NCBP1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NCBP1_MOUSE
• UniProt AC: Q3UYV9
• Protein Name: Nuclear cap-binding protein subunit 1
• Gene Name: Ncbp1
• Organism: Mus musculus (Mouse).
• Sequence Length: 790
• Subcellular Localization: Nucleus . Cytoplasm . Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
• Protein Description: Component of the cap-binding complex (CBC), which binds cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to the recruitment of the mRNA export machinery to the 5'-end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC) via its interaction with UPF1, promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2 and is required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of PARN, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP1/CBP80 does not bind directly capped RNAs (m7GpppG-capped RNA) but is required to stabilize the movement of the N-terminal loop of NCBP2/CBP20 and lock the CBC into a high affinity cap-binding state with the cap structure. Associates with NCBP3 to form an alternative cap-binding complex (CBC) which plays a key role in mRNA export and is particularly important in cellular stress situations such as virus infections. The conventional CBC with NCBP2 binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus whereas the alternative CBC with NCBP3 does not bind snRNA and associates only with mRNA thereby playing a role only in mRNA export. NCBP1/CBP80 is required for cell growth and viability (By similarity)..
• Protein Sequence: MSRRRHSYENDGGQPHKRRKTSDANETEDHLESLICKVGEKSACSLESNLEGLAGVLEADLPNYKSKILRLLCTVARLLPEKLTIYTTLVGLLNARNYNFGGEFVEAMIRQLKESLKANNYNEAVYLVRFLSDLVNCHVIAAPSMVAMFENFVSVTQEEDVPQVRRDWYVYAFLSSLPWVGKELYEKKDAEMDRIFSTTESYLKRRQKTHVPMLQVWTADKPHPQEEYLDCLWAQIQKLKKDRWQERHILRPYLAFDSILCEALQHNLPPFTPPPHTEDSVYPMPRVIFRMFDYTDDPEGPVMPGSHSVERFVIEENLHCIIKSYWKERKTCAAQLVSYPGKNKIPLNYHIVEVIFAELFQLPAPPHIDVMYTTLLIELCKLQPGSLPQVLAQATEMLYMRLDTMSTTCVDRFINWFSHHLSNFQFRWSWEDWSDCLTQDLESPKPKFVREVLEKCMRLSYHQHILDIVPPTFSALCPANPTCIYKYGDESSNSLPGHSVALCLSVAFKSKATNDEIFSILKDVPNPNQVDDDDEGFRFNPLKIEVFVQTLLHLAAKSFSHSFSALAKFHEVFKTLAESDKGKLHVLRVMFEVWRNHPQMIAVLVDKMIRTQIVDCAAVANWIFSSELSRDFTRLFVWEILHSTIRKMNKHVLKIQKELEEAKEKLARQHKRRSDDDDRSSDRKDGALEEQIERLQEKVEAAQSEQKNLFLVIFQRFIMILTEHLVRCETDGTSILTPWYKNCIERLQQIFLQHHQTIQQYMVTLENLLFTAELDPHILAVFQQFCALQA

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
2	Phosphorylation	------MSRRRHSYE ------CCCCCCCCC	34.20	20469934
7	Phosphorylation	-MSRRRHSYENDGGQ -CCCCCCCCCCCCCC	32.12	27087446
8	Phosphorylation	MSRRRHSYENDGGQP CCCCCCCCCCCCCCC	16.78	27149854
17	Ubiquitination	NDGGQPHKRRKTSDA CCCCCCCCCCCCCCC	61.66	-
21	Phosphorylation	QPHKRRKTSDANETE CCCCCCCCCCCCCCH	29.99	27087446
22	Phosphorylation	PHKRRKTSDANETED CCCCCCCCCCCCCHH	37.45	27087446
27	Phosphorylation	KTSDANETEDHLESL CCCCCCCCHHHHHHH	46.66	27087446
33	Phosphorylation	ETEDHLESLICKVGE CCHHHHHHHHHHHCC	29.42	27742792
73	S-nitrosocysteine	SKILRLLCTVARLLP HHHHHHHHHHHHHCC	3.22	-
73	S-nitrosylation	SKILRLLCTVARLLP HHHHHHHHHHHHHCC	3.22	20925432
201	Phosphorylation	RIFSTTESYLKRRQK HHHHHHHHHHHHHHC	33.40	-
204	Acetylation	STTESYLKRRQKTHV HHHHHHHHHHHCCCC	36.98	-
306	Phosphorylation	EGPVMPGSHSVERFV CCCCCCCCCCCEEEE	13.50	24719451
522	Ubiquitination	DEIFSILKDVPNPNQ CHHHHHHCCCCCCCC	55.82	-
625	Phosphorylation	AVANWIFSSELSRDF HHHHHHHCCCCCHHH	17.48	30635358
626	Phosphorylation	VANWIFSSELSRDFT HHHHHHCCCCCHHHH	31.63	30635358
629	Phosphorylation	WIFSSELSRDFTRLF HHHCCCCCHHHHHHH	26.25	30635358
654	Malonylation	KMNKHVLKIQKELEE HHHHHHHHHHHHHHH	41.84	26320211
668	Methylation	EAKEKLARQHKRRSD HHHHHHHHHHHHCCC	49.96	30988195
672	Methylation	KLARQHKRRSDDDDR HHHHHHHHCCCCCCC	41.01	30988601
673	Methylation	LARQHKRRSDDDDRS HHHHHHHCCCCCCCC	49.60	30988607
674	Phosphorylation	ARQHKRRSDDDDRSS HHHHHHCCCCCCCCC	49.80	22817900
680	Phosphorylation	RSDDDDRSSDRKDGA CCCCCCCCCHHHCCH	43.51	29899451
698	Acetylation	QIERLQEKVEAAQSE HHHHHHHHHHHHHHH	32.20	-

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

Oops, there are no upstream regulatory protein records of NCBP1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NCBP1_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of NCBP1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of NCBP1_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND MASSSPECTROMETRY.
PubMed: 17242355