HNRPK_MOUSE - dbPTM
HNRPK_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HNRPK_MOUSE
UniProt AC P61979
Protein Name Heterogeneous nuclear ribonucleoprotein K
Gene Name Hnrnpk
Organism Mus musculus (Mouse).
Sequence Length 463
Subcellular Localization Cytoplasm . Nucleus, nucleoplasm . Cell projection, podosome .
Protein Description One of the major pre-mRNA-binding proteins. Binds tenaciously to poly(C) sequences. Likely to play a role in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. Can also bind poly(C) single-stranded DNA. Plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. When sumoylated, acts as a transcriptional coactivator of p53/TP53, playing a role in p21/CDKN1A and 14-3-3 sigma/SFN induction (By similarity). As far as transcription repression is concerned, acts by interacting with long intergenic RNA p21 (lincRNA-p21), a non-coding RNA induced by p53/TP53. This interaction is necessary for the induction of apoptosis, but not cell cycle arrest..
Protein Sequence METEQPEETFPNTETNGEFGKRPAEDMEEEQAFKRSRNTDEMVELRILLQSKNAGAVIGKGGKNIKALRTDYNASVSVPDSSGPERILSISADIETIGEILKKIIPTLEEGLQLPSPTATSQLPLESDAVECLNYQHYKGSDFDCELRLLIHQSLAGGIIGVKGAKIKELRENTQTTIKLFQECCPHSTDRVVLIGGKPDRVVECIKIILDLISESPIKGRAQPYDPNFYDETYDYGGFTMMFDDRRGRPVGFPMRGRGGFDRMPPGRGGRPMPPSRRDYDDMSPRRGPPPPPPGRGGRGGSRARNLPLPPPPPPRGGDLMAYDRRGRPGDRYDGMVGFSADETWDSAIDTWSPSEWQMAYEPQGGSGYDYSYAGGRGSYGDLGGPIITTQVTIPKDLAGSIIGKGGQRIKQIRHESGASIKIDEPLEGSEDRIITITGTQDQIQNAQYLLQNSVKQYSGKFF
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
1Acetylation-------METEQPEE
-------CCCCCCCC		15.05-
3Phosphorylation-----METEQPEETF
-----CCCCCCCCCC		38.3319060867
21AcetylationETNGEFGKRPAEDME
CCCCCCCCCCHHHHH		61.6023236377
34AcetylationMEEEQAFKRSRNTDE
HHHHHHHHHCCCHHH		53.1023806337
34MalonylationMEEEQAFKRSRNTDE
HHHHHHHHHCCCHHH		53.1026320211
34UbiquitinationMEEEQAFKRSRNTDE
HHHHHHHHHCCCHHH		53.10-
34 (in isoform 3)Ubiquitination-53.1022790023
36PhosphorylationEEQAFKRSRNTDEMV
HHHHHHHCCCHHHHH		30.3926745281
39PhosphorylationAFKRSRNTDEMVELR
HHHHCCCHHHHHHHH		32.0226824392
52AcetylationLRILLQSKNAGAVIG
HHHHHHCCCCCCEEC		37.5422826441
52UbiquitinationLRILLQSKNAGAVIG
HHHHHHCCCCCCEEC		37.5422790023
52 (in isoform 3)Ubiquitination-37.5422790023
60UbiquitinationNAGAVIGKGGKNIKA
CCCCEECCCCCCCEE		54.0622790023
60 (in isoform 3)Ubiquitination-54.0622790023
66UbiquitinationGKGGKNIKALRTDYN
CCCCCCCEEEECCCE		51.2522790023
66 (in isoform 3)Ubiquitination-51.2522790023
70PhosphorylationKNIKALRTDYNASVS
CCCEEEECCCEECEE		43.6221189417
72PhosphorylationIKALRTDYNASVSVP
CEEEECCCEECEECC		16.4118779572
75PhosphorylationLRTDYNASVSVPDSS
EECCCEECEECCCCC		15.9921189417
77PhosphorylationTDYNASVSVPDSSGP
CCCEECEECCCCCCC		25.9921189417
81PhosphorylationASVSVPDSSGPERIL
ECEECCCCCCCCEEE		30.9921189417
82PhosphorylationSVSVPDSSGPERILS
CEECCCCCCCCEEEE		66.7930635358
89PhosphorylationSGPERILSISADIET
CCCCEEEEEEECHHH		16.4826745281
91PhosphorylationPERILSISADIETIG
CCEEEEEEECHHHHH		19.2626745281
96PhosphorylationSISADIETIGEILKK
EEEECHHHHHHHHHH		34.3221189417
107PhosphorylationILKKIIPTLEEGLQL
HHHHHHHHHHHHCCC		36.0725619855
116PhosphorylationEEGLQLPSPTATSQL
HHHCCCCCCCCCCCC		43.4027087446
118PhosphorylationGLQLPSPTATSQLPL
HCCCCCCCCCCCCCC		47.0727087446
120PhosphorylationQLPSPTATSQLPLES
CCCCCCCCCCCCCCC		21.3427087446
121PhosphorylationLPSPTATSQLPLESD
CCCCCCCCCCCCCCC		27.5327087446
127PhosphorylationTSQLPLESDAVECLN
CCCCCCCCCHHHHCC		38.2527087446
132S-nitrosocysteineLESDAVECLNYQHYK
CCCCHHHHCCCCCCC		2.10-
132GlutathionylationLESDAVECLNYQHYK
CCCCHHHHCCCCCCC		2.1024333276
132S-nitrosylationLESDAVECLNYQHYK
CCCCHHHHCCCCCCC		2.1022178444
132S-palmitoylationLESDAVECLNYQHYK
CCCCHHHHCCCCCCC		2.1028680068
135PhosphorylationDAVECLNYQHYKGSD
CHHHHCCCCCCCCCC		5.4525619855
138PhosphorylationECLNYQHYKGSDFDC
HHCCCCCCCCCCCHH		11.0825619855
139 (in isoform 3)Ubiquitination-50.22-
141PhosphorylationNYQHYKGSDFDCELR
CCCCCCCCCCHHHHH		30.8428066266
145S-nitrosocysteineYKGSDFDCELRLLIH
CCCCCCHHHHHHHHH		5.53-
145GlutathionylationYKGSDFDCELRLLIH
CCCCCCHHHHHHHHH		5.5324333276
145S-nitrosylationYKGSDFDCELRLLIH
CCCCCCHHHHHHHHH		5.5320925432
145S-palmitoylationYKGSDFDCELRLLIH
CCCCCCHHHHHHHHH		5.5328526873
154PhosphorylationLRLLIHQSLAGGIIG
HHHHHHHHHHCCCCC		13.16-
155 (in isoform 3)Ubiquitination-4.06-
163UbiquitinationAGGIIGVKGAKIKEL
HCCCCCCCCCCHHHH		48.1922790023
163 (in isoform 3)Ubiquitination-48.1922790023
166UbiquitinationIIGVKGAKIKELREN
CCCCCCCCHHHHHHH		64.08-
174 (in isoform 3)Ubiquitination-23.65-
179AcetylationENTQTTIKLFQECCP
HHHHHHHHHHHHHCC		40.9522826441
179UbiquitinationENTQTTIKLFQECCP
HHHHHHHHHHHHHCC		40.9522790023
179 (in isoform 3)Ubiquitination-40.9522790023
184S-nitrosocysteineTIKLFQECCPHSTDR
HHHHHHHHCCCCCCE		2.80-
184S-nitrosylationTIKLFQECCPHSTDR
HHHHHHHHCCCCCCE		2.8020925432
185S-nitrosocysteineIKLFQECCPHSTDRV
HHHHHHHCCCCCCEE		3.15-
185GlutathionylationIKLFQECCPHSTDRV
HHHHHHHCCCCCCEE		3.1524333276
185S-nitrosylationIKLFQECCPHSTDRV
HHHHHHHCCCCCCEE		3.1520925432
195 (in isoform 3)Ubiquitination-4.64-
198AcetylationRVVLIGGKPDRVVEC
EEEEECCCHHHHHHH		38.2323806337
198UbiquitinationRVVLIGGKPDRVVEC
EEEEECCCHHHHHHH		38.2322790023
198 (in isoform 3)Ubiquitination-38.2322790023
214PhosphorylationKIILDLISESPIKGR
HHHHHHHCCCCCCCC		39.0424068923
216PhosphorylationILDLISESPIKGRAQ
HHHHHCCCCCCCCCC		25.7427087446
219AcetylationLISESPIKGRAQPYD
HHCCCCCCCCCCCCC		45.8123806337
219SuccinylationLISESPIKGRAQPYD
HHCCCCCCCCCCCCC		45.81-
219SuccinylationLISESPIKGRAQPYD
HHCCCCCCCCCCCCC		45.8123806337
219UbiquitinationLISESPIKGRAQPYD
HHCCCCCCCCCCCCC		45.81-
219 (in isoform 3)Ubiquitination-45.8122790023
249MethylationMFDDRRGRPVGFPMR
EEECCCCCCCCCCCC		22.4016289139
256MethylationRPVGFPMRGRGGFDR
CCCCCCCCCCCCCCC		31.7116288855
258MethylationVGFPMRGRGGFDRMP
CCCCCCCCCCCCCCC		31.5324258847
280PhosphorylationMPPSRRDYDDMSPRR
CCCCCCCCCCCCCCC		16.4228833060
283OxidationSRRDYDDMSPRRGPP
CCCCCCCCCCCCCCC		5.6217242355
284PhosphorylationRRDYDDMSPRRGPPP
CCCCCCCCCCCCCCC		23.4227087446
296DimethylationPPPPPPGRGGRGGSR
CCCCCCCCCCCCCCC		50.60-
296MethylationPPPPPPGRGGRGGSR
CCCCCCCCCCCCCCC		50.6016185643
299DimethylationPPPGRGGRGGSRARN
CCCCCCCCCCCCCCC		49.47-
299MethylationPPPGRGGRGGSRARN
CCCCCCCCCCCCCCC		49.4716185649
302PhosphorylationGRGGRGGSRARNLPL
CCCCCCCCCCCCCCC		26.1218295448
303DimethylationRGGRGGSRARNLPLP
CCCCCCCCCCCCCCC		40.62-
303MethylationRGGRGGSRARNLPLP
CCCCCCCCCCCCCCC		40.6216185655
316MethylationLPPPPPPRGGDLMAY
CCCCCCCCCCCCCEE		68.4524129315
323PhosphorylationRGGDLMAYDRRGRPG
CCCCCCEECCCCCCC		8.9425367039
325MethylationGDLMAYDRRGRPGDR
CCCCEECCCCCCCCC		30.2218959211
353PhosphorylationDSAIDTWSPSEWQMA
CCCCHHCCHHHCEEE		22.2020960454
371PhosphorylationQGGSGYDYSYAGGRG
CCCCCCCCCCCCCCC		8.63-
372 (in isoform 3)Ubiquitination-12.95-
377MethylationDYSYAGGRGSYGDLG
CCCCCCCCCCCCCCC		29.9324129315
379PhosphorylationSYAGGRGSYGDLGGP
CCCCCCCCCCCCCCC		25.2827087446
380PhosphorylationYAGGRGSYGDLGGPI
CCCCCCCCCCCCCCE		19.9225521595
381 (in isoform 3)Ubiquitination-25.93-
389PhosphorylationDLGGPIITTQVTIPK
CCCCCEEEEEEECCH		16.3428833060
390PhosphorylationLGGPIITTQVTIPKD
CCCCEEEEEEECCHH		15.6128833060
393PhosphorylationPIITTQVTIPKDLAG
CEEEEEEECCHHHHC		23.0328833060
396UbiquitinationTTQVTIPKDLAGSII
EEEEECCHHHHCCCC		62.6222790023
396 (in isoform 3)Ubiquitination-62.6222790023
398 (in isoform 3)Ubiquitination-7.89-
401PhosphorylationIPKDLAGSIIGKGGQ
CCHHHHCCCCCCCCH		12.8628833060
405AcetylationLAGSIIGKGGQRIKQ
HHCCCCCCCCHHHEE		49.8423806337
405MalonylationLAGSIIGKGGQRIKQ
HHCCCCCCCCHHHEE		49.8426320211
405UbiquitinationLAGSIIGKGGQRIKQ
HHCCCCCCCCHHHEE		49.84-
405 (in isoform 3)Ubiquitination-49.8422790023
417PhosphorylationIKQIRHESGASIKID
HEEEECCCCCCEEEC		33.2728066266
420PhosphorylationIRHESGASIKIDEPL
EECCCCCCEEECCCC		28.1326824392
422AcetylationHESGASIKIDEPLEG
CCCCCCEEECCCCCC		41.4323806337
422SuccinylationHESGASIKIDEPLEG
CCCCCCEEECCCCCC		41.4323806337
422UbiquitinationHESGASIKIDEPLEG
CCCCCCEEECCCCCC		41.43-
422 (in isoform 3)Ubiquitination-41.4322790023
430PhosphorylationIDEPLEGSEDRIITI
ECCCCCCCCCEEEEE		27.2728066266
432 (in isoform 3)Ubiquitination-49.10-
436PhosphorylationGSEDRIITITGTQDQ
CCCCEEEEEECCHHH		15.32-
440PhosphorylationRIITITGTQDQIQNA
EEEEEECCHHHHHHH		21.96-
449PhosphorylationDQIQNAQYLLQNSVK
HHHHHHHHHHHHHHH		13.63-
456UbiquitinationYLLQNSVKQYSGKFF
HHHHHHHHHHCCCCC		43.2522790023
456 (in isoform 3)Ubiquitination-43.2522790023
461UbiquitinationSVKQYSGKFF-----
HHHHHCCCCC-----		37.34-
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
302SPhosphorylationKinasePRKCAP20444
GPS
302SPhosphorylationKinasePRKCBP68404
GPS
302SPhosphorylationKinasePRKCDP28867
GPS
302SPhosphorylationKinasePRKCGP63318
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HNRPK_MOUSE !!
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 HNRPK_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of HNRPK_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HNRPK_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND MASSSPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND MASSSPECTROMETRY.
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND MASSSPECTROMETRY.

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