NCBP2_HUMAN - dbPTM
NCBP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NCBP2_HUMAN
UniProt AC P52298
Protein Name Nuclear cap-binding protein subunit 2
Gene Name NCBP2
Organism Homo sapiens (Human).
Sequence Length 156
Subcellular Localization Nucleus . Cytoplasm .
Protein Description Component of the cap-binding complex (CBC), which binds co-transcriptionally 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, thereby being 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, NCBP2/CBP20 recognizes and binds capped RNAs (m7GpppG-capped RNA) but requires NCBP1/CBP80 to stabilize the movement of its N-terminal loop and lock the CBC into a high affinity cap-binding state with the cap structure. The conventional cap-binding complex with NCBP2 binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus. [PubMed: 26382858]
Protein Sequence MSGGLLKALRSDSYVELSQYRDQHFRGDNEEQEKLLKKSCTLYVGNLSFYTTEEQIYELFSKSGDIKKIIMGLDKMKKTACGFCFVEYYSRADAENAMRYINGTRLDDRIIRTDWDAGFKEGRQYGRGRSGGQVRDEYRQDYDAGRGGYGKLAQNQ
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 Orthologous
Protein Cluster
2Acetylation------MSGGLLKAL
------CCCHHHHHH		41.3822814378
7Ubiquitination-MSGGLLKALRSDSY
-CCCHHHHHHHCCCC		50.87-
7Ubiquitination-MSGGLLKALRSDSY
-CCCHHHHHHHCCCC		50.87-
7Methylation-MSGGLLKALRSDSY
-CCCHHHHHHHCCCC		50.87115973733
11PhosphorylationGLLKALRSDSYVELS
HHHHHHHCCCCEEHH		31.5822617229
13PhosphorylationLKALRSDSYVELSQY
HHHHHCCCCEEHHHH		32.1223401153
14PhosphorylationKALRSDSYVELSQYR
HHHHCCCCEEHHHHH		11.7020007894
18PhosphorylationSDSYVELSQYRDQHF
CCCCEEHHHHHHHHC		16.2017525332
34AcetylationGDNEEQEKLLKKSCT
CCHHHHHHHHHHHCE		59.83-
34AcetylationGDNEEQEKLLKKSCT
CCHHHHHHHHHHHCE		59.8326051181
34UbiquitinationGDNEEQEKLLKKSCT
CCHHHHHHHHHHHCE		59.83-
37AcetylationEEQEKLLKKSCTLYV
HHHHHHHHHHCEEEE		53.7526051181
39 (in isoform 3)Phosphorylation-15.67-
57PhosphorylationYTTEEQIYELFSKSG
EECHHHHHHHHHCCC		13.28-
61PhosphorylationEQIYELFSKSGDIKK
HHHHHHHHCCCCHHH		38.2424719451
67UbiquitinationFSKSGDIKKIIMGLD
HHCCCCHHHHHHCHH		42.5321906983
75UbiquitinationKIIMGLDKMKKTACG
HHHHCHHHHHHCCCC		58.63-
75AcetylationKIIMGLDKMKKTACG
HHHHCHHHHHHCCCC		58.6325953088
752-HydroxyisobutyrylationKIIMGLDKMKKTACG
HHHHCHHHHHHCCCC		58.63-
79PhosphorylationGLDKMKKTACGFCFV
CHHHHHHCCCCEEEE		22.97-
89PhosphorylationGFCFVEYYSRADAEN
CEEEEEEHHHHCHHH		4.34-
98AcetylationRADAENAMRYINGTR
HHCHHHHHHHHCCCC		5.1519608861
98UbiquitinationRADAENAMRYINGTR
HHCHHHHHHHHCCCC		5.1519608861
102 (in isoform 2)Ubiquitination-36.5321890473
120 (in isoform 1)Ubiquitination-59.3421890473
120AcetylationTDWDAGFKEGRQYGR
CCCCCCCCCCCCCCC		59.3425953088
120UbiquitinationTDWDAGFKEGRQYGR
CCCCCCCCCCCCCCC		59.3421890473
125PhosphorylationGFKEGRQYGRGRSGG
CCCCCCCCCCCCCCC		13.8726074081
130PhosphorylationRQYGRGRSGGQVRDE
CCCCCCCCCCCCCHH		50.5325159151
133UbiquitinationGRGRSGGQVRDEYRQ
CCCCCCCCCCHHHHH		30.5119608861
133AcetylationGRGRSGGQVRDEYRQ
CCCCCCCCCCHHHHH		30.5119608861
138PhosphorylationGGQVRDEYRQDYDAG
CCCCCHHHHHCCCCC		20.1929214152
139MethylationGQVRDEYRQDYDAGR
CCCCHHHHHCCCCCC		22.35115385865
142PhosphorylationRDEYRQDYDAGRGGY
CHHHHHCCCCCCCCC		10.1928796482
146MethylationRQDYDAGRGGYGKLA
HHCCCCCCCCCHHHH		36.7624129315
151UbiquitinationAGRGGYGKLAQNQ--
CCCCCCHHHHCCC--		31.9719608861
151MethylationAGRGGYGKLAQNQ--
CCCCCCHHHHCCC--		31.9722638809
151AcetylationAGRGGYGKLAQNQ--
CCCCCCHHHHCCC--		31.9719608861
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

Oops, there are no upstream regulatory protein records of NCBP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NCBP2_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 NCBP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NCBP1_HUMANNCBP1physical
7478990
HNRPF_HUMANHNRNPFphysical
9111328
HNRH1_HUMANHNRNPH1physical
9111328
NCBP1_HUMANNCBP1physical
22365833
LZTS2_HUMANLZTS2physical
25416956
ARHL2_HUMANADPRHL2physical
26344197
NCBP1_HUMANNCBP1physical
26344197
HNRPQ_HUMANSYNCRIPphysical
26344197
TZAP_HUMANZBTB48physical
26496610
IMA1_HUMANKPNA2physical
26496610
IMA4_HUMANKPNA3physical
26496610
IMA3_HUMANKPNA4physical
26496610
NCBP1_HUMANNCBP1physical
26496610
NUP98_HUMANNUP98physical
26496610
RL10_HUMANRPL10physical
26496610
STX3_HUMANSTX3physical
26496610
NELFE_HUMANNELFEphysical
26496610
ELL_HUMANELLphysical
26496610
PRP4B_HUMANPRPF4Bphysical
26496610
PPRC1_HUMANPPRC1physical
26496610
ICE1_HUMANICE1physical
26496610
SK2L2_HUMANSKIV2L2physical
26496610
IMA7_HUMANKPNA6physical
26496610
PHAX_HUMANPHAXphysical
26496610
ZCHC8_HUMANZCCHC8physical
26496610
LENG1_HUMANLENG1physical
26496610
SYTC2_HUMANTARSL2physical
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 NCBP2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-151, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASSSPECTROMETRY.

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