| General information | | DisProt: | DP00392 | | Name: | Nuclear cap-binding protein subunit 1 | | Synonym(s): | NCBP1_HUMAN
80 kDa nuclear cap-binding protein
NCBP 80 kDa subunit
CBP80
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | Q09161 | | UniGene: | Hs.595669 | | SwissProt: | NCBP1_HUMAN | | TrEMBL: | | | NCBI (GI): | 1705654 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 790 | | Percent disordered: | 7% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MSRRRHSDEN DGGQPHKRRK TSDANETEDH LESLICKVGE KSACSLESNL EGLAGVLEAD - 60
LPNYKSKILR LLCTVARLLP EKLTIYTTLV GLLNARNYNF GGEFVEAMIR QLKESLKANN - 120
YNEAVYLVRF LSDLVNCHVI AAPSMVAMFE NFVSVTQEED VPQVRRDWYV YAFLSSLPWV - 180
GKELYEKKDA EMDRIFANTE SYLKRRQKTH VPMLQVWTAD KPHPQEEYLD CLWAQIQKLK - 240
KDRWQERHIL RPYLAFDSIL CEALQHNLPP FTPPPHTEDS VYPMPRVIFR MFDYTDDPEG - 300
PVMPGSHSVE RFVIEENLHC IIKSHWKERK TCAAQLVSYP GKNKIPLNYH IVEVIFAELF - 360
QLPAPPHIDV MYTTLLIELC KLQPGSLPQV LAQATEMLYM RLDTMNTTCV DRFINWFSHH - 420
LSNFQFRWSW EDWSDCLSQD PESPKPKFVR EVLEKCMRLS YHQRILDIVP PTFSALCPAN - 480
PTCIYKYGDE SSNSLPGHSV ALCLAVAFKS KATNDEIFSI LKDVPNPNQD DDDDEGFSFN - 540
PLKIEVFVQT LLHLAAKSFS HSFSALAKFH EVFKTLAESD EGKLHVLRVM FEVWRNHPQM - 600
IAVLVDKMIR TQIVDCAAVA NWIFSSELSR DFTRLFVWEI LHSTIRKMNK HVLKIQKELE - 660
EAKEKLARQH KRRSDDDDRS SDRKDGVLEE QIERLQEKVE SAQSEQKNLF LVIFQRFIMI - 720
LTEHLVRCET DGTSVLTPWY KNCIERLQQI FLQHHQIIQQ YMVTLENLLF TAELDPHILA - 780
VFQQFCALQA
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| 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 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.
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| 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.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 1 - 19 | | Length: | 19 | | Region sequence: |
MSRRRHSDENDGGQPHKRR | | Modification type: | Complex
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Sensitivity to proteolysis (303 K; Buffer 7; Cap Binding Complex 3 mg/ml; Trypsin 15 ug/ml)
| References:
- 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:
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| Region 2 | | Type: | Disordered | | Name: | | | Location: | 671 - 684 | | Length: | 14 | | Region sequence: |
KRRSDDDDRSSDRK | | Modification type: | Complex
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- Sensitivity to proteolysis (303 K; Buffer 7; Cap Binding Complex 3 Mg/ml; Trypsin 15 ug/ml)
| References:
- 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:
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| Region 3 | | Type: | Disordered | | Name: | | | Location: | 20 - 26 | | Length: | 7 | | Region sequence: |
KTSDANE | | Modification type: | Complex
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (277 K; Magnesium formate (50-100 mM))
| References:
- 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:
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| Region 4 | | Type: | Disordered | | Name: | | | Location: | 527 - 537 | | Length: | 11 | | Region sequence: |
PNQDDDDDEGF | | Modification type: | Complex
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (277 K; Magnesium formate (50-100 mM))
| References:
- 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:
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| Region 5 | | Type: | Disordered | | Name: | | | Location: | 666 - 670 | | Length: | 5 | | Region sequence: |
LARQH | | Modification type: | Complex
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (277 K; Magnesium formate (50-100 mM))
| References:
- 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:
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| Region 6 | | Type: | Disordered | | Name: | | | Location: | 685 - 687 | | Length: | 3 | | Region sequence: |
DGV | | Modification type: | Complex
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (277 K; Magnesium formate (50-100 mM))
| References:
- 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:
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| Comments |
The SwissProt and NCBI sequences have an L at position 752. However, the referenced paper has a D at position 752.
Additional UniGene ID: Hs.686479
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