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Protein

Ribosomal protein S6 kinase alpha-3

Gene

RPS6KA3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Negatively regulates EGF-induced MAPK1/3 phosphorylation via phosphorylation of SOS1. Phosphorylates SOS1 at 'Ser-1134' and 'Ser-1161' that create YWHAB and YWHAE binding sites and which contribute to the negative regulation of MAPK1/3 phosphorylation (By similarity).By similarity7 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

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • central nervous system development Source: ProtInc
  • intracellular signal transduction Source: GO_Central
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • positive regulation of cell differentiation Source: UniProtKB
  • positive regulation of cell growth Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • regulation of DNA-templated transcription in response to stress Source: UniProtKB
  • regulation of translation in response to stress Source: UniProtKB
  • response to lipopolysaccharide Source: UniProtKB
  • signal transduction Source: ProtInc
  • skeletal system development Source: ProtInc
  • toll-like receptor signaling pathway Source: UniProtKB
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.
ReactomeiR-HSA-198753. ERK/MAPK targets.
R-HSA-199920. CREB phosphorylation.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-437239. Recycling pathway of L1.
R-HSA-442742. CREB phosphorylation through the activation of Ras.
R-HSA-444257. RSK activation.
R-HSA-881907. Gastrin-CREB signalling pathway via PKC and MAPK.
SignaLinkiP51812.
SIGNORiP51812.

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
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:10432. RPS6KA3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Coffin-Lowry syndrome (CLS)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA X-linked mental retardation associated with facial and digital dysmorphisms, progressive skeletal malformations, growth retardation, hearing deficit and paroxysmal movement disorders.
See also OMIM:303600
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti75 – 751G → V in CLS. 1 Publication
Corresponds to variant rs122454124 [ dbSNP | Ensembl ].
VAR_006189
Natural varianti82 – 821V → F in CLS. 1 Publication
Corresponds to variant rs122454126 [ dbSNP | Ensembl ].
VAR_006190
Natural varianti114 – 1141R → W in CLS. 1 Publication
Corresponds to variant rs122454127 [ dbSNP | Ensembl ].
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
Corresponds to variant rs122454130 [ dbSNP | Ensembl ].
VAR_065894
Natural varianti225 – 2251A → V in CLS. 1 Publication
VAR_006194
Natural varianti227 – 2271S → A in CLS. 1 Publication
Corresponds to variant rs122454125 [ dbSNP | Ensembl ].
VAR_006195
Natural varianti268 – 2681F → S in CLS. 1 Publication
Corresponds to variant rs122454131 [ dbSNP | Ensembl ].
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)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:300844
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti115 – 1151T → S in MRX19. 1 Publication
Corresponds to variant rs387906703 [ dbSNP | Ensembl ].
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
Corresponds to variant rs122454129 [ dbSNP | Ensembl ].
VAR_065897

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MalaCardsiRPS6KA3.
MIMi300844. phenotype.
303600. phenotype.
Orphaneti192. Coffin-Lowry syndrome.
777. X-linked non-syndromic intellectual disability.
PharmGKBiPA34847.

Chemistry

ChEMBLiCHEMBL2345.
DrugBankiDB00945. Acetylsalicylic acid.
GuidetoPHARMACOLOGYi1528.

Polymorphism and mutation databases

BioMutaiRPS6KA3.
DMDMi1730070.

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 – 3651PhosphothreonineCombined sources
Modified residuei369 – 3691PhosphoserineCombined sources
Modified residuei375 – 3751PhosphoserineCombined sources
Modified residuei386 – 3861Phosphoserine; by autocatalysis and MAPKAPK2Combined sources
Modified residuei415 – 4151PhosphoserineCombined sources
Modified residuei529 – 5291Phosphotyrosine; by FGFR3By similarity
Modified residuei556 – 5561PhosphoserineCombined sources
Modified residuei715 – 7151PhosphoserineCombined sources

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.
N-terminal myristoylation results in an activated kinase in the absence of added growth factors.

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP51812.
MaxQBiP51812.
PaxDbiP51812.
PeptideAtlasiP51812.
PRIDEiP51812.

PTM databases

iPTMnetiP51812.
PhosphoSiteiP51812.

Expressioni

Tissue specificityi

Expressed in many tissues, highest levels in skeletal muscle.

Gene expression databases

BgeeiENSG00000177189.
CleanExiHS_RPS6KA3.
ExpressionAtlasiP51812. baseline and differential.
GenevisibleiP51812. HS.

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. 55 interactions.
DIPiDIP-38247N.
IntActiP51812. 18 interactions.
MINTiMINT-1542962.
STRINGi9606.ENSP00000368884.

Chemistry

BindingDBiP51812.

Structurei

Secondary structure

1
740
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi50 – 545Combined sources
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
Beta strandi152 – 1543Combined 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
Helixi351 – 3533Combined 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[»]
5D9KX-ray2.55A/B39-366[»]
5D9LX-ray2.15A39-359[»]
ProteinModelPortaliP51812.
SMRiP51812. Positions 28-714.
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

eggNOGiKOG0598. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00820000126961.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiP51812.
KOiK04373.
OMAiYTLNRQD.
OrthoDBiEOG091G05Z7.
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.
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 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 (Ref. 3) Curated
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
Corresponds to variant rs122454124 [ dbSNP | Ensembl ].
VAR_006189
Natural varianti82 – 821V → F in CLS. 1 Publication
Corresponds to variant rs122454126 [ dbSNP | Ensembl ].
VAR_006190
Natural varianti114 – 1141R → W in CLS. 1 Publication
Corresponds to variant rs122454127 [ dbSNP | Ensembl ].
VAR_006191
Natural varianti115 – 1151T → S in MRX19. 1 Publication
Corresponds to variant rs387906703 [ dbSNP | Ensembl ].
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
Corresponds to variant rs122454130 [ dbSNP | Ensembl ].
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
Corresponds to variant rs122454125 [ dbSNP | Ensembl ].
VAR_006195
Natural varianti268 – 2681F → S in CLS. 1 Publication
Corresponds to variant rs122454131 [ dbSNP | Ensembl ].
VAR_065896
Natural varianti383 – 3831R → W in MRX19; kinase activity is decreased but not abolished. 1 Publication
Corresponds to variant rs122454129 [ dbSNP | Ensembl ].
VAR_065897
Natural varianti416 – 4161I → V in a breast cancer sample; somatic mutation. 1 Publication
Corresponds to variant rs148050184 [ dbSNP | Ensembl ].
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.4. human.

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.
CCDSiCCDS14197.1.
PIRiI38556.
RefSeqiNP_004577.1. NM_004586.2.
UniGeneiHs.445387.

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[»]
5D9KX-ray2.55A/B39-366[»]
5D9LX-ray2.15A39-359[»]
ProteinModelPortaliP51812.
SMRiP51812. Positions 28-714.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112111. 55 interactions.
DIPiDIP-38247N.
IntActiP51812. 18 interactions.
MINTiMINT-1542962.
STRINGi9606.ENSP00000368884.

Chemistry

BindingDBiP51812.
ChEMBLiCHEMBL2345.
DrugBankiDB00945. Acetylsalicylic acid.
GuidetoPHARMACOLOGYi1528.

PTM databases

iPTMnetiP51812.
PhosphoSiteiP51812.

Polymorphism and mutation databases

BioMutaiRPS6KA3.
DMDMi1730070.

Proteomic databases

EPDiP51812.
MaxQBiP51812.
PaxDbiP51812.
PeptideAtlasiP51812.
PRIDEiP51812.

Protocols and materials databases

DNASUi6197.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379565; ENSP00000368884; ENSG00000177189.
GeneIDi6197.
KEGGihsa:6197.
UCSCiuc004czu.4. human.

Organism-specific databases

CTDi6197.
GeneCardsiRPS6KA3.
GeneReviewsiRPS6KA3.
HGNCiHGNC:10432. RPS6KA3.
HPAiCAB003853.
CAB013520.
HPA003221.
MalaCardsiRPS6KA3.
MIMi300075. gene.
300844. phenotype.
303600. phenotype.
neXtProtiNX_P51812.
Orphaneti192. Coffin-Lowry syndrome.
777. X-linked non-syndromic intellectual disability.
PharmGKBiPA34847.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0598. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00820000126961.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiP51812.
KOiK04373.
OMAiYTLNRQD.
OrthoDBiEOG091G05Z7.
PhylomeDBiP51812.
TreeFamiTF313438.

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-198753. ERK/MAPK targets.
R-HSA-199920. CREB phosphorylation.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-437239. Recycling pathway of L1.
R-HSA-442742. CREB phosphorylation through the activation of Ras.
R-HSA-444257. RSK activation.
R-HSA-881907. Gastrin-CREB signalling pathway via PKC and MAPK.
SignaLinkiP51812.
SIGNORiP51812.

Miscellaneous databases

ChiTaRSiRPS6KA3. human.
GeneWikiiRPS6KA3.
GenomeRNAii6197.
PROiP51812.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000177189.
CleanExiHS_RPS6KA3.
ExpressionAtlasiP51812. baseline and differential.
GenevisibleiP51812. HS.

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.
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]
ProtoNetiSearch...

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: September 7, 2016
This is version 175 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.