SGK2_HUMAN - dbPTM
SGK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SGK2_HUMAN
UniProt AC Q9HBY8
Protein Name Serine/threonine-protein kinase Sgk2
Gene Name SGK2
Organism Homo sapiens (Human).
Sequence Length 427
Subcellular Localization Cytoplasm . Nucleus .
Protein Description 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..
Protein Sequence MQGLLTSGRKPSGGGRCTGRGGWRGQWCLKPWMGGADPPTPTLSCLLLPVPPELPDHCYRMNSSPAGTPSPQPSRANGNINLGPSANPNAQPTDFDFLKVIGKGNYGKVLLAKRKSDGAFYAVKVLQKKSILKKKEQSHIMAERSVLLKNVRHPFLVGLRYSFQTPEKLYFVLDYVNGGELFFHLQRERRFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGVEPEDTTSTFCGTPEYLAPEVLRKEPYDRAVDWWCLGAVLYEMLHGLPPFYSQDVSQMYENILHQPLQIPGGRTVAACDLLQSLLHKDQRQRLGSKADFLEIKNHVFFSPINWDDLYHKRLTPPFNPNVTGPADLKHFDPEFTQEAVSKSIGCTPDTVASSSGASSAFLGFSYAPEDDDILDC
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
8 (in isoform 2)Phosphorylation-36.0729116813
10PhosphorylationGLLTSGRKPSGGGRC
CCCCCCCCCCCCCCC
47.24-
10 (in isoform 2)Phosphorylation-47.2429116813
63PhosphorylationDHCYRMNSSPAGTPS
CCCCCCCCCCCCCCC
28.4925841592
64PhosphorylationHCYRMNSSPAGTPSP
CCCCCCCCCCCCCCC
17.4825841592
64UbiquitinationHCYRMNSSPAGTPSP
CCCCCCCCCCCCCCC
17.4821890473
68PhosphorylationMNSSPAGTPSPQPSR
CCCCCCCCCCCCCCC
23.7728857561
70PhosphorylationSSPAGTPSPQPSRAN
CCCCCCCCCCCCCCC
35.6828857561
74PhosphorylationGTPSPQPSRANGNIN
CCCCCCCCCCCCCCC
38.4825841592
99UbiquitinationPTDFDFLKVIGKGNY
CCCCCEEEEECCCCC
31.62-
116PhosphorylationVLLAKRKSDGAFYAV
EEEEEECCCCCEEHH
45.3628857561
121PhosphorylationRKSDGAFYAVKVLQK
ECCCCCEEHHHHHHH
15.2223312004
124UbiquitinationDGAFYAVKVLQKKSI
CCCEEHHHHHHHHHH
29.1121890473
130PhosphorylationVKVLQKKSILKKKEQ
HHHHHHHHHHCHHHH
39.9424719451
193PhosphorylationQRERRFLEPRARFYA
HHHHCCCCHHHHHHH
29.9910548550
251PhosphorylationGVEPEDTTSTFCGTP
CCCCCCCCCCCCCCH
37.7822322096
253PhosphorylationEPEDTTSTFCGTPEY
CCCCCCCCCCCCHHH
22.3522322096
285PhosphorylationWCLGAVLYEMLHGLP
HHHHHHHHHHHCCCC
7.8422817900
334PhosphorylationSLLHKDQRQRLGSKA
HHHCHHHHHHHCCCC
33.45-
339PhosphorylationDQRQRLGSKADFLEI
HHHHHHCCCCHHHEE
29.3023312004
356PhosphorylationHVFFSPINWDDLYHK
CEEEECCCHHHHCCC
39.24-
357PhosphorylationVFFSPINWDDLYHKR
EEEECCCHHHHCCCC
10.95-
366PhosphorylationDLYHKRLTPPFNPNV
HHCCCCCCCCCCCCC
32.7124719451
374PhosphorylationPPFNPNVTGPADLKH
CCCCCCCCCCCCCCC
44.0524719451
416PhosphorylationSSAFLGFSYAPEDDD
CCHHCCCCCCCCCCC
20.7010548550

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
253TPhosphorylationKinasePDK1Q15118
GPS
253TPhosphorylationKinasePDK1O15530
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
193TPhosphorylation

10548550
356SPhosphorylation

10548550

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SGK2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
TCPG_HUMANCCT3physical
25852190
TCPD_HUMANCCT4physical
25852190
TCPE_HUMANCCT5physical
25852190
TCPZ_HUMANCCT6Aphysical
25852190
TCPH_HUMANCCT7physical
25852190
TCPQ_HUMANCCT8physical
25852190
DDX5_HUMANDDX5physical
25852190
FKBP5_HUMANFKBP5physical
25852190
ILF3_HUMANILF3physical
25852190
TCPA_HUMANTCP1physical
25852190

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SGK2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Characterization of the structure and regulation of two novelisoforms of serum- and glucocorticoid-induced protein kinase.";
Kobayashi T., Deak M., Morrice N., Cohen P.;
Biochem. J. 344:189-197(1999).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY,PHOSPHORYLATION AT THR-253, AND MUTAGENESIS OF SER-416.

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