dbPTM

PTBP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PTBP2_HUMAN	Jmol._Canvas2D (Jmol) "myJmol"[x]
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

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDGIVTEV -------CCCCEEEE	10.85	22814378
16	Phosphorylation	AVGVKRGSDELLSGS ECEEECCCCCHHCCC	31.76	21406692
16 (in isoform 3)	Phosphorylation	-	31.76	21406692
21 (in isoform 3)	Phosphorylation	-	41.46	21406692
21	Phosphorylation	RGSDELLSGSVLSSP CCCCCHHCCCCCCCC	41.46	20068231
23	Phosphorylation	SDELLSGSVLSSPNS CCCHHCCCCCCCCCC	19.26	20068231
26	Phosphorylation	LLSGSVLSSPNSNMS HHCCCCCCCCCCCCC	41.41	20068231
26 (in isoform 3)	Phosphorylation	-	41.41	21406692
27	Phosphorylation	LSGSVLSSPNSNMSS HCCCCCCCCCCCCCE	24.76	20068231
27 (in isoform 3)	Phosphorylation	-	24.76	21406692
30	Phosphorylation	SVLSSPNSNMSSMVV CCCCCCCCCCCEEEE	36.98	20068231
33	Phosphorylation	SSPNSNMSSMVVTAN CCCCCCCCEEEEEEC	21.38	22496350
34	Phosphorylation	SPNSNMSSMVVTANG CCCCCCCEEEEEECC	12.58	20068231
38	Phosphorylation	NMSSMVVTANGNDSK CCCEEEEEECCCCCC	11.73	20068231
44	Phosphorylation	VTANGNDSKKFKGED EEECCCCCCCCCCCC	41.57	20068231
44 (in isoform 3)	Phosphorylation	-	41.57	21406692
65	Ubiquitination	SRVLHIRKLPGEVTE CEEEEEEECCCCCCC	59.43	-
84	Sumoylation	ALGLPFGKVTNILML ECCCCCCCEEEEEEE	46.39	-
90	Sulfoxidation	GKVTNILMLKGKNQA CCEEEEEEECCCCHH	3.00	21406390
92	Ubiquitination	VTNILMLKGKNQAFL EEEEEEECCCCHHHH	54.60	-
92	Acetylation	VTNILMLKGKNQAFL EEEEEEECCCCHHHH	54.60	26051181
127	Phosphorylation	HLRNQPIYIQYSNHK HHHCCCEEEEECCCC	6.67	17360941
130	Phosphorylation	NQPIYIQYSNHKELK CCCEEEEECCCCCCC	11.24	29083192
131	Phosphorylation	QPIYIQYSNHKELKT CCEEEEECCCCCCCC	18.97	29083192
137	Sumoylation	YSNHKELKTDNTLNQ ECCCCCCCCCCHHHH	55.73	-
137	Ubiquitination	YSNHKELKTDNTLNQ ECCCCCCCCCCHHHH	55.73	-
137	Sumoylation	YSNHKELKTDNTLNQ ECCCCCCCCCCHHHH	55.73	-
202	Phosphorylation	DVLHQIFSKFGAVLK HHHHHHHHHHCCEEE	28.80	24719451
215	Sumoylation	LKIITFTKNNQFQAL EEEEEECCCCHHHHH	50.11	-
256	Ubiquitination	TLRIDFSKLVNLNVK EEEECHHHHHCCCCE	57.35	-
269	Phosphorylation	VKYNNDKSRDYTRPD CEECCCCCCCCCCCC	32.99	-
298	Phosphorylation	AAAFAKETSLLAVPG HHHHHHCCCEEECCC	24.78	27251275
299	Phosphorylation	AAFAKETSLLAVPGA HHHHHCCCEEECCCC	23.60	27251275
308	Phosphorylation	LAVPGALSPLAIPNA EECCCCCCCCCCCCH	19.82	28674151
308 (in isoform 2)	Phosphorylation	-	19.82	21406692
313 (in isoform 6)	Phosphorylation	-	20.85	29523821
313 (in isoform 3)	Phosphorylation	-	20.85	29523821
313 (in isoform 4)	Phosphorylation	-	20.85	29523821
372	Phosphorylation	VQRVKILYNKKDSAL CEEEEEEEECCCCEE	28.54	20068231
377	Phosphorylation	ILYNKKDSALIQMAD EEEECCCCEEEEECC	33.58	20068231
388	Phosphorylation	QMADGNQSQLAMNHL EECCCCHHHHHHHHC	31.03	20068231
401	Phosphorylation	HLNGQKMYGKIIRVT HCCCCCCCCEEEEEE	23.46	20068231
429	Ubiquitination	LDDQGLTKDFGNSPL CCCCCCCCCCCCCCC	56.98	-
434	Phosphorylation	LTKDFGNSPLHRFKK CCCCCCCCCCCCCCC	29.26	25159151
444	Phosphorylation	HRFKKPGSKNFQNIF CCCCCCCCCCCCCCC	32.71	20068231
473	Phosphorylation	VAEEDLRTLFANTGG CCHHHHHHHHHHCCC	33.26	30377224
478	Phosphorylation	LRTLFANTGGTVKAF HHHHHHHCCCCEEEE	33.29	24719451
481	Phosphorylation	LFANTGGTVKAFKFF HHHHCCCCEEEEEHH	21.85	30377224
483	Ubiquitination	ANTGGTVKAFKFFQD HHCCCCEEEEEHHHH	48.20	-
525	Phosphorylation	ENHHLRVSFSKSTI- CCCEEEEEEECCCC-	19.85	24719451
527	Phosphorylation	HHLRVSFSKSTI--- CEEEEEEECCCC---	20.42	26434776
528 (in isoform 1)	Ubiquitination	-	50.00	21906983
528	Ubiquitination	HLRVSFSKSTI---- EEEEEEECCCC----	50.00	-
528	Acetylation	HLRVSFSKSTI---- EEEEEEECCCC----	50.00	21672273
529 (in isoform 2)	Ubiquitination	-	30.09	21906983
529	Phosphorylation	LRVSFSKSTI----- EEEEEECCCC-----	30.09	20873877
530	Phosphorylation	RVSFSKSTI------ EEEEECCCC------	34.15	20873877
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
UB2E2_HUMAN	UBE2E2	physical	22939629
SNRPA_HUMAN	SNRPA	physical	22365833
PUF60_HUMAN	PUF60	physical	22365833
RBM10_HUMAN	RBM10	physical	22365833
ELAV1_HUMAN	ELAVL1	physical	22365833
HNRPC_HUMAN	HNRNPC	physical	22365833
ROAA_HUMAN	HNRNPAB	physical	22365833
RBM4_HUMAN	RBM4	physical	22365833
MATR3_HUMAN	MATR3	physical	22365833
HNRPD_HUMAN	HNRNPD	physical	22365833
QKI_HUMAN	QKI	physical	22365833
KHDR3_HUMAN	KHDRBS3	physical	22365833
KHDR1_HUMAN	KHDRBS1	physical	22365833
TOM1_HUMAN	TOM1	physical	21988832
PTBP2_HUMAN	PTBP2	physical	25416956
MATR3_HUMAN	MATR3	physical	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

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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.	19413330 [Abstract]