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Q9HBY8

- SGK2_HUMAN

UniProt

Q9HBY8 - SGK2_HUMAN

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Protein

Serine/threonine-protein kinase Sgk2

Gene

SGK2

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

Functioni

Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cell growth, survival and proliferation. Up-regulates Na+ channels: SCNN1A/ENAC, K+ channels: KCNA3/Kv1.3, KCNE1 and KCNQ1, amino acid transporter: SLC6A19, glutamate transporter: SLC1A6/EAAT4, glutamate receptors: GRIA1/GLUR1 and GRIK2/GLUR6, Na+/H+ exchanger: SLC9A3/NHE3, and the Na+/K+ ATPase.7 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Two specific sites, one in the kinase domain (Thr-253) and the other in the C-terminal regulatory region (Ser-416), need to be phosphorylated for its full activation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei124 – 1241ATPPROSITE-ProRule annotation
Active sitei219 – 2191Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi101 – 1099ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. potassium channel regulator activity Source: UniProtKB
  3. protein serine/threonine kinase activity Source: ProtInc
  4. sodium channel regulator activity Source: UniProtKB

GO - Biological processi

  1. intracellular signal transduction Source: ProtInc
  2. ion transmembrane transport Source: Reactome
  3. positive regulation of transporter activity Source: UniProtKB
  4. protein phosphorylation Source: UniProtKB
  5. regulation of cell growth Source: UniProtKB
  6. regulation of cell proliferation Source: UniProtKB
  7. response to oxidative stress Source: ProtInc
  8. transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_160189. Stimuli-sensing channels.
SignaLinkiQ9HBY8.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase Sgk2 (EC:2.7.11.1)
Alternative name(s):
Serum/glucocorticoid-regulated kinase 2
Gene namesi
Name:SGK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:13900. SGK2.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi416 – 4161S → D: Increased activation. 1 Publication

Organism-specific databases

PharmGKBiPA37824.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 427427Serine/threonine-protein kinase Sgk2PRO_0000086646Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei253 – 2531Phosphothreonine; by PDPK11 Publication
Modified residuei416 – 4161PhosphoserineSequence Analysis

Post-translational modificationi

Activated by phosphorylation on Ser-416 by an unknown kinase (may be mTORC2 but not confirmed), transforming it into a substrate for PDPK1 which then phosphorylates it on Thr-253.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9HBY8.
PaxDbiQ9HBY8.
PRIDEiQ9HBY8.

PTM databases

PhosphoSiteiQ9HBY8.

Expressioni

Tissue specificityi

Highly expressed in liver, kidney and pancreas, and at lower levels in brain.1 Publication

Gene expression databases

BgeeiQ9HBY8.
CleanExiHS_SGK2.
ExpressionAtlasiQ9HBY8. baseline and differential.
GenevestigatoriQ9HBY8.

Organism-specific databases

HPAiHPA011387.

Interactioni

Protein-protein interaction databases

BioGridi115416. 7 interactions.
IntActiQ9HBY8. 2 interactions.
STRINGi9606.ENSP00000340608.

Structurei

3D structure databases

ProteinModelPortaliQ9HBY8.
SMRiQ9HBY8. Positions 80-418.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini95 – 352258Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini353 – 42775AGC-kinase C-terminalAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi128 – 13811Nuclear localization signalBy similarityAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00770000120449.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiQ9HBY8.
KOiK13303.
OMAiCQGHVVL.
OrthoDBiEOG7Q5HCW.
PhylomeDBiQ9HBY8.
TreeFamiTF320906.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 2 (identifier: Q9HBY8-1) [UniParc]FASTAAdd to Basket

Also known as: beta

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
MQGLLTSGRK PSGGGRCTGR GGWRGQWCLK PWMGGADPPT PTLSCLLLPV
60 70 80 90 100
PPELPDHCYR MNSSPAGTPS PQPSRANGNI NLGPSANPNA QPTDFDFLKV
110 120 130 140 150
IGKGNYGKVL LAKRKSDGAF YAVKVLQKKS ILKKKEQSHI MAERSVLLKN
160 170 180 190 200
VRHPFLVGLR YSFQTPEKLY FVLDYVNGGE LFFHLQRERR FLEPRARFYA
210 220 230 240 250
AEVASAIGYL HSLNIIYRDL KPENILLDCQ GHVVLTDFGL CKEGVEPEDT
260 270 280 290 300
TSTFCGTPEY LAPEVLRKEP YDRAVDWWCL GAVLYEMLHG LPPFYSQDVS
310 320 330 340 350
QMYENILHQP LQIPGGRTVA ACDLLQSLLH KDQRQRLGSK ADFLEIKNHV
360 370 380 390 400
FFSPINWDDL YHKRLTPPFN PNVTGPADLK HFDPEFTQEA VSKSIGCTPD
410 420
TVASSSGASS AFLGFSYAPE DDDILDC
Length:427
Mass (Da):47,604
Last modified:March 1, 2001 - v1
Checksum:iD8F0FA6DF54B1370
GO
Isoform 1 (identifier: Q9HBY8-2) [UniParc]FASTAAdd to Basket

Also known as: alpha

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: Missing.

Show »
Length:367
Mass (Da):41,175
Checksum:iE53F1ABE253F648B
GO
Isoform 3 (identifier: Q9HBY8-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     19-52: Missing.

Note: No experimental confirmation available.

Show »
Length:393
Mass (Da):43,977
Checksum:iDB7303AF95D844CE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti137 – 1371Missing in CAI42315. (PubMed:11780052)Curated
Sequence conflicti168 – 1681K → E in AAX88805. 1 PublicationCurated
Sequence conflicti208 – 2081G → D in AAV38901. 1 PublicationCurated
Sequence conflicti337 – 3371L → P in AAX88805. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121S → T.1 Publication
Corresponds to variant rs33969356 [ dbSNP | Ensembl ].
VAR_041073
Natural varianti259 – 2591E → K in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_041074
Natural varianti349 – 3491H → Y.1 Publication
Corresponds to variant rs35793869 [ dbSNP | Ensembl ].
VAR_041075

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6060Missing in isoform 1. 3 PublicationsVSP_004932Add
BLAST
Alternative sequencei19 – 5234Missing in isoform 3. 1 PublicationVSP_026682Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF169034 mRNA. Translation: AAF12757.2.
AF186470 mRNA. Translation: AAG17012.1.
AY987010 mRNA. Translation: AAX88805.1.
BT020098 mRNA. Translation: AAV38901.1.
Z98752 Genomic DNA. Translation: CAC18509.1.
Z98752 Genomic DNA. Translation: CAI42312.1.
Z98752 Genomic DNA. Translation: CAI42315.1.
BC014037 mRNA. Translation: AAH14037.3.
BC065511 mRNA. Translation: AAH65511.1.
CCDSiCCDS13320.1. [Q9HBY8-1]
CCDS13321.1. [Q9HBY8-2]
RefSeqiNP_001186193.1. NM_001199264.1. [Q9HBY8-2]
NP_057360.2. NM_016276.3. [Q9HBY8-1]
NP_733794.1. NM_170693.2. [Q9HBY8-2]
UniGeneiHs.300863.
Hs.740147.

Genome annotation databases

EnsembliENST00000341458; ENSP00000340608; ENSG00000101049. [Q9HBY8-1]
ENST00000373092; ENSP00000362184; ENSG00000101049. [Q9HBY8-2]
ENST00000373100; ENSP00000362192; ENSG00000101049. [Q9HBY8-2]
ENST00000423407; ENSP00000392795; ENSG00000101049. [Q9HBY8-2]
ENST00000426287; ENSP00000412214; ENSG00000101049. [Q9HBY8-3]
GeneIDi10110.
KEGGihsa:10110.
UCSCiuc002xkr.3. human. [Q9HBY8-1]

Polymorphism databases

DMDMi28558166.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF169034 mRNA. Translation: AAF12757.2 .
AF186470 mRNA. Translation: AAG17012.1 .
AY987010 mRNA. Translation: AAX88805.1 .
BT020098 mRNA. Translation: AAV38901.1 .
Z98752 Genomic DNA. Translation: CAC18509.1 .
Z98752 Genomic DNA. Translation: CAI42312.1 .
Z98752 Genomic DNA. Translation: CAI42315.1 .
BC014037 mRNA. Translation: AAH14037.3 .
BC065511 mRNA. Translation: AAH65511.1 .
CCDSi CCDS13320.1. [Q9HBY8-1 ]
CCDS13321.1. [Q9HBY8-2 ]
RefSeqi NP_001186193.1. NM_001199264.1. [Q9HBY8-2 ]
NP_057360.2. NM_016276.3. [Q9HBY8-1 ]
NP_733794.1. NM_170693.2. [Q9HBY8-2 ]
UniGenei Hs.300863.
Hs.740147.

3D structure databases

ProteinModelPortali Q9HBY8.
SMRi Q9HBY8. Positions 80-418.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115416. 7 interactions.
IntActi Q9HBY8. 2 interactions.
STRINGi 9606.ENSP00000340608.

Chemistry

BindingDBi Q9HBY8.
ChEMBLi CHEMBL5794.
GuidetoPHARMACOLOGYi 1535.

PTM databases

PhosphoSitei Q9HBY8.

Polymorphism databases

DMDMi 28558166.

Proteomic databases

MaxQBi Q9HBY8.
PaxDbi Q9HBY8.
PRIDEi Q9HBY8.

Protocols and materials databases

DNASUi 10110.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000341458 ; ENSP00000340608 ; ENSG00000101049 . [Q9HBY8-1 ]
ENST00000373092 ; ENSP00000362184 ; ENSG00000101049 . [Q9HBY8-2 ]
ENST00000373100 ; ENSP00000362192 ; ENSG00000101049 . [Q9HBY8-2 ]
ENST00000423407 ; ENSP00000392795 ; ENSG00000101049 . [Q9HBY8-2 ]
ENST00000426287 ; ENSP00000412214 ; ENSG00000101049 . [Q9HBY8-3 ]
GeneIDi 10110.
KEGGi hsa:10110.
UCSCi uc002xkr.3. human. [Q9HBY8-1 ]

Organism-specific databases

CTDi 10110.
GeneCardsi GC20P042187.
H-InvDB HIX0080189.
HGNCi HGNC:13900. SGK2.
HPAi HPA011387.
MIMi 607589. gene.
neXtProti NX_Q9HBY8.
PharmGKBi PA37824.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00770000120449.
HOGENOMi HOG000233033.
HOVERGENi HBG108317.
InParanoidi Q9HBY8.
KOi K13303.
OMAi CQGHVVL.
OrthoDBi EOG7Q5HCW.
PhylomeDBi Q9HBY8.
TreeFami TF320906.

Enzyme and pathway databases

Reactomei REACT_160189. Stimuli-sensing channels.
SignaLinki Q9HBY8.

Miscellaneous databases

GeneWikii SGK2.
GenomeRNAii 10110.
NextBioi 38243.
PROi Q9HBY8.
SOURCEi Search...

Gene expression databases

Bgeei Q9HBY8.
CleanExi HS_SGK2.
ExpressionAtlasi Q9HBY8. baseline and differential.
Genevestigatori Q9HBY8.

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.
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 ]
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. "Characterization of the structure and regulation of two novel isoforms of serum- and glucocorticoid-induced protein kinase."
    Kobayashi T., Deak M., Morrice N., Cohen P.
    Biochem. J. 344:189-197(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, PHOSPHORYLATION AT THR-253, MUTAGENESIS OF SER-416.
  2. Li H., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M., Xiao W., Lin L., Yang S.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [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: Brain and Colon.
  6. "Activation of Na+/K+-ATPase by the serum and glucocorticoid-dependent kinase isoforms."
    Henke G., Setiawan I., Boehmer C., Lang F.
    Kidney Blood Press. Res. 25:370-374(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THE REGULATION OF NA(+)/K(+) ATPASE.
  7. "K(+) channel activation by all three isoforms of serum- and glucocorticoid-dependent protein kinase SGK."
    Gamper N., Fillon S., Feng Y., Friedrich B., Lang P.A., Henke G., Huber S.M., Kobayashi T., Cohen P., Lang F.
    Pflugers Arch. 445:60-66(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Regulation of KCNE1-dependent K(+) current by the serum and glucocorticoid-inducible kinase (SGK) isoforms."
    Embark H.M., Boehmer C., Vallon V., Luft F., Lang F.
    Pflugers Arch. 445:601-606(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THE REGULATION OF KCNE1 AND KCNQ1.
  9. "The serine/threonine kinases SGK2 and SGK3 are potent stimulators of the epithelial Na+ channel alpha,beta,gamma-ENaC."
    Friedrich B., Feng Y., Cohen P., Risler T., Vandewalle A., Broeer S., Wang J., Pearce D., Lang F.
    Pflugers Arch. 445:693-696(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THE REGULATION OF SCNN1A/ENAC.
  10. "Regulation of the voltage gated K+ channel Kv1.3 by the ubiquitin ligase Nedd4-2 and the serum and glucocorticoid inducible kinase SGK1."
    Henke G., Maier G., Wallisch S., Boehmer C., Lang F.
    J. Cell. Physiol. 199:194-199(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THE REGULATION OF KCNA3/KV1.3.
  11. "The serum and glucocorticoid inducible kinases SGK1-3 stimulate the neutral amino acid transporter SLC6A19."
    Boehmer C., Sopjani M., Klaus F., Lindner R., Laufer J., Jeyaraj S., Lang F., Palmada M.
    Cell. Physiol. Biochem. 25:723-732(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THE REGULATION OF SLC6A19.
  12. "Serum- and glucocorticoid-induced kinase 3 in recycling endosomes mediates acute activation of Na+/H+ exchanger NHE3 by glucocorticoids."
    He P., Lee S.J., Lin S., Seidler U., Lang F., Fejes-Toth G., Naray-Fejes-Toth A., Yun C.C.
    Mol. Biol. Cell 22:3812-3825(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THE REGULATION OF SLC9A3/NHE3, SUBCELLULAR LOCATION.
  13. "Sgk kinases and their role in epithelial transport."
    Loffing J., Flores S.Y., Staub O.
    Annu. Rev. Physiol. 68:461-490(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  14. Cited for: REVIEW ON FUNCTION.
  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] THR-12; LYS-259 AND TYR-349.

Entry informationi

Entry nameiSGK2_HUMAN
AccessioniPrimary (citable) accession number: Q9HBY8
Secondary accession number(s): Q52PK5
, Q5H8Y6, Q5H8Z1, Q5TZR3, Q9UKG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2003
Last sequence update: March 1, 2001
Last modified: November 26, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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