKPRAPQAPL
410 420 430 440 450
HSVVQQLHGK NLVFSDGYVV KETIGVGSYS ECKRCVHKAT NMEYAVKVID
460 470 480 490 500
KSKRDPSEEI EILLRYGQHP NIITLKDVYD DGKHVYLVTE LMRGGELLDK
510 520 530 540 550
ILRQKFFSER EASFVLHTIG KTVEYLHSQG VVHRDLKPSN ILYVDESGNP
560 570 580 590 600
ECLRICDFGF AKQLRAENGL LMTPCYTANF VAPEVLKRQG YDEGCDIWSL
610 620 630 640 650
GILLYTMLAG YTPFANGPSD TPEEILTRIG SGKFTLSGGN WNTVSETAKD
660 670 680 690 700
LVSKMLHVDP HQRLTAKQVL QHPWVTQKDK LPQSQLSHQD LQLVKGAMAA
710 720 730
TYSALNSSKP TPQLKPIESS ILAQRRVRKL PSTTL
Length:735
Mass (Da):82,723
Last modified:April 16, 2002 - v2
Checksum:i765731A4442A53DF
GO
Isoform 2 (identifier: Q15418-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MPLAQLKEPW...GEEAGLQPSK → MEQDPKPPRL...GPGSGPQRDS

Show »
Length:744
Mass (Da):83,932
Checksum:i3121E64369EBDBBF
GO
Isoform 3 (identifier: Q15418-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-92: Missing.

Note: No experimental confirmation available.

Show »
Length:643
Mass (Da):72,698
Checksum:iB8362021FCCC17B5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti609 – 6091A → T in BAF85411. (PubMed:14702039)Curated
Sequence conflicti619 – 6191S → G in BAF85411. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti335 – 3351K → T.2 Publications
Corresponds to variant rs2229712 [ dbSNP | Ensembl ].
VAR_021864

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9292Missing in isoform 3. 1 PublicationVSP_041580Add
BLAST
Alternative sequencei1 – 3636MPLAQ…LQPSK → MEQDPKPPRLRLWALIPWLP RKQRPRISQTSLPVPGPGSG PQRDS in isoform 2. 1 PublicationVSP_041380Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07597 mRNA. Translation: AAC82497.1.
AK292722 mRNA. Translation: BAF85411.1.
AK299007 mRNA. Translation: BAH12926.1.
AK315730 mRNA. Translation: BAG38085.1.
AL109743 Genomic DNA. Translation: CAC36348.1.
AL627313 Genomic DNA. Translation: CAI14647.1.
AL627313 Genomic DNA. Translation: CAI14648.1.
AL627313 Genomic DNA. Translation: CAI14649.1.
CH471059 Genomic DNA. Translation: EAX07799.1.
BC014966 mRNA. Translation: AAH14966.1.
CCDSiCCDS284.1. [Q15418-1]
CCDS30649.1. [Q15418-2]
PIRiI51901.
RefSeqiNP_001006666.1. NM_001006665.1. [Q15418-2]
NP_002944.2. NM_002953.3. [Q15418-1]
XP_005246024.1. XM_005245967.2. [Q15418-3]
UniGeneiHs.149957.

Genome annotation databases

EnsembliENST00000374168; ENSP00000363283; ENSG00000117676. [Q15418-1]
ENST00000526792; ENSP00000431651; ENSG00000117676. [Q15418-3]
ENST00000531382; ENSP00000435412; ENSG00000117676. [Q15418-2]
GeneIDi6195.
KEGGihsa:6195.
UCSCiuc001bmr.1. human. [Q15418-1]
uc001bms.1. human. [Q15418-2]

Polymorphism databases

DMDMi20178306.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07597 mRNA. Translation: AAC82497.1 .
AK292722 mRNA. Translation: BAF85411.1 .
AK299007 mRNA. Translation: BAH12926.1 .
AK315730 mRNA. Translation: BAG38085.1 .
AL109743 Genomic DNA. Translation: CAC36348.1 .
AL627313 Genomic DNA. Translation: CAI14647.1 .
AL627313 Genomic DNA. Translation: CAI14648.1 .
AL627313 Genomic DNA. Translation: CAI14649.1 .
CH471059 Genomic DNA. Translation: EAX07799.1 .
BC014966 mRNA. Translation: AAH14966.1 .
CCDSi CCDS284.1. [Q15418-1 ]
CCDS30649.1. [Q15418-2 ]
PIRi I51901.
RefSeqi NP_001006666.1. NM_001006665.1. [Q15418-2 ]
NP_002944.2. NM_002953.3. [Q15418-1 ]
XP_005246024.1. XM_005245967.2. [Q15418-3 ]
UniGenei Hs.149957.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2WNT X-ray 2.40 A/B 413-719 [» ]
2Z7Q X-ray 2.00 A 33-353 [» ]
2Z7R X-ray 2.00 A 33-353 [» ]
2Z7S X-ray 2.10 A 33-353 [» ]
3RNY X-ray 2.70 A/B 411-735 [» ]
3TEI X-ray 2.40 B 712-735 [» ]
4H3P X-ray 2.30 B/E 712-735 [» ]
ProteinModelPortali Q15418.
SMRi Q15418. Positions 10-709.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112109. 57 interactions.
DIPi DIP-29987N.
IntActi Q15418. 28 interactions.
MINTi MINT-207205.
STRINGi 9606.ENSP00000363277.

Chemistry

BindingDBi Q15418.
ChEMBLi CHEMBL2553.
GuidetoPHARMACOLOGYi 1527.

PTM databases

PhosphoSitei Q15418.

Polymorphism databases

DMDMi 20178306.

2D gel databases

UCD-2DPAGE Q15418.

Proteomic databases

MaxQBi Q15418.
PaxDbi Q15418.
PRIDEi Q15418.

Protocols and materials databases

DNASUi 6195.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000374168 ; ENSP00000363283 ; ENSG00000117676 . [Q15418-1 ]
ENST00000526792 ; ENSP00000431651 ; ENSG00000117676 . [Q15418-3 ]
ENST00000531382 ; ENSP00000435412 ; ENSG00000117676 . [Q15418-2 ]
GeneIDi 6195.
KEGGi hsa:6195.
UCSCi uc001bmr.1. human. [Q15418-1 ]
uc001bms.1. human. [Q15418-2 ]

Organism-specific databases

CTDi 6195.
GeneCardsi GC01P026856.
HGNCi HGNC:10430. RPS6KA1.
HPAi CAB003852.
HPA007981.
MIMi 601684. gene.
neXtProti NX_Q15418.
PharmGKBi PA34845.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00770000120454.
HOVERGENi HBG108317.
InParanoidi Q15418.
KOi K04373.
OMAi PWITQKD.
OrthoDBi EOG7B8S38.
PhylomeDBi Q15418.
TreeFami TF313438.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 2681.
Reactomei REACT_120966. Gastrin-CREB signalling pathway via PKC and MAPK.
REACT_12524. CREB phosphorylation.
REACT_12599. ERK/MAPK targets.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_20510. RSK activation.
REACT_20568. CREB phosphorylation through the activation of Ras.
REACT_22365. Recycling pathway of L1.
SignaLinki Q15418.

Miscellaneous databases

ChiTaRSi RPS6KA1. human.
EvolutionaryTracei Q15418.
GeneWikii RPS6KA1.
GenomeRNAii 6195.
NextBioi 24057.
PROi Q15418.
SOURCEi Search...

Gene expression databases

Bgeei Q15418.
CleanExi HS_RPS6KA1.
ExpressionAtlasi Q15418. baseline and differential.
Genevestigatori Q15418.

Family and domain databases

InterProi IPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016239. Ribosomal_S6_kinase_II.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 2 hits.
PF00433. Pkinase_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF000606. Ribsml_S6_kin_2. 1 hit.
SMARTi SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 2 hits.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 2 hits.
PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 2 hits.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00108. PROTEIN_KINASE_ST. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human rsk isoforms: cloning and characterization of tissue-specific expression."
    Moller D.E., Xia C.-H., Tang W., Zhu A.X., Jakubowski M.
    Am. J. Physiol. 266:C351-C359(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-335.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
    Tissue: Testis and Thyroid.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Colon.
  6. "Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB."
    Deak M., Clifton A.D., Lucocq J.M., Alessi D.R.
    EMBO J. 17:4426-4441(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "Identification of regulatory phosphorylation sites in mitogen-activated protein kinase (MAPK)-activated protein kinase-1a/p90rsk that are inducible by MAPK."
    Dalby K.N., Morrice N., Caudwell F.B., Avruch J., Cohen P.
    J. Biol. Chem. 273:1496-1505(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT SER-221; THR-359; SER-363; SER-380; THR-573 AND SER-732.
  8. "Rsk1 mediates a MEK-MAP kinase cell survival signal."
    Shimamura A., Ballif B.A., Richards S.A., Blenis J.
    Curr. Biol. 10:127-135(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF BAD.
  9. "C/EBPbeta phosphorylation by RSK creates a functional XEXD caspase inhibitory box critical for cell survival."
    Buck M., Poli V., Hunter T., Chojkier M.
    Mol. Cell 8:807-816(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CEBPB.
  10. "Regulation of the ETS transcription factor ER81 by the 90-kDa ribosomal S6 kinase 1 and protein kinase A."
    Wu J., Janknecht R.
    J. Biol. Chem. 277:42669-42679(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF ETV1/ER81, INTERACTION WITH ETV1/ER81.
  11. "Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity."
    Roux P.P., Richards S.A., Blenis J.
    Mol. Cell. Biol. 23:4796-4804(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAPK1 OR MAPK3.
  12. "90-kDa ribosomal S6 kinase is a direct target for the nuclear fibroblast growth factor receptor 1 (FGFR1): role in FGFR1 signaling."
    Hu Y., Fang X., Dunham S.M., Prada C., Stachowiak E.K., Stachowiak M.K.
    J. Biol. Chem. 279:29325-29335(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FGFR1, ENZYME REGULATION, SUBCELLULAR LOCATION.
  13. "Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase."
    Roux P.P., Ballif B.A., Anjum R., Gygi S.P., Blenis J.
    Proc. Natl. Acad. Sci. U.S.A. 101:13489-13494(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MTOR SIGNALING, INTERACTION WITH TSC2.
  14. "The tumor suppressor DAP kinase is a target of RSK-mediated survival signaling."
    Anjum R., Roux P.P., Ballif B.A., Gygi S.P., Blenis J.
    Curr. Biol. 15:1762-1767(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF DAPK1.
  15. "Nur77 is phosphorylated in cells by RSK in response to mitogenic stimulation."
    Wingate A.D., Campbell D.G., Peggie M., Arthur J.S.
    Biochem. J. 393:715-724(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF NR4A1/NUR77.
  16. "The mTOR/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity."
    Shahbazian D., Roux P.P., Mieulet V., Cohen M.S., Raught B., Taunton J., Hershey J.W., Blenis J., Pende M., Sonenberg N.
    EMBO J. 25:2781-2791(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANSLATION REGULATION, FUNCTION IN PHOSPHORYLATION OF EIF4B.
  17. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "RAS/ERK signaling promotes site-specific ribosomal protein S6 phosphorylation via RSK and stimulates cap-dependent translation."
    Roux P.P., Shahbazian D., Vu H., Holz M.K., Cohen M.S., Taunton J., Sonenberg N., Blenis J.
    J. Biol. Chem. 282:14056-14064(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF RPS6.
  19. "Oncogenic MAPK signaling stimulates mTORC1 activity by promoting RSK-mediated raptor phosphorylation."
    Carriere A., Cargnello M., Julien L.A., Gao H., Bonneil E., Thibault P., Roux P.P.
    Curr. Biol. 18:1269-1277(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MTOR SIGNALING.
  20. "The RSK factors of activating the Ras/MAPK signaling cascade."
    Carriere A., Ray H., Blenis J., Roux P.P.
    Front. Biosci. 13:4258-4275(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION, REVIEW ON ENZYME REGULATION.
  21. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359; SER-363 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "The RSK family of kinases: emerging roles in cellular signalling."
    Anjum R., Blenis J.
    Nat. Rev. Mol. Cell Biol. 9:747-758(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION, REVIEW ON ENZYME REGULATION.
  23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359; SER-363; SER-369 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-307; THR-359; SER-363; SER-369 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359 AND SER-363, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "Crystal structures of the N-terminal kinase domain of human RSK1 bound to three different ligands: Implications for the design of RSK1 specific inhibitors."
    Ikuta M., Kornienko M., Byrne N., Reid J.C., Mizuarai S., Kotani H., Munshi S.K.
    Protein Sci. 16:2626-2635(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 33-353 IN COMPLEX WITH INHIBITOR.
  29. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-335.

Entry informationi

Entry nameiKS6A1_HUMAN
AccessioniPrimary (citable) accession number: Q15418
Secondary accession number(s): A6NGG4
, A8K9K7, B2RDY8, B7Z5J0, Q5SVM5, Q5SVM8, Q5SVM9, Q96C05, Q9BQK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: April 16, 2002
Last modified: November 26, 2014
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3