HNRPC_HUMAN - dbPTM
HNRPC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HNRPC_HUMAN
UniProt AC P07910
Protein Name Heterogeneous nuclear ribonucleoproteins C1/C2
Gene Name HNRNPC
Organism Homo sapiens (Human).
Sequence Length 306
Subcellular Localization Nucleus. Component of ribonucleosomes.
Protein Description Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. [PubMed: 8264621 Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules]
Protein Sequence MASNVTNKTDPRSMNSRVFIGNLNTLVVKKSDVEAIFSKYGKIVGCSVHKGFAFVQYVNERNARAAVAGEDGRMIAGQVLDINLAAEPKVNRGKAGVKRSAAEMYGSVTEHPSPSPLLSSSFDLDYDFQRDYYDRMYSYPARVPPPPPIARAVVPSKRQRVSGNTSRRGKSGFNSKSGQRGSSKSGKLKGDDLQAIKKELTQIKQKVDSLLENLEKIEKEQSKQAVEMKNDKSEEEQSSSSVKKDETNVKMESEGGADDSAEEGDLLDDDDNEDRGDDQLELIKDDEKEAEEGEDDRDSANGEDDS
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
2Acetylation------MASNVTNKT
------CCCCCCCCC		15.1522814378
3Phosphorylation-----MASNVTNKTD
-----CCCCCCCCCC		30.4523186163
6Phosphorylation--MASNVTNKTDPRS
--CCCCCCCCCCCCC		34.9420860994
8SumoylationMASNVTNKTDPRSMN
CCCCCCCCCCCCCCC		44.96-
8AcetylationMASNVTNKTDPRSMN
CCCCCCCCCCCCCCC		44.9623749302
8MalonylationMASNVTNKTDPRSMN
CCCCCCCCCCCCCCC		44.9626320211
8SumoylationMASNVTNKTDPRSMN
CCCCCCCCCCCCCCC		44.9628112733
8UbiquitinationMASNVTNKTDPRSMN
CCCCCCCCCCCCCCC		44.9623000965
8 (in isoform 2)Ubiquitination-44.96-
9PhosphorylationASNVTNKTDPRSMNS
CCCCCCCCCCCCCCC		53.9923882029
13PhosphorylationTNKTDPRSMNSRVFI
CCCCCCCCCCCEEEE		27.9224719451
25PhosphorylationVFIGNLNTLVVKKSD
EEEEECCEEEEEHHH		24.8930576142
292-HydroxyisobutyrylationNLNTLVVKKSDVEAI
ECCEEEEEHHHHHHH		38.80-
29MalonylationNLNTLVVKKSDVEAI
ECCEEEEEHHHHHHH		38.8026320211
29UbiquitinationNLNTLVVKKSDVEAI
ECCEEEEEHHHHHHH		38.8023000965
29 (in isoform 1)Ubiquitination-38.8021890473
29 (in isoform 2)Ubiquitination-38.8021890473
29 (in isoform 3)Ubiquitination-38.8021890473
29 (in isoform 4)Ubiquitination-38.8021890473
302-HydroxyisobutyrylationLNTLVVKKSDVEAIF
CCEEEEEHHHHHHHH		40.03-
30MalonylationLNTLVVKKSDVEAIF
CCEEEEEHHHHHHHH		40.0326320211
30UbiquitinationLNTLVVKKSDVEAIF
CCEEEEEHHHHHHHH		40.0323000965
31PhosphorylationNTLVVKKSDVEAIFS
CEEEEEHHHHHHHHH		40.9730266825
38PhosphorylationSDVEAIFSKYGKIVG
HHHHHHHHHCCCEEE		20.8921712546
39AcetylationDVEAIFSKYGKIVGC
HHHHHHHHCCCEEEE		47.4723749302
39MalonylationDVEAIFSKYGKIVGC
HHHHHHHHCCCEEEE		47.4726320211
39MethylationDVEAIFSKYGKIVGC
HHHHHHHHCCCEEEE		47.4788731
39SumoylationDVEAIFSKYGKIVGC
HHHHHHHHCCCEEEE		47.47-
39UbiquitinationDVEAIFSKYGKIVGC
HHHHHHHHCCCEEEE		47.4723000965
39 (in isoform 1)Ubiquitination-47.4721890473
39 (in isoform 2)Ubiquitination-47.4721890473
39 (in isoform 4)Ubiquitination-47.4721890473
42SumoylationAIFSKYGKIVGCSVH
HHHHHCCCEEEEEEE		31.00-
42AcetylationAIFSKYGKIVGCSVH
HHHHHCCCEEEEEEE		31.0025953088
42SumoylationAIFSKYGKIVGCSVH
HHHHHCCCEEEEEEE		31.00-
42UbiquitinationAIFSKYGKIVGCSVH
HHHHHCCCEEEEEEE		31.0023000965
42 (in isoform 1)Ubiquitination-31.0021890473
42 (in isoform 2)Ubiquitination-31.0021890473
42 (in isoform 4)Ubiquitination-31.0021890473
47PhosphorylationYGKIVGCSVHKGFAF
CCCEEEEEEECCEEE		22.7125159151
50SumoylationIVGCSVHKGFAFVQY
EEEEEEECCEEEEEE		54.27-
50AcetylationIVGCSVHKGFAFVQY
EEEEEEECCEEEEEE		54.2725825284
50MalonylationIVGCSVHKGFAFVQY
EEEEEEECCEEEEEE		54.2726320211
50SumoylationIVGCSVHKGFAFVQY
EEEEEEECCEEEEEE		54.2728112733
50UbiquitinationIVGCSVHKGFAFVQY
EEEEEEECCEEEEEE		54.2722817900
50 (in isoform 1)Ubiquitination-54.2721890473
50 (in isoform 2)Ubiquitination-54.2721890473
50 (in isoform 4)Ubiquitination-54.2721890473
57PhosphorylationKGFAFVQYVNERNAR
CCEEEEEEECCCCCC		10.4328152594
61MethylationFVQYVNERNARAAVA
EEEEECCCCCCHHHC		36.58115479003
74SulfoxidationVAGEDGRMIAGQVLD
HCCCCCCEECCEEEE		2.7721406390
89SumoylationINLAAEPKVNRGKAG
EEECCCCCCCCCCCC		43.58-
892-HydroxyisobutyrylationINLAAEPKVNRGKAG
EEECCCCCCCCCCCC		43.58-
89AcetylationINLAAEPKVNRGKAG
EEECCCCCCCCCCCC		43.5826051181
89SumoylationINLAAEPKVNRGKAG
EEECCCCCCCCCCCC		43.5828112733
89UbiquitinationINLAAEPKVNRGKAG
EEECCCCCCCCCCCC		43.5823000965
89 (in isoform 1)Ubiquitination-43.5821890473
89 (in isoform 2)Ubiquitination-43.5821890473
89 (in isoform 4)Ubiquitination-43.5821890473
94SumoylationEPKVNRGKAGVKRSA
CCCCCCCCCCCCCHH		38.4425772364
94UbiquitinationEPKVNRGKAGVKRSA
CCCCCCCCCCCCCHH		38.4423000965
96 (in isoform 3)Ubiquitination-29.0321890473
98MethylationNRGKAGVKRSAAEMY
CCCCCCCCCHHHHHH		39.45116252037
100PhosphorylationGKAGVKRSAAEMYGS
CCCCCCCHHHHHHCC		26.5528122231
100 (in isoform 2)Phosphorylation-26.5519690332
100 (in isoform 4)Phosphorylation-26.5519690332
105PhosphorylationKRSAAEMYGSVTEHP
CCHHHHHHCCCCCCC		9.5828122231
105 (in isoform 2)Phosphorylation-9.5830631047
105 (in isoform 4)Phosphorylation-9.5830631047
107PhosphorylationSAAEMYGSVTEHPSP
HHHHHHCCCCCCCCC		14.3725159151
107 (in isoform 2)Phosphorylation-14.3725159151
107 (in isoform 4)Phosphorylation-14.3725159151
108 (in isoform 2)Phosphorylation-6.7225159151
108 (in isoform 4)Phosphorylation-6.7225159151
109PhosphorylationAEMYGSVTEHPSPSP
HHHHCCCCCCCCCCC		30.2125159151
109 (in isoform 3)Ubiquitination-30.2121890473
113PhosphorylationGSVTEHPSPSPLLSS
CCCCCCCCCCCCCCC		39.6625159151
113 (in isoform 2)Phosphorylation-39.6623663014
113 (in isoform 4)Phosphorylation-39.6623663014
115PhosphorylationVTEHPSPSPLLSSSF
CCCCCCCCCCCCCCC		32.3025159151
118 (in isoform 3)Ubiquitination-5.4621890473
119PhosphorylationPSPSPLLSSSFDLDY
CCCCCCCCCCCCCCC		31.4525159151
120PhosphorylationSPSPLLSSSFDLDYD
CCCCCCCCCCCCCCC		34.6925159151
121PhosphorylationPSPLLSSSFDLDYDF
CCCCCCCCCCCCCCC		21.2825159151
124 (in isoform 3)Ubiquitination-6.5621890473
125 (in isoform 2)Phosphorylation-42.6827251275
125 (in isoform 4)Phosphorylation-42.6827251275
126PhosphorylationSSSFDLDYDFQRDYY
CCCCCCCCCCCHHHH		26.4228122231
126 (in isoform 3)Ubiquitination-26.4221890473
132PhosphorylationDYDFQRDYYDRMYSY
CCCCCHHHHHHHHCC		14.9521945579
133PhosphorylationYDFQRDYYDRMYSYP
CCCCHHHHHHHHCCC		11.0221945579
135MethylationFQRDYYDRMYSYPAR
CCHHHHHHHHCCCCC		15.15115478995
136 (in isoform 3)Ubiquitination-2.0821890473
137PhosphorylationRDYYDRMYSYPARVP
HHHHHHHHCCCCCCC		13.1221945579
138PhosphorylationDYYDRMYSYPARVPP
HHHHHHHCCCCCCCC		18.4621945579
139NitrationYYDRMYSYPARVPPP
HHHHHHCCCCCCCCC		5.39-
139PhosphorylationYYDRMYSYPARVPPP
HHHHHHCCCCCCCCC		5.3921945579
142MethylationRMYSYPARVPPPPPI
HHHCCCCCCCCCCCC		36.6597778405
143 (in isoform 3)Ubiquitination-10.1621890473
144UbiquitinationYSYPARVPPPPPIAR
HCCCCCCCCCCCCCE		30.0833845483
148 (in isoform 4)Ubiquitination-38.3521890473
149 (in isoform 3)Ubiquitination-5.1021890473
150 (in isoform 4)Ubiquitination-10.1121890473
151MethylationPPPPPIARAVVPSKR
CCCCCCCEEECCCCC		28.7454556581
152 (in isoform 3)Ubiquitination-9.5321890473
156PhosphorylationIARAVVPSKRQRVSG
CCEEECCCCCCCCCC		28.9430266825
157AcetylationARAVVPSKRQRVSGN
CEEECCCCCCCCCCC		46.6223749302
157UbiquitinationARAVVPSKRQRVSGN
CEEECCCCCCCCCCC		46.6227667366
160MethylationVVPSKRQRVSGNTSR
ECCCCCCCCCCCCCC		28.7154556589
160 (in isoform 4)Ubiquitination-28.7121890473
162PhosphorylationPSKRQRVSGNTSRRG
CCCCCCCCCCCCCCC		28.6328176443
163UbiquitinationSKRQRVSGNTSRRGK
CCCCCCCCCCCCCCC		38.2827667366
163 (in isoform 2)Ubiquitination-38.2821890473
163 (in isoform 3)Ubiquitination-38.2821890473
164 (in isoform 3)Ubiquitination-27.6321890473
165PhosphorylationRQRVSGNTSRRGKSG
CCCCCCCCCCCCCCC		27.4320363803
166PhosphorylationQRVSGNTSRRGKSGF
CCCCCCCCCCCCCCC		24.7929691806
167 (in isoform 4)Ubiquitination-49.7021890473
1702-HydroxyisobutyrylationGNTSRRGKSGFNSKS
CCCCCCCCCCCCCCC		45.66-
170AcetylationGNTSRRGKSGFNSKS
CCCCCCCCCCCCCCC		45.6625953088
170UbiquitinationGNTSRRGKSGFNSKS
CCCCCCCCCCCCCCC		45.6624816145
171PhosphorylationNTSRRGKSGFNSKSG
CCCCCCCCCCCCCCC		51.9828985074
171UbiquitinationNTSRRGKSGFNSKSG
CCCCCCCCCCCCCCC		51.9823000965
173 (in isoform 4)Ubiquitination-13.9021890473
174UbiquitinationRRGKSGFNSKSGQRG
CCCCCCCCCCCCCCC		52.6423000965
175PhosphorylationRGKSGFNSKSGQRGS
CCCCCCCCCCCCCCC		26.4120068231
176SumoylationGKSGFNSKSGQRGSS
CCCCCCCCCCCCCCC		60.76-
1762-HydroxyisobutyrylationGKSGFNSKSGQRGSS
CCCCCCCCCCCCCCC		60.76-
176AcetylationGKSGFNSKSGQRGSS
CCCCCCCCCCCCCCC		60.7625953088
176SuccinylationGKSGFNSKSGQRGSS
CCCCCCCCCCCCCCC		60.7623954790
176SumoylationGKSGFNSKSGQRGSS
CCCCCCCCCCCCCCC		60.7628112733
176UbiquitinationGKSGFNSKSGQRGSS
CCCCCCCCCCCCCCC		60.7623000965
176 (in isoform 1)Ubiquitination-60.7621890473
176 (in isoform 2)Ubiquitination-60.7621890473
176 (in isoform 4)Ubiquitination-60.7621890473
177PhosphorylationKSGFNSKSGQRGSSK
CCCCCCCCCCCCCCC		39.7226434776
182PhosphorylationSKSGQRGSSKSGKLK
CCCCCCCCCCCCCCC		36.4620068231
183PhosphorylationKSGQRGSSKSGKLKG
CCCCCCCCCCCCCCH		33.3920068231
184UbiquitinationSGQRGSSKSGKLKGD
CCCCCCCCCCCCCHH		65.9923000965
185PhosphorylationGQRGSSKSGKLKGDD
CCCCCCCCCCCCHHH		43.0126546556
185UbiquitinationGQRGSSKSGKLKGDD
CCCCCCCCCCCCHHH		43.0123000965
185 (in isoform 2)Ubiquitination-43.0121890473
187AcetylationRGSSKSGKLKGDDLQ
CCCCCCCCCCHHHHH		54.861206970525
187UbiquitinationRGSSKSGKLKGDDLQ
CCCCCCCCCCHHHHH		54.8623000965
187 (in isoform 4)Ubiquitination-54.8621890473
188 (in isoform 4)Ubiquitination-9.5221890473
1892-HydroxyisobutyrylationSSKSGKLKGDDLQAI
CCCCCCCCHHHHHHH		64.87-
189MalonylationSSKSGKLKGDDLQAI
CCCCCCCCHHHHHHH		64.8726320211
189MethylationSSKSGKLKGDDLQAI
CCCCCCCCHHHHHHH		64.8742352717
189SumoylationSSKSGKLKGDDLQAI
CCCCCCCCHHHHHHH		64.87-
189UbiquitinationSSKSGKLKGDDLQAI
CCCCCCCCHHHHHHH		64.8723000965
189 (in isoform 1)Ubiquitination-64.8721890473
191UbiquitinationKSGKLKGDDLQAIKK
CCCCCCHHHHHHHHH		52.4323000965
191 (in isoform 2)Ubiquitination-52.4321890473
193UbiquitinationGKLKGDDLQAIKKEL
CCCCHHHHHHHHHHH		4.3923000965
193 (in isoform 2)Ubiquitination-4.3921890473
1972-HydroxyisobutyrylationGDDLQAIKKELTQIK
HHHHHHHHHHHHHHH		43.12-
197AcetylationGDDLQAIKKELTQIK
HHHHHHHHHHHHHHH		43.1225953088
197SuccinylationGDDLQAIKKELTQIK
HHHHHHHHHHHHHHH		43.1223954790
197UbiquitinationGDDLQAIKKELTQIK
HHHHHHHHHHHHHHH		43.1223000965
1982-HydroxyisobutyrylationDDLQAIKKELTQIKQ
HHHHHHHHHHHHHHH		52.41-
198AcetylationDDLQAIKKELTQIKQ
HHHHHHHHHHHHHHH		52.4126051181
198MalonylationDDLQAIKKELTQIKQ
HHHHHHHHHHHHHHH		52.4126320211
198UbiquitinationDDLQAIKKELTQIKQ
HHHHHHHHHHHHHHH		52.4123000965
198 (in isoform 1)Ubiquitination-52.4121890473
203AcetylationIKKELTQIKQKVDSL
HHHHHHHHHHHHHHH		4.2619608861
203UbiquitinationIKKELTQIKQKVDSL
HHHHHHHHHHHHHHH		4.2633845483
203 (in isoform 2)Ubiquitination-4.2621890473
204SuccinylationKKELTQIKQKVDSLL
HHHHHHHHHHHHHHH		33.9623954790
204UbiquitinationKKELTQIKQKVDSLL
HHHHHHHHHHHHHHH		33.9623000965
204 (in isoform 1)Ubiquitination-33.9621890473
204 (in isoform 3)Ubiquitination-33.9621890473
2062-HydroxyisobutyrylationELTQIKQKVDSLLEN
HHHHHHHHHHHHHHH		42.90-
206MalonylationELTQIKQKVDSLLEN
HHHHHHHHHHHHHHH		42.9026320211
206UbiquitinationELTQIKQKVDSLLEN
HHHHHHHHHHHHHHH		42.9023000965
206 (in isoform 1)Ubiquitination-42.9021890473
209PhosphorylationQIKQKVDSLLENLEK
HHHHHHHHHHHHHHH		37.5330266825
210UbiquitinationIKQKVDSLLENLEKI
HHHHHHHHHHHHHHH		6.3527667366
210 (in isoform 2)Ubiquitination-6.3521890473
2162-HydroxyisobutyrylationSLLENLEKIEKEQSK
HHHHHHHHHHHHHHH		60.37-
216AcetylationSLLENLEKIEKEQSK
HHHHHHHHHHHHHHH		60.3722641111
216UbiquitinationSLLENLEKIEKEQSK
HHHHHHHHHHHHHHH		60.3727667366
216 (in isoform 1)Ubiquitination-60.3721890473
216 (in isoform 2)Ubiquitination-60.3721890473
219AcetylationENLEKIEKEQSKQAV
HHHHHHHHHHHHHHH		65.6125953088
219UbiquitinationENLEKIEKEQSKQAV
HHHHHHHHHHHHHHH		65.6133845483
219 (in isoform 2)Ubiquitination-65.6121890473
220PhosphorylationNLEKIEKEQSKQAVE
HHHHHHHHHHHHHHH		47.5032645325
222PhosphorylationEKIEKEQSKQAVEMK
HHHHHHHHHHHHHHH		28.0330108239
223SumoylationKIEKEQSKQAVEMKN
HHHHHHHHHHHHHHC		41.81-
2232-HydroxyisobutyrylationKIEKEQSKQAVEMKN
HHHHHHHHHHHHHHC		41.81-
223AcetylationKIEKEQSKQAVEMKN
HHHHHHHHHHHHHHC		41.8125953088
223SuccinylationKIEKEQSKQAVEMKN
HHHHHHHHHHHHHHC		41.8123954790
223SumoylationKIEKEQSKQAVEMKN
HHHHHHHHHHHHHHC		41.8128112733
223UbiquitinationKIEKEQSKQAVEMKN
HHHHHHHHHHHHHHC		41.8127667366
223 (in isoform 1)Ubiquitination-41.8121890473
225PhosphorylationEKEQSKQAVEMKNDK
HHHHHHHHHHHHCCC		11.7233259812
227 (in isoform 2)Phosphorylation-47.6718669648
228 (in isoform 4)Ubiquitination-3.8521890473
229SumoylationSKQAVEMKNDKSEEE
HHHHHHHHCCCCHHH		48.79-
229AcetylationSKQAVEMKNDKSEEE
HHHHHHHHCCCCHHH		48.7925953088
229SumoylationSKQAVEMKNDKSEEE
HHHHHHHHCCCCHHH		48.7928112733
229UbiquitinationSKQAVEMKNDKSEEE
HHHHHHHHCCCCHHH		48.7921906983
229 (in isoform 1)Ubiquitination-48.7921890473
230UbiquitinationKQAVEMKNDKSEEEQ
HHHHHHHCCCCHHHH		61.7121963094
230 (in isoform 2)Ubiquitination-61.7121890473
231UbiquitinationQAVEMKNDKSEEEQS
HHHHHHCCCCHHHHH		50.7921963094
231 (in isoform 2)Ubiquitination-50.7921890473
232SumoylationAVEMKNDKSEEEQSS
HHHHHCCCCHHHHHH		69.98-
232AcetylationAVEMKNDKSEEEQSS
HHHHHCCCCHHHHHH		69.9823749302
232SumoylationAVEMKNDKSEEEQSS
HHHHHCCCCHHHHHH		69.9825114211
232UbiquitinationAVEMKNDKSEEEQSS
HHHHHCCCCHHHHHH		69.9821906983
232 (in isoform 1)Ubiquitination-69.9821890473
233PhosphorylationVEMKNDKSEEEQSSS
HHHHCCCCHHHHHHC		53.7729255136
238PhosphorylationDKSEEEQSSSSVKKD
CCCHHHHHHCCCCCC		35.1529255136
239PhosphorylationKSEEEQSSSSVKKDE
CCHHHHHHCCCCCCC		26.7329255136
240PhosphorylationSEEEQSSSSVKKDET
CHHHHHHCCCCCCCC		44.3829255136
241PhosphorylationEEEQSSSSVKKDETN
HHHHHHCCCCCCCCC		39.6529255136
243SumoylationEQSSSSVKKDETNVK
HHHHCCCCCCCCCCE		57.35-
243AcetylationEQSSSSVKKDETNVK
HHHHCCCCCCCCCCE		57.3521339330
243SumoylationEQSSSSVKKDETNVK
HHHHCCCCCCCCCCE		57.3528112733
243UbiquitinationEQSSSSVKKDETNVK
HHHHCCCCCCCCCCE		57.3521906983
243 (in isoform 1)Ubiquitination-57.3521890473
244AcetylationQSSSSVKKDETNVKM
HHHCCCCCCCCCCEE		59.6521339330
244SumoylationQSSSSVKKDETNVKM
HHHCCCCCCCCCCEE		59.6525772364
244UbiquitinationQSSSSVKKDETNVKM
HHHCCCCCCCCCCEE		59.6521963094
244 (in isoform 1)Ubiquitination-59.6521890473
247PhosphorylationSSVKKDETNVKMESE
CCCCCCCCCCEEECC		56.2821955146
250SumoylationKKDETNVKMESEGGA
CCCCCCCEEECCCCC		38.73-
250SumoylationKKDETNVKMESEGGA
CCCCCCCEEECCCCC		38.7328112733
250UbiquitinationKKDETNVKMESEGGA
CCCCCCCEEECCCCC		38.73-
253PhosphorylationETNVKMESEGGADDS
CCCCEEECCCCCCCC		37.7322167270
260PhosphorylationSEGGADDSAEEGDLL
CCCCCCCCCCCCCCC		37.8222167270
271UbiquitinationGDLLDDDDNEDRGDD
CCCCCCCCCCCCCHH		68.3732015554
271 (in isoform 2)Ubiquitination-68.3721890473
284UbiquitinationDDQLELIKDDEKEAE
HHHHHEEECCHHHHH		72.2832015554
284 (in isoform 1)Ubiquitination-72.2821890473
286PhosphorylationQLELIKDDEKEAEEG
HHHEEECCHHHHHCC		64.9632142685
299PhosphorylationEGEDDRDSANGEDDS
CCCCCHHHCCCCCCC		25.2422167270
306PhosphorylationSANGEDDS-------
HCCCCCCC-------		55.2130266825
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
253SPhosphorylationKinaseCSNK1A1P48729
GPS
260SPhosphorylationKinaseCSNK2A1P68400
GPS
260SPhosphorylationKinaseCSNK1A1P48729
GPS
260SPhosphorylationKinaseCK2-FAMILY-GPS
260SPhosphorylationKinaseCK2_GROUP-PhosphoELM
299SPhosphorylationKinaseCSNK1A1P48729
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
253SPhosphorylation

12564933
260SPhosphorylation

12564933
299SPhosphorylation

12564933
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 HNRPC_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IMA4_HUMANKPNA3physical
16189514
RBM41_HUMANRBM41physical
16189514
CC85B_HUMANCCDC85Bphysical
16189514
RASK_HUMANKRASphysical
16189514
HNRPC_HUMANHNRNPCphysical
16189514
RALYL_HUMANRALYLphysical
16189514
ZN581_HUMANZNF581physical
16189514
FXR2_HUMANFXR2physical
16189514
KPBB_HUMANPHKBphysical
16189514
PIN1_HUMANPIN1physical
16189514
AP1M1_HUMANAP1M1physical
16189514
UBC9_HUMANUBE2Iphysical
16189514
LMO3_HUMANLMO3physical
16189514
HNRPC_HUMANHNRNPCphysical
10772858
SMCA4_HUMANSMARCA4physical
16217013
CHD4_HUMANCHD4physical
16217013
SMRC1_HUMANSMARCC1physical
16217013
DHX9_HUMANDHX9physical
11687588
BRNP1_HUMANBRINP1physical
22446626
XRCC5_HUMANXRCC5physical
14704337
DHX9_HUMANDHX9physical
14704337
ROA1_HUMANHNRNPA1physical
14704337
HNRPR_HUMANHNRNPRphysical
22939629
U5S1_HUMANEFTUD2physical
22939629
U520_HUMANSNRNP200physical
22939629
TOP1_HUMANTOP1physical
22939629
PUF60_HUMANPUF60physical
22939629
RBMX_HUMANRBMXphysical
22939629
SF3A1_HUMANSF3A1physical
22939629
HNRPM_HUMANHNRNPMphysical
22939629
NH2L1_HUMANNHP2L1physical
22939629
RNPS1_HUMANRNPS1physical
22939629
U2AF2_HUMANU2AF2physical
22939629
SFPQ_HUMANSFPQphysical
22939629
SNUT1_HUMANSART1physical
22939629
RALY_HUMANRALYphysical
22939629
SAP18_HUMANSAP18physical
22939629
SNUT2_HUMANUSP39physical
22939629
SMU1_HUMANSMU1physical
22939629
KHDR1_HUMANKHDRBS1physical
22939629
WDR18_HUMANWDR18physical
22939629
MBB1A_HUMANMYBBP1Aphysical
22939629
TRI55_HUMANTRIM55physical
22939629
SEPT7_HUMANSEPT7physical
22939629
RRP7A_HUMANRRP7Aphysical
22939629
TPBG_HUMANTPBGphysical
22939629
RRS1_HUMANRRS1physical
22939629
TRA2A_HUMANTRA2Aphysical
22939629
ILVBL_HUMANILVBLphysical
22939629
UT14A_HUMANUTP14Aphysical
22939629
VAPB_HUMANVAPBphysical
22939629
K1C14_HUMANKRT14physical
22939629
RT09_HUMANMRPS9physical
22939629
ZCH18_HUMANZC3H18physical
22939629
SSRG_HUMANSSR3physical
22939629
RM40_HUMANMRPL40physical
22939629
RM42_HUMANMRPL42physical
22939629
LMBD1_HUMANLMBRD1physical
22939629
NXF1_HUMANNXF1physical
18337511
ILF3_HUMANILF3physical
18337511
SF3B2_HUMANSF3B2physical
22365833
HNRPC_HUMANHNRNPCphysical
22365833
RALY_HUMANRALYphysical
22365833
HNRPD_HUMANHNRNPDphysical
22365833
PTBP2_HUMANPTBP2physical
22365833
CELF1_HUMANCELF1physical
22365833
IL7RA_HUMANIL7Rphysical
23151878
KHDR3_HUMANKHDRBS3physical
19447967
RALYL_HUMANRALYLphysical
19447967
IMA4_HUMANKPNA3physical
19447967
IMA1_HUMANKPNA2physical
21988832
SMRD1_HUMANSMARCD1physical
21988832
BRCA1_HUMANBRCA1physical
23585894
BRCA2_HUMANBRCA2physical
23585894
PALB2_HUMANPALB2physical
23585894
RAD51_HUMANRAD51physical
23585894
BARD1_HUMANBARD1physical
23585894
FANCJ_HUMANBRIP1physical
23585894
HNRPC_HUMANHNRNPCphysical
25416956
IMA1_HUMANKPNA2physical
25416956
IMA4_HUMANKPNA3physical
25416956
IMA3_HUMANKPNA4physical
25416956
RBTN2_HUMANLMO2physical
25416956
SDCB1_HUMANSDCBPphysical
25416956
UBC9_HUMANUBE2Iphysical
25416956
SUMO1_HUMANSUMO1physical
25416956
ZFY26_HUMANZFYVE26physical
25416956
RBM41_HUMANRBM41physical
25416956
RALYL_HUMANRALYLphysical
25416956
GNL1_HUMANGNL1physical
26344197
MED1_HUMANMED1physical
26344197
RALY_HUMANRALYphysical
26344197
RBP2_HUMANRANBP2physical
26344197
HNRPC_HUMANHNRNPCphysical
21516116
RBM41_HUMANRBM41physical
21516116
TRAF3_HUMANTRAF3physical
28031331
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 HNRPC_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-39; LYS-170 AND LYS-216, ANDMASS 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-107; THR-109; SER-113;SER-115; SER-138; SER-233 AND SER-260, AND MASS 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260, AND MASSSPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; SER-253; SER-260;SER-299 AND SER-306, 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-113; SER-120; SER-121;SER-233; SER-241; SER-253 AND SER-260, 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-253 AND SER-260, 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-299, 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-138; SER-233; SER-238;SER-239; SER-240; SER-241; SER-253 AND SER-260, AND MASS SPECTROMETRY.
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260, AND MASSSPECTROMETRY.
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline.";
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
Electrophoresis 28:2027-2034(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the human pituitary.";
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
Pituitary 9:109-120(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND MASSSPECTROMETRY.
"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-162; SER-233; SER-253;SER-260 AND SER-299, 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 SER-260 AND SER-299, ANDMASS SPECTROMETRY.
"Basal and hydrogen peroxide stimulated sites of phosphorylation inheterogeneous nuclear ribonucleoprotein C1/C2.";
Stone J.R., Maki J.L., Collins T.;
Biochemistry 42:1301-1308(2003).
Cited for: PHOSPHORYLATION AT SER-253; SER-260 AND SER-299, AND MASSSPECTROMETRY.
Sumoylation
ReferencePubMed
"SUMO modification of heterogeneous nuclear ribonucleoproteins.";
Vassileva M.T., Matunis M.J.;
Mol. Cell. Biol. 24:3623-3632(2004).
Cited for: MUTAGENESIS OF LYS-197 AND LYS-250, AND SUMOYLATION AT LYS-250.

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