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Protein

Ribosomal protein S6 kinase beta-1

Gene

RPS6KB1

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 mTOR signaling in response to growth factors and nutrients to promote cell proliferation, cell growth and cell cycle progression. Regulates protein synthesis through phosphorylation of EIF4B, RPS6 and EEF2K, and contributes to cell survival by repressing the pro-apoptotic function of BAD. Under conditions of nutrient depletion, the inactive form associates with the EIF3 translation initiation complex. Upon mitogenic stimulation, phosphorylation by the mammalian target of rapamycin complex 1 (mTORC1) leads to dissociation from the EIF3 complex and activation. The active form then phosphorylates and activates several substrates in the pre-initiation complex, including the EIF2B complex and the cap-binding complex component EIF4B. Also controls translation initiation by phosphorylating a negative regulator of EIF4A, PDCD4, targeting it for ubiquitination and subsequent proteolysis. Promotes initiation of the pioneer round of protein synthesis by phosphorylating POLDIP3/SKAR. In response to IGF1, activates translation elongation by phosphorylating EEF2 kinase (EEF2K), which leads to its inhibition and thus activation of EEF2. Also plays a role in feedback regulation of mTORC2 by mTORC1 by phosphorylating RICTOR, resulting in the inhibition of mTORC2 and AKT1 signaling. Mediates cell survival by phosphorylating the pro-apoptotic protein BAD and suppressing its pro-apoptotic function. Phosphorylates mitochondrial URI1 leading to dissociation of a URI1-PPP1CC complex. The free mitochondrial PPP1CC can then dephosphorylate RPS6KB1 at Thr-412, which is proposed to be a negative feedback mechanism for the RPS6KB1 anti-apoptotic function. Mediates TNF-alpha-induced insulin resistance by phosphorylating IRS1 at multiple serine residues, resulting in accelerated degradation of IRS1. In cells lacking functional TSC1-2 complex, constitutively phosphorylates and inhibits GSK3B. May be involved in cytoskeletal rearrangement through binding to neurabin. Phosphorylates and activates the pyrimidine biosynthesis enzyme CAD, downstream of MTOR.15 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activation requires multiple phosphorylation events on serine/threonine residues. Activation appears to be first mediated by phosphorylation of multiple sites in the autoinhibitory domain, which facilitates phosphorylation at Thr-412, disrupting the autoinhibitory mechanism and allowing phosphorylation of Thr-252 by PDPK1. The active conformation of the kinase is believed to be stabilized by a mechanism involving three conserved phosphorylation sites located in the kinase domain activation loop (Thr-252) and in the AGC-kinase C-terminal domain (Ser-394 in the middle of the tail/linker region and Thr-412 within a hydrophobic motif at its end). Activated by mTORC1; isoform Alpha I and isoform Alpha II are sensitive to rapamycin, which inhibits activating phosphorylation at Thr-412. Activated by PDPK1.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei123ATPPROSITE-ProRule annotation1
Active sitei218Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi97 – 105ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Cell cycle, Translation regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS03106-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-166208. mTORC1-mediated signalling.
SignaLinkiP23443.
SIGNORiP23443.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosomal protein S6 kinase beta-1 (EC:2.7.11.1)
Short name:
S6K-beta-1
Short name:
S6K1
Alternative name(s):
70 kDa ribosomal protein S6 kinase 1
Short name:
P70S6K1
Short name:
p70-S6K 1
Ribosomal protein S6 kinase I
Serine/threonine-protein kinase 14A
p70 ribosomal S6 kinase alpha
Short name:
p70 S6 kinase alpha
Short name:
p70 S6K-alpha
Short name:
p70 S6KA
Gene namesi
Name:RPS6KB1
Synonyms:STK14A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:10436. RPS6KB1.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cell surface Source: Ensembl
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • mitochondrial outer membrane Source: UniProtKB-SubCell
  • mitochondrion Source: UniProtKB
  • neuron projection Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: Ensembl
  • synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane, Nucleus, Synapse, Synaptosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi167K → N: Greatly reduces activity. Greatly reduces phosphorylation at T-412 and moderately reduces phosphorylation at T-252. 1 Publication1
Mutagenesisi394S → A: Loss of activity. Loss of phosphorylation at T-412. 1 Publication1
Mutagenesisi412T → E: Mimics phosphorylation. Facilitates phosphorylation of T-252 by PDPK1; when associated with E-434; E-441; E-444 and E-447. Mimics phosphorylation. No effect on interaction with PDPK1 and phosphorylation of T-252. Impairs association with the eIF3 complex. 3 Publications1
Mutagenesisi434S → E: Facilitates phosphorylation of T-252 by PDPK1; when associated with E-412; E-441; E-444 and E-447. 1 Publication1
Mutagenesisi441S → E: Facilitates phosphorylation of T-252 by PDPK1; when associated with E-412; E-434; E-444 and E-447. 1 Publication1
Mutagenesisi444T → E: Facilitates phosphorylation of T-252 by PDPK1; when associated with E-412; E-434; E-441 and E-447. 1 Publication1
Mutagenesisi447S → E: Facilitates phosphorylation of T-252 by PDPK1; when associated with E-412; E-434; E-441 and E-444. 1 Publication1

Organism-specific databases

DisGeNETi6198.
OpenTargetsiENSG00000108443.
PharmGKBiPA34851.

Chemistry databases

ChEMBLiCHEMBL4501.
GuidetoPHARMACOLOGYi1525.

Polymorphism and mutation databases

BioMutaiRPS6KB1.
DMDMi54041234.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000243421 – 525Ribosomal protein S6 kinase beta-1Add BLAST525

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei252Phosphothreonine; by PDPK12 Publications1
Modified residuei394Phosphoserine1 Publication1
Modified residuei412Phosphothreonine; by MTOR, NEK6 and NEK7By similarity1
Modified residuei434PhosphoserineBy similarity1
Modified residuei441PhosphoserineCombined sources1
Modified residuei444PhosphothreonineCombined sources1 Publication1
Modified residuei447PhosphoserineCombined sources1 Publication1
Modified residuei452PhosphoserineCombined sources1
Modified residuei516N6-acetyllysineBy similarity1

Post-translational modificationi

Phosphorylation at Thr-412 is regulated by mTORC1. The phosphorylation at this site is maintained by an agonist-dependent autophosphorylation mechanism (By similarity). Activated by phosphorylation at Thr-252 by PDPK1. Dephosphorylation by PPP1CC at Thr-412 in mitochondrion.By similarity5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP23443.
MaxQBiP23443.
PaxDbiP23443.
PeptideAtlasiP23443.
PRIDEiP23443.

PTM databases

iPTMnetiP23443.
PhosphoSitePlusiP23443.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000108443.
CleanExiHS_RPS6KB1.
ExpressionAtlasiP23443. baseline and differential.
GenevisibleiP23443. HS.

Organism-specific databases

HPAiCAB003838.
CAB018346.
HPA039442.

Interactioni

Subunit structurei

Interacts with PPP1R9A/neurabin-1 (By similarity). Interacts with RPTOR. Interacts with IRS1. Interacts with EIF3B and EIF3C. Interacts with POLDIP3 and TRAF4.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AKT1P317492EBI-1775921,EBI-296087
EIF3BP558843EBI-1775921,EBI-366696
GLI1P081514EBI-1775921,EBI-308084
IER5Q5VY092EBI-1775921,EBI-1774000
PPP2R2BQ000052EBI-1775921,EBI-1052159

Protein-protein interaction databases

BioGridi112112. 61 interactors.
DIPiDIP-29986N.
IntActiP23443. 27 interactors.
MINTiMINT-203709.
STRINGi9606.ENSP00000225577.

Chemistry databases

BindingDBiP23443.

Structurei

Secondary structure

1525
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi88 – 90Combined sources3
Beta strandi91 – 99Combined sources9
Beta strandi101 – 110Combined sources10
Turni114 – 117Combined sources4
Beta strandi119 – 126Combined sources8
Helixi127 – 132Combined sources6
Helixi137 – 149Combined sources13
Beta strandi158 – 164Combined sources7
Beta strandi167 – 173Combined sources7
Helixi180 – 187Combined sources8
Helixi192 – 212Combined sources21
Helixi221 – 223Combined sources3
Beta strandi224 – 226Combined sources3
Beta strandi232 – 234Combined sources3
Beta strandi246 – 249Combined sources4
Beta strandi252 – 255Combined sources4
Helixi262 – 265Combined sources4
Turni266 – 269Combined sources4
Helixi273 – 288Combined sources16
Helixi298 – 307Combined sources10
Beta strandi314 – 316Combined sources3
Helixi318 – 327Combined sources10
Helixi332 – 334Combined sources3
Turni340 – 342Combined sources3
Helixi343 – 347Combined sources5
Helixi350 – 352Combined sources3
Helixi357 – 361Combined sources5
Turni371 – 373Combined sources3
Beta strandi374 – 377Combined sources4
Turni380 – 382Combined sources3
Helixi409 – 411Combined sources3
Beta strandi413 – 415Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3A60X-ray2.80A/B75-399[»]
3A61X-ray3.43A75-399[»]
3A62X-ray2.35A75-399[»]
3WE4X-ray2.00A78-399[»]
3WF5X-ray2.10A78-399[»]
3WF6X-ray2.03A78-399[»]
3WF7X-ray1.85A78-399[»]
3WF8X-ray1.98A78-399[»]
3WF9X-ray2.04A78-399[»]
4L3JX-ray2.10A75-375[»]
4L3LX-ray2.10A75-375[»]
4L42X-ray2.80A75-417[»]
4L43X-ray3.00A75-417[»]
4L44X-ray2.90A75-417[»]
4L45X-ray2.90A75-417[»]
4L46X-ray3.01A75-417[»]
4RLOX-ray2.53A/B85-372[»]
4RLPX-ray2.79A85-372[»]
ProteinModelPortaliP23443.
SMRiP23443.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23443.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini91 – 352Protein kinasePROSITE-ProRule annotationAdd BLAST262
Domaini353 – 423AGC-kinase C-terminalAdd BLAST71

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni424 – 525Autoinhibitory domainAdd BLAST102

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi28 – 32TOS motif5

Domaini

The autoinhibitory domain is believed to block phosphorylation within the AGC-kinase C-terminal domain and the activation loop.
The TOS (TOR signaling) motif is essential for activation by mTORC1.By similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0598. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00860000133668.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiP23443.
KOiK04688.
OMAiHGGVGQY.
OrthoDBiEOG091G05Z7.
PhylomeDBiP23443.
TreeFamiTF313438.

Family and domain databases

CDDicd05584. STKc_p70S6K. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016238. Ribosomal_S6_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000605. Ribsml_S6_kin_1. 1 hit.
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

Note: Additional isoforms seem to exist.
Isoform Alpha I (identifier: P23443-1) [UniParc]FASTAAdd to basket
Also known as: p80-S6K 1

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
MRRRRRRDGF YPAPDFRDRE AEDMAGVFDI DLDQPEDAGS EDELEEGGQL
60 70 80 90 100
NESMDHGGVG PYELGMEHCE KFEISETSVN RGPEKIRPEC FELLRVLGKG
110 120 130 140 150
GYGKVFQVRK VTGANTGKIF AMKVLKKAMI VRNAKDTAHT KAERNILEEV
160 170 180 190 200
KHPFIVDLIY AFQTGGKLYL ILEYLSGGEL FMQLEREGIF MEDTACFYLA
210 220 230 240 250
EISMALGHLH QKGIIYRDLK PENIMLNHQG HVKLTDFGLC KESIHDGTVT
260 270 280 290 300
HTFCGTIEYM APEILMRSGH NRAVDWWSLG ALMYDMLTGA PPFTGENRKK
310 320 330 340 350
TIDKILKCKL NLPPYLTQEA RDLLKKLLKR NAASRLGAGP GDAGEVQAHP
360 370 380 390 400
FFRHINWEEL LARKVEPPFK PLLQSEEDVS QFDSKFTRQT PVDSPDDSTL
410 420 430 440 450
SESANQVFLG FTYVAPSVLE SVKEKFSFEP KIRSPRRFIG SPRTPVSPVK
460 470 480 490 500
FSPGDFWGRG ASASTANPQT PVEYPMETSG IEQMDVTMSG EASAPLPIRQ
510 520
PNSGPYKKQA FPMISKRPEH LRMNL
Length:525
Mass (Da):59,140
Last modified:October 11, 2004 - v2
Checksum:i2C3BA13CCDAF4AB3
GO
Isoform Alpha II (identifier: P23443-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.

Show »
Length:502
Mass (Da):56,189
Checksum:i2DE6CF3FCABB9FD2
GO
Isoform 2 (identifier: P23443-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: Missing.

Note: No experimental confirmation available.
Show »
Length:472
Mass (Da):52,997
Checksum:iC7296AB8D6151840
GO
Isoform 4 (identifier: P23443-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     104-126: Missing.

Show »
Length:502
Mass (Da):56,593
Checksum:iA4021FE84D488609
GO
Isoform 3 (identifier: P23443-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     448-525: PVKFSPGDFW...KRPEHLRMNL → TAMC

Note: No experimental confirmation available.
Show »
Length:451
Mass (Da):51,016
Checksum:iDE4CDC28ADBA8927
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti222E → V in BAG61973 (PubMed:14702039).Curated1
Sequence conflicti428F → L in BAG35726 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_040639225M → I.1 Publication1
Natural variantiVAR_040640272R → C.1 PublicationCorresponds to variant rs766645749dbSNPEnsembl.1
Natural variantiVAR_040641276W → C.1 Publication1
Natural variantiVAR_035628289G → E in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_040642398S → A.1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0546131 – 53Missing in isoform 2. 1 PublicationAdd BLAST53
Alternative sequenceiVSP_0188391 – 23Missing in isoform Alpha II. 1 PublicationAdd BLAST23
Alternative sequenceiVSP_055026104 – 126Missing in isoform 4. 1 PublicationAdd BLAST23
Alternative sequenceiVSP_054614448 – 525PVKFS…LRMNL → TAMC in isoform 3. 1 PublicationAdd BLAST78

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60724 mRNA. Translation: AAA36410.1.
M60725 mRNA. Translation: AAA36411.1.
AK297147 mRNA. Translation: BAG59646.1.
AK300202 mRNA. Translation: BAG61973.1.
AK312875 mRNA. Translation: BAG35726.1.
AC004686 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94384.1.
BC053365 mRNA. Translation: AAH53365.1.
CCDSiCCDS11621.1. [P23443-1]
CCDS62271.1. [P23443-4]
CCDS62272.1. [P23443-5]
CCDS62273.1. [P23443-3]
PIRiA41687.
RefSeqiNP_001258971.1. NM_001272042.1. [P23443-5]
NP_001258972.1. NM_001272043.1. [P23443-4]
NP_001258973.1. NM_001272044.1. [P23443-3]
NP_001258989.1. NM_001272060.1. [P23443-2]
NP_003152.1. NM_003161.3. [P23443-1]
UniGeneiHs.463642.

Genome annotation databases

EnsembliENST00000225577; ENSP00000225577; ENSG00000108443. [P23443-1]
ENST00000393021; ENSP00000376744; ENSG00000108443. [P23443-3]
ENST00000406116; ENSP00000384335; ENSG00000108443. [P23443-4]
ENST00000443572; ENSP00000441993; ENSG00000108443. [P23443-5]
GeneIDi6198.
KEGGihsa:6198.
UCSCiuc002ixy.5. human. [P23443-1]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60724 mRNA. Translation: AAA36410.1.
M60725 mRNA. Translation: AAA36411.1.
AK297147 mRNA. Translation: BAG59646.1.
AK300202 mRNA. Translation: BAG61973.1.
AK312875 mRNA. Translation: BAG35726.1.
AC004686 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94384.1.
BC053365 mRNA. Translation: AAH53365.1.
CCDSiCCDS11621.1. [P23443-1]
CCDS62271.1. [P23443-4]
CCDS62272.1. [P23443-5]
CCDS62273.1. [P23443-3]
PIRiA41687.
RefSeqiNP_001258971.1. NM_001272042.1. [P23443-5]
NP_001258972.1. NM_001272043.1. [P23443-4]
NP_001258973.1. NM_001272044.1. [P23443-3]
NP_001258989.1. NM_001272060.1. [P23443-2]
NP_003152.1. NM_003161.3. [P23443-1]
UniGeneiHs.463642.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3A60X-ray2.80A/B75-399[»]
3A61X-ray3.43A75-399[»]
3A62X-ray2.35A75-399[»]
3WE4X-ray2.00A78-399[»]
3WF5X-ray2.10A78-399[»]
3WF6X-ray2.03A78-399[»]
3WF7X-ray1.85A78-399[»]
3WF8X-ray1.98A78-399[»]
3WF9X-ray2.04A78-399[»]
4L3JX-ray2.10A75-375[»]
4L3LX-ray2.10A75-375[»]
4L42X-ray2.80A75-417[»]
4L43X-ray3.00A75-417[»]
4L44X-ray2.90A75-417[»]
4L45X-ray2.90A75-417[»]
4L46X-ray3.01A75-417[»]
4RLOX-ray2.53A/B85-372[»]
4RLPX-ray2.79A85-372[»]
ProteinModelPortaliP23443.
SMRiP23443.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112112. 61 interactors.
DIPiDIP-29986N.
IntActiP23443. 27 interactors.
MINTiMINT-203709.
STRINGi9606.ENSP00000225577.

Chemistry databases

BindingDBiP23443.
ChEMBLiCHEMBL4501.
GuidetoPHARMACOLOGYi1525.

PTM databases

iPTMnetiP23443.
PhosphoSitePlusiP23443.

Polymorphism and mutation databases

BioMutaiRPS6KB1.
DMDMi54041234.

Proteomic databases

EPDiP23443.
MaxQBiP23443.
PaxDbiP23443.
PeptideAtlasiP23443.
PRIDEiP23443.

Protocols and materials databases

DNASUi6198.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000225577; ENSP00000225577; ENSG00000108443. [P23443-1]
ENST00000393021; ENSP00000376744; ENSG00000108443. [P23443-3]
ENST00000406116; ENSP00000384335; ENSG00000108443. [P23443-4]
ENST00000443572; ENSP00000441993; ENSG00000108443. [P23443-5]
GeneIDi6198.
KEGGihsa:6198.
UCSCiuc002ixy.5. human. [P23443-1]

Organism-specific databases

CTDi6198.
DisGeNETi6198.
GeneCardsiRPS6KB1.
HGNCiHGNC:10436. RPS6KB1.
HPAiCAB003838.
CAB018346.
HPA039442.
MIMi608938. gene.
neXtProtiNX_P23443.
OpenTargetsiENSG00000108443.
PharmGKBiPA34851.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0598. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00860000133668.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiP23443.
KOiK04688.
OMAiHGGVGQY.
OrthoDBiEOG091G05Z7.
PhylomeDBiP23443.
TreeFamiTF313438.

Enzyme and pathway databases

BioCyciZFISH:HS03106-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-166208. mTORC1-mediated signalling.
SignaLinkiP23443.
SIGNORiP23443.

Miscellaneous databases

ChiTaRSiRPS6KB1. human.
EvolutionaryTraceiP23443.
GeneWikiiP70-S6_Kinase_1.
GenomeRNAii6198.
PROiP23443.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000108443.
CleanExiHS_RPS6KB1.
ExpressionAtlasiP23443. baseline and differential.
GenevisibleiP23443. HS.

Family and domain databases

CDDicd05584. STKc_p70S6K. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016238. Ribosomal_S6_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000605. Ribsml_S6_kin_1. 1 hit.
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKS6B1_HUMAN
AccessioniPrimary (citable) accession number: P23443
Secondary accession number(s): B2R779
, B4DLT4, B4DTG1, E7ESB8, F6UYM1, Q7Z721
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: October 11, 2004
Last modified: November 30, 2016
This is version 180 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 17
    Human chromosome 17: 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.