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P51812

- KS6A3_HUMAN

UniProt

P51812 - KS6A3_HUMAN

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Protein

Ribosomal protein S6 kinase alpha-3

Gene

RPS6KA3

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 and histone H3 at 'Ser-10', 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. In LPS-stimulated dendritic cells, is involved in TLR4-induced macropinocytosis, and in myeloma cells, acts as effector of FGFR3-mediated transformation signaling, after direct phosphorylation at Tyr-529 by FGFR3. Phosphorylates DAPK1.7 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Enzyme regulationi

Upon extracellular signal or mitogen stimulation, phosphorylated at Thr-577 in the C-terminal kinase domain (CTKD) by MAPK1/ERK2 and MAPK3/ERK1. The activated CTKD then autophosphorylates Ser-386, allowing binding of PDPK1, which in turn phosphorylates Ser-227 in the N-terminal kinase domain (NTDK) leading to the full activation of the protein and subsequent phosphorylation of the substrates by the NTKD.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei100 – 1001ATPPROSITE-ProRule annotation
Active sitei193 – 1931Proton acceptorBy similarity
Binding sitei451 – 4511ATPPROSITE-ProRule annotation
Active sitei539 – 5391Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi74 – 829ATPPROSITE-ProRule annotation
Nucleotide bindingi428 – 4369ATPPROSITE-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 kinase activity Source: ProtInc
  5. protein serine/threonine kinase activity Source: ProtInc

GO - Biological processi

  1. axon guidance Source: Reactome
  2. cell cycle Source: UniProtKB-KW
  3. central nervous system development Source: ProtInc
  4. innate immune response Source: Reactome
  5. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  6. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  7. negative regulation of apoptotic process Source: UniProtKB
  8. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  9. neurotrophin TRK receptor signaling pathway Source: Reactome
  10. positive regulation of cell differentiation Source: UniProtKB
  11. positive regulation of cell growth 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. response to lipopolysaccharide Source: UniProtKB
  16. signal transduction Source: ProtInc
  17. skeletal system development Source: ProtInc
  18. stress-activated MAPK cascade Source: Reactome
  19. synaptic transmission Source: Reactome
  20. toll-like receptor 10 signaling pathway Source: Reactome
  21. toll-like receptor 2 signaling pathway Source: Reactome
  22. toll-like receptor 3 signaling pathway Source: Reactome
  23. toll-like receptor 4 signaling pathway Source: Reactome
  24. toll-like receptor 5 signaling pathway Source: Reactome
  25. toll-like receptor 9 signaling pathway Source: Reactome
  26. toll-like receptor signaling pathway Source: UniProtKB
  27. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  28. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  29. 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.
SignaLinkiP51812.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosomal protein S6 kinase alpha-3 (EC:2.7.11.1)
Short name:
S6K-alpha-3
Alternative name(s):
90 kDa ribosomal protein S6 kinase 3
Short name:
p90-RSK 3
Short name:
p90RSK3
Insulin-stimulated protein kinase 1
Short name:
ISPK-1
MAP kinase-activated protein kinase 1b
Short name:
MAPK-activated protein kinase 1b
Short name:
MAPKAP kinase 1b
Short name:
MAPKAPK-1b
Ribosomal S6 kinase 2
Short name:
RSK-2
pp90RSK2
Gene namesi
Name:RPS6KA3
Synonyms:ISPK1, MAPKAPK1B, RSK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:10432. RPS6KA3.

Subcellular locationi

Nucleus By similarity. Cytoplasm By similarity

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Coffin-Lowry syndrome (CLS) [MIM:303600]: A X-linked mental retardation associated with facial and digital dysmorphisms, progressive skeletal malformations, growth retardation, hearing deficit and paroxysmal movement disorders.6 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti75 – 751G → V in CLS. 1 Publication
VAR_006189
Natural varianti82 – 821V → F in CLS. 1 Publication
VAR_006190
Natural varianti114 – 1141R → W in CLS. 1 Publication
VAR_006191
Natural varianti127 – 1271H → Q in CLS. 1 Publication
VAR_006192
Natural varianti154 – 1541D → Y in CLS. 1 Publication
VAR_006193
Natural varianti189 – 1891I → K in CLS. 1 Publication
VAR_065894
Natural varianti225 – 2251A → V in CLS. 1 Publication
VAR_006194
Natural varianti227 – 2271S → A in CLS. 1 Publication
VAR_006195
Natural varianti268 – 2681F → S in CLS. 1 Publication
VAR_065896
Natural varianti431 – 4311G → D in CLS. 1 Publication
VAR_006196
Natural varianti477 – 4771Missing in CLS. 1 Publication
VAR_065898
Natural varianti729 – 7291R → Q in CLS. 1 Publication
Corresponds to variant rs28935171 [ dbSNP | Ensembl ].
VAR_006197
Mental retardation, X-linked 19 (MRX19) [MIM:300844]: A non-syndromic form of mild to moderate mental retardation. Mental retardation is characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. In contrast to syndromic or specific X-linked mental retardation which also present with associated physical, neurological and/or psychiatric manifestations, intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti115 – 1151T → S in MRX19. 1 Publication
VAR_065892
Natural varianti152 – 1521Missing in MRX19. 1 Publication
VAR_065893
Natural varianti202 – 2021Missing in MRX19. 1 Publication
VAR_065895
Natural varianti383 – 3831R → W in MRX19; kinase activity is decreased but not abolished. 1 Publication
VAR_065897

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi300844. phenotype.
303600. phenotype.
Orphaneti192. Coffin-Lowry syndrome.
777. X-linked non-syndromic intellectual disability.
PharmGKBiPA34847.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 740740Ribosomal protein S6 kinase alpha-3PRO_0000086203Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei227 – 2271Phosphoserine; by PDPK1Curated
Modified residuei365 – 3651Phosphothreonine4 Publications
Modified residuei369 – 3691Phosphoserine4 Publications
Modified residuei375 – 3751Phosphoserine3 Publications
Modified residuei386 – 3861Phosphoserine; by autocatalysis and MAPKAPK22 Publications
Modified residuei415 – 4151Phosphoserine3 Publications
Modified residuei529 – 5291Phosphotyrosine; by FGFR3By similarity
Modified residuei556 – 5561Phosphoserine1 Publication
Modified residuei715 – 7151Phosphoserine4 Publications

Post-translational modificationi

Activated by phosphorylation at Ser-227 by PDPK1. Autophosphorylated on Ser-386, as part of the activation process. May be phosphorylated at Thr-365 and Ser-369 by MAPK1/ERK2 and MAPK3/ERK1. Can also be activated via phosphorylation at Ser-386 by MAPKAPK2.7 Publications
N-terminal myristoylation results in an activated kinase in the absence of added growth factors.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP51812.
PaxDbiP51812.
PeptideAtlasiP51812.
PRIDEiP51812.

PTM databases

PhosphoSiteiP51812.

Expressioni

Tissue specificityi

Expressed in many tissues, highest levels in skeletal muscle.

Gene expression databases

BgeeiP51812.
CleanExiHS_RPS6KA3.
ExpressionAtlasiP51812. baseline and differential.
GenevestigatoriP51812.

Organism-specific databases

HPAiCAB003853.
CAB013520.
HPA003221.

Interactioni

Subunit structurei

Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in quiescent cells. Transiently dissociates following mitogenic stimulation (By similarity). Interacts with NFATC4, ETV1/ER81 and FGFR1.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MAPK1P284823EBI-1046616,EBI-959949

Protein-protein interaction databases

BioGridi112111. 38 interactions.
DIPiDIP-38247N.
IntActiP51812. 14 interactions.
MINTiMINT-1542962.
STRINGi9606.ENSP00000368884.

Structurei

Secondary structure

1
740
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi65 – 673Combined sources
Beta strandi68 – 769Combined sources
Beta strandi78 – 8710Combined sources
Turni91 – 944Combined sources
Beta strandi96 – 1049Combined sources
Turni105 – 1073Combined sources
Helixi109 – 12416Combined sources
Beta strandi133 – 1397Combined sources
Beta strandi142 – 1487Combined sources
Helixi155 – 1628Combined sources
Helixi167 – 18620Combined sources
Beta strandi189 – 1924Combined sources
Helixi196 – 1983Combined sources
Beta strandi199 – 2013Combined sources
Beta strandi203 – 2053Combined sources
Beta strandi207 – 2093Combined sources
Beta strandi214 – 2163Combined sources
Helixi217 – 2237Combined sources
Turni224 – 2263Combined sources
Helixi232 – 2343Combined sources
Helixi237 – 2404Combined sources
Helixi249 – 26315Combined sources
Helixi273 – 28210Combined sources
Helixi293 – 30210Combined sources
Helixi307 – 3093Combined sources
Turni315 – 3184Combined sources
Helixi319 – 3224Combined sources
Helixi325 – 3273Combined sources
Helixi332 – 3365Combined sources
Beta strandi409 – 4113Combined sources
Helixi412 – 4143Combined sources
Turni419 – 4213Combined sources
Beta strandi422 – 4309Combined sources
Beta strandi432 – 44110Combined sources
Turni442 – 4454Combined sources
Beta strandi446 – 4549Combined sources
Turni455 – 4573Combined sources
Helixi461 – 47010Combined sources
Beta strandi479 – 4846Combined sources
Beta strandi486 – 4949Combined sources
Helixi501 – 5066Combined sources
Helixi513 – 53220Combined sources
Helixi542 – 5443Combined sources
Beta strandi545 – 5517Combined sources
Helixi554 – 5563Combined sources
Beta strandi557 – 5593Combined sources
Beta strandi571 – 5733Combined sources
Helixi587 – 61327Combined sources
Helixi626 – 63510Combined sources
Helixi643 – 6453Combined sources
Beta strandi646 – 6483Combined sources
Helixi650 – 65910Combined sources
Turni664 – 6663Combined sources
Helixi670 – 6734Combined sources
Helixi677 – 6804Combined sources
Helixi682 – 6843Combined sources
Helixi696 – 71015Combined sources
Helixi711 – 7133Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4D9TX-ray2.40A399-740[»]
4D9UX-ray2.40A399-740[»]
4JG6X-ray2.60A399-740[»]
4JG7X-ray3.00A399-740[»]
4JG8X-ray3.10A399-740[»]
4NUSX-ray2.39A39-359[»]
4NW5X-ray1.94A39-359[»]
4NW6X-ray1.74A39-359[»]
ProteinModelPortaliP51812.
SMRiP51812. Positions 12-714.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini68 – 327260Protein kinase 1PROSITE-ProRule annotationAdd
BLAST
Domaini328 – 39770AGC-kinase C-terminalAdd
BLAST
Domaini422 – 679258Protein 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.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiP51812.
KOiK04373.
OMAiHPWIVHC.
OrthoDBiEOG7B8S38.
PhylomeDBiP51812.
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]

Sequencei

Sequence statusi: Complete.

P51812-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPLAQLADPW QKMAVESPSD SAENGQQIMD EPMGEEEINP QTEEVSIKEI
60 70 80 90 100
AITHHVKEGH EKADPSQFEL LKVLGQGSFG KVFLVKKISG SDARQLYAMK
110 120 130 140 150
VLKKATLKVR DRVRTKMERD ILVEVNHPFI VKLHYAFQTE GKLYLILDFL
160 170 180 190 200
RGGDLFTRLS KEVMFTEEDV KFYLAELALA LDHLHSLGII YRDLKPENIL
210 220 230 240 250
LDEEGHIKLT DFGLSKESID HEKKAYSFCG TVEYMAPEVV NRRGHTQSAD
260 270 280 290 300
WWSFGVLMFE MLTGTLPFQG KDRKETMTMI LKAKLGMPQF LSPEAQSLLR
310 320 330 340 350
MLFKRNPANR LGAGPDGVEE IKRHSFFSTI DWNKLYRREI HPPFKPATGR
360 370 380 390 400
PEDTFYFDPE FTAKTPKDSP GIPPSANAHQ LFRGFSFVAI TSDDESQAMQ
410 420 430 440 450
TVGVHSIVQQ LHRNSIQFTD GYEVKEDIGV GSYSVCKRCI HKATNMEFAV
460 470 480 490 500
KIIDKSKRDP TEEIEILLRY GQHPNIITLK DVYDDGKYVY VVTELMKGGE
510 520 530 540 550
LLDKILRQKF FSEREASAVL FTITKTVEYL HAQGVVHRDL KPSNILYVDE
560 570 580 590 600
SGNPESIRIC DFGFAKQLRA ENGLLMTPCY TANFVAPEVL KRQGYDAACD
610 620 630 640 650
IWSLGVLLYT MLTGYTPFAN GPDDTPEEIL ARIGSGKFSL SGGYWNSVSD
660 670 680 690 700
TAKDLVSKML HVDPHQRLTA ALVLRHPWIV HWDQLPQYQL NRQDAPHLVK
710 720 730 740
GAMAATYSAL NRNQSPVLEP VGRSTLAQRR GIKKITSTAL
Length:740
Mass (Da):83,736
Last modified:October 1, 1996 - v1
Checksum:i486AE8357CEAB6C8
GO

Sequence cautioni

The sequence BAD92170.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 891S → L in AAH96303. (PubMed:15489334)Curated
Sequence conflicti410 – 4101Missing in BAD92170. 1 PublicationCurated
Sequence conflicti424 – 4241V → L in AAC82495. (PubMed:8141249)Curated
Sequence conflicti480 – 4801K → N in AAC82495. (PubMed:8141249)Curated
Sequence conflicti494 – 4941Missing in AAC82495. (PubMed:8141249)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381I → S.2 Publications
Corresponds to variant rs56218010 [ dbSNP | Ensembl ].
VAR_006188
Natural varianti75 – 751G → V in CLS. 1 Publication
VAR_006189
Natural varianti82 – 821V → F in CLS. 1 Publication
VAR_006190
Natural varianti114 – 1141R → W in CLS. 1 Publication
VAR_006191
Natural varianti115 – 1151T → S in MRX19. 1 Publication
VAR_065892
Natural varianti127 – 1271H → Q in CLS. 1 Publication
VAR_006192
Natural varianti152 – 1521Missing in MRX19. 1 Publication
VAR_065893
Natural varianti154 – 1541D → Y in CLS. 1 Publication
VAR_006193
Natural varianti189 – 1891I → K in CLS. 1 Publication
VAR_065894
Natural varianti202 – 2021Missing in MRX19. 1 Publication
VAR_065895
Natural varianti225 – 2251A → V in CLS. 1 Publication
VAR_006194
Natural varianti227 – 2271S → A in CLS. 1 Publication
VAR_006195
Natural varianti268 – 2681F → S in CLS. 1 Publication
VAR_065896
Natural varianti383 – 3831R → W in MRX19; kinase activity is decreased but not abolished. 1 Publication
VAR_065897
Natural varianti416 – 4161I → V in a breast cancer sample; somatic mutation. 1 Publication
VAR_035627
Natural varianti431 – 4311G → D in CLS. 1 Publication
VAR_006196
Natural varianti477 – 4771Missing in CLS. 1 Publication
VAR_065898
Natural varianti483 – 4831Y → C in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_040629
Natural varianti608 – 6081L → F in a glioblastoma multiforme sample; somatic mutation. 1 Publication
VAR_040630
Natural varianti723 – 7231R → C.1 Publication
Corresponds to variant rs35026425 [ dbSNP | Ensembl ].
VAR_040631
Natural varianti729 – 7291R → Q in CLS. 1 Publication
Corresponds to variant rs28935171 [ dbSNP | Ensembl ].
VAR_006197

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08316 mRNA. Translation: AAA81952.1.
AK313932 mRNA. Translation: BAG36651.1.
AB208933 mRNA. Translation: BAD92170.1. Different initiation.
AL732366, AL807772 Genomic DNA. Translation: CAI40548.1.
AL807772, AL732366 Genomic DNA. Translation: CAI39687.1.
BC096301 mRNA. Translation: AAH96301.1.
BC096302 mRNA. Translation: AAH96302.1.
BC096303 mRNA. Translation: AAH96303.1.
L07599 mRNA. Translation: AAC82495.1.
AB102662 mRNA. Translation: BAC81131.1.
CCDSiCCDS14197.1.
PIRiI38556.
RefSeqiNP_004577.1. NM_004586.2.
UniGeneiHs.445387.

Genome annotation databases

EnsembliENST00000379565; ENSP00000368884; ENSG00000177189.
GeneIDi6197.
KEGGihsa:6197.
UCSCiuc004czu.3. human.

Polymorphism databases

DMDMi1730070.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08316 mRNA. Translation: AAA81952.1 .
AK313932 mRNA. Translation: BAG36651.1 .
AB208933 mRNA. Translation: BAD92170.1 . Different initiation.
AL732366 , AL807772 Genomic DNA. Translation: CAI40548.1 .
AL807772 , AL732366 Genomic DNA. Translation: CAI39687.1 .
BC096301 mRNA. Translation: AAH96301.1 .
BC096302 mRNA. Translation: AAH96302.1 .
BC096303 mRNA. Translation: AAH96303.1 .
L07599 mRNA. Translation: AAC82495.1 .
AB102662 mRNA. Translation: BAC81131.1 .
CCDSi CCDS14197.1.
PIRi I38556.
RefSeqi NP_004577.1. NM_004586.2.
UniGenei Hs.445387.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4D9T X-ray 2.40 A 399-740 [» ]
4D9U X-ray 2.40 A 399-740 [» ]
4JG6 X-ray 2.60 A 399-740 [» ]
4JG7 X-ray 3.00 A 399-740 [» ]
4JG8 X-ray 3.10 A 399-740 [» ]
4NUS X-ray 2.39 A 39-359 [» ]
4NW5 X-ray 1.94 A 39-359 [» ]
4NW6 X-ray 1.74 A 39-359 [» ]
ProteinModelPortali P51812.
SMRi P51812. Positions 12-714.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112111. 38 interactions.
DIPi DIP-38247N.
IntActi P51812. 14 interactions.
MINTi MINT-1542962.
STRINGi 9606.ENSP00000368884.

Chemistry

BindingDBi P51812.
ChEMBLi CHEMBL2345.
DrugBanki DB00945. Acetylsalicylic acid.
GuidetoPHARMACOLOGYi 1528.

PTM databases

PhosphoSitei P51812.

Polymorphism databases

DMDMi 1730070.

Proteomic databases

MaxQBi P51812.
PaxDbi P51812.
PeptideAtlasi P51812.
PRIDEi P51812.

Protocols and materials databases

DNASUi 6197.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000379565 ; ENSP00000368884 ; ENSG00000177189 .
GeneIDi 6197.
KEGGi hsa:6197.
UCSCi uc004czu.3. human.

Organism-specific databases

CTDi 6197.
GeneCardsi GC0XM020168.
GeneReviewsi RPS6KA3.
HGNCi HGNC:10432. RPS6KA3.
HPAi CAB003853.
CAB013520.
HPA003221.
MIMi 300075. gene.
300844. phenotype.
303600. phenotype.
neXtProti NX_P51812.
Orphaneti 192. Coffin-Lowry syndrome.
777. X-linked non-syndromic intellectual disability.
PharmGKBi PA34847.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00770000120454.
HOGENOMi HOG000233033.
HOVERGENi HBG108317.
InParanoidi P51812.
KOi K04373.
OMAi HPWIVHC.
OrthoDBi EOG7B8S38.
PhylomeDBi P51812.
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 P51812.

Miscellaneous databases

ChiTaRSi RPS6KA3. human.
GeneWikii RPS6KA3.
GenomeRNAii 6197.
NextBioi 24069.
PROi P51812.
SOURCEi Search...

Gene expression databases

Bgeei P51812.
CleanExi HS_RPS6KA3.
ExpressionAtlasi P51812. baseline and differential.
Genevestigatori P51812.

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. "Cloning of a human insulin-stimulated protein kinase (ISPK-1) gene and analysis of coding regions and mRNA levels of the ISPK-1 and the protein phosphatase-1 genes in muscle from NIDDM patients."
    Bjoerbaek C., Vik T.A., Echwald S.M., Webb G.C., Wang J.P., Yang P.-Y., Vestergaard H., Richmond K., Hansen T., Erikson R.L., Miklos G.L.G., Cohen P.T.W., Pedersen O.
    Diabetes 44:90-97(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta and T-cell.
  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].
  3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    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].
  6. "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] OF 2-582.
    Tissue: Skeletal muscle.
  7. "Gene diversity patterns at 10 X-chromosomal loci in humans and chimpanzees."
    Kitano T., Schwarz C., Nickel B., Paeaebo S.
    Mol. Biol. Evol. 20:1281-1289(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-735.
  8. "Inactivation of glycogen synthase kinase-3 beta by phosphorylation: new kinase connections in insulin and growth-factor signalling."
    Sutherland C., Leighton I.A., Cohen P.
    Biochem. J. 296:15-19(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF GSK3B.
  9. "Rsk-2 activity is necessary for epidermal growth factor-induced phosphorylation of CREB protein and transcription of c-fos gene."
    De Cesare D., Jacquot S., Hanauer A., Sassone-Corsi P.
    Proc. Natl. Acad. Sci. U.S.A. 95:12202-12207(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CREB1.
  10. "Requirement of Rsk-2 for epidermal growth factor-activated phosphorylation of histone H3."
    Sassone-Corsi P., Mizzen C.A., Cheung P., Crosio C., Monaco L., Jacquot S., Hanauer A., Allis C.D.
    Science 285:886-891(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
  11. "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.
  12. "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.
  13. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-715, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: INTERACTION WITH NFATC4.
  15. "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.
  16. "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.
  17. "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.
  18. "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-365; SER-369; SER-375; SER-386; SER-415; SER-556 AND SER-715, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "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.
  20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-365; SER-369 AND SER-375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-365; SER-369; SER-375; SER-386; SER-415 AND SER-715, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  23. "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-715, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "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-365 AND SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. Cited for: VARIANTS CLS VAL-75 AND ALA-227.
  27. "Mutation analysis of the RSK2 gene in Coffin-Lowry patients: extensive allelic heterogeneity and a high rate of De novo mutations."
    Jacquot S., Merienne K., de Cesare D., Pannetier S., Mandel J.-L., Sassone-Corsi P., Hanauer A.
    Am. J. Hum. Genet. 63:1631-1640(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CLS PHE-82; GLN-127; TYR-154; VAL-225 AND ASP-431, VARIANT SER-38.
  28. "Novel mutations in Rsk-2, the gene for Coffin-Lowry syndrome (CLS)."
    Abidi F., Jacquot S., Lassiter C., Trivier E., Hanauer A., Schwartz C.E.
    Eur. J. Hum. Genet. 7:20-26(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CLS TRP-114 AND GLN-729.
  29. "Unreported RSK2 missense mutation in two male sibs with an unusually mild form of Coffin-Lowry syndrome."
    Manouvrier-Hanu S., Amiel J., Jacquot S., Merienne K., Moerman A., Coeslier A., Labarriere F., Vallee L., Croquette M.F., Hanauer A.
    J. Med. Genet. 36:775-778(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CLS LYS-189.
  30. "A missense mutation in RPS6KA3 (RSK2) responsible for non-specific mental retardation."
    Merienne K., Jacquot S., Pannetier S., Zeniou M., Bankier A., Gecz J., Mandel J.L., Mulley J., Sassone-Corsi P., Hanauer A.
    Nat. Genet. 22:13-14(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MRX19 TRP-383, CHARACTERIZATION OF VARIANT MRX19 TRP-383.
  31. "Intronic L1 insertion and F268S, novel mutations in RPS6KA3 (RSK2) causing Coffin-Lowry syndrome."
    Martinez-Garay I., Ballesta M.J., Oltra S., Orellana C., Palomeque A., Molto M.D., Prieto F., Martinez F.
    Clin. Genet. 64:491-496(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CLS SER-268.
  32. Cited for: VARIANT CLS ILE-477 DEL.
  33. "Mutations in the RSK2(RPS6KA3) gene cause Coffin-Lowry syndrome and nonsyndromic X-linked mental retardation."
    Field M., Tarpey P., Boyle J., Edkins S., Goodship J., Luo Y., Moon J., Teague J., Stratton M.R., Futreal P.A., Wooster R., Raymond F.L., Turner G.
    Clin. Genet. 70:509-515(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MRX19 SER-115; GLY-152 DEL AND ASP-202 DEL.
  34. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-416.
  35. "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: VARIANTS [LARGE SCALE ANALYSIS] SER-38; CYS-483; PHE-608 AND CYS-723.

Entry informationi

Entry nameiKS6A3_HUMAN
AccessioniPrimary (citable) accession number: P51812
Secondary accession number(s): B2R9V4
, Q4VAP3, Q59H26, Q5JPK8, Q7Z3Z7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 26, 2014
This is version 156 of the entry and version 1 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 X
    Human chromosome X: 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