dbPTM

PCBP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PCBP1_HUMAN
UniProt AC	Q15365
Protein Name	Poly(rC)-binding protein 1
Gene Name	PCBP1
Organism	Homo sapiens (Human).
Sequence Length	356
Subcellular Localization	Nucleus. Cytoplasm. Loosely bound in the nucleus. May shuttle between the nucleus and the cytoplasm.
Protein Description	Single-stranded nucleic acid binding protein that binds preferentially to oligo dC. In case of infection by poliovirus, plays a role in initiation of viral RNA replication in concert with the viral protein 3CD. [PubMed: 12414943]
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	22814378
23	Sumoylation	IRLLMHGKEVGSIIG EEHHHCCHHHHHHCC	34.25	19608861
23	Sumoylation	IRLLMHGKEVGSIIG EEHHHCCHHHHHHCC	34.25	-
23	Acetylation	IRLLMHGKEVGSIIG EEHHHCCHHHHHHCC	34.25	22638039
23	Ubiquitination	IRLLMHGKEVGSIIG EEHHHCCHHHHHHCC	34.25	21890473
27	Phosphorylation	MHGKEVGSIIGKKGE HCCHHHHHHCCCCCC	19.06	30108239
31	Sumoylation	EVGSIIGKKGESVKR HHHHHCCCCCCHHHH	47.39	-
31	Sumoylation	EVGSIIGKKGESVKR HHHHHCCCCCCHHHH	47.39	-
31	Acetylation	EVGSIIGKKGESVKR HHHHHCCCCCCHHHH	47.39	26051181
31	Ubiquitination	EVGSIIGKKGESVKR HHHHHCCCCCCHHHH	47.39	21906983
32	Ubiquitination	VGSIIGKKGESVKRI HHHHCCCCCCHHHHH	63.80	21890473
35	Phosphorylation	IIGKKGESVKRIREE HCCCCCCHHHHHHHH	41.42	-
37	Acetylation	GKKGESVKRIREESG CCCCCHHHHHHHHHC	51.92	24848933
43	Phosphorylation	VKRIREESGARINIS HHHHHHHHCCCEEEC	32.76	-
50	Phosphorylation	SGARINISEGNCPER HCCCEEECCCCCCCE	34.66	21815630
54	Glutathionylation	INISEGNCPERIITL EEECCCCCCCEEEEE	5.64	22555962
54	S-palmitoylation	INISEGNCPERIITL EEECCCCCCCEEEEE	5.64	29575903
60	Phosphorylation	NCPERIITLTGPTNA CCCCEEEEEECHHHH	18.85	22817900
74	Sulfoxidation	AIFKAFAMIIDKLEE HHHHHHHHHHHHHHH	1.92	30846556
85	Phosphorylation	KLEEDINSSMTNSTA HHHHHHHHHCCCCCC	23.09	25850435
86	Phosphorylation	LEEDINSSMTNSTAA HHHHHHHHCCCCCCC	25.74	25850435
87	Sulfoxidation	EEDINSSMTNSTAAS HHHHHHHCCCCCCCC	4.06	30846556
88	Phosphorylation	EDINSSMTNSTAASR HHHHHHCCCCCCCCC	28.15	25850435
90	Phosphorylation	INSSMTNSTAASRPP HHHHCCCCCCCCCCC	15.40	25850435
91	Phosphorylation	NSSMTNSTAASRPPV HHHCCCCCCCCCCCE	28.45	25850435
99	Phosphorylation	AASRPPVTLRLVVPA CCCCCCEEEEEEEEH	16.37	-
107	Phosphorylation	LRLVVPATQCGSLIG EEEEEEHHHHHHHCC	20.51	28450419
109	Glutathionylation	LVVPATQCGSLIGKG EEEEHHHHHHHCCCC	3.29	22555962
109	S-nitrosylation	LVVPATQCGSLIGKG EEEEHHHHHHHCCCC	3.29	2212679
109	S-palmitoylation	LVVPATQCGSLIGKG EEEEHHHHHHHCCCC	3.29	29575903
111	Phosphorylation	VPATQCGSLIGKGGC EEHHHHHHHCCCCCC	25.17	28450419
115	Malonylation	QCGSLIGKGGCKIKE HHHHHCCCCCCEEEH	45.17	26320211
115	Sumoylation	QCGSLIGKGGCKIKE HHHHHCCCCCCEEEH	45.17	-
115	Ubiquitination	QCGSLIGKGGCKIKE HHHHHCCCCCCEEEH	45.17	21906983
115	Acetylation	QCGSLIGKGGCKIKE HHHHHCCCCCCEEEH	45.17	25953088
115	Sumoylation	QCGSLIGKGGCKIKE HHHHHCCCCCCEEEH	45.17	28112733
119	Ubiquitination	LIGKGGCKIKEIRES HCCCCCCEEEHHHHH	61.15	-
126	Phosphorylation	KIKEIRESTGAQVQV EEEHHHHHHCCEEEE	23.46	25627689
127	Phosphorylation	IKEIRESTGAQVQVA EEHHHHHHCCEEEEE	31.61	25159151
137	Sulfoxidation	QVQVAGDMLPNSTER EEEEECCCCCCCCCC	7.02	30846556
147	Phosphorylation	NSTERAITIAGVPQS CCCCCCEECCCCCHH	12.09	29496963
147	O-linked_Glycosylation	NSTERAITIAGVPQS CCCCCCEECCCCCHH	12.09	OGP
154	Phosphorylation	TIAGVPQSVTECVKQ ECCCCCHHHHHHHHH	25.57	21712546
156	O-linked_Glycosylation	AGVPQSVTECVKQIC CCCCHHHHHHHHHHH	28.99	OGP
158	Glutathionylation	VPQSVTECVKQICLV CCHHHHHHHHHHHHH	3.19	22555962
158	S-palmitoylation	VPQSVTECVKQICLV CCHHHHHHHHHHHHH	3.19	26865113
169	Phosphorylation	ICLVMLETLSQSPQG HHHHHHHHHCCCCCC	27.96	23927012
171	Phosphorylation	LVMLETLSQSPQGRV HHHHHHHCCCCCCCE	35.71	22167270
173	Phosphorylation	MLETLSQSPQGRVMT HHHHHCCCCCCCEEE	18.80	29255136
180	Phosphorylation	SPQGRVMTIPYQPMP CCCCCEEEECCCCCC	18.88	21945579
183	Nitration	GRVMTIPYQPMPASS CCEEEECCCCCCCCC	22.77	-
183	Phosphorylation	GRVMTIPYQPMPASS CCEEEECCCCCCCCC	22.77	23401153
189	Phosphorylation	PYQPMPASSPVICAG CCCCCCCCCCEEEEC	29.33	29255136
190	Phosphorylation	YQPMPASSPVICAGG CCCCCCCCCEEEECC	25.87	29255136
194	Glutathionylation	PASSPVICAGGQDRC CCCCCEEEECCCCHH	2.68	22555962
202	Phosphorylation	AGGQDRCSDAAGYPH ECCCCHHHCCCCCCC	31.04	28387310
207	Phosphorylation	RCSDAAGYPHATHDL HHHCCCCCCCCCCCC	6.26	28152594
211	Phosphorylation	AAGYPHATHDLEGPP CCCCCCCCCCCCCCC	16.94	28152594
222	Phosphorylation	EGPPLDAYSIQGQHT CCCCCCCEEECCCCC	13.13	21082442
223	Phosphorylation	GPPLDAYSIQGQHTI CCCCCCEEECCCCCC	15.34	23401153
229	Phosphorylation	YSIQGQHTISPLDLA EEECCCCCCCHHHHH	18.43	25159151
231	Phosphorylation	IQGQHTISPLDLAKL ECCCCCCCHHHHHHH	22.14	25159151
237	Ubiquitination	ISPLDLAKLNQVARQ CCHHHHHHHHHHHHH	56.09	-
246	Phosphorylation	NQVARQQSHFAMMHG HHHHHHHHCHHHCCC	16.54	28176443
250	Sulfoxidation	RQQSHFAMMHGGTGF HHHHCHHHCCCCCCC	1.67	30846556
251	Sulfoxidation	QQSHFAMMHGGTGFA HHHCHHHCCCCCCCC	2.08	30846556
255	Phosphorylation	FAMMHGGTGFAGIDS HHHCCCCCCCCCCCC	33.45	28176443
262	Phosphorylation	TGFAGIDSSSPEVKG CCCCCCCCCCCCCCE	30.69	25159151
263	Phosphorylation	GFAGIDSSSPEVKGY CCCCCCCCCCCCCEE	46.28	28176443
264	Phosphorylation	FAGIDSSSPEVKGYW CCCCCCCCCCCCEEE	29.09	25159151
268	Sumoylation	DSSSPEVKGYWASLD CCCCCCCCEEEEEEC	44.62	-
270	Phosphorylation	SSPEVKGYWASLDAS CCCCCCEEEEEECCC	7.65	26074081
273	Phosphorylation	EVKGYWASLDASTQT CCCEEEEEECCCCCC	16.79	28112733
277	Phosphorylation	YWASLDASTQTTHEL EEEEECCCCCCEEEE	22.25	24275569
280	Phosphorylation	SLDASTQTTHELTIP EECCCCCCEEEEECC	30.15	27251275
281	Phosphorylation	LDASTQTTHELTIPN ECCCCCCEEEEECCC	11.97	28348404
306	Methylation	GANINEIRQMSGAQI CCCHHHHHHHCCCEE	21.70	-
308	Sulfoxidation	NINEIRQMSGAQIKI CHHHHHHHCCCEEEE	2.61	28183972
309	Phosphorylation	INEIRQMSGAQIKIA HHHHHHHCCCEEEEC	23.73	28857561
314	Sumoylation	QMSGAQIKIANPVEG HHCCCEEEECCCCCC	24.56	-
314	Sumoylation	QMSGAQIKIANPVEG HHCCCEEEECCCCCC	24.56	-
314	Ubiquitination	QMSGAQIKIANPVEG HHCCCEEEECCCCCC	24.56	21890473
322	Phosphorylation	IANPVEGSSGRQVTI ECCCCCCCCCCEEEE	19.00	30108239
323	Phosphorylation	ANPVEGSSGRQVTIT CCCCCCCCCCEEEEE	49.18	25159151
328	Phosphorylation	GSSGRQVTITGSAAS CCCCCEEEEECCHHH	12.41	28857561
328	O-linked_Glycosylation	GSSGRQVTITGSAAS CCCCCEEEEECCHHH	12.41	23301498
330	O-linked_Glycosylation	SGRQVTITGSAASIS CCCEEEEECCHHHHH	18.73	23301498
330	Phosphorylation	SGRQVTITGSAASIS CCCEEEEECCHHHHH	18.73	20068231
332	Phosphorylation	RQVTITGSAASISLA CEEEEECCHHHHHHH	16.41	26657352
335	Phosphorylation	TITGSAASISLAQYL EEECCHHHHHHHHHH	16.66	24719451
337	Phosphorylation	TGSAASISLAQYLIN ECCHHHHHHHHHHHH	18.37	20068231
341	Phosphorylation	ASISLAQYLINARLS HHHHHHHHHHHHHHH	12.16	20068231
351	Acetylation	NARLSSEKGMGCS-- HHHHHCCCCCCCC--	57.03	23749302
351	Ubiquitination	NARLSSEKGMGCS-- HHHHHCCCCCCCC--	57.03	21890473
356	Phosphorylation	SEKGMGCS------- CCCCCCCC-------	37.21	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
60	T	Phosphorylation	Kinase	PAK1	Q13153	PSP
127	T	Phosphorylation	Kinase	PAK1	Q13153	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PCBP1_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 PCBP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HNRPD_HUMAN	HNRNPD	physical	10373504
PABP1_HUMAN	PABPC1	physical	10373504
LMNA_HUMAN	LMNA	physical	16248985
PCGF2_HUMAN	PCGF2	physical	19727227
LMNA_HUMAN	LMNA	physical	19727227
EWS_HUMAN	EWSR1	physical	16713569
PDLI7_HUMAN	PDLIM7	physical	16713569
PTBP1_HUMAN	PTBP1	physical	16713569
HNRLL_HUMAN	HNRNPLL	physical	16713569
MATR3_HUMAN	MATR3	physical	16713569
RBM42_HUMAN	RBM42	physical	16713569
NOVA1_HUMAN	NOVA1	physical	16713569
PCBP4_HUMAN	PCBP4	physical	16713569
RBM11_HUMAN	RBM11	physical	16713569
SRSF3_HUMAN	SRSF3	physical	16713569
PCBP2_HUMAN	PCBP2	physical	16713569
T22D4_HUMAN	TSC22D4	physical	16713569
UGPA_HUMAN	UGP2	physical	16713569
CELF2_HUMAN	CELF2	physical	16713569
HNRPK_HUMAN	HNRNPK	physical	16713569
QKI_HUMAN	QKI	physical	16713569
RALY_HUMAN	RALY	physical	16713569
PUF60_HUMAN	PUF60	physical	16713569
CELF3_HUMAN	CELF3	physical	16713569
A4_HUMAN	APP	physical	21832049
TADBP_HUMAN	TARDBP	physical	22939629
PRP8_HUMAN	PRPF8	physical	22365833
PRPF3_HUMAN	PRPF3	physical	22365833
PPIL3_HUMAN	PPIL3	physical	22365833
PPIG_HUMAN	PPIG	physical	22365833
ZN830_HUMAN	ZNF830	physical	22365833
ZCH10_HUMAN	ZCCHC10	physical	22365833
HMGA1_HUMAN	HMGA1	physical	18850631
SNRPA_HUMAN	SNRPA	physical	25416956
PK3CB_HUMAN	PIK3CB	physical	26186194
HS90A_HUMAN	HSP90AA1	physical	26186194
HS90B_HUMAN	HSP90AB1	physical	26186194
CDC37_HUMAN	CDC37	physical	26186194
PK3CA_HUMAN	PIK3CA	physical	26186194
P85A_HUMAN	PIK3R1	physical	26186194
MET_HUMAN	MET	physical	26186194
FRK_HUMAN	FRK	physical	26186194
POLH_HUMAN	POLH	physical	25268038
CDK1_HUMAN	CDK1	physical	26344197
COF1_HUMAN	CFL1	physical	26344197
CRIP1_HUMAN	CRIP1	physical	26344197
FAHD1_HUMAN	FAHD1	physical	26344197
MIF_HUMAN	MIF	physical	26344197
PCBP2_HUMAN	PCBP2	physical	26344197
PIPNB_HUMAN	PITPNB	physical	26344197
RBM12_HUMAN	RBM12	physical	26344197
TALDO_HUMAN	TALDO1	physical	26344197
TRIA1_HUMAN	TRIAP1	physical	26344197
FRK_HUMAN	FRK	physical	28514442
PK3CA_HUMAN	PIK3CA	physical	28514442
PK3CB_HUMAN	PIK3CB	physical	28514442
MET_HUMAN	MET	physical	28514442
CRBB1_HUMAN	CRYBB1	physical	28514442
P85A_HUMAN	PIK3R1	physical	28514442
CDC37_HUMAN	CDC37	physical	28514442
HS90A_HUMAN	HSP90AA1	physical	28514442
HS90B_HUMAN	HSP90AB1	physical	28514442
TRI56_HUMAN	TRIM56	physical	28963376
PML_HUMAN	PML	physical	28963376
UBE3C_HUMAN	UBE3C	physical	28963376
SMUF1_HUMAN	SMURF1	physical	28963376
SKP1_HUMAN	SKP1	physical	28963376
TRI25_HUMAN	TRIM25	physical	28963376
TIF1B_HUMAN	TRIM28	physical	28963376
UBE4A_HUMAN	UBE4A	physical	28963376
CHIP_HUMAN	STUB1	physical	28963376
FOXN2_HUMAN	FOXN2	physical	28963376

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 PCBP1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-190, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"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-173, AND MASSSPECTROMETRY.	19369195 [Abstract]
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND SER-190, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"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-173 AND SER-190, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"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-173 AND SER-190, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-264, ANDMASS SPECTROMETRY.	19007248 [Abstract]
"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-173; SER-246; SER-262;SER-263 AND SER-264, AND MASS SPECTROMETRY.	17924679 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASSSPECTROMETRY.	17081983 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND MASSSPECTROMETRY.	15302935 [Abstract]