dbPTM

NCBP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NCBP1_HUMAN
UniProt AC	Q09161
Protein Name	Nuclear cap-binding protein subunit 1
Gene Name	NCBP1
Organism	Homo sapiens (Human).
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. [PubMed: 26382858]
Protein Sequence	MSRRRHSDENDGGQPHKRRKTSDANETEDHLESLICKVGEKSACSLESNLEGLAGVLEADLPNYKSKILRLLCTVARLLPEKLTIYTTLVGLLNARNYNFGGEFVEAMIRQLKESLKANNYNEAVYLVRFLSDLVNCHVIAAPSMVAMFENFVSVTQEEDVPQVRRDWYVYAFLSSLPWVGKELYEKKDAEMDRIFANTESYLKRRQKTHVPMLQVWTADKPHPQEEYLDCLWAQIQKLKKDRWQERHILRPYLAFDSILCEALQHNLPPFTPPPHTEDSVYPMPRVIFRMFDYTDDPEGPVMPGSHSVERFVIEENLHCIIKSHWKERKTCAAQLVSYPGKNKIPLNYHIVEVIFAELFQLPAPPHIDVMYTTLLIELCKLQPGSLPQVLAQATEMLYMRLDTMNTTCVDRFINWFSHHLSNFQFRWSWEDWSDCLSQDPESPKPKFVREVLEKCMRLSYHQRILDIVPPTFSALCPANPTCIYKYGDESSNSLPGHSVALCLAVAFKSKATNDEIFSILKDVPNPNQDDDDDEGFSFNPLKIEVFVQTLLHLAAKSFSHSFSALAKFHEVFKTLAESDEGKLHVLRVMFEVWRNHPQMIAVLVDKMIRTQIVDCAAVANWIFSSELSRDFTRLFVWEILHSTIRKMNKHVLKIQKELEEAKEKLARQHKRRSDDDDRSSDRKDGVLEEQIERLQEKVESAQSEQKNLFLVIFQRFIMILTEHLVRCETDGTSVLTPWYKNCIERLQQIFLQHHQIIQQYMVTLENLLFTAELDPHILAVFQQFCALQA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSRRRHSDE ------CCCCCCCCC	34.20	26074081
7	Phosphorylation	-MSRRRHSDENDGGQ -CCCCCCCCCCCCCC	44.82	22167270
21	Phosphorylation	QPHKRRKTSDANETE CCCCCCCCCCCCCCH	29.99	29255136
22	Phosphorylation	PHKRRKTSDANETED CCCCCCCCCCCCCHH	37.45	29255136
27	Phosphorylation	KTSDANETEDHLESL CCCCCCCCHHHHHHH	46.66	22167270
33	Phosphorylation	ETEDHLESLICKVGE CCHHHHHHHHHHHCC	29.42	23927012
36	Glutathionylation	DHLESLICKVGEKSA HHHHHHHHHHCCHHC	3.38	22555962
37	Ubiquitination	HLESLICKVGEKSAC HHHHHHHHHCCHHCC	46.40	-
37	Acetylation	HLESLICKVGEKSAC HHHHHHHHHCCHHCC	46.40	26051181
41	Ubiquitination	LICKVGEKSACSLES HHHHHCCHHCCCHHH	37.11	-
73	S-nitrosocysteine	SKILRLLCTVARLLP HHHHHHHHHHHHHCC	3.22	-
73	S-nitrosylation	SKILRLLCTVARLLP HHHHHHHHHHHHHCC	3.22	19483679
84	Phosphorylation	RLLPEKLTIYTTLVG HHCCHHHHHHHHHHH	24.01	20860994
86	Phosphorylation	LPEKLTIYTTLVGLL CCHHHHHHHHHHHHH	6.61	20860994
87	Phosphorylation	PEKLTIYTTLVGLLN CHHHHHHHHHHHHHH	15.14	23403867
88	Phosphorylation	EKLTIYTTLVGLLNA HHHHHHHHHHHHHHH	11.50	21406692
117	Acetylation	RQLKESLKANNYNEA HHHHHHHHCCCHHHH	59.35	25953088
117	Ubiquitination	RQLKESLKANNYNEA HHHHHHHHCCCHHHH	59.35	21890473
121	Phosphorylation	ESLKANNYNEAVYLV HHHHCCCHHHHHHHH	17.75	28152594
126	Phosphorylation	NNYNEAVYLVRFLSD CCHHHHHHHHHHHHH	13.41	28152594
132	Phosphorylation	VYLVRFLSDLVNCHV HHHHHHHHHHCCCCC	26.62	30175587
144	Phosphorylation	CHVIAAPSMVAMFEN CCCCCCHHHHHHHHH	22.59	30175587
175	Phosphorylation	WYVYAFLSSLPWVGK HHHHHHHHCCCCCCH	24.31	-
194	Methylation	KKDAEMDRIFANTES HCCHHHHHHHHCHHH	25.31	115484561
201	Phosphorylation	RIFANTESYLKRRQK HHHHCHHHHHHHHHH	33.45	20068231
202	Phosphorylation	IFANTESYLKRRQKT HHHCHHHHHHHHHHC	15.26	23186163
204	Methylation	ANTESYLKRRQKTHV HCHHHHHHHHHHCCC	36.98	-
204	Acetylation	ANTESYLKRRQKTHV HCHHHHHHHHHHCCC	36.98	19608861
204	Ubiquitination	ANTESYLKRRQKTHV HCHHHHHHHHHHCCC	36.98	21906983
204	2-Hydroxyisobutyrylation	ANTESYLKRRQKTHV HCHHHHHHHHHHCCC	36.98	-
294	Phosphorylation	VIFRMFDYTDDPEGP CEEEECCCCCCCCCC	10.78	21406692
295	Phosphorylation	IFRMFDYTDDPEGPV EEEECCCCCCCCCCC	35.45	21406692
306	Phosphorylation	EGPVMPGSHSVERFV CCCCCCCCCCEEEEE	13.50	28985074
308	Phosphorylation	PVMPGSHSVERFVIE CCCCCCCCEEEEEEE	27.63	21406692
320	Glutathionylation	VIEENLHCIIKSHWK EEECCHHHHHHHHHH	3.76	22555962
323	Ubiquitination	ENLHCIIKSHWKERK CCHHHHHHHHHHCCC	19.16	-
330	Ubiquitination	KSHWKERKTCAAQLV HHHHHCCCCHHHHHH	49.39	-
330	Malonylation	KSHWKERKTCAAQLV HHHHHCCCCHHHHHH	49.39	32601280
386	Phosphorylation	LCKLQPGSLPQVLAQ HHCCCCCCHHHHHHH	43.49	24719451
395	Phosphorylation	PQVLAQATEMLYMRL HHHHHHHHHHHHHHH	15.17	24719451
405	Sulfoxidation	LYMRLDTMNTTCVDR HHHHHHHCCCHHHHH	4.13	21406390
434	Phosphorylation	RWSWEDWSDCLSQDP ECCHHHHHHHHHCCC	30.67	20873877
438	Phosphorylation	EDWSDCLSQDPESPK HHHHHHHHCCCCCCC	38.58	20873877
443	Phosphorylation	CLSQDPESPKPKFVR HHHCCCCCCCCHHHH	43.54	20873877
455	Acetylation	FVREVLEKCMRLSYH HHHHHHHHHHHHHHH	29.21	26051181
455	2-Hydroxyisobutyrylation	FVREVLEKCMRLSYH HHHHHHHHHHHHHHH	29.21	-
455	Ubiquitination	FVREVLEKCMRLSYH HHHHHHHHHHHHHHH	29.21	-
477	S-nitrosocysteine	PPTFSALCPANPTCI CCCHHHHCCCCCCEE	2.75	-
477	S-nitrosylation	PPTFSALCPANPTCI CCCHHHHCCCCCCEE	2.75	19483679
483	S-nitrosocysteine	LCPANPTCIYKYGDE HCCCCCCEEEEECCC	3.18	-
483	S-nitrosylation	LCPANPTCIYKYGDE HCCCCCCEEEEECCC	3.18	19483679
511	Ubiquitination	LAVAFKSKATNDEIF HHHHHHCCCCCCHHH	60.87	-
511	2-Hydroxyisobutyrylation	LAVAFKSKATNDEIF HHHHHHCCCCCCHHH	60.87	-
513	Phosphorylation	VAFKSKATNDEIFSI HHHHCCCCCCHHHHH	47.11	21712546
519	Phosphorylation	ATNDEIFSILKDVPN CCCCHHHHHHHCCCC	32.45	24719451
522	Ubiquitination	DEIFSILKDVPNPNQ CHHHHHHHCCCCCCC	55.82	-
564	Phosphorylation	KSFSHSFSALAKFHE HHCCCCHHHHHHHHH	25.95	29507054
568	Acetylation	HSFSALAKFHEVFKT CCHHHHHHHHHHHHH	48.37	25953088
574	Acetylation	AKFHEVFKTLAESDE HHHHHHHHHHHHCCC	48.05	25825284
575	Phosphorylation	KFHEVFKTLAESDEG HHHHHHHHHHHCCCC	21.53	29507054
579	Phosphorylation	VFKTLAESDEGKLHV HHHHHHHCCCCCCHH	35.04	29507054
583	Ubiquitination	LAESDEGKLHVLRVM HHHCCCCCCHHHHHH	33.11	-
583	2-Hydroxyisobutyrylation	LAESDEGKLHVLRVM HHHCCCCCCHHHHHH	33.11	-
607	Acetylation	MIAVLVDKMIRTQIV HHHHHHHHHHHHHHC	28.84	26051181
607	2-Hydroxyisobutyrylation	MIAVLVDKMIRTQIV HHHHHHHHHHHHHHC	28.84	-
611	Phosphorylation	LVDKMIRTQIVDCAA HHHHHHHHHHCHHHH	16.24	-
625	O-linked_Glycosylation	AVANWIFSSELSRDF HHHHHHHCCCCCHHH	17.48	29351928
626	O-linked_Glycosylation	VANWIFSSELSRDFT HHHHHHCCCCCHHHH	31.63	29351928
633	Phosphorylation	SELSRDFTRLFVWEI CCCCHHHHHHHHHHH	30.65	-
643	Phosphorylation	FVWEILHSTIRKMNK HHHHHHHHHHHHHHH	23.29	-
644	Phosphorylation	VWEILHSTIRKMNKH HHHHHHHHHHHHHHH	17.66	-
654	Acetylation	KMNKHVLKIQKELEE HHHHHHHHHHHHHHH	41.84	25953088
654	Ubiquitination	KMNKHVLKIQKELEE HHHHHHHHHHHHHHH	41.84	-
657	Acetylation	KHVLKIQKELEEAKE HHHHHHHHHHHHHHH	68.67	26051181
657	Ubiquitination	KHVLKIQKELEEAKE HHHHHHHHHHHHHHH	68.67	-
665	Acetylation	ELEEAKEKLARQHKR HHHHHHHHHHHHHHH	46.90	25953088
674	Phosphorylation	ARQHKRRSDDDDRSS HHHHHHCCCCCCCCC	49.80	17081983
680	Phosphorylation	RSDDDDRSSDRKDGV CCCCCCCCCHHHCCH	43.51	27134283
681	Phosphorylation	SDDDDRSSDRKDGVL CCCCCCCCHHHCCHH	42.18	29496963
684	Sumoylation	DDRSSDRKDGVLEEQ CCCCCHHHCCHHHHH	64.92	28112733
684	Acetylation	DDRSSDRKDGVLEEQ CCCCCHHHCCHHHHH	64.92	19826797
684	Ubiquitination	DDRSSDRKDGVLEEQ CCCCCHHHCCHHHHH	64.92	-
698	2-Hydroxyisobutyrylation	QIERLQEKVESAQSE HHHHHHHHHHHHHHH	38.04	-
698	Ubiquitination	QIERLQEKVESAQSE HHHHHHHHHHHHHHH	38.04	19608861
698	Acetylation	QIERLQEKVESAQSE HHHHHHHHHHHHHHH	38.04	19608861
707	Acetylation	ESAQSEQKNLFLVIF HHHHHHHHHHHHHHH	52.12	19826807
734	Phosphorylation	RCETDGTSVLTPWYK CCCCCCCCCCCHHHH	22.21	-
737	Phosphorylation	TDGTSVLTPWYKNCI CCCCCCCCHHHHHHH	15.04	-

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
7	S	Phosphorylation	Kinase	P70S6K	P23443	PSP
21	T	Phosphorylation	Kinase	P70S6K	P23443	PSP
22	S	Phosphorylation	Kinase	P70S6K	P23443	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NCBP1_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 NCBP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BRE1B_HUMAN	RNF40	physical	16189514
HNRPF_HUMAN	HNRNPF	physical	9111328
HNRH1_HUMAN	HNRNPH1	physical	9111328
NCBP2_HUMAN	NCBP2	physical	12434151
NCBP2_HUMAN	NCBP2	physical	11545740
BNIP2_HUMAN	BNIP2	physical	7478990
BNIP3_HUMAN	BNIP3	physical	7478990
SEC20_HUMAN	BNIP1	physical	7478990
ICP27_HHV8P	ORF57	physical	18974867
SMAD4_HUMAN	SMAD4	physical	17190602
THOC4_HUMAN	ALYREF	physical	17190602
DX39B_HUMAN	DDX39B	physical	17190602
THOC2_HUMAN	THOC2	physical	17190602
THOC5_HUMAN	THOC5	physical	17190602
THOC1_HUMAN	THOC1	physical	17190602
THOC3_HUMAN	THOC3	physical	17190602
THOC6_HUMAN	THOC6	physical	17190602
NCBP2_HUMAN	NCBP2	physical	17190602
NCBP2_HUMAN	NCBP2	physical	22939629
RB6I2_HUMAN	ERC1	physical	22939629
NCBP2_HUMAN	NCBP2	physical	22365833
NCBP3_HUMAN	C17orf85	physical	22365833
GARS_HUMAN	GARS	physical	22863883
MVP_HUMAN	MVP	physical	22863883
NP1L4_HUMAN	NAP1L4	physical	22863883
NUCL_HUMAN	NCL	physical	22863883
PPM1G_HUMAN	PPM1G	physical	22863883
TTC1_HUMAN	TTC1	physical	22863883
VAT1_HUMAN	VAT1	physical	22863883
LN28A_HUMAN	LIN28A	physical	24778252
REN3B_HUMAN	UPF3B	physical	18423201
PDIP3_HUMAN	POLDIP3	physical	18423201
KS6B1_HUMAN	RPS6KB1	physical	18423201
MTOR_HUMAN	MTOR	physical	18423201
EIF3B_HUMAN	EIF3B	physical	18423201
PDIP3_HUMAN	POLDIP3	physical	25049393
IF4G1_HUMAN	EIF4G1	physical	25049393
DYHC1_HUMAN	DYNC1H1	physical	26344197
IMDH2_HUMAN	IMPDH2	physical	26344197
6PGD_HUMAN	PGD	physical	26344197
SNX2_HUMAN	SNX2	physical	26344197
STKL1_HUMAN	STKLD1	physical	26344197
PUR2_HUMAN	GART	physical	26496610
IMA1_HUMAN	KPNA2	physical	26496610
IMA4_HUMAN	KPNA3	physical	26496610
IMA3_HUMAN	KPNA4	physical	26496610
NFIC_HUMAN	NFIC	physical	26496610
2AAB_HUMAN	PPP2R1B	physical	26496610
NELFA_HUMAN	NELFA	physical	26496610
NELFE_HUMAN	NELFE	physical	26496610
UBL4A_HUMAN	UBL4A	physical	26496610
TRRAP_HUMAN	TRRAP	physical	26496610
GEMI2_HUMAN	GEMIN2	physical	26496610
AP1M1_HUMAN	AP1M1	physical	26496610
GCN1_HUMAN	GCN1L1	physical	26496610
NUPL2_HUMAN	NUPL2	physical	26496610
DDX20_HUMAN	DDX20	physical	26496610
NCBP2_HUMAN	NCBP2	physical	26496610
PPRC1_HUMAN	PPRC1	physical	26496610
RPRD2_HUMAN	RPRD2	physical	26496610
SK2L2_HUMAN	SKIV2L2	physical	26496610
APOL2_HUMAN	APOL2	physical	26496610
LTMD1_HUMAN	LETMD1	physical	26496610
NELFB_HUMAN	NELFB	physical	26496610
RSRC1_HUMAN	RSRC1	physical	26496610
NELFD_HUMAN	NELFCD	physical	26496610
SRRT_HUMAN	SRRT	physical	26496610
PHAX_HUMAN	PHAX	physical	26496610
LYAR_HUMAN	LYAR	physical	26496610
BRAT1_HUMAN	BRAT1	physical	26496610

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 NCBP1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-204 AND LYS-698, AND MASSSPECTROMETRY.	19608861 [Abstract]
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-22, AND MASSSPECTROMETRY.	19690332 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21 AND SER-22, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Cdc42 stimulates RNA splicing via the S6 kinase and a novel S6 kinasetarget, the nuclear cap-binding complex."; Wilson K.F., Wu W.J., Cerione R.A.; J. Biol. Chem. 275:37307-37310(2000). Cited for: PHOSPHORYLATION AT SER-7; THR-21 AND SER-22, AND MUTAGENESIS OF SER-7;17-LYS-ARG-18 AND 21-THR-SER-22.	10973943 [Abstract]