dbPTM

PCBP1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PCBP1_MOUSE
UniProt AC	P60335
Protein Name	Poly(rC)-binding protein 1
Gene Name	Pcbp1
Organism	Mus musculus (Mouse).
Sequence Length	356
Subcellular Localization	Nucleus.
Protein Description	Single-stranded nucleic acid binding protein that binds preferentially to oligo dC..
Protein Sequence	MDAGVTESGLNVTLTIRLLMHGKEVGSIIGKKGESVKRIREESGARINISEGNCPERIITLTGPTNAIFKAFAMIIDKLEEDINSSMTNSTAASRPPVTLRLVVPATQCGSLIGKGGCKIKEIRESTGAQVQVAGDMLPNSTERAITIAGVPQSVTECVKQICLVMLETLSQSPQGRVMTIPYQPMPASSPVICAGGQDRCSDAAGYPHATHDLEGPPLDAYSIQGQHTISPLDLAKLNQVARQQSHFAMMHGGTGFAGIDSSSPEVKGYWASLDASTQTTHELTIPNNLIGCIIGRQGANINEIRQMSGAQIKIANPVEGSSGRQVTITGSAASISLAQYLINARLSSEKGMGCS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDAGVTES -------CCCCCCCC	7.81	-
23	Acetylation	IRLLMHGKEVGSIIG EEHHHCCHHHHHHCC	34.25	22638041
23	Ubiquitination	IRLLMHGKEVGSIIG EEHHHCCHHHHHHCC	34.25	-
23	Malonylation	IRLLMHGKEVGSIIG EEHHHCCHHHHHHCC	34.25	26320211
31	Malonylation	EVGSIIGKKGESVKR HHHHHCCCCCCHHHH	47.39	26320211
43	Phosphorylation	VKRIREESGARINIS HHHHHHHHCCCEEEC	32.76	20154680
50	Phosphorylation	SGARINISEGNCPER HCCCEEECCCCCCCE	34.66	-
54	S-nitrosocysteine	INISEGNCPERIITL EEECCCCCCCEEEEE	5.64	-
54	Glutathionylation	INISEGNCPERIITL EEECCCCCCCEEEEE	5.64	24333276
54	S-nitrosylation	INISEGNCPERIITL EEECCCCCCCEEEEE	5.64	20925432
54	S-palmitoylation	INISEGNCPERIITL EEECCCCCCCEEEEE	5.64	28526873
109	S-nitrosocysteine	LVVPATQCGSLIGKG EEEEHHHHHHHCCCC	3.29	-
109	Glutathionylation	LVVPATQCGSLIGKG EEEEHHHHHHHCCCC	3.29	24333276
109	S-nitrosylation	LVVPATQCGSLIGKG EEEEHHHHHHHCCCC	3.29	24895380
109	S-palmitoylation	LVVPATQCGSLIGKG EEEEHHHHHHHCCCC	3.29	28526873
115	Acetylation	QCGSLIGKGGCKIKE HHHHHCCCCCCEEEH	45.17	23806337
115	Malonylation	QCGSLIGKGGCKIKE HHHHHCCCCCCEEEH	45.17	26320211
115	Ubiquitination	QCGSLIGKGGCKIKE HHHHHCCCCCCEEEH	45.17	-
118	Glutathionylation	SLIGKGGCKIKEIRE HHCCCCCCEEEHHHH	5.85	24333276
158	S-palmitoylation	VPQSVTECVKQICLV CCHHHHHHHHHHHHH	3.19	28526873
158	S-nitrosylation	VPQSVTECVKQICLV CCHHHHHHHHHHHHH	3.19	21278135
158	S-nitrosocysteine	VPQSVTECVKQICLV CCHHHHHHHHHHHHH	3.19	-
163	Glutathionylation	TECVKQICLVMLETL HHHHHHHHHHHHHHH	1.86	24333276
163	S-palmitoylation	TECVKQICLVMLETL HHHHHHHHHHHHHHH	1.86	28526873
169	Phosphorylation	ICLVMLETLSQSPQG HHHHHHHHHCCCCCC	27.96	24925903
171	Phosphorylation	LVMLETLSQSPQGRV HHHHHHHCCCCCCCE	35.71	24925903
173	Phosphorylation	MLETLSQSPQGRVMT HHHHHCCCCCCCEEE	18.80	24925903
180	Phosphorylation	SPQGRVMTIPYQPMP CCCCCEEEECCCCCC	18.88	24925903
183	Phosphorylation	GRVMTIPYQPMPASS CCEEEECCCCCCCCC	22.77	24925903
189	Phosphorylation	PYQPMPASSPVICAG CCCCCCCCCCEEEEC	29.33	24925903
190	Phosphorylation	YQPMPASSPVICAGG CCCCCCCCCEEEECC	25.87	24925903
194	S-palmitoylation	PASSPVICAGGQDRC CCCCCEEEECCCCHH	2.68	28526873
194	Glutathionylation	PASSPVICAGGQDRC CCCCCEEEECCCCHH	2.68	24333276
201	Glutathionylation	CAGGQDRCSDAAGYP EECCCCHHHCCCCCC	6.09	24333276
202	Phosphorylation	AGGQDRCSDAAGYPH ECCCCHHHCCCCCCC	31.04	25777480
207	Phosphorylation	RCSDAAGYPHATHDL HHHCCCCCCCCCCCC	6.26	25159016
211	Phosphorylation	AAGYPHATHDLEGPP CCCCCCCCCCCCCCC	16.94	25777480
222	Phosphorylation	EGPPLDAYSIQGQHT CCCCCCCEEECCCCC	13.13	25159016
223	Phosphorylation	GPPLDAYSIQGQHTI CCCCCCEEECCCCCC	15.34	25159016
229	Phosphorylation	YSIQGQHTISPLDLA EEECCCCCCCHHHHH	18.43	25159016
231	Phosphorylation	IQGQHTISPLDLAKL ECCCCCCCHHHHHHH	22.14	22942356
237	Ubiquitination	ISPLDLAKLNQVARQ CCHHHHHHHHHHHHH	56.09	22790023
246	Phosphorylation	NQVARQQSHFAMMHG HHHHHHHHCHHHCCC	16.54	22942356
255	Phosphorylation	FAMMHGGTGFAGIDS HHHCCCCCCCCCCCC	33.45	27742792
262	Phosphorylation	TGFAGIDSSSPEVKG CCCCCCCCCCCCCCE	30.69	25521595
263	Phosphorylation	GFAGIDSSSPEVKGY CCCCCCCCCCCCCEE	46.28	25521595
264	Phosphorylation	FAGIDSSSPEVKGYW CCCCCCCCCCCCEEE	29.09	25521595
270	Phosphorylation	SSPEVKGYWASLDAS CCCCCCEEEEEECCC	7.65	26643407
273	Phosphorylation	EVKGYWASLDASTQT CCCEEEEEECCCCCC	16.79	26643407
277	Phosphorylation	YWASLDASTQTTHEL EEEEECCCCCCEEEE	22.25	26643407
278	Phosphorylation	WASLDASTQTTHELT EEEECCCCCCEEEEE	31.49	26643407
280	Phosphorylation	SLDASTQTTHELTIP EECCCCCCEEEEECC	30.15	26643407
281	Phosphorylation	LDASTQTTHELTIPN ECCCCCCEEEEECCC	11.97	26643407
293	Glutathionylation	IPNNLIGCIIGRQGA CCCCEEHHHHCCCCC	1.30	24333276
309	Phosphorylation	INEIRQMSGAQIKIA HHHHHHHCCCEEEEC	23.73	29514104
314	Ubiquitination	QMSGAQIKIANPVEG HHCCCEEEECCCCCC	24.56	22790023
322	Phosphorylation	IANPVEGSSGRQVTI ECCCCCCCCCCEEEE	19.00	28066266
323	Phosphorylation	ANPVEGSSGRQVTIT CCCCCCCCCCEEEEE	49.18	28066266
328	Phosphorylation	GSSGRQVTITGSAAS CCCCCEEEEECCHHH	12.41	30352176
332	Phosphorylation	RQVTITGSAASISLA CEEEEECCHHHHHHH	16.41	30352176
351	Ubiquitination	NARLSSEKGMGCS-- HHHHHCCCCCCCC--	57.03	-
355	Glutathionylation	SSEKGMGCS------ HCCCCCCCC------	3.03	24333276
356	Phosphorylation	SEKGMGCS------- CCCCCCCC-------	37.21	-

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
43	S	Phosphorylation	Kinase	AKT1	P31749	PSP
43	S	Phosphorylation	Kinase	AKT2	P31751	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PCBP1_MOUSE !!

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 PCBP1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
IL6_MOUSE	Il6	physical	17383969

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PCBP1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASSSPECTROMETRY.	19131326 [Abstract]