NOVA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NOVA1_HUMAN
• UniProt AC: P51513
• Protein Name: RNA-binding protein Nova-1
• Gene Name: NOVA1
• Organism: Homo sapiens (Human).
• Sequence Length: 510
• Subcellular Localization: Nucleus.
• Protein Description: May regulate RNA splicing or metabolism in a specific subset of developing neurons..
• Protein Sequence: MMAAAPIQQNGTHTGVPIDLDPPDSRKRPLEAPPEAGSTKRTNTGEDGQYFLKVLIPSYAAGSIIGKGGQTIVQLQKETGATIKLSKLSKSKDFYPGTTERVCLIQGTVEALNAVHGFIAEKIREMPQNVAKTEPVSILQPQTTVNPDRIKQTLPSSPTTTKSSPSDPMTTSRANQVKIIVPNSTAGLIIGKGGATVKAVMEQSGAWVQLSQKPDGINLQERVVTVSGEPEQNRKAVELIIQKIQEDPQSGSCLNISYANVTGPVANSNPTGSPYANTAEVLPTAAAAAGLLGHANLAGVAAFPAVLSGFTGNDLVAITSALNTLASYGYNLNTLGLGLSQAAATGALAAAAASANPAAAAANLLATYASEASASGSTAGGTAGTFALGSLAAATAATNGYFGAASPLAASAILGTEKSTDGSKDVVEIAVPENLVGAILGKGGKTLVEYQELTGARIQISKKGEFVPGTRNRKVTITGTPAATQAAQYLITQRITYEQGVRAANPQKVG

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
58	Phosphorylation	FLKVLIPSYAAGSII EEEEEEHHHCCCCCC	22.02	-
59	Phosphorylation	LKVLIPSYAAGSIIG EEEEEHHHCCCCCCC	8.63	-
86	Phosphorylation	TGATIKLSKLSKSKD HCCEEEHHHCCCCCC	26.92	29449344
89	Phosphorylation	TIKLSKLSKSKDFYP EEEHHHCCCCCCCCC	38.32	29449344
91	Phosphorylation	KLSKLSKSKDFYPGT EHHHCCCCCCCCCCC	33.80	29449344
153 (in isoform 4)	Phosphorylation	-	35.32	24719451
153	Phosphorylation	NPDRIKQTLPSSPTT CHHHHHHHCCCCCCC	35.32	23403867
154 (in isoform 2)	Phosphorylation	-	3.43	-
154 (in isoform 4)	Phosphorylation	-	3.43	-
154	Phosphorylation	PDRIKQTLPSSPTTT HHHHHHHCCCCCCCC	3.43	19664995
156	Phosphorylation	RIKQTLPSSPTTTKS HHHHHCCCCCCCCCC	52.65	30266825
157	Phosphorylation	IKQTLPSSPTTTKSS HHHHCCCCCCCCCCC	25.07	19413330
159	Phosphorylation	QTLPSSPTTTKSSPS HHCCCCCCCCCCCCC	49.39	30266825
160	Phosphorylation	TLPSSPTTTKSSPSD HCCCCCCCCCCCCCC	35.29	26552605
161 (in isoform 4)	Phosphorylation	-	31.26	27251275
161	Phosphorylation	LPSSPTTTKSSPSDP CCCCCCCCCCCCCCC	31.26	28787133
163	Phosphorylation	SSPTTTKSSPSDPMT CCCCCCCCCCCCCCC	45.44	26074081
164	Phosphorylation	SPTTTKSSPSDPMTT CCCCCCCCCCCCCCC	29.94	26074081
166	Phosphorylation	TTTKSSPSDPMTTSR CCCCCCCCCCCCCCC	57.18	26074081
178 (in isoform 2)	Phosphorylation	-	19.56	22210691
181 (in isoform 2)	Phosphorylation	-	4.12	22210691
227	Phosphorylation	QERVVTVSGEPEQNR CEEEEEECCCHHHHH	28.24	-
476	Phosphorylation	GTRNRKVTITGTPAA CCCCCEEEEECCHHH	18.82	24043423
478	Phosphorylation	RNRKVTITGTPAATQ CCCEEEEECCHHHHH	26.15	24043423
480	Phosphorylation	RKVTITGTPAATQAA CEEEEECCHHHHHHH	10.91	24043423
484	Phosphorylation	ITGTPAATQAAQYLI EECCHHHHHHHHHHH	22.35	24043423

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

Oops, there are no upstream regulatory protein records of NOVA1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NOVA1_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 NOVA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
NOVA2_HUMAN	NOVA2	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

Phosphorylation

"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, AND MASSSPECTROMETRY.
PubMed: 19413330