PTBP1_HUMAN - dbPTM
PTBP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTBP1_HUMAN
UniProt AC P26599
Protein Name Polypyrimidine tract-binding protein 1
Gene Name PTBP1
Organism Homo sapiens (Human).
Sequence Length 531
Subcellular Localization Nucleus.
Protein Description Plays a role in pre-mRNA splicing and in the regulation of alternative splicing events. Activates exon skipping of its own pre-mRNA during muscle cell differentiation. Binds to the polypyrimidine tract of introns. May promote RNA looping when bound to two separate polypyrimidine tracts in the same pre-mRNA. May promote the binding of U2 snRNP to pre-mRNA. Cooperates with RAVER1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA. Represses the splicing of MAPT/Tau exon 10. [PubMed: 15009664 In case of infection by picornaviruses, binds to the viral internal ribosome entry site (IRES) and stimulates the IRES-mediated translation]
Protein Sequence MDGIVPDIAVGTKRGSDELFSTCVTNGPFIMSSNSASAANGNDSKKFKGDSRSAGVPSRVIHIRKLPIDVTEGEVISLGLPFGKVTNLLMLKGKNQAFIEMNTEEAANTMVNYYTSVTPVLRGQPIYIQFSNHKELKTDSSPNQARAQAALQAVNSVQSGNLALAASAAAVDAGMAMAGQSPVLRIIVENLFYPVTLDVLHQIFSKFGTVLKIITFTKNNQFQALLQYADPVSAQHAKLSLDGQNIYNACCTLRIDFSKLTSLNVKYNNDKSRDYTRPDLPSGDSQPSLDQTMAAAFGLSVPNVHGALAPLAIPSAAAAAAAAGRIAIPGLAGAGNSVLLVSNLNPERVTPQSLFILFGVYGDVQRVKILFNKKENALVQMADGNQAQLAMSHLNGHKLHGKPIRITLSKHQNVQLPREGQEDQGLTKDYGNSPLHRFKKPGSKNFQNIFPPSATLHLSNIPPSVSEEDLKVLFSSNGGVVKGFKFFQKDRKMALIQMGSVEEAVQALIDLHNHDLGENHHLRVSFSKSTI
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-------MDGIVPDI
-------CCCCCCCC		10.8519413330
1Sulfoxidation-------MDGIVPDI
-------CCCCCCCC		10.8528183972
12PhosphorylationVPDIAVGTKRGSDEL
CCCCCCCCCCCCCHH		15.8026074081
13SumoylationPDIAVGTKRGSDELF
CCCCCCCCCCCCHHH		49.16-
13AcetylationPDIAVGTKRGSDELF
CCCCCCCCCCCCHHH		49.1625953088
13SumoylationPDIAVGTKRGSDELF
CCCCCCCCCCCCHHH		49.16-
13UbiquitinationPDIAVGTKRGSDELF
CCCCCCCCCCCCHHH		49.1621906983
13 (in isoform 3)Ubiquitination-49.16-
13UbiquitinationPDIAVGTKRGSDELF
CCCCCCCCCCCCHHH		49.1621890473
15UbiquitinationIAVGTKRGSDELFST
CCCCCCCCCCHHHHH		40.7922817900
16PhosphorylationAVGTKRGSDELFSTC
CCCCCCCCCHHHHHH		31.7630266825
16 (in isoform 2)Phosphorylation-31.76-
16 (in isoform 3)Phosphorylation-31.7627251275
21PhosphorylationRGSDELFSTCVTNGP
CCCCHHHHHHEECCC		33.2630266825
22PhosphorylationGSDELFSTCVTNGPF
CCCHHHHHHEECCCE		12.0330266825
25O-linked_GlycosylationELFSTCVTNGPFIMS
HHHHHHEECCCEEEE		36.2855821479
25PhosphorylationELFSTCVTNGPFIMS
HHHHHHEECCCEEEE		36.2830576142
32PhosphorylationTNGPFIMSSNSASAA
ECCCEEEECCCCCCC		22.8823927012
33PhosphorylationNGPFIMSSNSASAAN
CCCEEEECCCCCCCC		19.8823927012
35PhosphorylationPFIMSSNSASAANGN
CEEEECCCCCCCCCC		26.0823927012
35 (in isoform 2)Phosphorylation-26.08-
35 (in isoform 3)Phosphorylation-26.0827251275
37PhosphorylationIMSSNSASAANGNDS
EEECCCCCCCCCCCC		27.9523927012
37 (in isoform 2)Phosphorylation-27.95-
37 (in isoform 3)Phosphorylation-27.95-
45AcetylationAANGNDSKKFKGDSR
CCCCCCCCCCCCCCC		66.1626051181
45UbiquitinationAANGNDSKKFKGDSR
CCCCCCCCCCCCCCC		66.1632015554
46AcetylationANGNDSKKFKGDSRS
CCCCCCCCCCCCCCC		57.1512422075
46UbiquitinationANGNDSKKFKGDSRS
CCCCCCCCCCCCCCC		57.1524816145
48UbiquitinationGNDSKKFKGDSRSAG
CCCCCCCCCCCCCCC		71.3524816145
51PhosphorylationSKKFKGDSRSAGVPS
CCCCCCCCCCCCCCC		36.4824719451
51 (in isoform 3)Phosphorylation-36.4824719451
52MethylationKKFKGDSRSAGVPSR
CCCCCCCCCCCCCCC		34.95115479187
53O-linked_GlycosylationKFKGDSRSAGVPSRV
CCCCCCCCCCCCCCE		33.0723301498
53PhosphorylationKFKGDSRSAGVPSRV
CCCCCCCCCCCCCCE		33.0720363803
53 (in isoform 3)Phosphorylation-33.0727251275
58PhosphorylationSRSAGVPSRVIHIRK
CCCCCCCCCEEEEEE		36.4523898821
65SumoylationSRVIHIRKLPIDVTE
CCEEEEEECCCCCCC		58.99-
65AcetylationSRVIHIRKLPIDVTE
CCEEEEEECCCCCCC		58.9926051181
65SumoylationSRVIHIRKLPIDVTE
CCEEEEEECCCCCCC		58.9928112733
65UbiquitinationSRVIHIRKLPIDVTE
CCEEEEEECCCCCCC		58.9923000965
65 (in isoform 1)Ubiquitination-58.9921890473
65 (in isoform 2)Ubiquitination-58.9921890473
65 (in isoform 3)Ubiquitination-58.99-
67UbiquitinationVIHIRKLPIDVTEGE
EEEEEECCCCCCCCC		24.6223000965
84SumoylationSLGLPFGKVTNLLML
ECCCCCCCCCEEEEE		46.39-
84SumoylationSLGLPFGKVTNLLML
ECCCCCCCCCEEEEE		46.39-
84UbiquitinationSLGLPFGKVTNLLML
ECCCCCCCCCEEEEE		46.3932015554
92SuccinylationVTNLLMLKGKNQAFI
CCEEEEECCCCCEEE		54.6023954790
92UbiquitinationVTNLLMLKGKNQAFI
CCEEEEECCCCCEEE		54.6021890473
92 (in isoform 3)Ubiquitination-54.60-
94UbiquitinationNLLMLKGKNQAFIEM
EEEEECCCCCEEEEC		44.2821890473
94 (in isoform 1)Ubiquitination-44.2821890473
94 (in isoform 2)Ubiquitination-44.2821890473
94 (in isoform 3)Ubiquitination-44.28-
103O-linked_GlycosylationQAFIEMNTEEAANTM
CEEEECCHHHHHHHH		33.6123301498
109O-linked_GlycosylationNTEEAANTMVNYYTS
CHHHHHHHHHHHHHC		20.1223301498
127PhosphorylationVLRGQPIYIQFSNHK
HHCCCCEEEECCCCC		8.7121945579
127 (in isoform 2)Phosphorylation-8.7125147952
127 (in isoform 3)Phosphorylation-8.7127642862
131PhosphorylationQPIYIQFSNHKELKT
CCEEEECCCCCCCCC		22.9621945579
134AcetylationYIQFSNHKELKTDSS
EEECCCCCCCCCCCC		69.8323236377
134UbiquitinationYIQFSNHKELKTDSS
EEECCCCCCCCCCCC		69.8321890473
134 (in isoform 1)Ubiquitination-69.8321890473
134 (in isoform 2)Ubiquitination-69.8321890473
134 (in isoform 3)Ubiquitination-69.83-
136UbiquitinationQFSNHKELKTDSSPN
ECCCCCCCCCCCCHH		9.6221890473
137SumoylationFSNHKELKTDSSPNQ
CCCCCCCCCCCCHHH		51.91-
137AcetylationFSNHKELKTDSSPNQ
CCCCCCCCCCCCHHH		51.9126051181
137SumoylationFSNHKELKTDSSPNQ
CCCCCCCCCCCCHHH		51.91-
137UbiquitinationFSNHKELKTDSSPNQ
CCCCCCCCCCCCHHH		51.9122817900
137 (in isoform 3)Ubiquitination-51.91-
138O-linked_GlycosylationSNHKELKTDSSPNQA
CCCCCCCCCCCHHHH		54.4623301498
138PhosphorylationSNHKELKTDSSPNQA
CCCCCCCCCCCHHHH		54.4630266825
138 (in isoform 2)Phosphorylation-54.46-
138 (in isoform 3)Phosphorylation-54.46-
139UbiquitinationNHKELKTDSSPNQAR
CCCCCCCCCCHHHHH		45.6022817900
140O-linked_GlycosylationHKELKTDSSPNQARA
CCCCCCCCCHHHHHH		53.5823301498
140PhosphorylationHKELKTDSSPNQARA
CCCCCCCCCHHHHHH		53.5822167270
140 (in isoform 2)Phosphorylation-53.58-
140 (in isoform 3)Phosphorylation-53.58-
141PhosphorylationKELKTDSSPNQARAQ
CCCCCCCCHHHHHHH		30.5822167270
141 (in isoform 2)Phosphorylation-30.58-
141 (in isoform 3)Phosphorylation-30.5824719451
159PhosphorylationQAVNSVQSGNLALAA
HHHHHHHHCCHHHHH		27.7428348404
159 (in isoform 3)Phosphorylation-27.7427251275
167PhosphorylationGNLALAASAAAVDAG
CCHHHHHHHHHHHHH		16.9127251275
167 (in isoform 3)Phosphorylation-16.9127251275
175SulfoxidationAAAVDAGMAMAGQSP
HHHHHHHHHHCCCCC		2.1828183972
177SulfoxidationAVDAGMAMAGQSPVL
HHHHHHHHCCCCCHH		2.9828183972
181PhosphorylationGMAMAGQSPVLRIIV
HHHHCCCCCHHHHHH		18.96-
193PhosphorylationIIVENLFYPVTLDVL
HHHHCCCCCCHHHHH		10.44-
205PhosphorylationDVLHQIFSKFGTVLK
HHHHHHHHHHCCEEE		28.8024719451
212UbiquitinationSKFGTVLKIITFTKN
HHHCCEEEEEEECCC		27.9423000965
214UbiquitinationFGTVLKIITFTKNNQ
HCCEEEEEEECCCCH		2.1823000965
218SumoylationLKIITFTKNNQFQAL
EEEEEECCCCHHHHH		50.11-
218AcetylationLKIITFTKNNQFQAL
EEEEEECCCCHHHHH		50.1125953088
218SumoylationLKIITFTKNNQFQAL
EEEEEECCCCHHHHH		50.1128112733
218UbiquitinationLKIITFTKNNQFQAL
EEEEEECCCCHHHHH		50.1123000965
218 (in isoform 1)Ubiquitination-50.1121890473
218 (in isoform 2)Ubiquitination-50.1121890473
218 (in isoform 3)Ubiquitination-50.11-
218UbiquitinationLKIITFTKNNQFQAL
EEEEEECCCCHHHHH		50.1121890473
220UbiquitinationIITFTKNNQFQALLQ
EEEECCCCHHHHHHH		45.6721890473
228PhosphorylationQFQALLQYADPVSAQ
HHHHHHHHCCCCCCC		16.9728152594
233PhosphorylationLQYADPVSAQHAKLS
HHHCCCCCCCCEEEC		27.8328152594
247NitrationSLDGQNIYNACCTLR
CCCCCCHHHEEEEEE		12.31-
247PhosphorylationSLDGQNIYNACCTLR
CCCCCCHHHEEEEEE		12.3128152594
250S-nitrosocysteineGQNIYNACCTLRIDF
CCCHHHEEEEEEECH		1.30-
250S-nitrosylationGQNIYNACCTLRIDF
CCCHHHEEEEEEECH		1.3019483679
251S-nitrosocysteineQNIYNACCTLRIDFS
CCHHHEEEEEEECHH		3.59-
251S-nitrosylationQNIYNACCTLRIDFS
CCHHHEEEEEEECHH		3.5919483679
252PhosphorylationNIYNACCTLRIDFSK
CHHHEEEEEEECHHH		20.9628152594
259SumoylationTLRIDFSKLTSLNVK
EEEECHHHCCEEEEE		56.64-
259AcetylationTLRIDFSKLTSLNVK
EEEECHHHCCEEEEE		56.6422635933
259SumoylationTLRIDFSKLTSLNVK
EEEECHHHCCEEEEE		56.6419608861
259UbiquitinationTLRIDFSKLTSLNVK
EEEECHHHCCEEEEE		56.6423000965
259 (in isoform 1)Ubiquitination-56.6421890473
259 (in isoform 2)Acetylation-56.64-
259 (in isoform 2)Ubiquitination-56.6421890473
259 (in isoform 3)Acetylation-56.64-
259 (in isoform 3)Ubiquitination-56.64-
261UbiquitinationRIDFSKLTSLNVKYN
EECHHHCCEEEEEEC		34.6023000965
262PhosphorylationIDFSKLTSLNVKYNN
ECHHHCCEEEEEECC		28.5127703031
266SumoylationKLTSLNVKYNNDKSR
HCCEEEEEECCCCCC		40.98-
266AcetylationKLTSLNVKYNNDKSR
HCCEEEEEECCCCCC		40.98129411
266NeddylationKLTSLNVKYNNDKSR
HCCEEEEEECCCCCC		40.9832015554
266SumoylationKLTSLNVKYNNDKSR
HCCEEEEEECCCCCC		40.9819608861
266UbiquitinationKLTSLNVKYNNDKSR
HCCEEEEEECCCCCC		40.9823000965
266 (in isoform 1)Ubiquitination-40.9821890473
266 (in isoform 2)Acetylation-40.98-
266 (in isoform 2)Ubiquitination-40.9821890473
266 (in isoform 3)Acetylation-40.98-
266 (in isoform 3)Ubiquitination-40.98-
267PhosphorylationLTSLNVKYNNDKSRD
CCEEEEEECCCCCCC		18.21-
268UbiquitinationTSLNVKYNNDKSRDY
CEEEEEECCCCCCCC		44.5023000965
271UbiquitinationNVKYNNDKSRDYTRP
EEEECCCCCCCCCCC		49.9023000965
272PhosphorylationVKYNNDKSRDYTRPD
EEECCCCCCCCCCCC		32.99-
273UbiquitinationKYNNDKSRDYTRPDL
EECCCCCCCCCCCCC		46.8523000965
282PhosphorylationYTRPDLPSGDSQPSL
CCCCCCCCCCCCCCH		63.6328348404
285PhosphorylationPDLPSGDSQPSLDQT
CCCCCCCCCCCHHHH		47.7328464451
288PhosphorylationPSGDSQPSLDQTMAA
CCCCCCCCHHHHHHH		36.6228348404
292O-linked_GlycosylationSQPSLDQTMAAAFGL
CCCCHHHHHHHHHCC		14.4023301498
292PhosphorylationSQPSLDQTMAAAFGL
CCCCHHHHHHHHHCC		14.4028464451
300O-linked_GlycosylationMAAAFGLSVPNVHGA
HHHHHCCCCCCCCCC		35.5923301498
300PhosphorylationMAAAFGLSVPNVHGA
HHHHHCCCCCCCCCC		35.5928464451
337PhosphorylationGLAGAGNSVLLVSNL
CCCCCCCEEEEEECC		17.1421712546
342PhosphorylationGNSVLLVSNLNPERV
CCEEEEEECCCHHHC		35.2521712546
368AcetylationYGDVQRVKILFNKKE
CCCCEEEEEEEECCC		35.5623749302
368UbiquitinationYGDVQRVKILFNKKE
CCCCEEEEEEEECCC		35.5622817900
368 (in isoform 1)Ubiquitination-35.5621890473
370UbiquitinationDVQRVKILFNKKENA
CCEEEEEEEECCCCE		2.9921890473
373AcetylationRVKILFNKKENALVQ
EEEEEEECCCCEEEE		54.8826051181
373UbiquitinationRVKILFNKKENALVQ
EEEEEEECCCCEEEE		54.8822817900
374UbiquitinationVKILFNKKENALVQM
EEEEEECCCCEEEEE		58.2529967540
375UbiquitinationKILFNKKENALVQMA
EEEEECCCCEEEEEC		49.7122817900
387UbiquitinationQMADGNQAQLAMSHL
EECCCCHHHHHHHHH		15.4521890473
387 (in isoform 2)Ubiquitination-15.4521890473
392PhosphorylationNQAQLAMSHLNGHKL
CHHHHHHHHHCCCCC		21.1527251275
392UbiquitinationNQAQLAMSHLNGHKL
CHHHHHHHHHCCCCC		21.1522817900
393UbiquitinationQAQLAMSHLNGHKLH
HHHHHHHHHCCCCCC		15.3829967540
394UbiquitinationAQLAMSHLNGHKLHG
HHHHHHHHCCCCCCC		6.8721890473
394 (in isoform 3)Ubiquitination-6.87-
394UbiquitinationAQLAMSHLNGHKLHG
HHHHHHHHCCCCCCC		6.8721890473
396UbiquitinationLAMSHLNGHKLHGKP
HHHHHHCCCCCCCCC		26.1821890473
398AcetylationMSHLNGHKLHGKPIR
HHHHCCCCCCCCCEE		43.5125953088
399UbiquitinationSHLNGHKLHGKPIRI
HHHCCCCCCCCCEEE		5.5222817900
400UbiquitinationHLNGHKLHGKPIRIT
HHCCCCCCCCCEEEE		47.2129967540
401UbiquitinationLNGHKLHGKPIRITL
HCCCCCCCCCEEEEE		48.1222817900
402UbiquitinationNGHKLHGKPIRITLS
CCCCCCCCCEEEEEE		26.90-
407PhosphorylationHGKPIRITLSKHQNV
CCCCEEEEEECCCCC		18.3529514088
409PhosphorylationKPIRITLSKHQNVQL
CCEEEEEECCCCCCC		21.3129514088
410AcetylationPIRITLSKHQNVQLP
CEEEEEECCCCCCCC		52.9321466224
410MalonylationPIRITLSKHQNVQLP
CEEEEEECCCCCCCC		52.9326320211
410UbiquitinationPIRITLSKHQNVQLP
CEEEEEECCCCCCCC		52.9323000965
410 (in isoform 1)Ubiquitination-52.9321890473
412UbiquitinationRITLSKHQNVQLPRE
EEEEECCCCCCCCCC		56.3721890473
418 (in isoform 3)Phosphorylation-70.0827251275
427PhosphorylationGQEDQGLTKDYGNSP
CCCCCCCCCCCCCCC		28.7928152594
428AcetylationQEDQGLTKDYGNSPL
CCCCCCCCCCCCCCC		54.7325953088
428MalonylationQEDQGLTKDYGNSPL
CCCCCCCCCCCCCCC		54.7326320211
428UbiquitinationQEDQGLTKDYGNSPL
CCCCCCCCCCCCCCC		54.7323000965
428 (in isoform 1)Ubiquitination-54.7321890473
429UbiquitinationEDQGLTKDYGNSPLH
CCCCCCCCCCCCCCC		51.8723000965
429 (in isoform 2)Ubiquitination-51.8721890473
430NitrationDQGLTKDYGNSPLHR
CCCCCCCCCCCCCCC		21.55-
430PhosphorylationDQGLTKDYGNSPLHR
CCCCCCCCCCCCCCC		21.5528152594
430UbiquitinationDQGLTKDYGNSPLHR
CCCCCCCCCCCCCCC		21.5521890473
433PhosphorylationLTKDYGNSPLHRFKK
CCCCCCCCCCCCCCC		25.1922167270
436UbiquitinationDYGNSPLHRFKKPGS
CCCCCCCCCCCCCCC		36.1923000965
436 (in isoform 3)Ubiquitination-36.19-
436UbiquitinationDYGNSPLHRFKKPGS
CCCCCCCCCCCCCCC		36.1921890473
438UbiquitinationGNSPLHRFKKPGSKN
CCCCCCCCCCCCCCC		9.2121890473
440UbiquitinationSPLHRFKKPGSKNFQ
CCCCCCCCCCCCCCC		52.4829967540
443PhosphorylationHRFKKPGSKNFQNIF
CCCCCCCCCCCCCCC		32.7120068231
444UbiquitinationRFKKPGSKNFQNIFP
CCCCCCCCCCCCCCC		68.6329967540
446 (in isoform 2)Phosphorylation-7.27-
447UbiquitinationKPGSKNFQNIFPPSA
CCCCCCCCCCCCCCC		52.0523000965
447 (in isoform 2)Ubiquitination-52.0521890473
452 (in isoform 2)Phosphorylation-26.33-
453PhosphorylationFQNIFPPSATLHLSN
CCCCCCCCCEEECCC		33.8428450419
453 (in isoform 3)Phosphorylation-33.84-
454UbiquitinationQNIFPPSATLHLSNI
CCCCCCCCEEECCCC		21.6923000965
454 (in isoform 3)Ubiquitination-21.69-
454UbiquitinationQNIFPPSATLHLSNI
CCCCCCCCEEECCCC		21.6921890473
455PhosphorylationNIFPPSATLHLSNIP
CCCCCCCEEECCCCC		21.0326434776
456UbiquitinationIFPPSATLHLSNIPP
CCCCCCEEECCCCCC		3.7021890473
459PhosphorylationPSATLHLSNIPPSVS
CCCEEECCCCCCCCC		23.2028450419
459UbiquitinationPSATLHLSNIPPSVS
CCCEEECCCCCCCCC		23.2029967540
459 (in isoform 3)Phosphorylation-23.2024719451
462 (in isoform 2)Phosphorylation-21.26-
463UbiquitinationLHLSNIPPSVSEEDL
EECCCCCCCCCHHHH		43.4929967540
464PhosphorylationHLSNIPPSVSEEDLK
ECCCCCCCCCHHHHE		32.6828450419
466PhosphorylationSNIPPSVSEEDLKVL
CCCCCCCCHHHHEEE		39.3428450419
466UbiquitinationSNIPPSVSEEDLKVL
CCCCCCCCHHHHEEE		39.3429967540
469 (in isoform 3)Phosphorylation-47.97-
470UbiquitinationPSVSEEDLKVLFSSN
CCCCHHHHEEEECCC		4.7129967540
471AcetylationSVSEEDLKVLFSSNG
CCCHHHHEEEECCCC		49.5726051181
476PhosphorylationDLKVLFSSNGGVVKG
HHEEEECCCCCEECE		31.9621712546
482AcetylationSSNGGVVKGFKFFQK
CCCCCEECEEEEECC		57.1125953088
482UbiquitinationSSNGGVVKGFKFFQK
CCCCCEECEEEEECC		57.1123000965
482 (in isoform 1)Ubiquitination-57.1121890473
484UbiquitinationNGGVVKGFKFFQKDR
CCCEECEEEEECCCC		5.3023000965
485SumoylationGGVVKGFKFFQKDRK
CCEECEEEEECCCCC		54.67-
485AcetylationGGVVKGFKFFQKDRK
CCEECEEEEECCCCC		54.6725825284
485SumoylationGGVVKGFKFFQKDRK
CCEECEEEEECCCCC		54.67-
485UbiquitinationGGVVKGFKFFQKDRK
CCEECEEEEECCCCC		54.6723000965
485 (in isoform 1)Ubiquitination-54.6721890473
487UbiquitinationVVKGFKFFQKDRKMA
EECEEEEECCCCCEE		10.2021890473
489AcetylationKGFKFFQKDRKMALI
CEEEEECCCCCEEEE		55.1119608861
489UbiquitinationKGFKFFQKDRKMALI
CEEEEECCCCCEEEE		55.1122817900
491UbiquitinationFKFFQKDRKMALIQM
EEEECCCCCEEEECC		37.3722817900
492 (in isoform 3)Phosphorylation-38.3627251275
501UbiquitinationALIQMGSVEEAVQAL
EEECCCCHHHHHHHH		6.8023000965
501 (in isoform 2)Ubiquitination-6.8021890473
504UbiquitinationQMGSVEEAVQALIDL
CCCCHHHHHHHHHHH		5.8023000965
504 (in isoform 2)Ubiquitination-5.8021890473
508AcetylationVEEAVQALIDLHNHD
HHHHHHHHHHHHCCC		1.4219608861
508UbiquitinationVEEAVQALIDLHNHD
HHHHHHHHHHHHCCC		1.4223000965
508 (in isoform 2)Acetylation-1.42-
508 (in isoform 3)Ubiquitination-1.42-
508UbiquitinationVEEAVQALIDLHNHD
HHHHHHHHHHHHCCC		1.4221890473
510UbiquitinationEAVQALIDLHNHDLG
HHHHHHHHHHCCCCC		42.6023000965
511UbiquitinationAVQALIDLHNHDLGE
HHHHHHHHHCCCCCC		3.2723000965
511 (in isoform 3)Ubiquitination-3.27-
511UbiquitinationAVQALIDLHNHDLGE
HHHHHHHHHCCCCCC		3.2721890473
513UbiquitinationQALIDLHNHDLGENH
HHHHHHHCCCCCCCC		37.3521890473
515AcetylationLIDLHNHDLGENHHL
HHHHHCCCCCCCCEE		62.7819608861
515UbiquitinationLIDLHNHDLGENHHL
HHHHHCCCCCCCCEE		62.7822817900
515 (in isoform 3)Acetylation-62.78-
515 (in isoform 3)Ubiquitination-62.78-
517UbiquitinationDLHNHDLGENHHLRV
HHHCCCCCCCCEEEE		39.4522817900
525PhosphorylationENHHLRVSFSKSTI-
CCCEEEEEEECCCC-		19.8524719451
527PhosphorylationHHLRVSFSKSTI---
CEEEEEEECCCC---		20.4226434776
528AcetylationHLRVSFSKSTI----
EEEEEEECCCC----		50.0021670987
528UbiquitinationHLRVSFSKSTI----
EEEEEEECCCC----		50.0033845483
528 (in isoform 1)Ubiquitination-50.0021890473
529PhosphorylationLRVSFSKSTI-----
EEEEEECCCC-----		30.0920873877
530PhosphorylationRVSFSKSTI------
EEEEECCCC------		34.1520873877
530UbiquitinationRVSFSKSTI------
EEEEECCCC------		34.1521987572
547Acetylation-----------------------
-----------------------		19608861
547Ubiquitination-----------------------
-----------------------		33845483
547 (in isoform 2)Acetylation--
547 (in isoform 2)Ubiquitination-21890473
551 (in isoform 3)Phosphorylation-24719451
554Acetylation------------------------------
------------------------------		19608861
554Ubiquitination------------------------------
------------------------------		33845483
554 (in isoform 3)Acetylation--
554 (in isoform 3)Ubiquitination--
556Ubiquitination--------------------------------
--------------------------------		21987572
556 (in isoform 3)Phosphorylation-24719451
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
16SPhosphorylationKinasePRKACAP17612
GPS
16SPhosphorylationKinasePKA-FAMILY-GPS
16SPhosphorylationKinasePKA_GROUP-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTBP1_HUMAN !!
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 PTBP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HNRPL_HUMANHNRNPLphysical
9563502
CACO2_HUMANCALCOCO2physical
16189514
SNRPA_HUMANSNRPAphysical
16189514
PTBP1_HUMANPTBP1physical
16189514
RAVR1_MOUSERaver1physical
11724819
PCBP2_HUMANPCBP2physical
10772858
PTBP1_HUMANPTBP1physical
10772858
HNRPK_HUMANHNRNPKphysical
10772858
HNRPL_HUMANHNRNPLphysical
10772858
PTBP1_HUMANPTBP1physical
9563502
SFPQ_HUMANSFPQphysical
10653975
ISG15_HUMANISG15physical
16009940
NPM_HUMANNPM1physical
16376875
A4_HUMANAPPphysical
21832049
ROA2_HUMANHNRNPA2B1physical
22939629
SRSF5_HUMANSRSF5physical
22939629
ROA1_HUMANHNRNPA1physical
22939629
ROA3_HUMANHNRNPA3physical
22939629
ROA0_HUMANHNRNPA0physical
22939629
RS7_HUMANRPS7physical
22939629
RL36_HUMANRPL36physical
22939629
TM177_HUMANTMEM177physical
22939629
RAB1A_HUMANRAB1Aphysical
22939629
SNRPA_HUMANSNRPAphysical
22365833
RBM10_HUMANRBM10physical
22365833
ELAV1_HUMANELAVL1physical
22365833
ROAA_HUMANHNRNPABphysical
22365833
HNRPD_HUMANHNRNPDphysical
22365833
QKI_HUMANQKIphysical
22365833
RFOX2_HUMANRBFOX2physical
22365833
IL7RA_HUMANIL7Rphysical
23151878
HMGA1_HUMANHMGA1physical
18850631
AIMP1_HUMANAIMP1physical
22863883
HNRPD_HUMANHNRNPDphysical
22863883
IQGA1_HUMANIQGAP1physical
22863883
RSSA_HUMANRPSAphysical
22863883
SPTN1_HUMANSPTAN1physical
22863883
SFPQ_HUMANSFPQphysical
17507659
PTBP1_HUMANPTBP1physical
25416956
SNRPA_HUMANSNRPAphysical
25416956
MARK4_HUMANMARK4physical
25578778
THIL_HUMANACAT1physical
26344197
AMGO2_HUMANAMIGO2physical
26344197
ATPA_HUMANATP5A1physical
26344197
ATPB_HUMANATP5Bphysical
26344197
ATPG_HUMANATP5C1physical
26344197
CALX_HUMANCANXphysical
26344197
CCNH_HUMANCCNHphysical
26344197
CHK1_HUMANCHEK1physical
26344197
DDX17_HUMANDDX17physical
26344197
FUS_HUMANFUSphysical
26344197
HNRPD_HUMANHNRNPDphysical
26344197
HNRPK_HUMANHNRNPKphysical
26344197
HNRPL_HUMANHNRNPLphysical
26344197
HCD2_HUMANHSD17B10physical
26344197
GRP78_HUMANHSPA5physical
26344197
HSPB1_HUMANHSPB1physical
26344197
PCBP1_HUMANPCBP1physical
26344197
ODPA_HUMANPDHA1physical
26344197
ODPB_HUMANPDHBphysical
26344197
RAB2A_HUMANRAB2Aphysical
26344197
RAGP1_HUMANRANGAP1physical
26344197
SAR1A_HUMANSAR1Aphysical
26344197
4F2_HUMANSLC3A2physical
26344197
STML2_HUMANSTOML2physical
26344197
TIM13_HUMANTIMM13physical
26344197
TOM70_HUMANTOMM70Aphysical
26344197
EFTU_HUMANTUFMphysical
26344197
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 PTBP1_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, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, AND MASSSPECTROMETRY.
"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-16 AND SER-141, AND MASSSPECTROMETRY.
"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-433, AND MASSSPECTROMETRY.
"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-141 AND SER-433, ANDMASS SPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-127, AND MASSSPECTROMETRY.

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