HNRPK_HUMAN - dbPTM
HNRPK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HNRPK_HUMAN
UniProt AC P61978
Protein Name Heterogeneous nuclear ribonucleoprotein K
Gene Name HNRNPK
Organism Homo sapiens (Human).
Sequence Length 463
Subcellular Localization Cytoplasm . Nucleus, nucleoplasm . Cell projection, podosome . Recruited to p53/TP53-responsive promoters, in the presence of functional p53/TP53 (PubMed:16360036). In case of ASFV infection, there is a shift in the localization which becomes predomi
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		15.0522814378
1Sulfoxidation-------METEQPEE
-------CCCCCCCC		15.0528183972
3Phosphorylation-----METEQPEETF
-----CCCCCCCCCC		38.3328355574
9PhosphorylationETEQPEETFPNTETN
CCCCCCCCCCCCCCC		42.6130377224
13PhosphorylationPEETFPNTETNGEFG
CCCCCCCCCCCCCCC		44.4127251275
15PhosphorylationETFPNTETNGEFGKR
CCCCCCCCCCCCCCC		46.6225627689
21AcetylationETNGEFGKRPAEDME
CCCCCCCCCCHHHHH		61.6023236377
22MethylationTNGEFGKRPAEDMEE
CCCCCCCCCHHHHHH		35.7218583659
27SulfoxidationGKRPAEDMEEEQAFK
CCCCHHHHHHHHHHH		5.4121406390
34SumoylationMEEEQAFKRSRNTDE
HHHHHHHHHCCCHHH		53.10-
34AcetylationMEEEQAFKRSRNTDE
HHHHHHHHHCCCHHH		53.1023954790
34MethylationMEEEQAFKRSRNTDE
HHHHHHHHHCCCHHH		53.1068937
34SumoylationMEEEQAFKRSRNTDE
HHHHHHHHHCCCHHH		53.1025114211
34UbiquitinationMEEEQAFKRSRNTDE
HHHHHHHHHCCCHHH		53.1021890473
34 (in isoform 1)Ubiquitination-53.1021890473
34 (in isoform 2)Ubiquitination-53.1021890473
34 (in isoform 3)Ubiquitination-53.1021890473
34UbiquitinationMEEEQAFKRSRNTDE
HHHHHHHHHCCCHHH		53.1021890473
36PhosphorylationEEQAFKRSRNTDEMV
HHHHHHHCCCHHHHH		30.3923401153
39PhosphorylationAFKRSRNTDEMVELR
HHHHCCCHHHHHHHH		32.0230266825
42SulfoxidationRSRNTDEMVELRILL
HCCCHHHHHHHHHHH		2.9421406390
46MethylationTDEMVELRILLQSKN
HHHHHHHHHHHHCCC		12.1918583671
52SumoylationLRILLQSKNAGAVIG
HHHHHHCCCCCCEEC		37.54-
522-HydroxyisobutyrylationLRILLQSKNAGAVIG
HHHHHHCCCCCCEEC		37.54-
52AcetylationLRILLQSKNAGAVIG
HHHHHHCCCCCCEEC		37.5425953088
52MalonylationLRILLQSKNAGAVIG
HHHHHHCCCCCCEEC		37.5426320211
52SumoylationLRILLQSKNAGAVIG
HHHHHHCCCCCCEEC		37.5428112733
52UbiquitinationLRILLQSKNAGAVIG
HHHHHHCCCCCCEEC		37.54-
52 (in isoform 1)Ubiquitination-37.5421890473
52 (in isoform 2)Ubiquitination-37.5421890473
52 (in isoform 3)Ubiquitination-37.5421890473
52UbiquitinationLRILLQSKNAGAVIG
HHHHHHCCCCCCEEC		37.5421890473
60SumoylationNAGAVIGKGGKNIKA
CCCCEECCCCCCCEE		54.06-
602-HydroxyisobutyrylationNAGAVIGKGGKNIKA
CCCCEECCCCCCCEE		54.06-
60AcetylationNAGAVIGKGGKNIKA
CCCCEECCCCCCCEE		54.0621466224
60SumoylationNAGAVIGKGGKNIKA
CCCCEECCCCCCCEE		54.0628112733
60UbiquitinationNAGAVIGKGGKNIKA
CCCCEECCCCCCCEE		54.0621906983
60 (in isoform 1)Ubiquitination-54.0621890473
60 (in isoform 2)Ubiquitination-54.0621890473
60 (in isoform 3)Ubiquitination-54.0621890473
63AcetylationAVIGKGGKNIKALRT
CEECCCCCCCEEEEC		65.2621466224
63UbiquitinationAVIGKGGKNIKALRT
CEECCCCCCCEEEEC		65.26-
66AcetylationGKGGKNIKALRTDYN
CCCCCCCEEEECCCE		51.2521466224
66UbiquitinationGKGGKNIKALRTDYN
CCCCCCCEEEECCCE		51.2518655026
66 (in isoform 1)Ubiquitination-51.2521890473
70PhosphorylationKNIKALRTDYNASVS
CCCEEEECCCEECEE		43.6228152594
72NitrationIKALRTDYNASVSVP
CEEEECCCEECEECC		16.41-
72PhosphorylationIKALRTDYNASVSVP
CEEEECCCEECEECC		16.4128152594
75PhosphorylationLRTDYNASVSVPDSS
EECCCEECEECCCCC		15.9925159151
77PhosphorylationTDYNASVSVPDSSGP
CCCEECEECCCCCCC		25.9920164059
81PhosphorylationASVSVPDSSGPERIL
ECEECCCCCCCCEEE		30.9928450419
82PhosphorylationSVSVPDSSGPERILS
CEECCCCCCCCEEEE		66.7928450419
89PhosphorylationSGPERILSISADIET
CCCCEEEEEEECHHH		16.4828450419
91PhosphorylationPERILSISADIETIG
CCEEEEEEECHHHHH		19.2627732954
96PhosphorylationSISADIETIGEILKK
EEEECHHHHHHHHHH		34.3227732954
1022-HydroxyisobutyrylationETIGEILKKIIPTLE
HHHHHHHHHHHHHHH		47.81-
102UbiquitinationETIGEILKKIIPTLE
HHHHHHHHHHHHHHH		47.8121906983
102 (in isoform 1)Ubiquitination-47.8121890473
102 (in isoform 2)Ubiquitination-47.8121890473
102 (in isoform 3)Ubiquitination-47.8121890473
102UbiquitinationETIGEILKKIIPTLE
HHHHHHHHHHHHHHH		47.8121890473
103UbiquitinationTIGEILKKIIPTLEE
HHHHHHHHHHHHHHH		42.28-
107PhosphorylationILKKIIPTLEEGLQL
HHHHHHHHHHHHCCC		36.0726846344
111 (in isoform 3)Phosphorylation-14.8928152594
114 (in isoform 3)Phosphorylation-5.6528152594
116PhosphorylationEEGLQLPSPTATSQL
HHHCCCCCCCCCCCC		43.4026846344
118PhosphorylationGLQLPSPTATSQLPL
HCCCCCCCCCCCCCC		47.0726846344
120O-linked_GlycosylationQLPSPTATSQLPLES
CCCCCCCCCCCCCCC		21.34OGP
120PhosphorylationQLPSPTATSQLPLES
CCCCCCCCCCCCCCC		21.3426846344
121PhosphorylationLPSPTATSQLPLESD
CCCCCCCCCCCCCCC		27.5326846344
127PhosphorylationTSQLPLESDAVECLN
CCCCCCCCCHHHHCC		38.2526846344
135PhosphorylationDAVECLNYQHYKGSD
CHHHHCCCCCCCCCC		5.4526846344
138PhosphorylationECLNYQHYKGSDFDC
HHCCCCCCCCCCCHH		11.0826846344
139AcetylationCLNYQHYKGSDFDCE
HCCCCCCCCCCCHHH		50.2226051181
139MethylationCLNYQHYKGSDFDCE
HCCCCCCCCCCCHHH		50.2223583077
139UbiquitinationCLNYQHYKGSDFDCE
HCCCCCCCCCCCHHH		50.22-
139 (in isoform 3)Ubiquitination-50.2221890473
141PhosphorylationNYQHYKGSDFDCELR
CCCCCCCCCCHHHHH		30.8421815630
145GlutathionylationYKGSDFDCELRLLIH
CCCCCCHHHHHHHHH		5.5322555962
148MethylationSDFDCELRLLIHQSL
CCCHHHHHHHHHHHH		12.73115479195
154O-linked_GlycosylationLRLLIHQSLAGGIIG
HHHHHHHHHHCCCCC		13.1623576270
154PhosphorylationLRLLIHQSLAGGIIG
HHHHHHHHHHCCCCC		13.1628450419
155 (in isoform 3)Ubiquitination-4.0621890473
163SumoylationAGGIIGVKGAKIKEL
HCCCCCCCCCCHHHH		48.19-
163AcetylationAGGIIGVKGAKIKEL
HCCCCCCCCCCHHHH		48.1925953088
163SumoylationAGGIIGVKGAKIKEL
HCCCCCCCCCCHHHH		48.1925114211
163UbiquitinationAGGIIGVKGAKIKEL
HCCCCCCCCCCHHHH		48.1921906983
163 (in isoform 1)Ubiquitination-48.1921890473
163 (in isoform 2)Ubiquitination-48.1921890473
163UbiquitinationAGGIIGVKGAKIKEL
HCCCCCCCCCCHHHH		48.1921890473
166UbiquitinationIIGVKGAKIKELREN
CCCCCCCCHHHHHHH		64.08-
168UbiquitinationGVKGAKIKELRENTQ
CCCCCCHHHHHHHHH		50.41-
174PhosphorylationIKELRENTQTTIKLF
HHHHHHHHHHHHHHH		23.6527067055
174 (in isoform 3)Ubiquitination-23.6521890473
177PhosphorylationLRENTQTTIKLFQEC
HHHHHHHHHHHHHHH		13.2927067055
179AcetylationENTQTTIKLFQECCP
HHHHHHHHHHHHHCC		40.9525825284
179UbiquitinationENTQTTIKLFQECCP
HHHHHHHHHHHHHCC		40.9521906983
179 (in isoform 1)Ubiquitination-40.9521890473
179 (in isoform 2)Ubiquitination-40.9521890473
179UbiquitinationENTQTTIKLFQECCP
HHHHHHHHHHHHHCC		40.9521890473
183 (in isoform 3)Ubiquitination-30.6521890473
184S-nitrosocysteineTIKLFQECCPHSTDR
HHHHHHHHCCCCCCE		2.80-
184GlutathionylationTIKLFQECCPHSTDR
HHHHHHHHCCCCCCE		2.8022555962
184S-nitrosylationTIKLFQECCPHSTDR
HHHHHHHHCCCCCCE		2.8019483679
185S-nitrosocysteineIKLFQECCPHSTDRV
HHHHHHHCCCCCCEE		3.15-
185S-nitrosylationIKLFQECCPHSTDRV
HHHHHHHCCCCCCEE		3.1519483679
188PhosphorylationFQECCPHSTDRVVLI
HHHHCCCCCCEEEEE		19.6923898821
189PhosphorylationQECCPHSTDRVVLIG
HHHCCCCCCEEEEEC		25.4523898821
191MethylationCCPHSTDRVVLIGGK
HCCCCCCEEEEECCC		22.11115479211
195 (in isoform 3)Ubiquitination-4.6421890473
1982-HydroxyisobutyrylationRVVLIGGKPDRVVEC
EEEEECCCHHHHHHH		38.23-
198AcetylationRVVLIGGKPDRVVEC
EEEEECCCHHHHHHH		38.2325953088
198MethylationRVVLIGGKPDRVVEC
EEEEECCCHHHHHHH		38.2366699929
198UbiquitinationRVVLIGGKPDRVVEC
EEEEECCCHHHHHHH		38.2321890473
198 (in isoform 1)Ubiquitination-38.2321890473
198 (in isoform 2)Ubiquitination-38.2321890473
198UbiquitinationRVVLIGGKPDRVVEC
EEEEECCCHHHHHHH		38.2321890473
201MethylationLIGGKPDRVVECIKI
EECCCHHHHHHHHHH		42.80115479227
207UbiquitinationDRVVECIKIILDLIS
HHHHHHHHHHHHHHC		35.0421906983
207 (in isoform 1)Ubiquitination-35.0421890473
207 (in isoform 2)Ubiquitination-35.0421890473
207UbiquitinationDRVVECIKIILDLIS
HHHHHHHHHHHHHHC		35.0421890473
214PhosphorylationKIILDLISESPIKGR
HHHHHHHCCCCCCCC		39.0423927012
216PhosphorylationILDLISESPIKGRAQ
HHHHHCCCCCCCCCC		25.7419664994
2192-HydroxyisobutyrylationLISESPIKGRAQPYD
HHCCCCCCCCCCCCC		45.81-
219AcetylationLISESPIKGRAQPYD
HHCCCCCCCCCCCCC		45.8125953088
219SuccinylationLISESPIKGRAQPYD
HHCCCCCCCCCCCCC		45.81-
219SuccinylationLISESPIKGRAQPYD
HHCCCCCCCCCCCCC		45.8123954790
219SumoylationLISESPIKGRAQPYD
HHCCCCCCCCCCCCC		45.8128112733
219UbiquitinationLISESPIKGRAQPYD
HHCCCCCCCCCCCCC		45.81-
219 (in isoform 1)Ubiquitination-45.8121890473
219 (in isoform 2)Ubiquitination-45.8121890473
219UbiquitinationLISESPIKGRAQPYD
HHCCCCCCCCCCCCC		45.8121890473
225PhosphorylationIKGRAQPYDPNFYDE
CCCCCCCCCCCCCCC		31.7712052863
230PhosphorylationQPYDPNFYDETYDYG
CCCCCCCCCCEECCC		21.3612052863
234PhosphorylationPNFYDETYDYGGFTM
CCCCCCEECCCCEEE		12.7212052863
236PhosphorylationFYDETYDYGGFTMMF
CCCCEECCCCEEEEE		14.5612052863
241SulfoxidationYDYGGFTMMFDDRRG
ECCCCEEEEEECCCC		2.0528465586
242SulfoxidationDYGGFTMMFDDRRGR
CCCCEEEEEECCCCC		2.7928465586
246MethylationFTMMFDDRRGRPVGF
EEEEEECCCCCCCCC		44.8154556673
247MethylationTMMFDDRRGRPVGFP
EEEEECCCCCCCCCC		53.0954556689
249DimethylationMFDDRRGRPVGFPMR
EEECCCCCCCCCCCC		22.40-
249MethylationMFDDRRGRPVGFPMR
EEECCCCCCCCCCCC		22.4016289147
256DimethylationRPVGFPMRGRGGFDR
CCCCCCCCCCCCCCC		31.71-
256MethylationRPVGFPMRGRGGFDR
CCCCCCCCCCCCCCC		31.7120679681
258DimethylationVGFPMRGRGGFDRMP
CCCCCCCCCCCCCCC		31.53-
258MethylationVGFPMRGRGGFDRMP
CCCCCCCCCCCCCCC		31.5324156205
263MethylationRGRGGFDRMPPGRGG
CCCCCCCCCCCCCCC		36.9354556705
268DimethylationFDRMPPGRGGRPMPP
CCCCCCCCCCCCCCC		50.60-
268MethylationFDRMPPGRGGRPMPP
CCCCCCCCCCCCCCC		50.6054556665
271MethylationMPPGRGGRPMPPSRR
CCCCCCCCCCCCCCC		27.4554556697
276PhosphorylationGGRPMPPSRRDYDDM
CCCCCCCCCCCCCCC		33.79-
277MethylationGRPMPPSRRDYDDMS
CCCCCCCCCCCCCCC		41.0658854733
278MethylationRPMPPSRRDYDDMSP
CCCCCCCCCCCCCCC		51.7081449363
280PhosphorylationMPPSRRDYDDMSPRR
CCCCCCCCCCCCCCC		16.4223927012
284PhosphorylationRRDYDDMSPRRGPPP
CCCCCCCCCCCCCCC		23.4219664994
286MethylationDYDDMSPRRGPPPPP
CCCCCCCCCCCCCCC		49.2126494259
287MethylationYDDMSPRRGPPPPPP
CCCCCCCCCCCCCCC		66.41-
296DimethylationPPPPPPGRGGRGGSR
CCCCCCCCCCCCCCC		50.60-
296MethylationPPPPPPGRGGRGGSR
CCCCCCCCCCCCCCC		50.6020679687
299DimethylationPPPGRGGRGGSRARN
CCCCCCCCCCCCCCC		49.47-
299MethylationPPPGRGGRGGSRARN
CCCCCCCCCCCCCCC		49.4715782174
302PhosphorylationGRGGRGGSRARNLPL
CCCCCCCCCCCCCCC		26.1217581920
303DimethylationRGGRGGSRARNLPLP
CCCCCCCCCCCCCCC		40.62-
303MethylationRGGRGGSRARNLPLP
CCCCCCCCCCCCCCC		40.6220679699
305DimethylationGRGGSRARNLPLPPP
CCCCCCCCCCCCCCC		44.07-
305MethylationGRGGSRARNLPLPPP
CCCCCCCCCCCCCCC		44.0718600977
316MethylationLPPPPPPRGGDLMAY
CCCCCCCCCCCCCEE		68.4524129315
321SulfoxidationPPRGGDLMAYDRRGR
CCCCCCCCEECCCCC		3.7521406390
323NitrationRGGDLMAYDRRGRPG
CCCCCCEECCCCCCC		8.94-
323PhosphorylationRGGDLMAYDRRGRPG
CCCCCCEECCCCCCC		8.9421945579
325MethylationGDLMAYDRRGRPGDR
CCCCEECCCCCCCCC		30.2218959219
326MethylationDLMAYDRRGRPGDRY
CCCEECCCCCCCCCC		42.4480702175
328MethylationMAYDRRGRPGDRYDG
CEECCCCCCCCCCCC		30.1654556681
333PhosphorylationRGRPGDRYDGMVGFS
CCCCCCCCCCCCCCC		22.91-
347PhosphorylationSADETWDSAIDTWSP
CCCCCCCCCCHHCCH		20.7726074081
351PhosphorylationTWDSAIDTWSPSEWQ
CCCCCCHHCCHHHCE		23.0226074081
353PhosphorylationDSAIDTWSPSEWQMA
CCCCHHCCHHHCEEE		22.2026074081
355PhosphorylationAIDTWSPSEWQMAYE
CCHHCCHHHCEEECC		46.0526074081
361PhosphorylationPSEWQMAYEPQGGSG
HHHCEEECCCCCCCC		23.85-
369PhosphorylationEPQGGSGYDYSYAGG
CCCCCCCCCCCCCCC		17.2625884760
371PhosphorylationQGGSGYDYSYAGGRG
CCCCCCCCCCCCCCC		8.6325884760
372PhosphorylationGGSGYDYSYAGGRGS
CCCCCCCCCCCCCCC		12.9524144214
372 (in isoform 3)Ubiquitination-12.9521890473
373PhosphorylationGSGYDYSYAGGRGSY
CCCCCCCCCCCCCCC		11.7524144214
377MethylationDYSYAGGRGSYGDLG
CCCCCCCCCCCCCCC		29.9358857885
379PhosphorylationSYAGGRGSYGDLGGP
CCCCCCCCCCCCCCC		25.2829255136
380PhosphorylationYAGGRGSYGDLGGPI
CCCCCCCCCCCCCCE		19.9222167270
381 (in isoform 3)Ubiquitination-25.9321890473
389PhosphorylationDLGGPIITTQVTIPK
CCCCCEEEEEEECCH		16.3425867546
390PhosphorylationLGGPIITTQVTIPKD
CCCCEEEEEEECCHH		15.6120044836
393PhosphorylationPIITTQVTIPKDLAG
CEEEEEEECCHHHHC		23.0325867546
396AcetylationTTQVTIPKDLAGSII
EEEEECCHHHHCCCC		62.6226051181
396UbiquitinationTTQVTIPKDLAGSII
EEEEECCHHHHCCCC		62.6218655026
396 (in isoform 1)Ubiquitination-62.6221890473
396 (in isoform 2)Ubiquitination-62.6221890473
398 (in isoform 3)Ubiquitination-7.8921890473
401PhosphorylationIPKDLAGSIIGKGGQ
CCHHHHCCCCCCCCH		12.8623401153
405SumoylationLAGSIIGKGGQRIKQ
HHCCCCCCCCHHHEE		49.84-
4052-HydroxyisobutyrylationLAGSIIGKGGQRIKQ
HHCCCCCCCCHHHEE		49.84-
405AcetylationLAGSIIGKGGQRIKQ
HHCCCCCCCCHHHEE		49.8423236377
405SuccinylationLAGSIIGKGGQRIKQ
HHCCCCCCCCHHHEE		49.8423954790
405SumoylationLAGSIIGKGGQRIKQ
HHCCCCCCCCHHHEE		49.8428112733
405UbiquitinationLAGSIIGKGGQRIKQ
HHCCCCCCCCHHHEE		49.84-
405 (in isoform 1)Ubiquitination-49.8421890473
405 (in isoform 2)Ubiquitination-49.8421890473
405UbiquitinationLAGSIIGKGGQRIKQ
HHCCCCCCCCHHHEE		49.8421890473
417O-linked_GlycosylationIKQIRHESGASIKID
HEEEECCCCCCEEEC		33.2723576270
417PhosphorylationIKQIRHESGASIKID
HEEEECCCCCCEEEC		33.2723401153
420PhosphorylationIRHESGASIKIDEPL
EECCCCCCEEECCCC		28.1323401153
422SumoylationHESGASIKIDEPLEG
CCCCCCEEECCCCCC		41.43-
422AcetylationHESGASIKIDEPLEG
CCCCCCEEECCCCCC		41.4323954790
422MalonylationHESGASIKIDEPLEG
CCCCCCEEECCCCCC		41.4326320211
422SumoylationHESGASIKIDEPLEG
CCCCCCEEECCCCCC		41.4325114211
422UbiquitinationHESGASIKIDEPLEG
CCCCCCEEECCCCCC		41.43-
422 (in isoform 1)Ubiquitination-41.4321890473
422 (in isoform 2)Ubiquitination-41.4321890473
422UbiquitinationHESGASIKIDEPLEG
CCCCCCEEECCCCCC		41.4321890473
430PhosphorylationIDEPLEGSEDRIITI
ECCCCCCCCCEEEEE		27.2729255136
430 (in isoform 3)Phosphorylation-27.27-
433MethylationPLEGSEDRIITITGT
CCCCCCCEEEEEECC		20.39115479203
434 (in isoform 3)Phosphorylation-5.1528442448
436PhosphorylationGSEDRIITITGTQDQ
CCCCEEEEEECCHHH		15.3221712546
438PhosphorylationEDRIITITGTQDQIQ
CCEEEEEECCHHHHH		26.0630377224
440PhosphorylationRIITITGTQDQIQNA
EEEEEECCHHHHHHH		21.9628464451
449PhosphorylationDQIQNAQYLLQNSVK
HHHHHHHHHHHHHHH		13.6327273156
454PhosphorylationAQYLLQNSVKQYSGK
HHHHHHHHHHHHCCC		20.1021712546
454 (in isoform 2)Phosphorylation-20.10-
456UbiquitinationYLLQNSVKQYSGKFF
HHHHHHHHHHCCCCC		43.2518655026
456 (in isoform 1)Ubiquitination-43.2521890473
456 (in isoform 2)Ubiquitination-43.25-
458PhosphorylationLQNSVKQYSGKFF--
HHHHHHHHCCCCC--		17.4229214152
458 (in isoform 2)Phosphorylation-17.4228442448
459PhosphorylationQNSVKQYSGKFF---
HHHHHHHCCCCC---		32.7727134283
4612-HydroxyisobutyrylationSVKQYSGKFF-----
HHHHHCCCCC-----		37.34-
461AcetylationSVKQYSGKFF-----
HHHHHCCCCC-----		37.3425825284
461UbiquitinationSVKQYSGKFF-----
HHHHHCCCCC-----		37.34-
461 (in isoform 1)Ubiquitination-37.3421890473
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
72YPhosphorylationKinaseSRCP12931
PSP
216SPhosphorylationKinaseCDK1P06493
PSP
216SPhosphorylationKinaseCDK2P24941
PSP
216SPhosphorylationKinaseMAPK8P45983
GPS
216SPhosphorylationKinaseMAPK10P53779
GPS
225YPhosphorylationKinaseSRCP12931
PSP
230YPhosphorylationKinaseSRC64-PhosphoELM
230YPhosphorylationKinaseSRCP12931
PSP
234YPhosphorylationKinaseSRC64-PhosphoELM
234YPhosphorylationKinaseSRCP12931
PSP
236YPhosphorylationKinaseSRC64-PhosphoELM
236YPhosphorylationKinaseSRCP12931
PSP
284SPhosphorylationKinaseMAPK3P27361
GPS
284SPhosphorylationKinaseMAPK1P28482
GPS
284SPhosphorylationKinasePRKCDQ05655
GPS
284SPhosphorylationKinaseCDK2P24941
PSP
302SPhosphorylationKinasePRKCDQ05655
GPS
353SPhosphorylationKinaseMAPK10P53779
GPS
353SPhosphorylationKinaseMAPK8P45983
GPS
353SPhosphorylationKinaseMAPK3P27361
GPS
379SPhosphorylationKinaseAURAO14965
PSP
380YPhosphorylationKinaseSRCP12931
PSP
380YPhosphorylationKinaseSRC64-PhosphoELM
458YPhosphorylationKinaseSRCP12931
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
296RMethylation

-
299RMethylation

-
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBM41_HUMANRBM41physical
16189514
CNNM3_HUMANCNNM3physical
16189514
GRAP2_HUMANGRAP2physical
16189514
HNRPK_HUMANHNRNPKphysical
16189514
MATR3_HUMANMATR3physical
16189514
RBM42_HUMANRBM42physical
16189514
RBM7_HUMANRBM7physical
16189514
NPDC1_HUMANNPDC1physical
16189514
KHDR3_HUMANKHDRBS3physical
16189514
KHDR2_HUMANKHDRBS2physical
16189514
RBMX_HUMANRBMXphysical
16189514
QKI_HUMANQKIphysical
16189514
VINEX_HUMANSORBS3physical
16189514
UBC9_HUMANUBE2Iphysical
16189514
NCK2_HUMANNCK2physical
16189514
DIDO1_HUMANDIDO1physical
16189514
ANM1_HUMANPRMT1physical
12529443
DDX1_HUMANDDX1physical
12183465
PCBP2_HUMANPCBP2physical
10772858
PTBP1_HUMANPTBP1physical
10772858
HNRPK_HUMANHNRNPKphysical
10772858
HNRPL_HUMANHNRNPLphysical
10772858
CSK_HUMANCSKphysical
12052863
VAV_HUMANVAV1physical
8051112
CEBPB_HUMANCEBPBphysical
9553145
HMGB1_HUMANHMGB1physical
11748221
KHDR1_HUMANKHDRBS1physical
12370808
KHDR1_HUMANKHDRBS1genetic
12370808
PABP1_HUMANPABPC1physical
15303970
CBX4_HUMANCBX4physical
22825850
MDM2_HUMANMDM2physical
19249676
NCK2_HUMANNCK2physical
11557983
CBLB_HUMANCBLBphysical
9399639
HNRPL_HUMANHNRNPLphysical
22939629
SF3B3_HUMANSF3B3physical
22939629
ROA1_HUMANHNRNPA1physical
22939629
HNRPU_HUMANHNRNPUphysical
22939629
YBOX1_HUMANYBX1physical
22939629
PTBP1_HUMANPTBP1physical
22939629
SF3B1_HUMANSF3B1physical
22939629
HNRPR_HUMANHNRNPRphysical
22939629
ROA3_HUMANHNRNPA3physical
22939629
SRSF1_HUMANSRSF1physical
22939629
U5S1_HUMANEFTUD2physical
22939629
SMD1_HUMANSNRPD1physical
22939629
SF3A1_HUMANSF3A1physical
22939629
HNRPM_HUMANHNRNPMphysical
22939629
U2AF2_HUMANU2AF2physical
22939629
NH2L1_HUMANNHP2L1physical
22939629
RU17_HUMANSNRNP70physical
22939629
SRS11_HUMANSRSF11physical
22939629
ILF3_HUMANILF3physical
22939629
HNRPQ_HUMANSYNCRIPphysical
22939629
PABP1_HUMANPABPC1physical
22939629
ROA0_HUMANHNRNPA0physical
22939629
SRRM2_HUMANSRRM2physical
22939629
TADBP_HUMANTARDBPphysical
22939629
SPT5H_HUMANSUPT5Hphysical
22939629
RBP2_HUMANRANBP2physical
22939629
TF3C4_HUMANGTF3C4physical
22939629
TB182_HUMANTNKS1BP1physical
22939629
TPM4_HUMANTPM4physical
22939629
SART3_HUMANSART3physical
22939629
UBP14_HUMANUSP14physical
22939629
IDH3G_HUMANIDH3Gphysical
22939629
LYAG_HUMANGAAphysical
22939629
RAB7A_HUMANRAB7Aphysical
22939629
NXF1_HUMANNXF1physical
22939629
HSP74_HUMANHSPA4physical
22939629
RS7_HUMANRPS7physical
22939629
SPTN1_HUMANSPTAN1physical
22939629
RCC1_HUMANRCC1physical
22939629
KCC2A_HUMANCAMK2Aphysical
22939629
RM23_HUMANMRPL23physical
22939629
MDM2_HUMANMDM2physical
23092970
P53_HUMANTP53physical
23092970
PIAS3_HUMANPIAS3physical
23092970
SENP2_HUMANSENP2physical
23092970
PP1RA_HUMANPPP1R10physical
12574161
SNRPA_HUMANSNRPAphysical
22365833
U2AF2_HUMANU2AF2physical
22365833
CCAR1_HUMANCCAR1physical
22365833
RBM10_HUMANRBM10physical
22365833
SF01_HUMANSF1physical
22365833
ELAV1_HUMANELAVL1physical
22365833
SRRT_HUMANSRRTphysical
22365833
ROA0_HUMANHNRNPA0physical
22365833
RALY_HUMANRALYphysical
22365833
CTBL1_HUMANCTNNBL1physical
22365833
DDX17_HUMANDDX17physical
22365833
DDX5_HUMANDDX5physical
22365833
HNRPQ_HUMANSYNCRIPphysical
22365833
HNRPK_HUMANHNRNPKphysical
22365833
RBMX_HUMANRBMXphysical
22365833
DHX9_HUMANDHX9physical
22365833
CIRBP_HUMANCIRBPphysical
22365833
RBM4_HUMANRBM4physical
22365833
HNRPD_HUMANHNRNPDphysical
22365833
RBM42_HUMANRBM42physical
22365833
PABP1_HUMANPABPC1physical
22365833
KHDR3_HUMANKHDRBS3physical
22365833
KHDR1_HUMANKHDRBS1physical
22365833
RFOX2_HUMANRBFOX2physical
22365833
P63_HUMANTP63physical
20085233
SMAD3_HUMANSMAD3physical
21988832
KHDR1_HUMANKHDRBS1physical
21988832
PELI2_HUMANPELI2physical
21988832
APEX1_HUMANAPEX1physical
22863883
PNCB_HUMANNAPRTphysical
22863883
NUCL_HUMANNCLphysical
22863883
HNRPK_HUMANHNRNPKphysical
25416956
RBM3_HUMANRBM3physical
25416956
RBY1A_HUMANRBMY1A1physical
25416956
SNRPA_HUMANSNRPAphysical
25416956
SPG7_HUMANSPG7physical
25416956
TYK2_HUMANTYK2physical
25416956
U2AF1_HUMANU2AF1physical
25416956
QKI_HUMANQKIphysical
25416956
MATR3_HUMANMATR3physical
25416956
ABI2_HUMANABI2physical
25416956
VINEX_HUMANSORBS3physical
25416956
PRP31_HUMANPRPF31physical
25416956
RBMX_HUMANRBMXphysical
25416956
RASD1_HUMANRASD1physical
25416956
DALD3_HUMANDALRD3physical
25416956
PCDBE_HUMANPCDHB14physical
25416956
MARK4_HUMANMARK4physical
25416956
FXL18_HUMANFBXL18physical
25416956
CCD33_HUMANCCDC33physical
25416956
PRR3_HUMANPRR3physical
25416956
YTDC1_HUMANYTHDC1physical
25416956
HNRLL_HUMANHNRNPLLphysical
25416956
ZN792_HUMANZNF792physical
25416956
RBY1F_HUMANRBMY1Fphysical
25416956
ZC3H1_HUMANZFC3H1physical
25416956
RTP5_HUMANRTP5physical
25416956
CF226_HUMANC6orf226physical
25416956
CARM1_HUMANCARM1physical
26344197
NPL4_HUMANNPLOC4physical
26344197
PDIA3_HUMANPDIA3physical
26344197
SEPT2_HUMANSEPT2physical
26344197
TERA_HUMANVCPphysical
26344197
XRCC6_HUMANXRCC6physical
26344197
SNX33_HUMANSNX33physical
28514442
FBP1L_HUMANFNBP1Lphysical
28514442
CASP2_HUMANCASP2physical
28514442
KLH23_HUMANKLHL23physical
28514442
PLCG1_HUMANPLCG1physical
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 HNRPK_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-216 AND SER-284, AND MASS SPECTROMETRY.
Methylation
ReferencePubMed
"Identifying and quantifying in vivo methylation sites by heavy methylSILAC.";
Ong S.E., Mittler G., Mann M.;
Nat. Methods 1:119-126(2004).
Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-296 AND ARG-299, AND MASSSPECTROMETRY.
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-216 AND TYR-380, ANDMASS SPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-216 AND SER-284, 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-116; SER-216 ANDSER-284, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 AND SER-284, ANDMASS SPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-284, ANDMASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-216 ANDSER-379, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-284 ANDSER-379, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-216 AND SER-284,AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3; SER-116 AND SER-284,AND MASS SPECTROMETRY.
"PITK, a PP1 targeting subunit that modulates the phosphorylation ofthe transcriptional regulator hnRNP K.";
Kwiek N.C., Thacker D.F., Datto M.B., Megosh H.B., Haystead T.A.J.;
Cell. Signal. 18:1769-1778(2006).
Cited for: INTERACTION WITH ANKRD28, AND PHOSPHORYLATION AT SER-284.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Proteomic analysis of ubiquitinated proteins in normal hepatocytecell line Chang liver cells.";
Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E.,Wu J., Luo Y., Qiang B., Yuan J., Sun X., Peng X.;
Proteomics 8:2885-2896(2008).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-422, AND MASSSPECTROMETRY.

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