SIK2_HUMAN - dbPTM
SIK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SIK2_HUMAN
UniProt AC Q9H0K1
Protein Name Serine/threonine-protein kinase SIK2
Gene Name SIK2
Organism Homo sapiens (Human).
Sequence Length 926
Subcellular Localization Cytoplasm.
Protein Description Phosphorylates 'Ser-794' of IRS1 in insulin-stimulated adipocytes, potentially modulating the efficiency of insulin signal transduction. Inhibits CREB activity by phosphorylating and repressing TORCs, the CREB-specific coactivators..
Protein Sequence MVMADGPRHLQRGPVRVGFYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWMLIEVPVQRPVLYPQEQENEPSIGEFNEQVLRLMHSLGIDQQKTIESLQNKSYNHFAAIYFLLVERLKSHRSSFPVEQRLDGRQRRPSTIAEQTVAKAQTVGLPVTMHSPNMRLLRSALLPQASNVEAFSFPASGCQAEAAFMEEECVDTPKVNGCLLDPVPPVLVRKGCQSLPSNMMETSIDEGLETEGEAEEDPAHAFEAFQSTRSGQRRHTLSEVTNQLVVMPGAGKIFSMNDSPSLDSVDSEYDMGSVQRDLNFLEDNPSLKDIMLANQPSPRMTSPFISLRPTNPAMQALSSQKREVHNRSPVSFREGRRASDTSLTQGIVAFRQHLQNLARTKGILELNKVQLLYEQIGPEADPNLAPAAPQLQDLASSCPQEEVSQQQESVSTLPASVHPQLSPRQSLETQYLQHRLQKPSLLSKAQNTCQLYCKEPPRSLEQQLQEHRLQQKRLFLQKQSQLQAYFNQMQIAESSYPQPSQQLPLPRQETPPPSQQAPPFSLTQPLSPVLEPSSEQMQYSPFLSQYQEMQLQPLPSTSGPRAAPPLPTQLQQQQPPPPPPPPPPRQPGAAPAPLQFSYQTCELPSAASPAPDYPTPCQYPVDGAQQSDLTGPDCPRSPGLQEAPSSYDPLALSELPGLFDCEMLDAVDPQHNGYVLVN
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
25PhosphorylationGFYDIEGTLGKGNFA
EEEEEECCCCCCCEE		21.3922817900
28UbiquitinationDIEGTLGKGNFAVVK
EEECCCCCCCEEEEE		54.52-
43UbiquitinationLGRHRITKTEVAIKI
ECCCCCCCEEEEEEE		40.07-
49UbiquitinationTKTEVAIKIIDKSQL
CCEEEEEEECCHHHH		24.70-
53UbiquitinationVAIKIIDKSQLDAVN
EEEEECCHHHHCCCC		29.6823322770
53AcetylationVAIKIIDKSQLDAVN
EEEEECCHHHHCCCC		29.6823322770
63UbiquitinationLDAVNLEKIYREVQI
HCCCCHHHHHHHHHH		48.48-
65PhosphorylationAVNLEKIYREVQIMK
CCCHHHHHHHHHHHH		16.2822817900
81UbiquitinationLDHPHIIKLYQVMET
CCCHHHHHHHHHHHH		40.30-
83PhosphorylationHPHIIKLYQVMETKS
CHHHHHHHHHHHHHH		8.2822210691
90PhosphorylationYQVMETKSMLYLVTE
HHHHHHHHHHHHHHH		22.8022462548
93PhosphorylationMETKSMLYLVTEYAK
HHHHHHHHHHHHHHH		7.1822210691
98PhosphorylationMLYLVTEYAKNGEIF
HHHHHHHHHHCCCHH		17.3222210691
100UbiquitinationYLVTEYAKNGEIFDY
HHHHHHHHCCCHHHH		65.66-
117PhosphorylationNHGRLNESEARRKFW
HHCCCCHHHHHHHHH		35.1725849741
144UbiquitinationKIVHRDLKAENLLLD
CCCCCCCCHHHEEEC		58.9221890473
168SumoylationFGFGNFFKSGELLAT
ECCCCCCCCCCEEHH		54.11-
175PhosphorylationKSGELLATWCGSPPY
CCCCEEHHHCCCCCC		22.6614976552
258UbiquitinationMLVLDPSKRLTIAQI
HHHCCHHHCEEEEEH		57.74-
266UbiquitinationRLTIAQIKEHKWMLI
CEEEEEHHHCCEEEE		41.51-
269UbiquitinationIAQIKEHKWMLIEVP
EEEHHHCCEEEEEEE		35.08-
283PhosphorylationPVQRPVLYPQEQENE
ECCCCCCCCCCCCCC		11.7822817900
313UbiquitinationSLGIDQQKTIESLQN
HCCCCHHHHHHHHHC		45.92-
330PhosphorylationYNHFAAIYFLLVERL
CCHHHHHHHHHHHHH		5.3922210691
339PhosphorylationLLVERLKSHRSSFPV
HHHHHHHHCCCCCCH		28.8222210691
342PhosphorylationERLKSHRSSFPVEQR
HHHHHCCCCCCHHHC		30.7926657352
343PhosphorylationRLKSHRSSFPVEQRL
HHHHCCCCCCHHHCC		33.2629691806
358PhosphorylationDGRQRRPSTIAEQTV
CCCCCCCCHHHHHHH		30.5429255136
359PhosphorylationGRQRRPSTIAEQTVA
CCCCCCCHHHHHHHH		27.2129255136
364PhosphorylationPSTIAEQTVAKAQTV
CCHHHHHHHHHHHHC		17.5923403867
367UbiquitinationIAEQTVAKAQTVGLP
HHHHHHHHHHHCCCC		36.37-
370PhosphorylationQTVAKAQTVGLPVTM
HHHHHHHHCCCCCEE		22.7729978859
376PhosphorylationQTVGLPVTMHSPNMR
HHCCCCCEECCCCHH		13.7629978859
379PhosphorylationGLPVTMHSPNMRLLR
CCCCEECCCCHHHHH		13.7225159151
442PhosphorylationLVRKGCQSLPSNMME
EECCCCCCCCCCCCC		46.4522210691
445PhosphorylationKGCQSLPSNMMETSI
CCCCCCCCCCCCCCH		42.5222210691
450PhosphorylationLPSNMMETSIDEGLE
CCCCCCCCCHHCCCC		17.0628348404
451PhosphorylationPSNMMETSIDEGLET
CCCCCCCCHHCCCCC		18.0928348404
458PhosphorylationSIDEGLETEGEAEED
CHHCCCCCCCCCCCC		55.0922210691
475PhosphorylationHAFEAFQSTRSGQRR
HHHHHHHCCCCCCCC		21.2322210691
476PhosphorylationAFEAFQSTRSGQRRH
HHHHHHCCCCCCCCC		20.3322210691
484PhosphorylationRSGQRRHTLSEVTNQ
CCCCCCCCHHHHCCE		30.1223401153
486PhosphorylationGQRRHTLSEVTNQLV
CCCCCCHHHHCCEEE		31.0423403867
489PhosphorylationRHTLSEVTNQLVVMP
CCCHHHHCCEEEEEC		17.1323403867
503PhosphorylationPGAGKIFSMNDSPSL
CCCCCEEECCCCCCC		21.8323090842
507PhosphorylationKIFSMNDSPSLDSVD
CEEECCCCCCCCCCC		16.0423090842
509PhosphorylationFSMNDSPSLDSVDSE
EECCCCCCCCCCCCC		49.0823090842
512PhosphorylationNDSPSLDSVDSEYDM
CCCCCCCCCCCCCCH		32.8723090842
515PhosphorylationPSLDSVDSEYDMGSV
CCCCCCCCCCCHHHH		35.5823090842
517PhosphorylationLDSVDSEYDMGSVQR
CCCCCCCCCHHHHHH		18.3823090842
521PhosphorylationDSEYDMGSVQRDLNF
CCCCCHHHHHHHHHH		14.4023090842
534PhosphorylationNFLEDNPSLKDIMLA
HHHCCCCCHHHHHHH		55.0630266825
536UbiquitinationLEDNPSLKDIMLANQ
HCCCCCHHHHHHHCC		49.9321890473
545PhosphorylationIMLANQPSPRMTSPF
HHHHCCCCCCCCCCC		18.5129632367
547MethylationLANQPSPRMTSPFIS
HHCCCCCCCCCCCEE		45.40115388631
576PhosphorylationKREVHNRSPVSFREG
CCHHHCCCCCCCCCC		34.6623898821
579PhosphorylationVHNRSPVSFREGRRA
HHCCCCCCCCCCCCC		23.2123403867
587PhosphorylationFREGRRASDTSLTQG
CCCCCCCCCCCCHHH		39.3414976552
589PhosphorylationEGRRASDTSLTQGIV
CCCCCCCCCCHHHHH		24.1230266825
590PhosphorylationGRRASDTSLTQGIVA
CCCCCCCCCHHHHHH		34.1223927012
592PhosphorylationRASDTSLTQGIVAFR
CCCCCCCHHHHHHHH		25.2323927012
670PhosphorylationASVHPQLSPRQSLET
CCCCCCCCCCCCHHH		16.8822468782
674PhosphorylationPQLSPRQSLETQYLQ
CCCCCCCCHHHHHHH		29.4724501219
686UbiquitinationYLQHRLQKPSLLSKA
HHHHHHCCHHHHHHH		40.96-
688PhosphorylationQHRLQKPSLLSKAQN
HHHHCCHHHHHHHHH		49.3224719451
692UbiquitinationQKPSLLSKAQNTCQL
CCHHHHHHHHHCHHH		54.7021890473
692UbiquitinationQKPSLLSKAQNTCQL
CCHHHHHHHHHCHHH		54.7021890473
700PhosphorylationAQNTCQLYCKEPPRS
HHHCHHHHCCCCCCC		3.90-
702UbiquitinationNTCQLYCKEPPRSLE
HCHHHHCCCCCCCHH		60.75-
707PhosphorylationYCKEPPRSLEQQLQE
HCCCCCCCHHHHHHH		41.8728555341
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
90SPhosphorylationKinaseSIK2Q9H0K1
GPS
175TPhosphorylationKinaseSTK11Q15831
PhosphoELM
343SPhosphorylationKinaseSIK2Q9H0K1
GPS
358SPhosphorylationKinasePRKACAP17612
GPS
358SPhosphorylationKinaseSIK2Q9H0K1
GPS
-KUbiquitinationE3 ubiquitin ligaseFBXW7Q969H0
PMID:32437091
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
53KAcetylation

23322770
175TPhosphorylation

14976552
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 SIK2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CRTC2_HUMANCRTC2physical
15454081
HDAC5_HUMANHDAC5physical
22462548
CRTC2_HUMANCRTC2physical
22462548
A4_HUMANAPPphysical
21832049
CP250_HUMANCEP250physical
20708153
HDAC5_HUMANHDAC5physical
23393134
TERA_HUMANVCPphysical
24129571
HSP74_HUMANHSPA4physical
24129571
1433Z_HUMANYWHAZphysical
24129571
1433E_HUMANYWHAEphysical
24129571
BAG2_HUMANBAG2physical
25852190
KC1A_HUMANCSNK1A1physical
25852190
EMD_HUMANEMDphysical
25852190
FUS_HUMANFUSphysical
25852190
HSP72_HUMANHSPA2physical
25852190
HSPB1_HUMANHSPB1physical
25852190
SHRM3_HUMANSHROOM3physical
25852190
TXTP_HUMANSLC25A1physical
25852190
CMC2_HUMANSLC25A13physical
25852190
TIF1B_HUMANTRIM28physical
25852190
TBA4A_HUMANTUBA4Aphysical
25852190
1433E_HUMANYWHAEphysical
25852190
TERA_HUMANVCPphysical
24841198
PP2AA_HUMANPPP2CAphysical
24841198
2ABG_HUMANPPP2R2Cphysical
24841198
2AAA_HUMANPPP2R1Aphysical
24841198
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 SIK2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-587, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25; SER-342; SER-576 ANDSER-587, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-587, AND MASSSPECTROMETRY.
"LKB1 is a master kinase that activates 13 kinases of the AMPKsubfamily, including MARK/PAR-1.";
Lizcano J.M., Goeransson O., Toth R., Deak M., Morrice N.A.,Boudeau J., Hawley S.A., Udd L., Maekelae T.P., Hardie D.G.,Alessi D.R.;
EMBO J. 23:833-843(2004).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME REGULATION, PHOSPHORYLATION ATTHR-175, AND MUTAGENESIS OF THR-175.

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