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DP00393: Nuclear cap-binding protein subunit 2 [Isoform 1]FASTA viewXML view

General information
DisProt:DP00393
Name:Nuclear cap-binding protein subunit 2 [Isoform 1]
Synonym(s):NCBP2_HUMAN
NCBP-interacting protein 1
NIP1
20 kDa nuclear cap-binding protein
NCBP 20 kDa subunit
CBP20
Cell proliferation-inducing gene 55 protein
First appeared in release:Release 3.0 (02/17/2006)
UniProt:P52298-1
UniGene:Hs.591671
SwissProt: NCBP2_HUMAN
TrEMBL:  
NCBI (GI): 1705651
Source organism:Homo sapiens (Human)
Sequence length:156
Percent disordered:51%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MSGGLLKALR SDSYVELSQY RDQHFRGDNE EQEKLLKKSC TLYVGNLSFY TTEEQIYELF - 60
SKSGDIKKII MGLDKMKKTA CGFCFVEYYS RADAENAMRY INGTRLDDRI IRTDWDAGFK - 120
EGRQYGRGRS GGQVRDEYRQ DYDAGRGGYG KLAQNQ



Functional narrative    

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 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.

Region 1: 1-21 Region 2: 22-37 Region 3: 77-78 Region 4: 79-80 Region 6: 119-120 Region 5: 121-156

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name: 
Location:1 - 21
Length:21
Region sequence:

MSGGLLKALRSDSYVELSQYR

Modification type: Complex
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Molecular assembly
Functional subclasses: Protein-genomic RNA binding
Protein-protein binding
Detection methods:
  1. Sensitivity to proteolysis (303 K; Buffer 7; Cap Binding Complex 3 mg/ml; Tryspin 15 ug/ml)

References:
  1. Mazza C, Ohno M, Segref A, Mattaj IW, Cusack S. "Crystal structure of the human nuclear cap binding complex." Mol Cell. 2001; 8(2): 383-96. PubMed: 11545740

Comments:
 



Region 2
Type:Disordered
Name: 
Location:22 - 37
Length:16
Region sequence:

DQHFRGDNEEQEKLLK

Modification type: Complex
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Molecular assembly
Functional subclasses: Protein-genomic RNA binding
Protein-protein binding
Detection methods:
  1. X-ray crystallography (277 K; Magnesium formate (50-100 mM))

References:
  1. Mazza C, Ohno M, Segref A, Mattaj IW, Cusack S. "Crystal structure of the human nuclear cap binding complex." Mol Cell. 2001; 8(2): 383-96. PubMed: 11545740

Comments:
 



Region 3
Type:Disordered
Name: 
Location:77 - 78
Length:2
Region sequence:

KK

Modification type: Complex
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. Sensitivity to proteolysis (303 K; Buffer 7; Cap Binding Complex 3 mg/ml; Trypsin 15 ug/ml)

References:
  1. Mazza C, Ohno M, Segref A, Mattaj IW, Cusack S. "Crystal structure of the human nuclear cap binding complex." Mol Cell. 2001; 8(2): 383-96. PubMed: 11545740

Comments:
 



Region 4
Type:Disordered
Name: 
Location:79 - 80
Length:2
Region sequence:

TA

Modification type: Complex
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography (277 K; Magnesium formate (50-100 mM))

References:
  1. Mazza C, Ohno M, Segref A, Mattaj IW, Cusack S. "Crystal structure of the human nuclear cap binding complex." Mol Cell. 2001; 8(2): 383-96. PubMed: 11545740

Comments:
 



Region 5
Type:Disordered
Name: 
Location:121 - 156
Length:36
Region sequence:

EGRQYGRGRSGGQVRDEYRQDYDAGRGGYGKLAQNQ

Modification type: Complex
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Molecular assembly
Functional subclasses: Protein-genomic RNA binding
Protein-protein binding
Detection methods:
  1. Sensitivity to proteolysis (303 K; Buffer 7; Cap Binding Complex 3 mg/ml; Trypsin 15 ug/ml)

References:
  1. Mazza C, Ohno M, Segref A, Mattaj IW, Cusack S. "Crystal structure of the human nuclear cap binding complex." Mol Cell. 2001; 8(2): 383-96. PubMed: 11545740

Comments:
 



Region 6
Type:Disordered
Name: 
Location:119 - 120
Length:2
Region sequence:

FK

Modification type: Complex
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Molecular assembly
Functional subclasses: Protein-genomic RNA binding
Protein-protein binding
Detection methods:
  1. X-ray crystallography (277 K; Magnesium formate (50-100 mM))

References:
  1. Mazza C, Ohno M, Segref A, Mattaj IW, Cusack S. "Crystal structure of the human nuclear cap binding complex." Mol Cell. 2001; 8(2): 383-96. PubMed: 11545740

Comments:
 



References

  1. Izaurralde E, Lewis J, Gamberi C, Jarmolowski A, McGuigan C, Mattaj IW. "A cap-binding protein complex mediating U snRNA export." Nature. 1995; 376(6542): 709-12. PubMed: 7651522


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