dbPTM

PDIP3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PDIP3_HUMAN
UniProt AC	Q9BY77
Protein Name	Polymerase delta-interacting protein 3
Gene Name	POLDIP3
Organism	Homo sapiens (Human).
Sequence Length	421
Subcellular Localization	Nucleus. Nucleus speckle. Cytoplasm. Nucleocytoplasmic shuttling protein.
Protein Description	Is involved in regulation of translation. Is preferentially associated with CBC-bound spliced mRNA-protein complexes during the pioneer round of mRNA translation. Contributes to enhanced translational efficiency of spliced over nonspliced mRNAs. Recruits activated ribosomal protein S6 kinase beta-1 I/RPS6KB1 to newly synthesized mRNA. Involved in nuclear mRNA export; probably mediated by assoociation with the TREX complex..
Protein Sequence	MADISLDELIRKRGAAAKGRLNARPGVGGVRSRVGIQQGLLSQSTRTATFQQRFDARQKIGLSDARLKLGVKDAREKLLQKDARFRIKGKVQDAREMLNSRKQQTTVPQKPRQVADAREKISLKRSSPAAFINPPIGTVTPALKLTKTIQVPQQKAMAPLHPHPAGMRINVVNNHQAKQNLYDLDEDDDGIASVPTKQMKFAASGGFLHHMAGLSSSKLSMSKALPLTKVVQNDAYTAPALPSSIRTKALTNMSRTLVNKEEPPKELPAAEPVLSPLEGTKMTVNNLHPRVTEEDIVELFCVCGALKRARLVHPGVAEVVFVKKDDAITAYKKYNNRCLDGQPMKCNLHMNGNVITSDQPILLRLSDSPSMKKESELPRRVNSASSSNPPAEVDPDTILKALFKSSGASVTTQPTEFKIKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADISLDEL ------CCCCCHHHH	23.89	22223895
5	Phosphorylation	---MADISLDELIRK ---CCCCCHHHHHHH	30.25	25159151
11	Methylation	ISLDELIRKRGAAAK CCHHHHHHHHCHHHH	34.93	115917017
33	Methylation	GVGGVRSRVGIQQGL CCCCHHHHHHHCCCC	21.81	24129315
42	Phosphorylation	GIQQGLLSQSTRTAT HHCCCCCCCCCCCCH	27.42	17525332
44	Phosphorylation	QQGLLSQSTRTATFQ CCCCCCCCCCCCHHH	19.24	23911959
45	Phosphorylation	QGLLSQSTRTATFQQ CCCCCCCCCCCHHHH	25.13	26074081
63	Phosphorylation	ARQKIGLSDARLKLG HHHHHCCCHHHHHHC	24.82	20068231
66	Methylation	KIGLSDARLKLGVKD HHCCCHHHHHHCCHH	37.03	115917021
72	Acetylation	ARLKLGVKDAREKLL HHHHHCCHHHHHHHH	43.82	25953088
88	Methylation	KDARFRIKGKVQDAR CCCHHHHCCHHHHHH	48.71	116253695
102	Ubiquitination	REMLNSRKQQTTVPQ HHHHHCCCCCCCCCC	46.72	-
102	Methylation	REMLNSRKQQTTVPQ HHHHHCCCCCCCCCC	46.72	116253689
105	Phosphorylation	LNSRKQQTTVPQKPR HHCCCCCCCCCCCHH	27.54	20363803
106	Phosphorylation	NSRKQQTTVPQKPRQ HCCCCCCCCCCCHHH	26.33	20363803
110	Ubiquitination	QQTTVPQKPRQVADA CCCCCCCCHHHHHHH	35.78	-
122	Phosphorylation	ADAREKISLKRSSPA HHHHHHHCCCCCCCC	38.62	29449344
126	Phosphorylation	EKISLKRSSPAAFIN HHHCCCCCCCCCCCC	38.80	29255136
127	Phosphorylation	KISLKRSSPAAFINP HHCCCCCCCCCCCCC	23.69	29255136
138 (in isoform 2)	Phosphorylation	-	23.17	25159151
138	Phosphorylation	FINPPIGTVTPALKL CCCCCCCCCCHHHHC	23.17	25159151
140 (in isoform 2)	Phosphorylation	-	11.59	25159151
140	Phosphorylation	NPPIGTVTPALKLTK CCCCCCCCHHHHCCC	11.59	23927012
144	Acetylation	GTVTPALKLTKTIQV CCCCHHHHCCCEECC	57.10	25953088
144	Ubiquitination	GTVTPALKLTKTIQV CCCCHHHHCCCEECC	57.10	-
146	Phosphorylation	VTPALKLTKTIQVPQ CCHHHHCCCEECCCC	25.26	23312004
147 (in isoform 2)	Ubiquitination	-	54.81	-
147	Ubiquitination	TPALKLTKTIQVPQQ CHHHHCCCEECCCCC	54.81	-
148 (in isoform 2)	Phosphorylation	-	16.06	28796482
153 (in isoform 2)	Phosphorylation	-	59.56	28796482
155	Ubiquitination	TIQVPQQKAMAPLHP EECCCCCCCCCCCCC	34.58	-
168 (in isoform 2)	Ubiquitination	-	19.19	21890473
171 (in isoform 2)	Ubiquitination	-	4.54	-
178	Ubiquitination	VVNNHQAKQNLYDLD EECCCHHHHCCCCCC	32.90	-
182	Phosphorylation	HQAKQNLYDLDEDDD CHHHHCCCCCCCCCC	23.24	28796482
193	Phosphorylation	EDDDGIASVPTKQMK CCCCCCCCCCHHHEE	27.06	24532841
197	Ubiquitination	GIASVPTKQMKFAAS CCCCCCHHHEEEHHC	42.18	21906983
200 (in isoform 2)	Ubiquitination	-	29.38	21890473
200	Ubiquitination	SVPTKQMKFAASGGF CCCHHHEEEHHCCCH	29.38	21890473
200	Sumoylation	SVPTKQMKFAASGGF CCCHHHEEEHHCCCH	29.38	28112733
204	Phosphorylation	KQMKFAASGGFLHHM HHEEEHHCCCHHHHH	35.70	28450419
214 (in isoform 1)	Ubiquitination	-	3.05	21890473
215	Phosphorylation	LHHMAGLSSSKLSMS HHHHCCCCCCCCCHH	31.48	25159151
216	Phosphorylation	HHMAGLSSSKLSMSK HHHCCCCCCCCCHHH	36.21	29396449
217	Phosphorylation	HMAGLSSSKLSMSKA HHCCCCCCCCCHHHH	33.95	29396449
218	Acetylation	MAGLSSSKLSMSKAL HCCCCCCCCCHHHHC	46.67	25953088
223	Sumoylation	SSKLSMSKALPLTKV CCCCCHHHHCCCCEE	45.35	28112733
223	Ubiquitination	SSKLSMSKALPLTKV CCCCCHHHHCCCCEE	45.35	-
229	Ubiquitination	SKALPLTKVVQNDAY HHHCCCCEEECCCCC	48.36	21890473
236	Phosphorylation	KVVQNDAYTAPALPS EEECCCCCCCCCCCH	13.29	21945579
237	Phosphorylation	VVQNDAYTAPALPSS EECCCCCCCCCCCHH	28.08	21945579
243	Phosphorylation	YTAPALPSSIRTKAL CCCCCCCHHHHHHHH	38.97	21945579
244	Phosphorylation	TAPALPSSIRTKALT CCCCCCHHHHHHHHH	17.72	21945579
247	Phosphorylation	ALPSSIRTKALTNMS CCCHHHHHHHHHHHC	20.99	26074081
248	Ubiquitination	LPSSIRTKALTNMSR CCHHHHHHHHHHHCC	31.39	-
248	Sumoylation	LPSSIRTKALTNMSR CCHHHHHHHHHHHCC	31.39	28112733
251	Phosphorylation	SIRTKALTNMSRTLV HHHHHHHHHHCCCCC	33.46	29978859
254	Phosphorylation	TKALTNMSRTLVNKE HHHHHHHCCCCCCCC	24.96	28985074
256	Phosphorylation	ALTNMSRTLVNKEEP HHHHHCCCCCCCCCC	27.96	28387310
260	Acetylation	MSRTLVNKEEPPKEL HCCCCCCCCCCCCCC	56.85	26051181
260	Ubiquitination	MSRTLVNKEEPPKEL HCCCCCCCCCCCCCC	56.85	-
265	Ubiquitination	VNKEEPPKELPAAEP CCCCCCCCCCCCCCC	80.66	-
265	Acetylation	VNKEEPPKELPAAEP CCCCCCCCCCCCCCC	80.66	26051181
275	Phosphorylation	PAAEPVLSPLEGTKM CCCCCCCCCCCCCCC	27.89	29255136
280	Phosphorylation	VLSPLEGTKMTVNNL CCCCCCCCCCCCCCC	14.31	29255136
303 (in isoform 2)	Ubiquitination	-	2.51	21890473
307	Acetylation	FCVCGALKRARLVHP HHHHHHHHHHCCCCC	43.40	20167786
323	Acetylation	VAEVVFVKKDDAITA EEEEEEEECCCHHHH	38.73	26051181
329	Phosphorylation	VKKDDAITAYKKYNN EECCCHHHHHHHHCC	26.17	-
332	Ubiquitination	DDAITAYKKYNNRCL CCHHHHHHHHCCEEC	46.44	2190698
349 (in isoform 1)	Ubiquitination	-	8.15	21890473
366	Phosphorylation	QPILLRLSDSPSMKK CCEEEEECCCCCCCC	29.61	24732914
368	Phosphorylation	ILLRLSDSPSMKKES EEEEECCCCCCCCHH	18.59	23401153
370	Phosphorylation	LRLSDSPSMKKESEL EEECCCCCCCCHHHC	47.38	25159151
372	Ubiquitination	LSDSPSMKKESELPR ECCCCCCCCHHHCCC	58.70	-
372	Sumoylation	LSDSPSMKKESELPR ECCCCCCCCHHHCCC	58.70	28112733
373	Ubiquitination	SDSPSMKKESELPRR CCCCCCCCHHHCCCC	58.81	-
375	Phosphorylation	SPSMKKESELPRRVN CCCCCCHHHCCCCCC	54.00	24732914
383	Phosphorylation	ELPRRVNSASSSNPP HCCCCCCCCCCCCCC	27.03	29255136
385	Phosphorylation	PRRVNSASSSNPPAE CCCCCCCCCCCCCCC	33.83	29255136
386	Phosphorylation	RRVNSASSSNPPAEV CCCCCCCCCCCCCCC	33.57	29255136
387	Phosphorylation	RVNSASSSNPPAEVD CCCCCCCCCCCCCCC	51.35	29255136
400	Ubiquitination	VDPDTILKALFKSSG CCHHHHHHHHHHCCC	38.91	-
404	Ubiquitination	TILKALFKSSGASVT HHHHHHHHCCCCCCC	44.56	-
404	Methylation	TILKALFKSSGASVT HHHHHHHHCCCCCCC	44.56	115981161
405	Phosphorylation	ILKALFKSSGASVTT HHHHHHHCCCCCCCC	27.03	22817900
406	Phosphorylation	LKALFKSSGASVTTQ HHHHHHCCCCCCCCC	38.68	22817900
409	Phosphorylation	LFKSSGASVTTQPTE HHHCCCCCCCCCCCE	24.42	23312004
411	Phosphorylation	KSSGASVTTQPTEFK HCCCCCCCCCCCEEE	19.74	23312004
412	Phosphorylation	SSGASVTTQPTEFKI CCCCCCCCCCCEEEE	30.32	23312004
418	Methylation	TTQPTEFKIKL---- CCCCCEEEECC----	32.47	30795303
418	Ubiquitination	TTQPTEFKIKL---- CCCCCEEEECC----	32.47	-
418	Sumoylation	TTQPTEFKIKL---- CCCCCEEEECC----	32.47	28112733

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
63	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
383	S	Phosphorylation	Kinase	KS6B1	P23443	PhosphoELM
383	S	Phosphorylation	Kinase	P70-SUBFAMILY	-	GPS
385	S	Phosphorylation	Kinase	P70S6K	P23443	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
383	S	Phosphorylation	15341740
Phosphorylated at Ser-383 and Ser-385 by RPS6KB1.
385	S	Phosphorylation	15341740
Phosphorylated at Ser-383 and Ser-385 by RPS6KB1.

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 PDIP3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KS6B1_HUMAN	RPS6KB1	physical	15341740
NCBP1_HUMAN	NCBP1	physical	18423201
IF4A3_HUMAN	EIF4A3	physical	18423201
IF4G1_HUMAN	EIF4G1	physical	25049393
LZTS2_HUMAN	LZTS2	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
IMA4_HUMAN	KPNA3	physical	26186194
UBR1_HUMAN	UBR1	physical	28514442
KLH22_HUMAN	KLHL22	physical	28514442

Drug and Disease Associations

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

Regulatory Network of PDIP3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND MASSSPECTROMETRY.	17525332 [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-127, AND MASSSPECTROMETRY.	17924679 [Abstract]
"SKAR is a specific target of S6 kinase 1 in cell growth control."; Richardson C.J., Broenstrup M., Fingar D.C., Julich K., Ballif B.A.,Gygi S., Blenis J.; Curr. Biol. 14:1540-1549(2004). Cited for: INTERACTION WITH RPS6KB1, SUBCELLULAR LOCATION, PHOSPHORYLATION ATSER-127; SER-275; SER-383 AND SER-385, MUTAGENESIS OF SER-383 ANDSER-385, AND MASS SPECTROMETRY.	15341740 [Abstract]
"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 THR-140, AND MASSSPECTROMETRY.	19690332 [Abstract]

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