SNRK_HUMAN - dbPTM
SNRK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNRK_HUMAN
UniProt AC Q9NRH2
Protein Name SNF-related serine/threonine-protein kinase
Gene Name SNRK {ECO:0000312|EMBL:AAH71567.1}
Organism Homo sapiens (Human).
Sequence Length 765
Subcellular Localization Nucleus.
Protein Description May play a role in hematopoietic cell proliferation or differentiation. Potential mediator of neuronal apoptosis..
Protein Sequence MAGFKRGYDGKIAGLYDLDKTLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDTLATGHLFQEVRCMKLVQHPNIVRLYEVIDTQTKLYLILELGDGGDMFDYIMKHEEGLNEDLAKKYFAQIVHAISYCHKLHVVHRDLKPENVVFFEKQGLVKLTDFGFSNKFQPGKKLTTSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILFMLVCGQPPFQEANDSETLTMIMDCKYTVPSHVSKECKDLITRMLQRDPKRRASLEEIENHPWLQGVDPSPATKYNIPLVSYKNLSEEEHNSIIQRMVLGDIADRDAIVEALETNRYNHITATYFLLAERILREKQEKEIQTRSASPSNIKAQFRQSWPTKIDVPQDLEDDLTATPLSHATVPQSPARAADSVLNGHRSKGLCDSAKKDDLPELAGPALSTVPPASLKPTASGRKCLFRVEEDEEEDEEDKKPMSLSTQVVLRRKPSVTNRLTSRKSAPVLNQIFEEGESDDEFDMDENLPPKLSRLKMNIASPGTVHKRYHRRKSQGRGSSCSSSETSDDDSESRRRLDKDSGFTYSWHRRDSSEGPPGSEGDGGGQSKPSNASGGVDKASPSENNAGGGSPSSGSGGNPTNTSGTTRRCAGPSNSMQLASRSAGELVESLKLMSLCLGSQLHGSTKYIIDPQNGLSFSSVKVQEKSTWKMCISSTGNAGQVPAVGGIKFFSDHMADTTTELERIKSKNLKNNVLQLPLCEKTISVNIQRNPKEGLLCASSPASCCHVI
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
11AcetylationFKRGYDGKIAGLYDL
CCCCCCCCEEEEEEH		26.8719608861
11UbiquitinationFKRGYDGKIAGLYDL
CCCCCCCCEEEEEEH		26.8719608861
16PhosphorylationDGKIAGLYDLDKTLG
CCCEEEEEEHHHCCC		17.3425022875
20UbiquitinationAGLYDLDKTLGRGHF
EEEEEHHHCCCCCHH		53.60-
21PhosphorylationGLYDLDKTLGRGHFA
EEEEHHHCCCCCHHH		33.8328857561
41UbiquitinationRHVFTGEKVAVKVID
HHHHCCCEEEEEEEC		36.52-
45UbiquitinationTGEKVAVKVIDKTKL
CCCEEEEEEECHHHC		24.60-
68AcetylationFQEVRCMKLVQHPNI
HHHHHHHHHCCCCCE		49.48133775
141UbiquitinationHVVHRDLKPENVVFF
CEECCCCCHHHEEEE		55.35-
150UbiquitinationENVVFFEKQGLVKLT
HHEEEEEECCEEEEE		44.50-
157PhosphorylationKQGLVKLTDFGFSNK
ECCEEEEECCCCCCC		24.46-
162PhosphorylationKLTDFGFSNKFQPGK
EEECCCCCCCCCCCC		39.2223403867
164UbiquitinationTDFGFSNKFQPGKKL
ECCCCCCCCCCCCEE		44.15-
172PhosphorylationFQPGKKLTTSCGSLA
CCCCCEEECCCCHHH		26.08-
173PhosphorylationQPGKKLTTSCGSLAY
CCCCEEECCCCHHHC		32.2422817900
174PhosphorylationPGKKLTTSCGSLAYS
CCCEEECCCCHHHCC		15.96-
236PhosphorylationDCKYTVPSHVSKECK
ECCCCCCHHHCHHHH		31.9823322592
239PhosphorylationYTVPSHVSKECKDLI
CCCCHHHCHHHHHHH		19.8123322592
247PhosphorylationKECKDLITRMLQRDP
HHHHHHHHHHHHHCH		19.8123322592
259PhosphorylationRDPKRRASLEEIENH
HCHHHHCCHHHHHCC		34.2123927012
275PhosphorylationWLQGVDPSPATKYNI
CCCCCCCCCCCCCCC		23.7825159151
279UbiquitinationVDPSPATKYNIPLVS
CCCCCCCCCCCCEEE		38.10-
347PhosphorylationKQEKEIQTRSASPSN
HHHHHHHHCCCCHHH		32.0529514088
349PhosphorylationEKEIQTRSASPSNIK
HHHHHHCCCCHHHHH		36.1629396449
351PhosphorylationEIQTRSASPSNIKAQ
HHHHCCCCHHHHHHH		30.0625159151
353PhosphorylationQTRSASPSNIKAQFR
HHCCCCHHHHHHHHH		49.0128985074
362PhosphorylationIKAQFRQSWPTKIDV
HHHHHHHHCCCCCCC		30.6630266825
365PhosphorylationQFRQSWPTKIDVPQD
HHHHHCCCCCCCCCC		34.0823403867
378PhosphorylationQDLEDDLTATPLSHA
CCCCCCCCCCCCCCC		35.1623663014
380PhosphorylationLEDDLTATPLSHATV
CCCCCCCCCCCCCCC		21.3723663014
383PhosphorylationDLTATPLSHATVPQS
CCCCCCCCCCCCCCC		16.5723663014
386PhosphorylationATPLSHATVPQSPAR
CCCCCCCCCCCCHHH		27.5625159151
390PhosphorylationSHATVPQSPARAADS
CCCCCCCCHHHHHHH		17.9223401153
437PhosphorylationASLKPTASGRKCLFR
HHCCCCCCCCEEEEE		41.4228555341
460PhosphorylationEEDKKPMSLSTQVVL
CCCCCCCCCHHHHHH		27.9129083192
462PhosphorylationDKKPMSLSTQVVLRR
CCCCCCCHHHHHHCC		14.9729083192
463PhosphorylationKKPMSLSTQVVLRRK
CCCCCCHHHHHHCCC		30.5829083192
482PhosphorylationNRLTSRKSAPVLNQI
HHCCCCCCCHHHHHH		36.3730624053
495PhosphorylationQIFEEGESDDEFDMD
HHHHCCCCCCCCCCC		62.3125159151
518PhosphorylationRLKMNIASPGTVHKR
HHHHCCCCCCCHHHH		21.7729255136
521PhosphorylationMNIASPGTVHKRYHR
HCCCCCCCHHHHHHC		23.8730266825
531PhosphorylationKRYHRRKSQGRGSSC
HHHHCCCCCCCCCCC		35.74-
534MethylationHRRKSQGRGSSCSSS
HCCCCCCCCCCCCCC		33.9016186555
536PhosphorylationRKSQGRGSSCSSSET
CCCCCCCCCCCCCCC		27.15-
537PhosphorylationKSQGRGSSCSSSETS
CCCCCCCCCCCCCCC		22.35-
543PhosphorylationSSCSSSETSDDDSES
CCCCCCCCCCCCHHH		39.13-
544PhosphorylationSCSSSETSDDDSESR
CCCCCCCCCCCHHHH		34.6825307156
548PhosphorylationSETSDDDSESRRRLD
CCCCCCCHHHHHHCC		44.4525307156
550PhosphorylationTSDDDSESRRRLDKD
CCCCCHHHHHHCCCC		34.73-
558PhosphorylationRRRLDKDSGFTYSWH
HHHCCCCCCCCCEEE		41.3623882029
561PhosphorylationLDKDSGFTYSWHRRD
CCCCCCCCCEEECCC		21.8528796482
562PhosphorylationDKDSGFTYSWHRRDS
CCCCCCCCEEECCCC		13.9128796482
563PhosphorylationKDSGFTYSWHRRDSS
CCCCCCCEEECCCCC		17.2228796482
569PhosphorylationYSWHRRDSSEGPPGS
CEEECCCCCCCCCCC		28.6023401153
570PhosphorylationSWHRRDSSEGPPGSE
EEECCCCCCCCCCCC		51.3527273156
576PhosphorylationSSEGPPGSEGDGGGQ
CCCCCCCCCCCCCCC		44.1523403867
584PhosphorylationEGDGGGQSKPSNASG
CCCCCCCCCCCCCCC		50.2123403867
587PhosphorylationGGGQSKPSNASGGVD
CCCCCCCCCCCCCCC		49.0823403867
590PhosphorylationQSKPSNASGGVDKAS
CCCCCCCCCCCCCCC		40.0923403867
597PhosphorylationSGGVDKASPSENNAG
CCCCCCCCCCCCCCC		34.4028450419
599PhosphorylationGVDKASPSENNAGGG
CCCCCCCCCCCCCCC		50.9228450419
607PhosphorylationENNAGGGSPSSGSGG
CCCCCCCCCCCCCCC		25.5325159151
609PhosphorylationNAGGGSPSSGSGGNP
CCCCCCCCCCCCCCC		49.3730576142
610PhosphorylationAGGGSPSSGSGGNPT
CCCCCCCCCCCCCCC		40.1228450419
612PhosphorylationGGSPSSGSGGNPTNT
CCCCCCCCCCCCCCC		45.5428450419
617PhosphorylationSGSGGNPTNTSGTTR
CCCCCCCCCCCCCCE		55.9423186163
619PhosphorylationSGGNPTNTSGTTRRC
CCCCCCCCCCCCEEC		30.8923186163
620PhosphorylationGGNPTNTSGTTRRCA
CCCCCCCCCCCEECC		35.8923186163
623PhosphorylationPTNTSGTTRRCAGPS
CCCCCCCCEECCCCC		21.46-
639PhosphorylationSMQLASRSAGELVES
HHHHHHCCHHHHHHH		37.8230576142
646PhosphorylationSAGELVESLKLMSLC
CHHHHHHHHHHHHHH		24.2721815630
664PhosphorylationQLHGSTKYIIDPQNG
CCCCCCEEEECCCCC		11.8226074081
673PhosphorylationIDPQNGLSFSSVKVQ
ECCCCCCCCCCEEEE		25.2026074081
675PhosphorylationPQNGLSFSSVKVQEK
CCCCCCCCCEEEEEC		30.7426074081
676PhosphorylationQNGLSFSSVKVQEKS
CCCCCCCCEEEEECC		24.7726074081
727UbiquitinationRIKSKNLKNNVLQLP
HHHHCCCCCCEECCC		56.73-
738UbiquitinationLQLPLCEKTISVNIQ
ECCCCCEEEEEEECC		50.60-
749UbiquitinationVNIQRNPKEGLLCAS
EECCCCCCCCCEECC		68.88-
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
173TPhosphorylationKinaseSTK11Q15831
PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
173TPhosphorylation

15733851
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 SNRK_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STK16_HUMANSTK16physical
17353931
ABHD5_HUMANABHD5physical
28514442
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 SNRK_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-11, AND MASS SPECTROMETRY.
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-390, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-607, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, AND MASSSPECTROMETRY.
"Identification of the sucrose non-fermenting related kinase SNRK, asa novel LKB1 substrate.";
Jaleel M., McBride A., Lizcano J.M., Deak M., Toth R., Morrice N.A.,Alessi D.R.;
FEBS Lett. 579:1417-1423(2005).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION,PHOSPHORYLATION AT THR-173, AND MUTAGENESIS OF THR-173.

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