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O75676

- KS6A4_HUMAN

UniProt

O75676 - KS6A4_HUMAN

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Protein

Ribosomal protein S6 kinase alpha-4

Gene
RPS6KA4, MSK2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factor RELA, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflammatory genes. Phosphorylates CREB1 and ATF1 in response to mitogenic or stress stimuli such as UV-C irradiation, epidermal growth factor (EGF) and anisomycin. Plays an essential role in the control of RELA transcriptional activity in response to TNF. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and EGF, which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14). In lipopolysaccharide-stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro-inflammatory cytokines. Functions probably by inducing transcription of the MAP kinase phosphatase DUSP1 and the anti-inflammatory cytokine interleukin 10 (IL10), via CREB1 and ATF1 transcription factors.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Magnesium.1 Publication

Enzyme regulationi

Activated by phosphorylation at Ser-343, Thr-568 and Thr-687 by MAPK1/ERK2, MAPK3/ERK1 and MAPK14/p38-alpha, and by further autophosphorylation of Ser-196, Ser-360 and Ser-365 by the activated C-terminal kinase domain By similarity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei65 – 651ATP By similarityBy similarity
Active sitei161 – 1611Proton acceptor By similarityBy similarity
Binding sitei440 – 4401ATP By similarityBy similarity
Active sitei530 – 5301Proton acceptor By similarityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi39 – 479ATP By similarityBy similarity
Nucleotide bindingi417 – 4259ATP By similarityBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. magnesium ion binding Source: InterPro
  3. mitogen-activated protein kinase p38 binding Source: UniProtKB
  4. protein binding Source: IntAct
  5. protein serine/threonine kinase activity Source: UniProtKB
  6. ribosomal protein S6 kinase activity Source: UniProtKB

GO - Biological processi

  1. axon guidance Source: Reactome
  2. histone H3-S10 phosphorylation Source: UniProtKB
  3. histone H3-S28 phosphorylation Source: UniProtKB
  4. histone phosphorylation Source: BHF-UCL
  5. inflammatory response Source: UniProtKB-KW
  6. interleukin-1-mediated signaling pathway Source: BHF-UCL
  7. intracellular signal transduction Source: UniProtKB
  8. negative regulation of cytokine production Source: UniProtKB
  9. positive regulation of CREB transcription factor activity Source: UniProtKB
  10. positive regulation of histone acetylation Source: BHF-UCL
  11. positive regulation of histone phosphorylation Source: BHF-UCL
  12. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  13. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  14. protein phosphorylation Source: UniProtKB
  15. regulation of transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Inflammatory response, Stress response

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_22365. Recycling pathway of L1.
SignaLinkiO75676.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosomal protein S6 kinase alpha-4 (EC:2.7.11.1)
Short name:
S6K-alpha-4
Alternative name(s):
90 kDa ribosomal protein S6 kinase 4
Nuclear mitogen- and stress-activated protein kinase 2
Ribosomal protein kinase B
Short name:
RSKB
Gene namesi
Name:RPS6KA4
Synonyms:MSK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:10433. RPS6KA4.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi709 – 7091F → A: Strongly elevates basal activity. 1 Publication

Organism-specific databases

PharmGKBiPA34848.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 772772Ribosomal protein S6 kinase alpha-4PRO_0000086205Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei196 – 1961Phosphoserine; by autocatalysis By similarityBy similarity
Modified residuei343 – 3431Phosphoserine; by MAPK1, MAPK3 and MAPK14 InferredBy similarity
Modified residuei347 – 3471Phosphoserine2 Publications
Modified residuei360 – 3601Phosphoserine; by autocatalysis By similarityBy similarity
Modified residuei365 – 3651Phosphoserine; by autocatalysis By similarity
Modified residuei542 – 5421Phosphothreonine1 Publication
Modified residuei568 – 5681Phosphothreonine; by MAPK1, MAPK3 and MAPK14 By similarityBy similarity
Modified residuei634 – 6341Phosphoserine1 Publication
Modified residuei678 – 6781Phosphoserine1 Publication
Modified residuei687 – 6871Phosphothreonine2 Publications
Modified residuei737 – 7371Phosphoserine; by autocatalysis InferredBy similarity
Modified residuei745 – 7451Phosphoserine1 Publication

Post-translational modificationi

Ser-343 and Thr-568 phosphorylation is required for kinase activity. Ser-343 and Ser-196 are autophosphorylated by the C-terminal kinase domain, and their phosphorylation is essential for the catalytic activity of the N-terminal kinase domain. Phosphorylated at Ser-343, Thr-568 and Thr-687 by MAPK1/ERK2, MAPK3/ERK1 and MAPK14/p38-alpha. Autophosphorylated at Ser-737 and Ser-745 by the N-terminal kinase domain By similarity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO75676.
PaxDbiO75676.
PRIDEiO75676.

PTM databases

PhosphoSiteiO75676.

Expressioni

Gene expression databases

ArrayExpressiO75676.
BgeeiO75676.
CleanExiHS_RPS6KA4.
GenevestigatoriO75676.

Organism-specific databases

HPAiCAB008649.
HPA023225.

Interactioni

Subunit structurei

Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in quiescent cells which transiently dissociates following mitogenic stimulation. Also associates with MAPK14/p38-alpha. Activated RPS6KA4 associates with and phosphorylates the NF-kappa-B p65 subunit RELA.

Binary interactionsi

WithEntry#Exp.IntActNotes
MAPK14Q165393EBI-73933,EBI-73946

Protein-protein interaction databases

BioGridi114468. 13 interactions.
IntActiO75676. 5 interactions.
MINTiMINT-7944429.
STRINGi9606.ENSP00000333896.

Structurei

3D structure databases

ProteinModelPortaliO75676.
SMRiO75676. Positions 13-365, 369-716.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 301269Protein kinase 1Add
BLAST
Domaini302 – 37170AGC-kinase C-terminalAdd
BLAST
Domaini411 – 674264Protein kinase 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni725 – 77248Required for nuclear targeting and association with MAPK14Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiO75676.
KOiK16510.
OMAiYHTYLVM.
PhylomeDBiO75676.
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_dom.
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75676-1) [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

MGDEDDDESC AVELRITEAN LTGHEEKVSV ENFELLKVLG TGAYGKVFLV    50
RKAGGHDAGK LYAMKVLRKA ALVQRAKTQE HTRTERSVLE LVRQAPFLVT 100
LHYAFQTDAK LHLILDYVSG GEMFTHLYQR QYFKEAEVRV YGGEIVLALE 150
HLHKLGIIYR DLKLENVLLD SEGHIVLTDF GLSKEFLTEE KERTFSFCGT 200
IEYMAPEIIR SKTGHGKAVD WWSLGILLFE LLTGASPFTL EGERNTQAEV 250
SRRILKCSPP FPPRIGPVAQ DLLQRLLCKD PKKRLGAGPQ GAQEVRNHPF 300
FQGLDWVALA ARKIPAPFRP QIRSELDVGN FAEEFTRLEP VYSPPGSPPP 350
GDPRIFQGYS FVAPSILFDH NNAVMTDGLE APGAGDRPGR AAVARSAMMQ 400
DSPFFQQYEL DLREPALGQG SFSVCRRCRQ RQSGQEFAVK ILSRRLEANT 450
QREVAALRLC QSHPNVVNLH EVHHDQLHTY LVLELLRGGE LLEHIRKKRH 500
FSESEASQIL RSLVSAVSFM HEEAGVVHRD LKPENILYAD DTPGAPVKII 550
DFGFARLRPQ SPGVPMQTPC FTLQYAAPEL LAQQGYDESC DLWSLGVILY 600
MMLSGQVPFQ GASGQGGQSQ AAEIMCKIRE GRFSLDGEAW QGVSEEAKEL 650
VRGLLTVDPA KRLKLEGLRG SSWLQDGSAR SSPPLRTPDV LESSGPAVRS 700
GLNATFMAFN RGKREGFFLK SVENAPLAKR RKQKLRSATA SRRGSPAPAN 750
PGRAPVASKG APRRANGPLP PS 772
Length:772
Mass (Da):85,606
Last modified:November 1, 1998 - v1
Checksum:i3606209693D0B5F3
GO
Isoform 2 (identifier: O75676-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     401-406: Missing.

Show »
Length:766
Mass (Da):84,884
Checksum:iDE27817E248DA71E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti236 – 2361S → L in a breast infiltrating ductal carcinoma sample; somatic mutation. 1 Publication
VAR_040632
Natural varianti758 – 7581S → A.2 Publications
Corresponds to variant rs17857342 [ dbSNP | Ensembl ].
VAR_040633

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei401 – 4066Missing in isoform 2. VSP_017733

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti477 – 4771L → P in BAD97281. 1 Publication
Isoform 2 (identifier: O75676-2)
Sequence conflicti400 – 4012QQ → Q in BAD97281. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ010119 mRNA. Translation: CAA09009.1.
AK223561 mRNA. Translation: BAD97281.1.
AK292163 mRNA. Translation: BAF84852.1.
CH471076 Genomic DNA. Translation: EAW74260.1.
AF074715 mRNA. Translation: AAC67395.1.
CCDSiCCDS8073.1. [O75676-1]
RefSeqiNP_001006945.1. NM_001006944.1. [O75676-2]
NP_003933.1. NM_003942.2. [O75676-1]
UniGeneiHs.105584.

Genome annotation databases

EnsembliENST00000334205; ENSP00000333896; ENSG00000162302. [O75676-1]
ENST00000530504; ENSP00000432945; ENSG00000162302.
GeneIDi8986.
KEGGihsa:8986.
UCSCiuc001oad.3. human. [O75676-2]
uc001oae.3. human. [O75676-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ010119 mRNA. Translation: CAA09009.1 .
AK223561 mRNA. Translation: BAD97281.1 .
AK292163 mRNA. Translation: BAF84852.1 .
CH471076 Genomic DNA. Translation: EAW74260.1 .
AF074715 mRNA. Translation: AAC67395.1 .
CCDSi CCDS8073.1. [O75676-1 ]
RefSeqi NP_001006945.1. NM_001006944.1. [O75676-2 ]
NP_003933.1. NM_003942.2. [O75676-1 ]
UniGenei Hs.105584.

3D structure databases

ProteinModelPortali O75676.
SMRi O75676. Positions 13-365, 369-716.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114468. 13 interactions.
IntActi O75676. 5 interactions.
MINTi MINT-7944429.
STRINGi 9606.ENSP00000333896.

Chemistry

BindingDBi O75676.
ChEMBLi CHEMBL3125.
GuidetoPHARMACOLOGYi 1524.

PTM databases

PhosphoSitei O75676.

Proteomic databases

MaxQBi O75676.
PaxDbi O75676.
PRIDEi O75676.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000334205 ; ENSP00000333896 ; ENSG00000162302 . [O75676-1 ]
ENST00000530504 ; ENSP00000432945 ; ENSG00000162302 .
GeneIDi 8986.
KEGGi hsa:8986.
UCSCi uc001oad.3. human. [O75676-2 ]
uc001oae.3. human. [O75676-1 ]

Organism-specific databases

CTDi 8986.
GeneCardsi GC11P064126.
HGNCi HGNC:10433. RPS6KA4.
HPAi CAB008649.
HPA023225.
MIMi 603606. gene.
neXtProti NX_O75676.
PharmGKBi PA34848.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233033.
HOVERGENi HBG108317.
InParanoidi O75676.
KOi K16510.
OMAi YHTYLVM.
PhylomeDBi O75676.
TreeFami TF313438.

Enzyme and pathway databases

Reactomei REACT_22365. Recycling pathway of L1.
SignaLinki O75676.

Miscellaneous databases

GeneWikii RPS6KA4.
GenomeRNAii 8986.
NextBioi 33697.
PROi O75676.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75676.
Bgeei O75676.
CleanExi HS_RPS6KA4.
Genevestigatori O75676.

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_dom.
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. "RSK-B, a novel ribosomal S6 kinase family member, is a CREB kinase under dominant control of p38alpha mitogen-activated protein kinase (p38alphaMAPK)."
    Pierrat B., Correia J.D.S., Mary J.L., Tomas-Zuber M., Lesslauer W.
    J. Biol. Chem. 273:29661-29671(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, INTERACTION WITH MAPK14; MAPK1 AND MAPK3, SUBCELLULAR LOCATION.
    Tissue: Placenta.
  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] (ISOFORM 1).
    Tissue: Synovium.
  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] (ISOFORM 2), VARIANT ALA-758.
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB."
    Deak M., Clifton A.D., Lucocq J.M., Alessi D.R.
    EMBO J. 17:4426-4441(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-727 (ISOFORM 2).
  6. "C-terminal elements control location, activation threshold, and p38 docking of ribosomal S6 kinase B (RSKB)."
    Tomas-Zuber M., Mary J.L., Lamour F., Bur D., Lesslauer W.
    J. Biol. Chem. 276:5892-5899(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAPK14, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-709.
  7. "MSK2 and MSK1 mediate the mitogen- and stress-induced phosphorylation of histone H3 and HMG-14."
    Soloaga A., Thomson S., Wiggin G.R., Rampersaud N., Dyson M.H., Hazzalin C.A., Mahadevan L.C., Arthur J.S.
    EMBO J. 22:2788-2797(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3 AND HMGN1/HMG14.
  8. "MSK activation and physiological roles."
    Arthur J.S.
    Front. Biosci. 13:5866-5879(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  9. "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 SER-347; SER-634; SER-678; THR-687 AND SER-745, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347; THR-542 AND THR-687, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: REVIEW ON FUNCTION.
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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] LEU-236 AND ALA-758.

Entry informationi

Entry nameiKS6A4_HUMAN
AccessioniPrimary (citable) accession number: O75676
Secondary accession number(s): A8K7Z8, O75585, Q53ES8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: November 1, 1998
Last modified: September 3, 2014
This is version 143 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

Miscellaneous

Enzyme activity requires the presence of both kinase domains By similarity.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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

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