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Q9UBS0

- KS6B2_HUMAN

UniProt

Q9UBS0 - KS6B2_HUMAN

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Protein

Ribosomal protein S6 kinase beta-2

Gene

RPS6KB2

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

Functioni

Phosphorylates specifically ribosomal protein S6.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei99 – 991ATPPROSITE-ProRule annotation
Active sitei194 – 1941Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi73 – 819ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. peptide binding Source: Ensembl
  3. protein kinase activity Source: ProtInc
  4. protein serine/threonine kinase activity Source: ProtInc
  5. ribosomal protein S6 kinase activity Source: Ensembl

GO - Biological processi

  1. epidermal growth factor receptor signaling pathway Source: Reactome
  2. Fc-epsilon receptor signaling pathway Source: Reactome
  3. fibroblast growth factor receptor signaling pathway Source: Reactome
  4. innate immune response Source: Reactome
  5. neurotrophin TRK receptor signaling pathway Source: Reactome
  6. phosphatidylinositol-mediated signaling Source: Reactome
  7. positive regulation of translational initiation Source: UniProtKB
  8. protein kinase B signaling Source: Ensembl
  9. signal transduction Source: ProtInc
  10. translation Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiREACT_12442. AKT phosphorylates targets in the nucleus.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
SignaLinkiQ9UBS0.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosomal protein S6 kinase beta-2 (EC:2.7.11.1)
Short name:
S6K-beta-2
Short name:
S6K2
Alternative name(s):
70 kDa ribosomal protein S6 kinase 2
Short name:
P70S6K2
Short name:
p70-S6K 2
S6 kinase-related kinase
Short name:
SRK
Serine/threonine-protein kinase 14B
p70 ribosomal S6 kinase beta
Short name:
S6K-beta
Short name:
p70 S6 kinase beta
Short name:
p70 S6K-beta
Short name:
p70 S6KB
Short name:
p70-beta
Gene namesi
Name:RPS6KB2
Synonyms:STK14B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:10437. RPS6KB2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34852.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 482482Ribosomal protein S6 kinase beta-2PRO_0000086214Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151Phosphoserine1 Publication
Modified residuei423 – 4231PhosphoserineBy similarity
Modified residuei473 – 4731Phosphoserine; by PKC1 Publication

Post-translational modificationi

Phosphorylated and activated by MTOR. Phosphorylation by PKC within the NLS in response to mitogenic stimuli causes cytoplasmic retention.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UBS0.
PaxDbiQ9UBS0.
PRIDEiQ9UBS0.

PTM databases

PhosphoSiteiQ9UBS0.

Expressioni

Gene expression databases

BgeeiQ9UBS0.
CleanExiHS_RPS6KB2.
ExpressionAtlasiQ9UBS0. baseline and differential.
GenevestigatoriQ9UBS0.

Organism-specific databases

HPAiCAB019404.
HPA010010.

Interactioni

Protein-protein interaction databases

BioGridi112113. 16 interactions.
IntActiQ9UBS0. 7 interactions.
MINTiMINT-207158.
STRINGi9606.ENSP00000308413.

Structurei

3D structure databases

ProteinModelPortaliQ9UBS0.
SMRiQ9UBS0. Positions 58-393.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini67 – 328262Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini329 – 39971AGC-kinase C-terminalAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi471 – 4777Nuclear localization signal1 Publication

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi411 – 48272Pro-richAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118793.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiQ9UBS0.
KOiK04688.
OMAiLEPAGHY.
PhylomeDBiQ9UBS0.
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.
IPR016238. Ribosomal_S6_kinase.
IPR002290. Ser/Thr_dual-sp_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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UBS0-1) [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
MAAVFDLDLE TEEGSEGEGE PELSPADACP LAELRAAGLE PVGHYEEVEL
60 70 80 90 100
TETSVNVGPE RIGPHCFELL RVLGKGGYGK VFQVRKVQGT NLGKIYAMKV
110 120 130 140 150
LRKAKIVRNA KDTAHTRAER NILESVKHPF IVELAYAFQT GGKLYLILEC
160 170 180 190 200
LSGGELFTHL EREGIFLEDT ACFYLAEITL ALGHLHSQGI IYRDLKPENI
210 220 230 240 250
MLSSQGHIKL TDFGLCKESI HEGAVTHTFC GTIEYMAPEI LVRSGHNRAV
260 270 280 290 300
DWWSLGALMY DMLTGSPPFT AENRKKTMDK IIRGKLALPP YLTPDARDLV
310 320 330 340 350
KKFLKRNPSQ RIGGGPGDAA DVQRHPFFRH MNWDDLLAWR VDPPFRPCLQ
360 370 380 390 400
SEEDVSQFDT RFTRQTPVDS PDDTALSESA NQAFLGFTYV APSVLDSIKE
410 420 430 440 450
GFSFQPKLRS PRRLNSSPRA PVSPLKFSPF EGFRPSPSLP EPTELPLPPL
460 470 480
LPPPPPSTTA PLPIRPPSGT KKSKRGRGRP GR
Length:482
Mass (Da):53,455
Last modified:May 18, 2010 - v2
Checksum:i5D33660D24A2C7BE
GO
Isoform 2 (identifier: Q9UBS0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     153-154: GG → VD
     155-482: Missing.

Note: No experimental confirmation available.

Show »
Length:154
Mass (Da):16,868
Checksum:iB556CDA0AE062FBC
GO

Sequence cautioni

The sequence BAA34402.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti90 – 901Missing in BAA37145. (PubMed:9878560)Curated
Sequence conflicti409 – 4091R → C in BAA37145. (PubMed:9878560)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti267 – 2671P → L.1 Publication
Corresponds to variant rs55987642 [ dbSNP | Ensembl ].
VAR_040643
Natural varianti368 – 3681V → M.1 Publication
Corresponds to variant rs55642995 [ dbSNP | Ensembl ].
VAR_040644
Natural varianti420 – 4201A → V.5 Publications
Corresponds to variant rs13859 [ dbSNP | Ensembl ].
VAR_040645
Natural varianti443 – 4431T → M in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication
VAR_040646

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei153 – 1542GG → VD in isoform 2. 1 PublicationVSP_056441
Alternative sequencei155 – 482328Missing in isoform 2. 1 PublicationVSP_056442Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB016869 mRNA. Translation: BAA34402.1. Different initiation.
AB019245 mRNA. Translation: BAA37145.1.
AF076931 mRNA. Translation: AAD46063.1.
AF099739 mRNA. Translation: AAD20990.1.
AK297527 mRNA. Translation: BAG59930.1.
AP003419 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74621.1.
BC000094 mRNA. Translation: AAH00094.3.
BC136564 mRNA. Translation: AAI36565.1.
CCDSiCCDS41677.1. [Q9UBS0-1]
PIRiJE0377.
RefSeqiNP_003943.2. NM_003952.2.
UniGeneiHs.534345.

Genome annotation databases

EnsembliENST00000312629; ENSP00000308413; ENSG00000175634. [Q9UBS0-1]
ENST00000528964; ENSP00000432847; ENSG00000175634. [Q9UBS0-2]
GeneIDi6199.
KEGGihsa:6199.
UCSCiuc001old.3. human. [Q9UBS0-1]

Polymorphism databases

DMDMi296434560.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB016869 mRNA. Translation: BAA34402.1 . Different initiation.
AB019245 mRNA. Translation: BAA37145.1 .
AF076931 mRNA. Translation: AAD46063.1 .
AF099739 mRNA. Translation: AAD20990.1 .
AK297527 mRNA. Translation: BAG59930.1 .
AP003419 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74621.1 .
BC000094 mRNA. Translation: AAH00094.3 .
BC136564 mRNA. Translation: AAI36565.1 .
CCDSi CCDS41677.1. [Q9UBS0-1 ]
PIRi JE0377.
RefSeqi NP_003943.2. NM_003952.2.
UniGenei Hs.534345.

3D structure databases

ProteinModelPortali Q9UBS0.
SMRi Q9UBS0. Positions 58-393.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112113. 16 interactions.
IntActi Q9UBS0. 7 interactions.
MINTi MINT-207158.
STRINGi 9606.ENSP00000308413.

Chemistry

ChEMBLi CHEMBL3111.
GuidetoPHARMACOLOGYi 1526.

PTM databases

PhosphoSitei Q9UBS0.

Polymorphism databases

DMDMi 296434560.

Proteomic databases

MaxQBi Q9UBS0.
PaxDbi Q9UBS0.
PRIDEi Q9UBS0.

Protocols and materials databases

DNASUi 6199.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000312629 ; ENSP00000308413 ; ENSG00000175634 . [Q9UBS0-1 ]
ENST00000528964 ; ENSP00000432847 ; ENSG00000175634 . [Q9UBS0-2 ]
GeneIDi 6199.
KEGGi hsa:6199.
UCSCi uc001old.3. human. [Q9UBS0-1 ]

Organism-specific databases

CTDi 6199.
GeneCardsi GC11P067195.
H-InvDB HIX0009859.
HGNCi HGNC:10437. RPS6KB2.
HPAi CAB019404.
HPA010010.
MIMi 608939. gene.
neXtProti NX_Q9UBS0.
PharmGKBi PA34852.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118793.
HOGENOMi HOG000233033.
HOVERGENi HBG108317.
InParanoidi Q9UBS0.
KOi K04688.
OMAi LEPAGHY.
PhylomeDBi Q9UBS0.
TreeFami TF313438.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 2681.
Reactomei REACT_12442. AKT phosphorylates targets in the nucleus.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
SignaLinki Q9UBS0.

Miscellaneous databases

GeneWikii RPS6KB2.
GenomeRNAii 6199.
NextBioi 24077.
PROi Q9UBS0.
SOURCEi Search...

Gene expression databases

Bgeei Q9UBS0.
CleanExi HS_RPS6KB2.
ExpressionAtlasi Q9UBS0. baseline and differential.
Genevestigatori Q9UBS0.

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.
IPR016238. Ribosomal_S6_kinase.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF000605. Ribsml_S6_kin_1. 1 hit.
SMARTi SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS51285. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of a novel p70 S6 kinase, p70 S6 kinase beta containing a proline-rich region."
    Gout I., Minami T., Hara K., Tsujishita Y., Filonenko V., Waterfield M.D., Yonezawa K.
    J. Biol. Chem. 273:30061-30064(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-420.
  2. "Cloning and characterization of p70 S6Kbeta defines a novel family of p70 S6 kinases."
    Saitoh M., ten Dijke P., Miyazono K., Ichijo H.
    Biochem. Biophys. Res. Commun. 253:470-476(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-420.
  3. "Characterization of S6K2, a novel kinase homologous to S6K1."
    Lee-Fruman K.K., Kuo C.J., Lippincott J., Terada N., Blenis J.
    Oncogene 18:5108-5114(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-420.
  4. "Cloning and characterization of a novel S6 kinase-related kinase, SRK."
    Koh H.J., Lee B.N., Choi H.S., Chung J.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. "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 2).
    Tissue: Brain.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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), VARIANT VAL-420.
    Tissue: Brain.
  9. "Regulation of ribosomal S6 kinase 2 by mammalian target of rapamycin."
    Park I.H., Bachmann R., Shirazi H., Chen J.
    J. Biol. Chem. 277:31423-31429(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY MTOR, SUBCELLULAR LOCATION.
  10. "Protein kinase C phosphorylates ribosomal protein S6 kinase betaII and regulates its subcellular localization."
    Valovka T., Verdier F., Cramer R., Zhyvoloup A., Fenton T., Rebholz H., Wang M.L., Gzhegotsky M., Lutsyk A., Matsuka G., Filonenko V., Wang L., Proud C.G., Parker P.J., Gout I.T.
    Mol. Cell. Biol. 23:852-863(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-473, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL.
  11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-267; MET-368; VAL-420 AND MET-443.

Entry informationi

Entry nameiKS6B2_HUMAN
AccessioniPrimary (citable) accession number: Q9UBS0
Secondary accession number(s): B2RMZ9
, B4DML8, O94809, Q9UEC1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 18, 2010
Last modified: October 29, 2014
This is version 148 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 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