PNO1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PNO1_HUMAN
• UniProt AC: Q9NRX1
• Protein Name: RNA-binding protein PNO1
• Gene Name: PNO1
• Organism: Homo sapiens (Human).
• Sequence Length: 252
• Subcellular Localization: Nucleus, nucleolus .
• Protein Description: Positively regulates dimethylation of two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA. [PubMed: 25851604]
• Protein Sequence: MESEMETQSARAEEGFTQVTRKGGRRAKKRQAEQLSAAGEGGDAGRMDTEEARPAKRPVFPPLCGDGLLSGKEETRKIPVPANRYTPLKENWMKIFTPIVEHLGLQIRFNLKSRNVEIRTCKETKDVSALTKAADFVKAFILGFQVEDALALIRLDDLFLESFEITDVKPLKGDHLSRAIGRIAGKGGKTKFTIENVTRTRIVLADVKVHILGSFQNIKMARTAICNLILGNPPSKVYGNIRAVASRSADRF

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
1	Acetylation	-------MESEMETQ -------CCCHHHHH	13.27	19413330
7	Phosphorylation	-MESEMETQSARAEE -CCCHHHHHHHHHHH	26.89	17081983
17	Phosphorylation	ARAEEGFTQVTRKGG HHHHHCCHHHHHHCC	32.74	24532841
20	Phosphorylation	EEGFTQVTRKGGRRA HHCCHHHHHHCCHHH	19.49	24532841
36	Phosphorylation	KRQAEQLSAAGEGGD HHHHHHHHHHCCCCC	18.77	29255136
49	Phosphorylation	GDAGRMDTEEARPAK CCCCCCCHHHCCCCC	26.78	28555341
56	Ubiquitination	TEEARPAKRPVFPPL HHHCCCCCCCCCCCC	60.97	24816145
72	Acetylation	GDGLLSGKEETRKIP CCCCCCCCCCCCCCC	49.34	26051181
72	Ubiquitination	GDGLLSGKEETRKIP CCCCCCCCCCCCCCC	49.34	29967540
77	Ubiquitination	SGKEETRKIPVPANR CCCCCCCCCCCCCCC	59.80	29967540
84	Methylation	KIPVPANRYTPLKEN CCCCCCCCCCCCCHH	38.52	115488001
85	Phosphorylation	IPVPANRYTPLKENW CCCCCCCCCCCCHHH	16.71	28555341
86	Phosphorylation	PVPANRYTPLKENWM CCCCCCCCCCCHHHH	20.93	27067055
89	Ubiquitination	ANRYTPLKENWMKIF CCCCCCCCHHHHHHH	50.64	29967540
89	Acetylation	ANRYTPLKENWMKIF CCCCCCCCHHHHHHH	50.64	27452117
125	Acetylation	IRTCKETKDVSALTK EEECCCCCCHHHHHH	58.17	26051181
125	Ubiquitination	IRTCKETKDVSALTK EEECCCCCCHHHHHH	58.17	29967540
131	Phosphorylation	TKDVSALTKAADFVK CCCHHHHHHHHHHHH	20.53	21964256
132	Ubiquitination	KDVSALTKAADFVKA CCHHHHHHHHHHHHH	42.29	29967540
132	2-Hydroxyisobutyrylation	KDVSALTKAADFVKA CCHHHHHHHHHHHHH	42.29	-
191	2-Hydroxyisobutyrylation	AGKGGKTKFTIENVT CCCCCCCEEEEECCC	43.95	-
193	Phosphorylation	KGGKTKFTIENVTRT CCCCCEEEEECCCEE	29.01	20068231
235	Phosphorylation	LILGNPPSKVYGNIR HHHCCCCHHHHHHHH	35.69	28555341
236	Ubiquitination	ILGNPPSKVYGNIRA HHCCCCHHHHHHHHH	45.29	-

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

Oops, there are no upstream regulatory protein records of PNO1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PNO1_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 PNO1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
WDR3_HUMAN	WDR3	physical	22939629
RB_HUMAN	RB1	physical	22939629
RS15A_HUMAN	RPS15A	physical	22863883
RS3_HUMAN	RPS3	physical	22863883
RS6_HUMAN	RPS6	physical	22863883
TSR1_HUMAN	TSR1	physical	22863883
CMTD1_HUMAN	COMTD1	physical	26186194
UT14A_HUMAN	UTP14A	physical	26186194
UT14C_HUMAN	UTP14C	physical	26186194
MTMR3_HUMAN	MTMR3	physical	26186194
NOB1_HUMAN	NOB1	physical	26186194
KC1E_HUMAN	CSNK1E	physical	26344197
LRC47_HUMAN	LRRC47	physical	26344197
NOB1_HUMAN	NOB1	physical	26344197
NOC3L_HUMAN	NOC3L	physical	26344197
RSSA_HUMAN	RPSA	physical	26344197
UT14C_HUMAN	UTP14C	physical	28514442
NOB1_HUMAN	NOB1	physical	28514442
CMTD1_HUMAN	COMTD1	physical	28514442
UT14A_HUMAN	UTP14A	physical	28514442
MTMR3_HUMAN	MTMR3	physical	28514442

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

"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
PubMed: 19413330

Phosphorylation

"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-36, AND MASSSPECTROMETRY.
PubMed: 19007248