PABP5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PABP5_HUMAN
• UniProt AC: Q96DU9
• Protein Name: Polyadenylate-binding protein 5
• Gene Name: PABPC5
• Organism: Homo sapiens (Human).
• Sequence Length: 382
• Subcellular Localization: Cytoplasm.; Isoform 2: Mitochondrion matrix . Co-fractionates with mtDNA and co-immunoprecipitates with the mitochondrial poly(A) polymerase.
• Protein Description: Binds the poly(A) tail of mRNA. May be involved in cytoplasmic regulatory processes of mRNA metabolism. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo (By similarity)..
• Protein Sequence: MGSGEPNPAGKKKKYLKAALYVGDLDPDVTEDMLYKKFRPAGPLRFTRICRDPVTRSPLGYGYVNFRFPADAEWALNTMNFDLINGKPFRLMWSQPDDRLRKSGVGNIFIKNLDKSIDNRALFYLFSAFGNILSCKVVCDDNGSKGYAYVHFDSLAAANRAIWHMNGVRLNNRQVYVGRFKFPEERAAEVRTRDRATFTNVFVKNIGDDIDDEKLKELFCEYGPTESVKVIRDASGKSKGFGFVRYETHEAAQKAVLDLHGKSIDGKVLYVGRAQKKIERLAELRRRFERLRLKEKSRPPGVPIYIKNLDETINDEKLKEEFSSFGSISRAKVMMEVGQGKGFGVVCFSSFEEATKAVDEMNGRIVGSKPLHVTLGQARRRC

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
14	Ubiquitination	NPAGKKKKYLKAALY CCCCCCHHHHHHEEE	65.77	25015289
15	Phosphorylation	PAGKKKKYLKAALYV CCCCCHHHHHHEEEE	23.47	-
17	Ubiquitination	GKKKKYLKAALYVGD CCCHHHHHHEEEECC	28.64	25015289
35	Phosphorylation	DVTEDMLYKKFRPAG CCCHHHHHHHHCCCC	12.90	-
36	Ubiquitination	VTEDMLYKKFRPAGP CCHHHHHHHHCCCCC	41.28	25015289
57	Phosphorylation	CRDPVTRSPLGYGYV ECCCCCCCCCCCCEE	18.34	28122231
78	Phosphorylation	DAEWALNTMNFDLIN CHHHHHHHCCEEEEC	17.84	23879269
102	Ubiquitination	QPDDRLRKSGVGNIF CCCHHHHHCCCCCEE	57.04	21906983
103	Phosphorylation	PDDRLRKSGVGNIFI CCHHHHHCCCCCEEE	32.07	30266825
111	Ubiquitination	GVGNIFIKNLDKSID CCCCEEECCCCCCCC	40.48	23000965
111	Acetylation	GVGNIFIKNLDKSID CCCCEEECCCCCCCC	40.48	88775
115	Ubiquitination	IFIKNLDKSIDNRAL EEECCCCCCCCHHHH	53.10	23000965
144	Phosphorylation	VVCDDNGSKGYAYVH EEECCCCCEEEEEEE	29.21	22210691
147	Phosphorylation	DDNGSKGYAYVHFDS CCCCCEEEEEEEHHH	9.86	-
149	Phosphorylation	NGSKGYAYVHFDSLA CCCEEEEEEEHHHHH	5.98	-
154	Phosphorylation	YAYVHFDSLAAANRA EEEEEHHHHHHHCHH	20.97	-
199	Phosphorylation	TRDRATFTNVFVKNI CCCCHHEEEEEEECC	26.56	19664995
235	Phosphorylation	VKVIRDASGKSKGFG EEEEECCCCCCCCCC	51.55	-
238	Phosphorylation	IRDASGKSKGFGFVR EECCCCCCCCCCEEE	41.35	-
270	Phosphorylation	SIDGKVLYVGRAQKK CCCCEEEEECCHHHH	12.12	-
368	Phosphorylation	MNGRIVGSKPLHVTL HCCEECCCCCCEEEE	21.87	24719451

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

Oops, there are no upstream regulatory protein records of PABP5_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PABP5_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 PABP5_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of PABP5_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.

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-111, AND MASS SPECTROMETRY.
PubMed: 19608861