HNRPK_RAT - dbPTM
HNRPK_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HNRPK_RAT
UniProt AC P61980
Protein Name Heterogeneous nuclear ribonucleoprotein K
Gene Name Hnrnpk
Organism Rattus norvegicus (Rat).
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. 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 (By similarity)..
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-
21AcetylationETNGEFGKRPAEDME
CCCCCCCCCCHHHHH		61.6022902405
34AcetylationMEEEQAFKRSRNTDE
HHHHHHHHHCCCHHH		53.1022902405
36PhosphorylationEEQAFKRSRNTDEMV
HHHHHHHCCCHHHHH		30.3925575281
39PhosphorylationAFKRSRNTDEMVELR
HHHHCCCHHHHHHHH		32.0228432305
52AcetylationLRILLQSKNAGAVIG
HHHHHHCCCCCCEEC		37.5472621189
66AcetylationGKGGKNIKALRTDYN
CCCCCCCEEEECCCE		51.2572593513
75PhosphorylationLRTDYNASVSVPDSS
EECCCEECEECCCCC		15.99-
89PhosphorylationSGPERILSISADIET
CCCCEEEEEEECHHH		16.4823984901
91PhosphorylationPERILSISADIETIG
CCEEEEEEECHHHHH		19.2623984901
107PhosphorylationILKKIIPTLEEGLQL
HHHHHHHHHHHHCCC		36.0727097102
116PhosphorylationEEGLQLPSPTATSQL
HHHCCCCCCCCCCCC		43.4023712012
118PhosphorylationGLQLPSPTATSQLPL
HCCCCCCCCCCCCCC		47.0721738781
120PhosphorylationQLPSPTATSQLPLES
CCCCCCCCCCCCCCC		21.3427097102
121PhosphorylationLPSPTATSQLPLESD
CCCCCCCCCCCCCCC		27.5327097102
127PhosphorylationTSQLPLESDAVECLN
CCCCCCCCCHHHHCC		38.2527097102
135PhosphorylationDAVECLNYQHYKGSD
CHHHHCCCCCCCCCC		5.4528551015
138PhosphorylationECLNYQHYKGSDFDC
HHCCCCCCCCCCCHH		11.0828551015
154PhosphorylationLRLLIHQSLAGGIIG
HHHHHHHHHHCCCCC		13.1623984901
163AcetylationAGGIIGVKGAKIKEL
HCCCCCCCCCCHHHH		48.1925786129
176PhosphorylationELRENTQTTIKLFQE
HHHHHHHHHHHHHHH		28.5723984901
177PhosphorylationLRENTQTTIKLFQEC
HHHHHHHHHHHHHHH		13.2923984901
188PhosphorylationFQECCPHSTDRVVLI
HHHHCCCCCCEEEEE		19.6927097102
189PhosphorylationQECCPHSTDRVVLIG
HHHCCCCCCEEEEEC		25.4527097102
198AcetylationRVVLIGGKPDRVVEC
EEEEECCCHHHHHHH		38.23-
214PhosphorylationKIILDLISESPIKGR
HHHHHHHCCCCCCCC		39.0423984901
216PhosphorylationILDLISESPIKGRAQ
HHHHHCCCCCCCCCC		25.7427097102
219UbiquitinationLISESPIKGRAQPYD
HHCCCCCCCCCCCCC		45.81-
219SuccinylationLISESPIKGRAQPYD
HHCCCCCCCCCCCCC		45.81-
219SuccinylationLISESPIKGRAQPYD
HHCCCCCCCCCCCCC		45.81-
225PhosphorylationIKGRAQPYDPNFYDE
CCCCCCCCCCCCCCC		31.77-
230PhosphorylationQPYDPNFYDETYDYG
CCCCCCCCCCEECCC		21.36-
280PhosphorylationMPPSRRDYDDMSPRR
CCCCCCCCCCCCCCC		16.4228551015
284PhosphorylationRRDYDDMSPRRGPPP
CCCCCCCCCCCCCCC		23.4223712012
286MethylationDYDDMSPRRGPPPPP
CCCCCCCCCCCCCCC		49.2126494257
296MethylationPPPPPPGRGGRGGSR
CCCCCCCCCCCCCCC		50.6020679683
299MethylationPPPGRGGRGGSRARN
CCCCCCCCCCCCCCC		49.4720679689
303MethylationRGGRGGSRARNLPLP
CCCCCCCCCCCCCCC		40.6220679695
316MethylationLPPPPPPRGGDLMAY
CCCCCCCCCCCCCEE		68.4512018929
325MethylationGDLMAYDRRGRPGDR
CCCCEECCCCCCCCC		30.2218959217
371PhosphorylationQGGSGYDYSYAGGRG
CCCCCCCCCCCCCCC		8.6321940666
377MethylationDYSYAGGRGSYGDLG
CCCCCCCCCCCCCCC		29.93-
379PhosphorylationSYAGGRGSYGDLGGP
CCCCCCCCCCCCCCC		25.2824259510
380PhosphorylationYAGGRGSYGDLGGPI
CCCCCCCCCCCCCCE		19.9227097102
389PhosphorylationDLGGPIITTQVTIPK
CCCCCEEEEEEECCH		16.3425575281
390PhosphorylationLGGPIITTQVTIPKD
CCCCEEEEEEECCHH		15.6125575281
401PhosphorylationIPKDLAGSIIGKGGQ
CCHHHHCCCCCCCCH		12.8627097102
405AcetylationLAGSIIGKGGQRIKQ
HHCCCCCCCCHHHEE		49.84-
405UbiquitinationLAGSIIGKGGQRIKQ
HHCCCCCCCCHHHEE		49.84-
420PhosphorylationIRHESGASIKIDEPL
EECCCCCCEEECCCC		28.13-
430PhosphorylationIDEPLEGSEDRIITI
ECCCCCCCCCEEEEE		27.2728432305
461AcetylationSVKQYSGKFF-----
HHHHHCCCCC-----		37.3422902405
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
216SPhosphorylationKinaseCDK1P06493
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS.";
Moser K., White F.M.;
J. Proteome Res. 5:98-104(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND MASSSPECTROMETRY.

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