HNRPC_MOUSE - dbPTM
HNRPC_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HNRPC_MOUSE
UniProt AC Q9Z204
Protein Name Heterogeneous nuclear ribonucleoproteins C1/C2
Gene Name Hnrnpc
Organism Mus musculus (Mouse).
Sequence Length 313
Subcellular Localization Nucleus . Component of ribonucleosomes.
Protein Description Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. 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. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. N6-methyladenosine (m6A) has been shown to alter the local structure in mRNAs and long non-coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch', facilitating binding of HNRNPC, leading to regulation of mRNA splicing..
Protein Sequence MASNVTNKTDPRSMNSRVFIGNLNTLVVKKSDVEAIFSKYGKIVGCSVHKGFAFVQYVNERNARAAVAGEDGRMIAGQVLDINLAAEPKVNRGKAGVKRSAAEMYGSVPEHPSPSPLLSSSFDLDYDFQRDYYDRMYSYPARVPPPPPIARAVVPSKRQRVSGNTSRRGKSGFNSKSGQRGSSSKSGKLKGDDLQAIKKELTQIKQKVDSLLESLEKIEKEQSKQADLSFSSPVEMKNEKSEEEQSSASVKKDETNVKMESEAGADDSAEEGDLLDDDDNEDRGDDQLELKDDEKEPEEGEDDRDSANGEDDS
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		15.15-
3Phosphorylation-----MASNVTNKTD
-----CCCCCCCCCC		30.4529514104
8AcetylationMASNVTNKTDPRSMN
CCCCCCCCCCCCCCC		44.9623806337
8MalonylationMASNVTNKTDPRSMN
CCCCCCCCCCCCCCC		44.9626320211
8SuccinylationMASNVTNKTDPRSMN
CCCCCCCCCCCCCCC		44.9623806337
29UbiquitinationNLNTLVVKKSDVEAI
ECCEEEEEHHHHHHH		38.8022790023
29 (in isoform 2)Ubiquitination-38.8022790023
31PhosphorylationNTLVVKKSDVEAIFS
CEEEEEHHHHHHHHH		40.9727600695
39AcetylationDVEAIFSKYGKIVGC
HHHHHHHHCCCEEEE		47.4722826441
39UbiquitinationDVEAIFSKYGKIVGC
HHHHHHHHCCCEEEE		47.4722790023
39 (in isoform 2)Ubiquitination-47.4722790023
42MalonylationAIFSKYGKIVGCSVH
HHHHHCCCEEEEEEE		31.0032601280
89UbiquitinationINLAAEPKVNRGKAG
EEECCCCCCCCCCCC		43.5822790023
89 (in isoform 2)Ubiquitination-43.5822790023
100PhosphorylationGKAGVKRSAAEMYGS
CCCCCCHHHHHHHCC		26.5530635358
100 (in isoform 2)Phosphorylation-26.5521149613
100 (in isoform 3)Phosphorylation-26.5521149613
100 (in isoform 4)Phosphorylation-26.5521149613
105PhosphorylationKRSAAEMYGSVPEHP
CHHHHHHHCCCCCCC		9.5826239621
105 (in isoform 2)Phosphorylation-9.5830635358
105 (in isoform 3)Phosphorylation-9.5830635358
105 (in isoform 4)Phosphorylation-9.5830635358
107PhosphorylationSAAEMYGSVPEHPSP
HHHHHHCCCCCCCCC		19.6023984901
107 (in isoform 2)Phosphorylation-19.6021149613
107 (in isoform 3)Phosphorylation-19.6021149613
107 (in isoform 4)Phosphorylation-19.6021149613
108 (in isoform 2)Phosphorylation-5.8321149613
108 (in isoform 3)Phosphorylation-5.8321149613
108 (in isoform 4)Phosphorylation-5.8321149613
113PhosphorylationGSVPEHPSPSPLLSS
CCCCCCCCCCCCCCC		39.6626239621
113 (in isoform 2)Phosphorylation-39.6626643407
113 (in isoform 3)Phosphorylation-39.6626643407
113 (in isoform 4)Phosphorylation-39.6626643407
115PhosphorylationVPEHPSPSPLLSSSF
CCCCCCCCCCCCCCC		32.3026239621
119PhosphorylationPSPSPLLSSSFDLDY
CCCCCCCCCCCCCCC		31.4521149613
120PhosphorylationSPSPLLSSSFDLDYD
CCCCCCCCCCCCCCC		34.6921149613
121PhosphorylationPSPLLSSSFDLDYDF
CCCCCCCCCCCCCCC		21.2821149613
126PhosphorylationSSSFDLDYDFQRDYY
CCCCCCCCCCCHHHH		26.4223984901
132PhosphorylationDYDFQRDYYDRMYSY
CCCCCHHHHHHHHCC		14.9527149854
133PhosphorylationYDFQRDYYDRMYSYP
CCCCHHHHHHHHCCC		11.0227149854
137PhosphorylationRDYYDRMYSYPARVP
HHHHHHHHCCCCCCC		13.1225159016
138PhosphorylationDYYDRMYSYPARVPP
HHHHHHHCCCCCCCC		18.4625159016
139PhosphorylationYYDRMYSYPARVPPP
HHHHHHCCCCCCCCC		5.3929514104
144UbiquitinationYSYPARVPPPPPIAR
HCCCCCCCCCCCCCE		30.0827667366
156PhosphorylationIARAVVPSKRQRVSG
CCEEECCCCCCCCCC		28.94-
157MalonylationARAVVPSKRQRVSGN
CEEECCCCCCCCCCC		46.6226320211
157UbiquitinationARAVVPSKRQRVSGN
CEEECCCCCCCCCCC		46.6227667366
162PhosphorylationPSKRQRVSGNTSRRG
CCCCCCCCCCCCCCC		28.6328066266
163UbiquitinationSKRQRVSGNTSRRGK
CCCCCCCCCCCCCCC		38.2827667366
165PhosphorylationRQRVSGNTSRRGKSG
CCCCCCCCCCCCCCC		27.4328066266
166PhosphorylationQRVSGNTSRRGKSGF
CCCCCCCCCCCCCCC		24.7928066266
170AcetylationGNTSRRGKSGFNSKS
CCCCCCCCCCCCCCC		45.6623806337
171PhosphorylationNTSRRGKSGFNSKSG
CCCCCCCCCCCCCCC		51.9826824392
175PhosphorylationRGKSGFNSKSGQRGS
CCCCCCCCCCCCCCC		26.4127149854
176AcetylationGKSGFNSKSGQRGSS
CCCCCCCCCCCCCCC		60.7623806337
176MalonylationGKSGFNSKSGQRGSS
CCCCCCCCCCCCCCC		60.7626320211
176SuccinylationGKSGFNSKSGQRGSS
CCCCCCCCCCCCCCC		60.7623806337
176UbiquitinationGKSGFNSKSGQRGSS
CCCCCCCCCCCCCCC		60.7627667366
177UbiquitinationKSGFNSKSGQRGSSS
CCCCCCCCCCCCCCC		39.7227667366
177 (in isoform 2)Ubiquitination-39.72-
185UbiquitinationGQRGSSSKSGKLKGD
CCCCCCCCCCCCCHH		66.2427667366
186 (in isoform 2)Ubiquitination-43.01-
190UbiquitinationSSKSGKLKGDDLQAI
CCCCCCCCHHHHHHH		64.8722790023
190 (in isoform 2)Ubiquitination-64.8722790023
192UbiquitinationKSGKLKGDDLQAIKK
CCCCCCHHHHHHHHH		52.4327667366
194 (in isoform 2)Ubiquitination-4.39-
198AcetylationGDDLQAIKKELTQIK
HHHHHHHHHHHHHHH		43.1222902405
198UbiquitinationGDDLQAIKKELTQIK
HHHHHHHHHHHHHHH		43.1227667366
199MalonylationDDLQAIKKELTQIKQ
HHHHHHHHHHHHHHH		52.4126320211
199UbiquitinationDDLQAIKKELTQIKQ
HHHHHHHHHHHHHHH		52.4122790023
199 (in isoform 2)Ubiquitination-52.4122790023
201 (in isoform 3)Phosphorylation-6.1629514104
201 (in isoform 4)Phosphorylation-6.1629514104
204 (in isoform 2)Ubiquitination-4.26-
205UbiquitinationKKELTQIKQKVDSLL
HHHHHHHHHHHHHHH		33.9627667366
207AcetylationELTQIKQKVDSLLES
HHHHHHHHHHHHHHH		42.9023806337
207UbiquitinationELTQIKQKVDSLLES
HHHHHHHHHHHHHHH		42.9022790023
207 (in isoform 2)Ubiquitination-42.9022790023
210PhosphorylationQIKQKVDSLLESLEK
HHHHHHHHHHHHHHH		37.5329514104
211UbiquitinationIKQKVDSLLESLEKI
HHHHHHHHHHHHHHH		5.4927667366
211 (in isoform 2)Ubiquitination-5.49-
214PhosphorylationKVDSLLESLEKIEKE
HHHHHHHHHHHHHHH		41.6228066266
214 (in isoform 5)Phosphorylation-41.6229514104
216 (in isoform 2)Phosphorylation-62.3619144319
217AcetylationSLLESLEKIEKEQSK
HHHHHHHHHHHHHHH		62.5522826441
217UbiquitinationSLLESLEKIEKEQSK
HHHHHHHHHHHHHHH		62.5522790023
217 (in isoform 2)Ubiquitination-62.5522790023
220UbiquitinationESLEKIEKEQSKQAD
HHHHHHHHHHHHCCC		65.6127667366
220 (in isoform 4)Phosphorylation-65.6125266776
221 (in isoform 3)Phosphorylation-47.5024453211
224UbiquitinationKIEKEQSKQADLSFS
HHHHHHHHCCCCCCC		49.5622790023
224 (in isoform 2)Ubiquitination-49.5622790023
225 (in isoform 4)Phosphorylation-45.4126824392
226 (in isoform 3)Phosphorylation-24.3720531401
226 (in isoform 4)Phosphorylation-24.3725266776
227UbiquitinationKEQSKQADLSFSSPV
HHHHHCCCCCCCCCC		40.1127667366
227 (in isoform 3)Phosphorylation-40.1125266776
228 (in isoform 2)Phosphorylation-6.6219144319
228 (in isoform 4)Phosphorylation-6.6226824392
229PhosphorylationQSKQADLSFSSPVEM
HHHCCCCCCCCCCCC		24.5125521595
229 (in isoform 3)Phosphorylation-24.5120531401
231PhosphorylationKQADLSFSSPVEMKN
HCCCCCCCCCCCCCC		30.2925521595
232PhosphorylationQADLSFSSPVEMKNE
CCCCCCCCCCCCCCC		30.8424925903
233UbiquitinationADLSFSSPVEMKNEK
CCCCCCCCCCCCCCC		25.5327667366
234 (in isoform 5)Phosphorylation-14.0024453211
237AcetylationFSSPVEMKNEKSEEE
CCCCCCCCCCCCHHH		48.7422826441
237UbiquitinationFSSPVEMKNEKSEEE
CCCCCCCCCCCCHHH		48.7422790023
237 (in isoform 2)Ubiquitination-48.7422790023
239 (in isoform 5)Phosphorylation-53.0620531401
240AcetylationPVEMKNEKSEEEQSS
CCCCCCCCCHHHHHC		72.9822826441
240UbiquitinationPVEMKNEKSEEEQSS
CCCCCCCCCHHHHHC		72.9827667366
240 (in isoform 5)Phosphorylation-72.9825266776
241PhosphorylationVEMKNEKSEEEQSSA
CCCCCCCCHHHHHCC		44.0227087446
242 (in isoform 5)Phosphorylation-76.3020531401
246PhosphorylationEKSEEEQSSASVKKD
CCCHHHHHCCCCCCC		31.0227087446
247PhosphorylationKSEEEQSSASVKKDE
CCHHHHHCCCCCCCC		25.0227087446
249PhosphorylationEEEQSSASVKKDETN
HHHHHCCCCCCCCCC		36.1025521595
255PhosphorylationASVKKDETNVKMESE
CCCCCCCCCCCEEEC		56.2825619855
261PhosphorylationETNVKMESEAGADDS
CCCCCEEECCCCCCC		29.2825521595
268PhosphorylationSEAGADDSAEEGDLL
ECCCCCCCCCCCCCC		37.8227087446
306PhosphorylationEGEDDRDSANGEDDS
CCCCCHHHCCCCCCC		25.2425521595
313PhosphorylationSANGEDDS-------
HCCCCCCC-------		55.2125521595
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

Oops, there are no upstream regulatory protein records of HNRPC_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
268SPhosphorylation

15345747
306SPhosphorylation

21183079
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of HNRPC_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HNRPC_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-241 AND SER-268, ANDMASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241 AND SER-249, ANDMASS SPECTROMETRY.
"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-232, 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-232, AND MASSSPECTROMETRY.

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