PCBP3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PCBP3_HUMAN
• UniProt AC: P57721
• Protein Name: Poly(rC)-binding protein 3
• Gene Name: PCBP3 {ECO:0000312|HGNC:HGNC:8651}
• Organism: Homo sapiens (Human).
• Sequence Length: 371
• Subcellular Localization: Cytoplasm .
• Protein Description: Single-stranded nucleic acid binding protein that binds preferentially to oligo dC..
• Protein Sequence: MGEGDAFWAPSVLPHSTLSTLSHHPQPQFGRRMESKVSEGGLNVTLTIRLLMHGKEVGSIIGKKGETVKKMREESGARINISEGNCPERIVTITGPTDAIFKAFAMIAYKFEEDIINSMSNSPATSKPPVTLRLVVPASQCGSLIGKGGSKIKEIRESTGAQVQVAGDMLPNSTERAVTISGTPDAIIQCVKQICVVMLESPPKGATIPYRPKPASTPVIFAGGQAYTIQGQYAIPHPDQLTKLHQLAMQQTPFPPLGQTNPAFPGEKLPLHSSEEAQNLMGQSSGLDASPPASTHELTIPNDLIGCIIGRQGTKINEIRQMSGAQIKIANATEGSSERQITITGTPANISLAQYLINARLTSEVTGMGTL

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
23 (in isoform 3)	Ubiquitination	-	39.50	21890473
23	Ubiquitination	STLSTLSHHPQPQFG CHHHHHCCCCCCCCC	39.50	30230243
31 (in isoform 3)	Ubiquitination	-	35.74	21890473
31	Ubiquitination	HPQPQFGRRMESKVS CCCCCCCCCCCCCCC	35.74	32015554
38	Phosphorylation	RRMESKVSEGGLNVT CCCCCCCCCCCCEEE	33.97	22210691
45	Phosphorylation	SEGGLNVTLTIRLLM CCCCCEEEEEEEHHH	19.67	22210691
47	Phosphorylation	GGLNVTLTIRLLMHG CCCEEEEEEEHHHCC	8.49	20068231
55	Sumoylation	IRLLMHGKEVGSIIG EEHHHCCHHHHHHCC	34.25	-
55 (in isoform 5)	Ubiquitination	-	34.25	21890473
55 (in isoform 4)	Ubiquitination	-	34.25	21890473
55 (in isoform 2)	Ubiquitination	-	34.25	21890473
55 (in isoform 1)	Ubiquitination	-	34.25	21890473
55	Malonylation	IRLLMHGKEVGSIIG EEHHHCCHHHHHHCC	34.25	26320211
55	Sumoylation	IRLLMHGKEVGSIIG EEHHHCCHHHHHHCC	34.25	-
55	Acetylation	IRLLMHGKEVGSIIG EEHHHCCHHHHHHCC	34.25	23954790
55	Ubiquitination	IRLLMHGKEVGSIIG EEHHHCCHHHHHHCC	34.25	23000965
59	Phosphorylation	MHGKEVGSIIGKKGE HCCHHHHHHCCCCCH	19.06	30108239
63	Sumoylation	EVGSIIGKKGETVKK HHHHHCCCCCHHHHH	47.39	-
63	Ubiquitination	EVGSIIGKKGETVKK HHHHHCCCCCHHHHH	47.39	25015289
63 (in isoform 1)	Ubiquitination	-	47.39	21890473
63 (in isoform 2)	Ubiquitination	-	47.39	21890473
63	Acetylation	EVGSIIGKKGETVKK HHHHHCCCCCHHHHH	47.39	25953088
63	Sumoylation	EVGSIIGKKGETVKK HHHHHCCCCCHHHHH	47.39	-
63 (in isoform 4)	Ubiquitination	-	47.39	21890473
63 (in isoform 5)	Ubiquitination	-	47.39	21890473
64	Ubiquitination	VGSIIGKKGETVKKM HHHHCCCCCHHHHHH	57.68	25015289
75	Phosphorylation	VKKMREESGARINIS HHHHHHHHCCCEEEC	32.76	-
82	Phosphorylation	SGARINISEGNCPER HCCCEEECCCCCCCC	34.66	21815630
86	Glutathionylation	INISEGNCPERIVTI EEECCCCCCCCEEEE	5.64	22555962
86	S-palmitoylation	INISEGNCPERIVTI EEECCCCCCCCEEEE	5.64	29575903
118	Phosphorylation	FEEDIINSMSNSPAT HHHHHHHHCCCCCCC	17.12	27732954
120	Phosphorylation	EDIINSMSNSPATSK HHHHHHCCCCCCCCC	33.70	27732954
122	Phosphorylation	IINSMSNSPATSKPP HHHHCCCCCCCCCCC	14.49	27732954
125	Phosphorylation	SMSNSPATSKPPVTL HCCCCCCCCCCCEEE	40.44	27732954
126	Phosphorylation	MSNSPATSKPPVTLR CCCCCCCCCCCEEEE	45.32	27732954
131	Phosphorylation	ATSKPPVTLRLVVPA CCCCCCEEEEEEEEH	16.37	27732954
139	Phosphorylation	LRLVVPASQCGSLIG EEEEEEHHHHHHHCC	21.67	23898821
141	S-palmitoylation	LVVPASQCGSLIGKG EEEEHHHHHHHCCCC	3.56	29575903
141	Glutathionylation	LVVPASQCGSLIGKG EEEEHHHHHHHCCCC	3.56	22555962
143	Phosphorylation	VPASQCGSLIGKGGS EEHHHHHHHCCCCCH	25.17	23898821
147	Acetylation	QCGSLIGKGGSKIKE HHHHHCCCCCHHHHH	53.78	18528505
150	Phosphorylation	SLIGKGGSKIKEIRE HHCCCCCHHHHHHHH	39.62	26853621
159	Phosphorylation	IKEIRESTGAQVQVA HHHHHHHHCCEEEEE	31.61	22817900
169	Sulfoxidation	QVQVAGDMLPNSTER EEEEECCCCCCCCCC	7.02	21406390
195	Glutathionylation	IQCVKQICVVMLESP HHHHHHHEEEEECCC	1.42	22555962
198	Sulfoxidation	VKQICVVMLESPPKG HHHHEEEEECCCCCC	1.39	21406390
201	Phosphorylation	ICVVMLESPPKGATI HEEEEECCCCCCCCC	42.41	28102081
227	Phosphorylation	IFAGGQAYTIQGQYA EEECCEEEEEECCEE	9.11	-
228	Phosphorylation	FAGGQAYTIQGQYAI EECCEEEEEECCEEC	15.16	-
233	Phosphorylation	AYTIQGQYAIPHPDQ EEEEECCEECCCHHH	17.21	-
320	Methylation	GTKINEIRQMSGAQI CCCHHHHHHHCCCEE	21.70	-
322	Sulfoxidation	KINEIRQMSGAQIKI CHHHHHHHCCCEEEE	2.61	28183972
323	Phosphorylation	INEIRQMSGAQIKIA HHHHHHHCCCEEEEE	23.73	28857561
342	Phosphorylation	GSSERQITITGTPAN CCCCCEEEEECCCCC	12.26	24043423
344	Phosphorylation	SERQITITGTPANIS CCCEEEEECCCCCHH	26.76	24043423
346	Phosphorylation	RQITITGTPANISLA CEEEEECCCCCHHHH	15.58	24043423
351	Phosphorylation	TGTPANISLAQYLIN ECCCCCHHHHHHHHH	19.91	24043423
355	Phosphorylation	ANISLAQYLINARLT CCHHHHHHHHHHHHC	12.16	24043423

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PCBP3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PCBP3_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PCBP3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PTBP1_HUMAN	PTBP1	physical	16713569
PTBP2_HUMAN	PTBP2	physical	16713569
PCBP1_HUMAN	PCBP1	physical	23640898

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.

Related Literatures of Post-Translational Modification

Acetylation

"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-55, AND MASS SPECTROMETRY.
PubMed: 19608861