PTBP3_HUMAN - dbPTM
PTBP3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTBP3_HUMAN
UniProt AC O95758
Protein Name Polypyrimidine tract-binding protein 3
Gene Name PTBP3
Organism Homo sapiens (Human).
Sequence Length 552
Subcellular Localization
Protein Description RNA-binding protein that mediates pre-mRNA alternative splicing regulation. Plays a role in the regulation of cell proliferation, differentiation and migration. Positive regulator of EPO-dependent erythropoiesis. Participates in cell differentiation regulation by repressing tissue-specific exons. Promotes FAS exon 6 skipping. Binds RNA, preferentially to both poly(G) and poly(U)..
Protein Sequence MDGVVTDLITVGLKRGSDELLSSGIINGPFTMNSSTPSTANGNDSKKFKRDRPPCSPSRVLHLRKIPCDVTEAEIISLGLPFGKVTNLLMLKGKSQAFLEMASEEAAVTMVNYYTPITPHLRSQPVYIQYSNHRELKTDNLPNQARAQAALQAVSAVQSGSLALSGGPSNEGTVLPGQSPVLRIIIENLFYPVTLEVLHQIFSKFGTVLKIITFTKNNQFQALLQYADPVNAHYAKMALDGQNIYNACCTLRIDFSKLTSLNVKYNNDKSRDFTRLDLPTGDGQPSLEPPMAAAFGAPGIISSPYAGAAGFAPAIGFPQATGLSVPAVPGALGPLTITSSAVTGRMAIPGASGIPGNSVLLVTNLNPDLITPHGLFILFGVYGDVHRVKIMFNKKENALVQMADANQAQLAMNHLSGQRLYGKVLRATLSKHQAVQLPREGQEDQGLTKDFSNSPLHRFKKPGSKNFQNIFPPSATLHLSNIPPSVTVDDLKNLFIEAGCSVKAFKFFQKDRKMALIQLGSVEEAIQALIELHNHDLGENHHLRVSFSKSTI
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-------MDGVVTDL
-------CCCCEEEE		10.25-
1 (in isoform 1)Acetylation-10.2519413330
3 (in isoform 1)Phosphorylation-17.9422210691
3 (in isoform 2)Phosphorylation-17.9424043423
3 (in isoform 6)Phosphorylation-17.9424043423
4 (in isoform 1)Phosphorylation-3.5025159151
4 (in isoform 2)Phosphorylation-3.5025159151
4 (in isoform 4)Phosphorylation-3.5025159151
4 (in isoform 6)Phosphorylation-3.5025159151
5 (in isoform 1)Phosphorylation-4.1622210691
5 (in isoform 2)Phosphorylation-4.1624043423
5 (in isoform 6)Phosphorylation-4.1624043423
6Phosphorylation--MDGVVTDLITVGL
--CCCCEEEEEHHCC		23.7628188228
6 (in isoform 4)Phosphorylation-23.7625627689
7 (in isoform 2)Phosphorylation-25.1924043423
7 (in isoform 6)Phosphorylation-25.1924043423
8 (in isoform 2)Phosphorylation-2.3024043423
8 (in isoform 6)Phosphorylation-2.3024043423
10PhosphorylationGVVTDLITVGLKRGS
CCEEEEEHHCCCCCC		18.8028188228
11 (in isoform 2)Phosphorylation-7.2024043423
11 (in isoform 6)Phosphorylation-7.2024043423
14 (in isoform 5)Ubiquitination-49.11-
16 (in isoform 1)Ubiquitination-37.55-
17PhosphorylationTVGLKRGSDELLSSG
HHCCCCCCHHHHHCC		31.7624247654
17 (in isoform 2)Phosphorylation-31.7624043423
17 (in isoform 5)Phosphorylation-31.7628348404
17 (in isoform 6)Phosphorylation-31.7624043423
22PhosphorylationRGSDELLSSGIINGP
CCCHHHHHCCCCCCC		38.8622210691
34 (in isoform 1)Ubiquitination-25.43-
34 (in isoform 5)Phosphorylation-25.4324043423
35PhosphorylationGPFTMNSSTPSTANG
CCEEECCCCCCCCCC		39.0625627689
35 (in isoform 5)Phosphorylation-39.0624043423
36 (in isoform 5)Phosphorylation-22.5325627689
37 (in isoform 4)Phosphorylation-31.4622210691
38PhosphorylationTMNSSTPSTANGNDS
EECCCCCCCCCCCCC		39.9922210691
38 (in isoform 5)Phosphorylation-39.9924043423
39PhosphorylationMNSSTPSTANGNDSK
ECCCCCCCCCCCCCC		25.9122210691
39 (in isoform 5)Phosphorylation-25.9124043423
40 (in isoform 4)Phosphorylation-26.6922210691
42 (in isoform 5)Phosphorylation-36.5424043423
47UbiquitinationANGNDSKKFKRDRPP
CCCCCCCCCCCCCCC		61.13-
48 (in isoform 5)Phosphorylation-10.1024043423
56PhosphorylationKRDRPPCSPSRVLHL
CCCCCCCCHHHEEEE		31.5123401153
58PhosphorylationDRPPCSPSRVLHLRK
CCCCCCHHHEEEEEE		20.8030266825
64PhosphorylationPSRVLHLRKIPCDVT
HHHEEEEEECCCCCC		24.9020068231
65UbiquitinationSRVLHLRKIPCDVTE
HHEEEEEECCCCCCH		58.31-
71PhosphorylationRKIPCDVTEAEIISL
EECCCCCCHHHHHHC		19.0729396449
77PhosphorylationVTEAEIISLGLPFGK
CCHHHHHHCCCCCCC		23.2629396449
92AcetylationVTNLLMLKGKSQAFL
CHHHHHHCCCCHHHH		50.7825953088
92UbiquitinationVTNLLMLKGKSQAFL
CHHHHHHCCCCHHHH		50.78-
95PhosphorylationLLMLKGKSQAFLEMA
HHHHCCCCHHHHHHH		35.1024043423
98 (in isoform 4)Ubiquitination-4.62-
103PhosphorylationQAFLEMASEEAAVTM
HHHHHHHCHHHHHHE		34.3624043423
106 (in isoform 1)Ubiquitination-11.8121890473
109PhosphorylationASEEAAVTMVNYYTP
HCHHHHHHEEECCCC		15.6324043423
109 (in isoform 2)Ubiquitination-15.6321890473
113PhosphorylationAAVTMVNYYTPITPH
HHHHEEECCCCCCHH		9.4124043423
114PhosphorylationAVTMVNYYTPITPHL
HHHEEECCCCCCHHH		10.8024043423
115PhosphorylationVTMVNYYTPITPHLR
HHEEECCCCCCHHHH		9.6124043423
118PhosphorylationVNYYTPITPHLRSQP
EECCCCCCHHHHCCC		13.0821552520
123PhosphorylationPITPHLRSQPVYIQY
CCCHHHHCCCEEEEE		45.24-
127PhosphorylationHLRSQPVYIQYSNHR
HHHCCCEEEEECCCC		6.7621945579
130PhosphorylationSQPVYIQYSNHRELK
CCCEEEEECCCCCCC		11.2421945579
131PhosphorylationQPVYIQYSNHRELKT
CCEEEEECCCCCCCC		15.1321945579
137SumoylationYSNHRELKTDNLPNQ
ECCCCCCCCCCCCHH		49.43-
137UbiquitinationYSNHRELKTDNLPNQ
ECCCCCCCCCCCCHH		49.4321906983
137 (in isoform 3)Ubiquitination-49.4321890473
138PhosphorylationSNHRELKTDNLPNQA
CCCCCCCCCCCCHHH		42.6228102081
140 (in isoform 5)Ubiquitination-63.7321890473
143 (in isoform 4)Ubiquitination-51.8421890473
159PhosphorylationQAVSAVQSGSLALSG
HHHHHHHHCCEEECC		24.6128348404
161PhosphorylationVSAVQSGSLALSGGP
HHHHHHCCEEECCCC		18.7328348404
162UbiquitinationSAVQSGSLALSGGPS
HHHHHCCEEECCCCC		6.7521890473
165PhosphorylationQSGSLALSGGPSNEG
HHCCEEECCCCCCCC		35.7828348404
169UbiquitinationLALSGGPSNEGTVLP
EEECCCCCCCCCCCC		51.2721890473
169PhosphorylationLALSGGPSNEGTVLP
EEECCCCCCCCCCCC		51.2728348404
173PhosphorylationGGPSNEGTVLPGQSP
CCCCCCCCCCCCCCC		16.8228348404
203PhosphorylationEVLHQIFSKFGTVLK
HHHHHHHHHHCCEEE		28.8024719451
210UbiquitinationSKFGTVLKIITFTKN
HHHCCEEEEEEECCC		27.94-
216AcetylationLKIITFTKNNQFQAL
EEEEEECCCCHHHHH		50.1126051181
216UbiquitinationLKIITFTKNNQFQAL
EEEEEECCCCHHHHH		50.11-
226 (in isoform 1)Ubiquitination-16.9721890473
229UbiquitinationALLQYADPVNAHYAK
HHHHHCCCCCHHHEE		17.0621890473
229UbiquitinationALLQYADPVNAHYAK
HHHHHCCCCCHHHEE		17.0621890473
229 (in isoform 2)Ubiquitination-17.0621890473
233 (in isoform 1)Ubiquitination-20.2021890473
236UbiquitinationPVNAHYAKMALDGQN
CCCHHHEEECCCCCC		19.9621890473
236UbiquitinationPVNAHYAKMALDGQN
CCCHHHEEECCCCCC		19.9621890473
236UbiquitinationPVNAHYAKMALDGQN
CCCHHHEEECCCCCC		19.96-
236 (in isoform 2)Ubiquitination-19.9621890473
257SumoylationTLRIDFSKLTSLNVK
EEEECHHHCCCCEEE		56.64-
257AcetylationTLRIDFSKLTSLNVK
EEEECHHHCCCCEEE		56.6423954790
257MalonylationTLRIDFSKLTSLNVK
EEEECHHHCCCCEEE		56.6426320211
257UbiquitinationTLRIDFSKLTSLNVK
EEEECHHHCCCCEEE		56.64-
257 (in isoform 3)Ubiquitination-56.6421890473
260PhosphorylationIDFSKLTSLNVKYNN
ECHHHCCCCEEEECC		28.5127703031
260 (in isoform 5)Ubiquitination-28.5121890473
263UbiquitinationSKLTSLNVKYNNDKS
HHCCCCEEEECCCCC		9.3821890473
263 (in isoform 4)Ubiquitination-9.3821890473
264SumoylationKLTSLNVKYNNDKSR
HCCCCEEEECCCCCC		40.98-
264AcetylationKLTSLNVKYNNDKSR
HCCCCEEEECCCCCC		40.9823954790
264UbiquitinationKLTSLNVKYNNDKSR
HCCCCEEEECCCCCC		40.9821906983
264 (in isoform 3)Ubiquitination-40.9821890473
265PhosphorylationLTSLNVKYNNDKSRD
CCCCEEEECCCCCCC		18.21-
267 (in isoform 5)Ubiquitination-55.8021890473
269UbiquitinationNVKYNNDKSRDFTRL
EEEECCCCCCCEEEE		49.90-
270UbiquitinationVKYNNDKSRDFTRLD
EEECCCCCCCEEEEE		39.6921890473
270PhosphorylationVKYNNDKSRDFTRLD
EEECCCCCCCEEEEE		39.69-
270 (in isoform 4)Ubiquitination-39.6921890473
328UbiquitinationTGLSVPAVPGALGPL
CCCCCCCCCCCCCCE		3.5321890473
328AcetylationTGLSVPAVPGALGPL
CCCCCCCCCCCCCCE		3.5319608861
328UbiquitinationTGLSVPAVPGALGPL
CCCCCCCCCCCCCCE		3.5319608861
336UbiquitinationPGALGPLTITSSAVT
CCCCCCEEEECCCCC		25.9121890473
354UbiquitinationAIPGASGIPGNSVLL
CCCCCCCCCCCEEEE		3.5121890473
389UbiquitinationYGDVHRVKIMFNKKE
ECCEEEEEEEEECCC		28.54-
392 (in isoform 1)Ubiquitination-16.0721890473
395UbiquitinationVKIMFNKKENALVQM
EEEEEECCCCEEEEE		58.2521890473
395UbiquitinationVKIMFNKKENALVQM
EEEEEECCCCEEEEE		58.2521890473
395AcetylationVKIMFNKKENALVQM
EEEEEECCCCEEEEE		58.2519608861
395UbiquitinationVKIMFNKKENALVQM
EEEEEECCCCEEEEE		58.2519608861
395 (in isoform 2)Ubiquitination-58.2521890473
400 (in isoform 1)Ubiquitination-3.2121890473
403UbiquitinationENALVQMADANQAQL
CCEEEEECCHHHHHH		8.8221890473
403UbiquitinationENALVQMADANQAQL
CCEEEEECCHHHHHH		8.8221890473
403 (in isoform 2)Ubiquitination-8.8221890473
418 (in isoform 1)Ubiquitination-28.9121890473
421UbiquitinationHLSGQRLYGKVLRAT
HHCHHHHHHHHHHHH		19.6521890473
421UbiquitinationHLSGQRLYGKVLRAT
HHCHHHHHHHHHHHH		19.6521890473
421 (in isoform 2)Ubiquitination-19.6521890473
423AcetylationSGQRLYGKVLRATLS
CHHHHHHHHHHHHHC		25.2519608861
423UbiquitinationSGQRLYGKVLRATLS
CHHHHHHHHHHHHHC		25.2521890473
423 (in isoform 3)Ubiquitination-25.2521890473
426AcetylationRLYGKVLRATLSKHQ
HHHHHHHHHHHCHHC		28.6319608861
426UbiquitinationRLYGKVLRATLSKHQ
HHHHHHHHHHHCHHC		28.6319608861
426 (in isoform 5)Ubiquitination-28.6321890473
428PhosphorylationYGKVLRATLSKHQAV
HHHHHHHHHCHHCCE		25.7328857561
429UbiquitinationGKVLRATLSKHQAVQ
HHHHHHHHCHHCCEE		6.6521890473
429AcetylationGKVLRATLSKHQAVQ
HHHHHHHHCHHCCEE		6.6519608861
429UbiquitinationGKVLRATLSKHQAVQ
HHHHHHHHCHHCCEE		6.6519608861
429 (in isoform 4)Ubiquitination-6.6521890473
430PhosphorylationKVLRATLSKHQAVQL
HHHHHHHCHHCCEEC		24.6027067055
431UbiquitinationVLRATLSKHQAVQLP
HHHHHHCHHCCEECC		42.7321890473
431 (in isoform 3)Ubiquitination-42.7321890473
434 (in isoform 1)Ubiquitination-7.25-
434 (in isoform 5)Ubiquitination-7.2521890473
437UbiquitinationSKHQAVQLPREGQED
CHHCCEECCCCCCCC		3.2921890473
437 (in isoform 4)Ubiquitination-3.2921890473
448PhosphorylationGQEDQGLTKDFSNSP
CCCCCCCCCCCCCCC		35.0820068231
449UbiquitinationQEDQGLTKDFSNSPL
CCCCCCCCCCCCCCC		62.9221906983
449 (in isoform 3)Ubiquitination-62.9221890473
452PhosphorylationQGLTKDFSNSPLHRF
CCCCCCCCCCCCCCC		46.6730206219
452 (in isoform 5)Ubiquitination-46.6721890473
454PhosphorylationLTKDFSNSPLHRFKK
CCCCCCCCCCCCCCC		27.8623401153
455UbiquitinationTKDFSNSPLHRFKKP
CCCCCCCCCCCCCCC		36.1121890473
455 (in isoform 4)Ubiquitination-36.1121890473
460PhosphorylationNSPLHRFKKPGSKNF
CCCCCCCCCCCCCCC		59.0020068231
464PhosphorylationHRFKKPGSKNFQNIF
CCCCCCCCCCCCCCC		32.7120068231
472 (in isoform 1)Ubiquitination-20.38-
475 (in isoform 1)Ubiquitination-21.69-
479 (in isoform 1)Ubiquitination-4.76-
503AcetylationIEAGCSVKAFKFFQK
HHCCCEEEEEHHHHH		31.6326051181
503UbiquitinationIEAGCSVKAFKFFQK
HHCCCEEEEEHHHHH		31.63-
506AcetylationGCSVKAFKFFQKDRK
CCEEEEEHHHHHCCC		50.5625825284
506UbiquitinationGCSVKAFKFFQKDRK
CCEEEEEHHHHHCCC		50.56-
510AcetylationKAFKFFQKDRKMALI
EEEHHHHHCCCEEEH		55.1119608861
510UbiquitinationKAFKFFQKDRKMALI
EEEHHHHHCCCEEEH		55.11-
518 (in isoform 1)Ubiquitination-40.3921890473
546PhosphorylationENHHLRVSFSKSTI-
CCCEEEEEEECCCC-		19.8524719451
548PhosphorylationHHLRVSFSKSTI---
CEEEEEEECCCC---		20.4226434776
549AcetylationHLRVSFSKSTI----
EEEEEEECCCC----		50.0025953088
549UbiquitinationHLRVSFSKSTI----
EEEEEEECCCC----		50.0021906983
549 (in isoform 3)Ubiquitination-50.0021890473
550PhosphorylationLRVSFSKSTI-----
EEEEEECCCC-----		30.0920873877
551PhosphorylationRVSFSKSTI------
EEEEECCCC------		34.1520873877
552 (in isoform 5)Ubiquitination-7.3921890473
555 (in isoform 4)Ubiquitination-21890473
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 PTBP3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTBP3_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 PTBP3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
THIOM_HUMANTXN2physical
22939629
CHK1_HUMANCHEK1physical
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 PTBP3_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-257; LYS-264; LYS-423 ANDLYS-549, AND MASS SPECTROMETRY.

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