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Q15349

- KS6A2_HUMAN

UniProt

Q15349 - KS6A2_HUMAN

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Protein

Ribosomal protein S6 kinase alpha-2

Gene

RPS6KA2

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 transcription factors, regulates translation, and mediates cellular proliferation, survival, and differentiation. May function as tumor suppressor in epithelial ovarian cancer cells.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Magnesium.

Enzyme regulationi

Upon extracellular signal or mitogen stimulation, phosphorylated at Thr-570 in the C-terminal kinase domain (CTKD) by MAPK1/ERK2 and MAPK3/ERK1. The activated CTKD then autophosphorylates Ser-377, allowing binding of PDPK1, which in turn phosphorylates Ser-218 in the N-terminal kinase domain (NTDK) leading to the full activation of the protein and subsequent phosphorylation of the substrates by the NTKD.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei91 – 911ATPPROSITE-ProRule annotation
Active sitei184 – 1841Proton acceptorBy similarity
Binding sitei444 – 4441ATPPROSITE-ProRule annotation
Active sitei532 – 5321Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi65 – 739ATPPROSITE-ProRule annotation
Nucleotide bindingi421 – 4299ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: InterPro
  3. protein serine/threonine/tyrosine kinase activity Source: MGI
  4. protein serine/threonine kinase activity Source: ProtInc
  5. ribosomal protein S6 kinase activity Source: Ensembl

GO - Biological processi

  1. axon guidance Source: Reactome
  2. brain renin-angiotensin system Source: Ensembl
  3. cardiac muscle cell apoptotic process Source: Ensembl
  4. cellular response to carbohydrate stimulus Source: Ensembl
  5. heart contraction Source: Ensembl
  6. heart development Source: Ensembl
  7. innate immune response Source: Reactome
  8. intracellular signal transduction Source: ProtInc
  9. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  10. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  11. negative regulation of cell cycle Source: UniProtKB
  12. negative regulation of cell proliferation Source: UniProtKB
  13. negative regulation of meiosis Source: Ensembl
  14. neurotrophin TRK receptor signaling pathway Source: Reactome
  15. oocyte maturation Source: Ensembl
  16. peptidyl-serine phosphorylation Source: Ensembl
  17. positive regulation of apoptotic process Source: UniProtKB
  18. positive regulation of gene expression Source: Ensembl
  19. regulation of protein processing Source: Ensembl
  20. signal transduction Source: ProtInc
  21. stress-activated MAPK cascade Source: Reactome
  22. synaptic transmission Source: Reactome
  23. toll-like receptor 10 signaling pathway Source: Reactome
  24. toll-like receptor 2 signaling pathway Source: Reactome
  25. toll-like receptor 3 signaling pathway Source: Reactome
  26. toll-like receptor 4 signaling pathway Source: Reactome
  27. toll-like receptor 5 signaling pathway Source: Reactome
  28. toll-like receptor 9 signaling pathway Source: Reactome
  29. toll-like receptor signaling pathway Source: Reactome
  30. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  31. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  32. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

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.
SignaLinkiQ15349.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosomal protein S6 kinase alpha-2 (EC:2.7.11.1)
Short name:
S6K-alpha-2
Alternative name(s):
90 kDa ribosomal protein S6 kinase 2
Short name:
p90-RSK 2
Short name:
p90RSK2
MAP kinase-activated protein kinase 1c
Short name:
MAPK-activated protein kinase 1c
Short name:
MAPKAP kinase 1c
Short name:
MAPKAPK-1c
Ribosomal S6 kinase 3
Short name:
RSK-3
pp90RSK3
Gene namesi
Name:RPS6KA2
Synonyms:MAPKAPK1C, RSK3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:10431. RPS6KA2.

Subcellular locationi

Nucleus 1 Publication. Cytoplasm 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA34846.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 733733Ribosomal protein S6 kinase alpha-2PRO_0000086201Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei218 – 2181Phosphoserine; by PDPK11 Publication
Modified residuei377 – 3771Phosphoserine1 Publication
Cross-linki630 – 630Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Activated by phosphorylation at Ser-218 by PDPK1. Autophosphorylated on Ser-377, as part of the activation process. May be phosphorylated at Thr-356 and Ser-360 by MAPK1/ERK2 and MAPK3/ERK1 (By similarity).By similarity
N-terminal myristoylation results in an activated kinase in the absence of added growth factors.By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ15349.
PaxDbiQ15349.
PRIDEiQ15349.

2D gel databases

REPRODUCTION-2DPAGEQ15349.

PTM databases

PhosphoSiteiQ15349.

Expressioni

Tissue specificityi

Widely expressed with higher expression in lung, skeletal muscle, brain, uterus, ovary, thyroid and prostate.2 Publications

Gene expression databases

BgeeiQ15349.
CleanExiHS_RPS6KA2.
ExpressionAtlasiQ15349. baseline and differential.
GenevestigatoriQ15349.

Organism-specific databases

HPAiCAB026243.
HPA045061.
HPA054237.

Interactioni

Subunit structurei

Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in quiescent cells. Transiently dissociates following mitogenic stimulation (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
BRAFP150562EBI-1384149,EBI-365980
MAPK3P273612EBI-1384149,EBI-73995
PRKCEQ021562EBI-1384149,EBI-706254

Protein-protein interaction databases

BioGridi112110. 15 interactions.
DIPiDIP-295N.
IntActiQ15349. 11 interactions.
MINTiMINT-1542928.
STRINGi9606.ENSP00000386050.

Structurei

3D structure databases

ProteinModelPortaliQ15349.
SMRiQ15349. Positions 24-704.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini59 – 318260Protein kinase 1PROSITE-ProRule annotationAdd
BLAST
Domaini319 – 38870AGC-kinase C-terminalAdd
BLAST
Domaini415 – 672258Protein 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.
GeneTreeiENSGT00760000119016.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiQ15349.
KOiK04373.
OrthoDBiEOG7B8S38.
PhylomeDBiQ15349.
TreeFamiTF313438.

Family and domain databases

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

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15349-1) [UniParc]FASTAAdd to Basket

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

« Hide

        10         20         30         40         50
MDLSMKKFAV RRFFSVYLRR KSRSKSSSLS RLEEEGVVKE IDISHHVKEG
60 70 80 90 100
FEKADPSQFE LLKVLGQGSY GKVFLVRKVK GSDAGQLYAM KVLKKATLKV
110 120 130 140 150
RDRVRSKMER DILAEVNHPF IVKLHYAFQT EGKLYLILDF LRGGDLFTRL
160 170 180 190 200
SKEVMFTEED VKFYLAELAL ALDHLHSLGI IYRDLKPENI LLDEEGHIKI
210 220 230 240 250
TDFGLSKEAI DHDKRAYSFC GTIEYMAPEV VNRRGHTQSA DWWSFGVLMF
260 270 280 290 300
EMLTGSLPFQ GKDRKETMAL ILKAKLGMPQ FLSGEAQSLL RALFKRNPCN
310 320 330 340 350
RLGAGIDGVE EIKRHPFFVT IDWNTLYRKE IKPPFKPAVG RPEDTFHFDP
360 370 380 390 400
EFTARTPTDS PGVPPSANAH HLFRGFSFVA SSLIQEPSQQ DLHKVPVHPI
410 420 430 440 450
VQQLHGNNIH FTDGYEIKED IGVGSYSVCK RCVHKATDTE YAVKIIDKSK
460 470 480 490 500
RDPSEEIEIL LRYGQHPNII TLKDVYDDGK FVYLVMELMR GGELLDRILR
510 520 530 540 550
QRYFSEREAS DVLCTITKTM DYLHSQGVVH RDLKPSNILY RDESGSPESI
560 570 580 590 600
RVCDFGFAKQ LRAGNGLLMT PCYTANFVAP EVLKRQGYDA ACDIWSLGIL
610 620 630 640 650
LYTMLAGFTP FANGPDDTPE EILARIGSGK YALSGGNWDS ISDAAKDVVS
660 670 680 690 700
KMLHVDPHQR LTAMQVLKHP WVVNREYLSP NQLSRQDVHL VKGAMAATYF
710 720 730
ALNRTPQAPR LEPVLSSNLA QRRGMKRLTS TRL
Length:733
Mass (Da):83,239
Last modified:March 21, 2006 - v2
Checksum:i087CFB819A313760
GO
Isoform 2 (identifier: Q15349-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: MDLSMKKFAVRRFFSVYLRRKSRSKSSSLSRL → MPIAQLLELW...ACKTKVAGSV

Note: No experimental confirmation available.

Show »
Length:758
Mass (Da):85,532
Checksum:i1C30759D0B188D4A
GO
Isoform 3 (identifier: Q15349-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: MDLSMKKFAVRRFFSVYLRRKSRSKSSSLSRL → MPIAQLLELWKKIEVEPMEIETTEEDLNLDVEPTTEDTAE

Show »
Length:741
Mass (Da):84,014
Checksum:i146D3569D1C9A193
GO

Sequence cautioni

The sequence BAG53121.1 differs from that shown. Reason: Frameshift at position 527.
The sequence AAC82496.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence BAD92353.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti256 – 2561S → A in AAC82496. (PubMed:8141249)Curated
Sequence conflicti269 – 2691A → S in AAC82496. (PubMed:8141249)Curated
Sequence conflicti339 – 3391V → L in CAA59427. (PubMed:7623830)Curated
Sequence conflicti339 – 3391V → L in AAC82496. (PubMed:8141249)Curated
Sequence conflicti447 – 4471D → G in AAC82496. (PubMed:8141249)Curated
Isoform 3 (identifier: Q15349-3)
Sequence conflicti32 – 321E → G in BAG53121. (PubMed:14702039)Curated
Sequence conflicti34 – 341T → A in BAG53121. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti311 – 3111E → K in a metastatic melanoma sample; somatic mutation. 1 Publication
VAR_040627
Natural varianti732 – 7321R → Q in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_040628

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3232MDLSM…SLSRL → MPIAQLLELWKKIEVEPMEI ETTEEDLNLDVGPATEDTAE EGKSDSAACKTKVAGSV in isoform 2. 1 PublicationVSP_017732Add
BLAST
Alternative sequencei1 – 3232MDLSM…SLSRL → MPIAQLLELWKKIEVEPMEI ETTEEDLNLDVEPTTEDTAE in isoform 3. 1 PublicationVSP_041836Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X85106 mRNA. Translation: CAA59427.1.
AB209116 mRNA. Translation: BAD92353.1. Different initiation.
AK095751 mRNA. Translation: BAG53121.1. Frameshift.
AL022069, Z98049 Genomic DNA. Translation: CAI19651.1.
AL023775 Genomic DNA. No translation available.
AL159163 Genomic DNA. No translation available.
Z98049, AL022069 Genomic DNA. Translation: CAI20579.1.
BC002363 mRNA. Translation: AAH02363.1.
L07598 mRNA. Translation: AAC82496.1. Different initiation.
CCDSiCCDS34570.1. [Q15349-3]
CCDS5294.1. [Q15349-1]
PIRiA57459.
RefSeqiNP_001006933.1. NM_001006932.1. [Q15349-3]
NP_066958.2. NM_021135.4. [Q15349-1]
UniGeneiHs.655277.

Genome annotation databases

EnsembliENST00000265678; ENSP00000265678; ENSG00000071242. [Q15349-1]
ENST00000503859; ENSP00000427015; ENSG00000071242. [Q15349-3]
GeneIDi6196.
KEGGihsa:6196.
UCSCiuc003qvb.1. human. [Q15349-1]
uc003qvc.1. human. [Q15349-3]

Polymorphism databases

DMDMi90110031.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X85106 mRNA. Translation: CAA59427.1 .
AB209116 mRNA. Translation: BAD92353.1 . Different initiation.
AK095751 mRNA. Translation: BAG53121.1 . Frameshift.
AL022069 , Z98049 Genomic DNA. Translation: CAI19651.1 .
AL023775 Genomic DNA. No translation available.
AL159163 Genomic DNA. No translation available.
Z98049 , AL022069 Genomic DNA. Translation: CAI20579.1 .
BC002363 mRNA. Translation: AAH02363.1 .
L07598 mRNA. Translation: AAC82496.1 . Different initiation.
CCDSi CCDS34570.1. [Q15349-3 ]
CCDS5294.1. [Q15349-1 ]
PIRi A57459.
RefSeqi NP_001006933.1. NM_001006932.1. [Q15349-3 ]
NP_066958.2. NM_021135.4. [Q15349-1 ]
UniGenei Hs.655277.

3D structure databases

ProteinModelPortali Q15349.
SMRi Q15349. Positions 24-704.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112110. 15 interactions.
DIPi DIP-295N.
IntActi Q15349. 11 interactions.
MINTi MINT-1542928.
STRINGi 9606.ENSP00000386050.

Chemistry

BindingDBi Q15349.
ChEMBLi CHEMBL3906.
GuidetoPHARMACOLOGYi 1529.

PTM databases

PhosphoSitei Q15349.

Polymorphism databases

DMDMi 90110031.

2D gel databases

REPRODUCTION-2DPAGE Q15349.

Proteomic databases

MaxQBi Q15349.
PaxDbi Q15349.
PRIDEi Q15349.

Protocols and materials databases

DNASUi 6196.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265678 ; ENSP00000265678 ; ENSG00000071242 . [Q15349-1 ]
ENST00000503859 ; ENSP00000427015 ; ENSG00000071242 . [Q15349-3 ]
GeneIDi 6196.
KEGGi hsa:6196.
UCSCi uc003qvb.1. human. [Q15349-1 ]
uc003qvc.1. human. [Q15349-3 ]

Organism-specific databases

CTDi 6196.
GeneCardsi GC06M166822.
HGNCi HGNC:10431. RPS6KA2.
HPAi CAB026243.
HPA045061.
HPA054237.
MIMi 601685. gene.
neXtProti NX_Q15349.
PharmGKBi PA34846.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119016.
HOGENOMi HOG000233033.
HOVERGENi HBG108317.
InParanoidi Q15349.
KOi K04373.
OrthoDBi EOG7B8S38.
PhylomeDBi Q15349.
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 Q15349.

Miscellaneous databases

ChiTaRSi RPS6KA2. human.
GeneWikii RPS6KA2.
GenomeRNAii 6196.
NextBioi 24063.
PROi Q15349.
SOURCEi Search...

Gene expression databases

Bgeei Q15349.
CleanExi HS_RPS6KA2.
ExpressionAtlasi Q15349. baseline and differential.
Genevestigatori Q15349.

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. "RSK3 encodes a novel pp90rsk isoform with a unique N-terminal sequence: growth factor-stimulated kinase function and nuclear translocation."
    Zhao Y., Bjoerbaek C., Weremowicz S., Morton C.C., Moller D.E.
    Mol. Cell. Biol. 15:4353-4363(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  2. 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] (ISOFORM 2).
    Tissue: Brain.
  3. "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] (ISOFORM 3).
    Tissue: Brain.
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [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] (ISOFORM 1).
    Tissue: Muscle.
  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 1-540 (ISOFORM 1).
  7. "90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-phosphoinositide-dependent protein kinase-1."
    Jensen C.J., Buch M.-B., Krag T.O., Hemmings B.A., Gammeltoft S., Froedin M.
    J. Biol. Chem. 274:27168-27176(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, PHOSPHORYLATION AT SER-218.
  8. "RPS6KA2, a putative tumour suppressor gene at 6q27 in sporadic epithelial ovarian cancer."
    Bignone P.A., Lee K.Y., Liu Y., Emilion G., Finch J., Soosay A.E., Charnock F.M., Beck S., Dunham I., Mungall A.J., Ganesan T.S.
    Oncogene 26:683-700(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TUMORIGENESIS, TISSUE SPECIFICITY.
  9. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
    Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
    Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-630.
    Tissue: Mammary cancer.
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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] LYS-311 AND GLN-732.

Entry informationi

Entry nameiKS6A2_HUMAN
AccessioniPrimary (citable) accession number: Q15349
Secondary accession number(s): B3KTK9
, Q15419, Q59GJ3, Q5TI68, Q96J38, Q9UJN5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: March 21, 2006
Last modified: October 29, 2014
This is version 153 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3