PTBP2_HUMAN - dbPTM
PTBP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTBP2_HUMAN
UniProt AC Q9UKA9
Protein Name Polypyrimidine tract-binding protein 2
Gene Name PTBP2
Organism Homo sapiens (Human).
Sequence Length 531
Subcellular Localization Nucleus.
Protein Description RNA-binding protein which binds to intronic polypyrimidine tracts and mediates negative regulation of exons splicing. May antagonize in a tissue-specific manner the ability of NOVA1 to activate exon selection. In addition to its function in pre-mRNA splicing, plays also a role in the regulation of translation. Isoform 5 has a reduced affinity for RNA..
Protein Sequence MDGIVTEVAVGVKRGSDELLSGSVLSSPNSNMSSMVVTANGNDSKKFKGEDKMDGAPSRVLHIRKLPGEVTETEVIALGLPFGKVTNILMLKGKNQAFLELATEEAAITMVNYYSAVTPHLRNQPIYIQYSNHKELKTDNTLNQRAQAVLQAVTAVQTANTPLSGTTVSESAVTPAQSPVLRIIIDNMYYPVTLDVLHQIFSKFGAVLKIITFTKNNQFQALLQYGDPVNAQQAKLALDGQNIYNACCTLRIDFSKLVNLNVKYNNDKSRDYTRPDLPSGDGQPALDPAIAAAFAKETSLLAVPGALSPLAIPNAAAAAAAAAAGRVGMPGVSAGGNTVLLVSNLNEEMVTPQSLFTLFGVYGDVQRVKILYNKKDSALIQMADGNQSQLAMNHLNGQKMYGKIIRVTLSKHQTVQLPREGLDDQGLTKDFGNSPLHRFKKPGSKNFQNIFPPSATLHLSNIPPSVAEEDLRTLFANTGGTVKAFKFFQDHKMALLQMATVEEAIQALIDLHNYNLGENHHLRVSFSKSTI
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-------MDGIVTEV
-------CCCCEEEE		10.8522814378
16PhosphorylationAVGVKRGSDELLSGS
ECEEECCCCCHHCCC		31.7621406692
16 (in isoform 3)Phosphorylation-31.7621406692
21 (in isoform 3)Phosphorylation-41.4621406692
21PhosphorylationRGSDELLSGSVLSSP
CCCCCHHCCCCCCCC		41.4620068231
23PhosphorylationSDELLSGSVLSSPNS
CCCHHCCCCCCCCCC		19.2620068231
26PhosphorylationLLSGSVLSSPNSNMS
HHCCCCCCCCCCCCC		41.4120068231
26 (in isoform 3)Phosphorylation-41.4121406692
27PhosphorylationLSGSVLSSPNSNMSS
HCCCCCCCCCCCCCE		24.7620068231
27 (in isoform 3)Phosphorylation-24.7621406692
30PhosphorylationSVLSSPNSNMSSMVV
CCCCCCCCCCCEEEE		36.9820068231
33PhosphorylationSSPNSNMSSMVVTAN
CCCCCCCCEEEEEEC		21.3822496350
34PhosphorylationSPNSNMSSMVVTANG
CCCCCCCEEEEEECC		12.5820068231
38PhosphorylationNMSSMVVTANGNDSK
CCCEEEEEECCCCCC		11.7320068231
44PhosphorylationVTANGNDSKKFKGED
EEECCCCCCCCCCCC		41.5720068231
44 (in isoform 3)Phosphorylation-41.5721406692
65UbiquitinationSRVLHIRKLPGEVTE
CEEEEEEECCCCCCC		59.43-
84SumoylationALGLPFGKVTNILML
ECCCCCCCEEEEEEE		46.39-
90SulfoxidationGKVTNILMLKGKNQA
CCEEEEEEECCCCHH		3.0021406390
92UbiquitinationVTNILMLKGKNQAFL
EEEEEEECCCCHHHH		54.60-
92AcetylationVTNILMLKGKNQAFL
EEEEEEECCCCHHHH		54.6026051181
127PhosphorylationHLRNQPIYIQYSNHK
HHHCCCEEEEECCCC		6.6717360941
130PhosphorylationNQPIYIQYSNHKELK
CCCEEEEECCCCCCC		11.2429083192
131PhosphorylationQPIYIQYSNHKELKT
CCEEEEECCCCCCCC		18.9729083192
137SumoylationYSNHKELKTDNTLNQ
ECCCCCCCCCCHHHH		55.73-
137UbiquitinationYSNHKELKTDNTLNQ
ECCCCCCCCCCHHHH		55.73-
137SumoylationYSNHKELKTDNTLNQ
ECCCCCCCCCCHHHH		55.73-
202PhosphorylationDVLHQIFSKFGAVLK
HHHHHHHHHHCCEEE		28.8024719451
215SumoylationLKIITFTKNNQFQAL
EEEEEECCCCHHHHH		50.11-
256UbiquitinationTLRIDFSKLVNLNVK
EEEECHHHHHCCCCE		57.35-
269PhosphorylationVKYNNDKSRDYTRPD
CEECCCCCCCCCCCC		32.99-
298PhosphorylationAAAFAKETSLLAVPG
HHHHHHCCCEEECCC		24.7827251275
299PhosphorylationAAFAKETSLLAVPGA
HHHHHCCCEEECCCC		23.6027251275
308PhosphorylationLAVPGALSPLAIPNA
EECCCCCCCCCCCCH		19.8228674151
308 (in isoform 2)Phosphorylation-19.8221406692
313 (in isoform 6)Phosphorylation-20.8529523821
313 (in isoform 3)Phosphorylation-20.8529523821
313 (in isoform 4)Phosphorylation-20.8529523821
372PhosphorylationVQRVKILYNKKDSAL
CEEEEEEEECCCCEE		28.5420068231
377PhosphorylationILYNKKDSALIQMAD
EEEECCCCEEEEECC		33.5820068231
388PhosphorylationQMADGNQSQLAMNHL
EECCCCHHHHHHHHC		31.0320068231
401PhosphorylationHLNGQKMYGKIIRVT
HCCCCCCCCEEEEEE		23.4620068231
429UbiquitinationLDDQGLTKDFGNSPL
CCCCCCCCCCCCCCC		56.98-
434PhosphorylationLTKDFGNSPLHRFKK
CCCCCCCCCCCCCCC		29.2625159151
444PhosphorylationHRFKKPGSKNFQNIF
CCCCCCCCCCCCCCC		32.7120068231
473PhosphorylationVAEEDLRTLFANTGG
CCHHHHHHHHHHCCC		33.2630377224
478PhosphorylationLRTLFANTGGTVKAF
HHHHHHHCCCCEEEE		33.2924719451
481PhosphorylationLFANTGGTVKAFKFF
HHHHCCCCEEEEEHH		21.8530377224
483UbiquitinationANTGGTVKAFKFFQD
HHCCCCEEEEEHHHH		48.20-
525PhosphorylationENHHLRVSFSKSTI-
CCCEEEEEEECCCC-		19.8524719451
527PhosphorylationHHLRVSFSKSTI---
CEEEEEEECCCC---		20.4226434776
528 (in isoform 1)Ubiquitination-50.0021906983
528UbiquitinationHLRVSFSKSTI----
EEEEEEECCCC----		50.00-
528AcetylationHLRVSFSKSTI----
EEEEEEECCCC----		50.0021672273
529 (in isoform 2)Ubiquitination-30.0921906983
529PhosphorylationLRVSFSKSTI-----
EEEEEECCCC-----		30.0920873877
530PhosphorylationRVSFSKSTI------
EEEEECCCC------		34.1520873877
533 (in isoform 4)Ubiquitination-21906983
545 (in isoform 3)Ubiquitination-21906983
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 PTBP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTBP2_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 PTBP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UB2E2_HUMANUBE2E2physical
22939629
SNRPA_HUMANSNRPAphysical
22365833
PUF60_HUMANPUF60physical
22365833
RBM10_HUMANRBM10physical
22365833
ELAV1_HUMANELAVL1physical
22365833
HNRPC_HUMANHNRNPCphysical
22365833
ROAA_HUMANHNRNPABphysical
22365833
RBM4_HUMANRBM4physical
22365833
MATR3_HUMANMATR3physical
22365833
HNRPD_HUMANHNRNPDphysical
22365833
QKI_HUMANQKIphysical
22365833
KHDR3_HUMANKHDRBS3physical
22365833
KHDR1_HUMANKHDRBS1physical
22365833
TOM1_HUMANTOM1physical
21988832
PTBP2_HUMANPTBP2physical
25416956
MATR3_HUMANMATR3physical
21516116
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 PTBP2_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.

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