dbPTM

GLD2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GLD2_HUMAN
UniProt AC	Q6PIY7
Protein Name	Poly(A) RNA polymerase GLD2
Gene Name	PAPD4
Organism	Homo sapiens (Human).
Sequence Length	484
Subcellular Localization	Cytoplasm. Nucleus.
Protein Description	Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. In contrast to the canonical nuclear poly(A) RNA polymerase, it only adds poly(A) to selected cytoplasmic mRNAs. Does not play a role in replication-dependent histone mRNA degradation..
Protein Sequence	MFPNSILGRPPFTPNHQQHNNFFTLSPTVYSHQQLIDAQFNFQNADLSRAVSLQQLTYGNVSPIQTSASPLFRGRKRLSDEKNLPLDGKRQRFHSPHQEPTVVNQIVPLSGERRYSMPPLFHTHYVPDIVRCVPPFREIAFLEPREITLPEAKDKLSQQILELFETCQQQISDLKKKELCRTQLQREIQLLFPQSRLFLVGSSLNGFGTRSSDGDLCLVVKEEPCFFQVNQKTEARHILTLVHKHFCTRLSGYIERPQLIRAKVPIVKFRDKVSCVEFDLNVNNIVGIRNTFLLRTYAYLENRVRPLVLVIKKWASHHQINDASRGTLSSYSLVLMVLHYLQTLPEPILPSLQKIYPESFSPAIQLHLVHQAPCNVPPYLSKNESNLGDLLLGFLKYYATEFDWNSQMISVREAKAIPRPDGIEWRNKYICVEEPFDGTNTARAVHEKQKFDMIKDQFLKSWHRLKNKRDLNSILPVRAAVLKR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
52	Phosphorylation	ADLSRAVSLQQLTYG CCHHHCCCHHHCCCC	21.34	27174698
57	Phosphorylation	AVSLQQLTYGNVSPI CCCHHHCCCCCCCCC	25.66	27174698
58	Phosphorylation	VSLQQLTYGNVSPIQ CCHHHCCCCCCCCCC	18.46	20090780
62	Phosphorylation	QLTYGNVSPIQTSAS HCCCCCCCCCCCCCC	21.93	21712546
66	Phosphorylation	GNVSPIQTSASPLFR CCCCCCCCCCCHHCC	27.29	30108239
67	Phosphorylation	NVSPIQTSASPLFRG CCCCCCCCCCHHCCC	15.46	22199227
69	Phosphorylation	SPIQTSASPLFRGRK CCCCCCCCHHCCCCC	23.15	22199227
73	Methylation	TSASPLFRGRKRLSD CCCCHHCCCCCCCCC	52.25	12019631
75	Methylation	ASPLFRGRKRLSDEK CCHHCCCCCCCCCCC	19.37	30760605
82	Ubiquitination	RKRLSDEKNLPLDGK CCCCCCCCCCCCCCC	69.63	-
89	Ubiquitination	KNLPLDGKRQRFHSP CCCCCCCCCCCCCCC	45.05	-
90	Methylation	NLPLDGKRQRFHSPH CCCCCCCCCCCCCCC	38.14	115486401
92	Methylation	PLDGKRQRFHSPHQE CCCCCCCCCCCCCCC	34.97	115486407
95	Phosphorylation	GKRQRFHSPHQEPTV CCCCCCCCCCCCCCE	22.74	23401153
101	Phosphorylation	HSPHQEPTVVNQIVP CCCCCCCCEEEEEEE	36.01	30576142
110	Phosphorylation	VNQIVPLSGERRYSM EEEEEECCCCCCCCC	32.32	21712546
115	Phosphorylation	PLSGERRYSMPPLFH ECCCCCCCCCCCCCC	18.62	30108239
116	Phosphorylation	LSGERRYSMPPLFHT CCCCCCCCCCCCCCC	24.01	30108239
123	Phosphorylation	SMPPLFHTHYVPDIV CCCCCCCCCCCCCHH	13.94	28387310
125	Phosphorylation	PPLFHTHYVPDIVRC CCCCCCCCCCCHHHC	18.16	28387310
131	Methylation	HYVPDIVRCVPPFRE CCCCCHHHCCCCCHH	18.95	54557899
153	Ubiquitination	EITLPEAKDKLSQQI EECCHHHHHHHHHHH	54.45	-
155	Ubiquitination	TLPEAKDKLSQQILE CCHHHHHHHHHHHHH	49.70	-
175	Ubiquitination	QQQISDLKKKELCRT HHHHHHHHHHHHHHH	67.78	-
211	Phosphorylation	LNGFGTRSSDGDLCL CCCCCCCCCCCCEEE	32.39	29083192
212	Phosphorylation	NGFGTRSSDGDLCLV CCCCCCCCCCCEEEE	42.18	29083192
251	Phosphorylation	KHFCTRLSGYIERPQ HHHHHHHHCCCCCCH	26.68	27251275
253	Phosphorylation	FCTRLSGYIERPQLI HHHHHHCCCCCCHHH	9.02	-
268	Ubiquitination	RAKVPIVKFRDKVSC HCCCCEEECCCCEEE	35.09	-
325	Methylation	HQINDASRGTLSSYS CCCCCCCCCCCHHHH	43.78	30762835
325	Dimethylation	HQINDASRGTLSSYS CCCCCCCCCCCHHHH	43.78	-
428	Ubiquitination	DGIEWRNKYICVEEP CCCCEECCEEEEECC	27.67	-
429	Phosphorylation	GIEWRNKYICVEEPF CCCEECCEEEEECCC	11.78	-
439	Phosphorylation	VEEPFDGTNTARAVH EECCCCCCHHHHHHH	31.10	-
441	Phosphorylation	EPFDGTNTARAVHEK CCCCCCHHHHHHHHH	19.84	-
455	Ubiquitination	KQKFDMIKDQFLKSW HHHHHHHHHHHHHHH	38.55	-
461	Phosphorylation	IKDQFLKSWHRLKNK HHHHHHHHHHHHCCC	30.20	20068231

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
116	S	Phosphorylation	Kinase	AKT1	P31749	PSP
116	S	Phosphorylation	Kinase	PKACA	P17612	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GLD2_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 GLD2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of GLD2_HUMAN !!

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 GLD2_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-69, AND MASSSPECTROMETRY.	19690332 [Abstract]