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P52298

- NCBP2_HUMAN

UniProt

P52298 - NCBP2_HUMAN

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Protein
Nuclear cap-binding protein subunit 2
Gene
NCBP2, CBP20, PIG55
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.7 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei20 – 201mRNA cap
Binding sitei43 – 431mRNA cap

GO - Molecular functioni

  1. RNA 7-methylguanosine cap binding Source: UniProtKB
  2. RNA cap binding Source: UniProtKB
  3. nucleotide binding Source: InterPro
  4. poly(A) RNA binding Source: UniProtKB
  5. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. 7-methylguanosine mRNA capping Source: UniProtKB
  2. RNA metabolic process Source: Reactome
  3. RNA splicing Source: UniProtKB
  4. gene expression Source: Reactome
  5. gene silencing by RNA Source: UniProtKB-KW
  6. histone mRNA metabolic process Source: Reactome
  7. mRNA 3'-end processing Source: Reactome
  8. mRNA cis splicing, via spliceosome Source: UniProtKB
  9. mRNA export from nucleus Source: Reactome
  10. mRNA metabolic process Source: Reactome
  11. mRNA splicing, via spliceosome Source: Reactome
  12. ncRNA metabolic process Source: Reactome
  13. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
  14. positive regulation of RNA export from nucleus Source: UniProtKB
  15. positive regulation of viral transcription Source: Reactome
  16. regulation of translational initiation Source: UniProtKB
  17. snRNA export from nucleus Source: UniProtKB
  18. spliceosomal snRNP assembly Source: Reactome
  19. termination of RNA polymerase II transcription Source: Reactome
  20. transcription elongation from RNA polymerase II promoter Source: Reactome
  21. transcription from RNA polymerase II promoter Source: Reactome
  22. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

mRNA capping, mRNA processing, mRNA splicing, mRNA transport, Nonsense-mediated mRNA decay, RNA-mediated gene silencing, Translation regulation, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_1096. Processing of Intronless Pre-mRNAs.
REACT_11066. snRNP Assembly.
REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_1364. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
REACT_1470. mRNA Capping.
REACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
REACT_1753. mRNA Splicing - Minor Pathway.
REACT_1835. Transport of Mature mRNA Derived from an Intronless Transcript.
REACT_1849. mRNA 3'-end processing.
REACT_185. SLBP independent Processing of Histone Pre-mRNAs.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_405. Transport of the SLBP Dependant Mature mRNA.
REACT_424. Transport of the SLBP independent Mature mRNA.
REACT_467. mRNA Splicing - Major Pathway.
REACT_6261. Abortive elongation of HIV-1 transcript in the absence of Tat.
REACT_6319. Formation of the HIV-1 Early Elongation Complex.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_846. Formation of the Early Elongation Complex.

Protein family/group databases

TCDBi9.A.60.1.1. the small nuclear rna exporter (snrna-e).

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear cap-binding protein subunit 2
Alternative name(s):
20 kDa nuclear cap-binding protein
Cell proliferation-inducing gene 55 protein
NCBP 20 kDa subunit
Short name:
CBP20
NCBP-interacting protein 1
Short name:
NIP1
Gene namesi
Name:NCBP2
Synonyms:CBP20
ORF Names:PIG55
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:7659. NCBP2.

Subcellular locationi

Nucleus. Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. mRNA cap binding complex Source: UniProtKB
  4. nuclear cap binding complex Source: InterPro
  5. nucleoplasm Source: UniProtKB
  6. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi20 – 201Y → A: Abolishes mRNA cap-binding. 1 Publication
Mutagenesisi20 – 201Y → F: Strongly impairs mRNA cap-binding. 1 Publication
Mutagenesisi25 – 251F → A: Does not affect mRNA cap-binding. 1 Publication
Mutagenesisi43 – 431Y → A: Abolishes mRNA cap-binding. 2 Publications
Mutagenesisi43 – 431Y → F: Does not affect mRNA cap-binding. 2 Publications
Mutagenesisi46 – 461N → A: Does not affect mRNA cap-binding. 1 Publication
Mutagenesisi83 – 831F → A: Abolishes mRNA cap-binding. 1 Publication
Mutagenesisi85 – 851F → A: Impairs mRNA cap-binding.
Mutagenesisi112 – 1121R → A or T: Does not affect mRNA cap-binding. 1 Publication
Mutagenesisi114 – 1141D → A: Does not affect mRNA cap-binding. 1 Publication
Mutagenesisi116 – 1161D → A: Abolishes mRNA cap-binding. 1 Publication
Mutagenesisi119 – 1191F → A: Does not affect mRNA cap-binding. 1 Publication
Mutagenesisi138 – 1381Y → A: Does not affect mRNA cap-binding. 1 Publication

Organism-specific databases

PharmGKBiPA31462.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 156155Nuclear cap-binding protein subunit 2
PRO_0000081499Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei18 – 181Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP52298.
PaxDbiP52298.
PRIDEiP52298.

PTM databases

PhosphoSiteiP52298.

Expressioni

Gene expression databases

ArrayExpressiP52298.
BgeeiP52298.
CleanExiHS_NCBP2.
GenevestigatoriP52298.

Organism-specific databases

HPAiHPA044850.

Interactioni

Subunit structurei

Component of the nuclear cap-binding complex (CBC), a heterodimer composed of NCBP1/CBP80 and NCBP2/CBP20 that interacts with m7GpppG-capped RNA. Found in a U snRNA export complex with RNUXA/PHAX, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA. Interacts with RNUXA/PHAX, EIF4G1, HNRNPF, HNRNPH1 and ALYREF/THOC4/ALY.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NCBP1Q091616EBI-464729,EBI-464743

Protein-protein interaction databases

BioGridi116578. 15 interactions.
DIPiDIP-33246N.
IntActiP52298. 8 interactions.
MINTiMINT-248711.
STRINGi9606.ENSP00000326806.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 104
Helixi13 – 153
Beta strandi23 – 275
Turni34 – 385
Beta strandi41 – 466
Helixi53 – 608
Helixi61 – 633
Beta strandi66 – 738
Turni75 – 773
Beta strandi80 – 9011
Helixi91 – 10010
Turni101 – 1033
Beta strandi104 – 1063
Beta strandi112 – 1176
Turni121 – 1244
Helixi134 – 1374
Helixi144 – 1463

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H2TX-ray2.15Z1-156[»]
1H2UX-ray2.40X/Y1-156[»]
1H2VX-ray2.00Z1-156[»]
1H6KX-ray2.00X/Y/Z22-120[»]
1N52X-ray2.11B1-156[»]
1N54X-ray2.72B1-156[»]
3FEXX-ray3.55B1-156[»]
3FEYX-ray2.20B1-156[»]
DisProtiDP00393.
ProteinModelPortaliP52298.
SMRiP52298. Positions 5-149.

Miscellaneous databases

EvolutionaryTraceiP52298.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 11879RRM
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni112 – 1165mRNA cap-binding
Regioni123 – 1275mRNA cap-binding
Regioni133 – 1342mRNA cap-binding

Sequence similaritiesi

Belongs to the RRM NCBP2 family.

Phylogenomic databases

eggNOGiCOG0724.
HOGENOMiHOG000217589.
HOVERGENiHBG052581.
InParanoidiP52298.
KOiK12883.
OMAiGNRYEQE.
PhylomeDBiP52298.
TreeFamiTF313897.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR027157. NCBP2.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PANTHERiPTHR18847. PTHR18847. 1 hit.
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P52298-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MSGGLLKALR SDSYVELSQY RDQHFRGDNE EQEKLLKKSC TLYVGNLSFY    50
TTEEQIYELF SKSGDIKKII MGLDKMKKTA CGFCFVEYYS RADAENAMRY 100
INGTRLDDRI IRTDWDAGFK EGRQYGRGRS GGQVRDEYRQ DYDAGRGGYG 150
KLAQNQ 156
Length:156
Mass (Da):18,001
Last modified:October 1, 1996 - v1
Checksum:iB6C94F3182A2CC3D
GO
Isoform 2 (identifier: P52298-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MSGGLLKALRSDSYVELSQYRDQHFR → MVLRKLYA

Show »
Length:138
Mass (Da):15,937
Checksum:iD2475AF0597FDC0F
GO
Isoform 3 (identifier: P52298-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     40-93: CTLYVGNLSFYTTEEQIYELFSKSGDIKKIIMGLDKMKKTACGFCFVEYYSRAD → Y

Note: Gene prediction based on EST data.

Show »
Length:103
Mass (Da):11,932
Checksum:i0790F40FF3E16B61
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2626MSGGL…DQHFR → MVLRKLYA in isoform 2.
VSP_038125Add
BLAST
Alternative sequencei40 – 9354CTLYV…YSRAD → Y in isoform 3.
VSP_053823Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971A → S in BAA09599. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X84157 mRNA. Translation: CAA58962.1.
D59253 mRNA. Translation: BAA09599.1.
AK297506 mRNA. Translation: BAG59919.1.
AK315903 mRNA. Translation: BAH14274.1.
AK316601 mRNA. Translation: BAG38188.1.
AY644767 mRNA. Translation: AAV85455.1.
BT006842 mRNA. Translation: AAP35488.1.
AC011322 Genomic DNA. No translation available.
CH471191 Genomic DNA. Translation: EAW53624.1.
BC001255 mRNA. Translation: AAH01255.1.
CCDSiCCDS3323.1. [P52298-1]
CCDS46986.1. [P52298-3]
PIRiI37222.
S60109.
RefSeqiNP_001036005.1. NM_001042540.1. [P52298-3]
NP_031388.2. NM_007362.3. [P52298-1]
XP_005269370.1. XM_005269313.1. [P52298-2]
UniGeneiHs.591671.

Genome annotation databases

EnsembliENST00000321256; ENSP00000326806; ENSG00000114503. [P52298-1]
ENST00000427641; ENSP00000397619; ENSG00000114503.
ENST00000452404; ENSP00000412785; ENSG00000114503. [P52298-2]
GeneIDi22916.
KEGGihsa:22916.
UCSCiuc003fxb.1. human. [P52298-1]
uc011btz.1. human. [P52298-2]

Polymorphism databases

DMDMi1705651.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X84157 mRNA. Translation: CAA58962.1 .
D59253 mRNA. Translation: BAA09599.1 .
AK297506 mRNA. Translation: BAG59919.1 .
AK315903 mRNA. Translation: BAH14274.1 .
AK316601 mRNA. Translation: BAG38188.1 .
AY644767 mRNA. Translation: AAV85455.1 .
BT006842 mRNA. Translation: AAP35488.1 .
AC011322 Genomic DNA. No translation available.
CH471191 Genomic DNA. Translation: EAW53624.1 .
BC001255 mRNA. Translation: AAH01255.1 .
CCDSi CCDS3323.1. [P52298-1 ]
CCDS46986.1. [P52298-3 ]
PIRi I37222.
S60109.
RefSeqi NP_001036005.1. NM_001042540.1. [P52298-3 ]
NP_031388.2. NM_007362.3. [P52298-1 ]
XP_005269370.1. XM_005269313.1. [P52298-2 ]
UniGenei Hs.591671.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1H2T X-ray 2.15 Z 1-156 [» ]
1H2U X-ray 2.40 X/Y 1-156 [» ]
1H2V X-ray 2.00 Z 1-156 [» ]
1H6K X-ray 2.00 X/Y/Z 22-120 [» ]
1N52 X-ray 2.11 B 1-156 [» ]
1N54 X-ray 2.72 B 1-156 [» ]
3FEX X-ray 3.55 B 1-156 [» ]
3FEY X-ray 2.20 B 1-156 [» ]
DisProti DP00393.
ProteinModelPortali P52298.
SMRi P52298. Positions 5-149.
ModBasei Search...

Protein-protein interaction databases

BioGridi 116578. 15 interactions.
DIPi DIP-33246N.
IntActi P52298. 8 interactions.
MINTi MINT-248711.
STRINGi 9606.ENSP00000326806.

Protein family/group databases

TCDBi 9.A.60.1.1. the small nuclear rna exporter (snrna-e).

PTM databases

PhosphoSitei P52298.

Polymorphism databases

DMDMi 1705651.

Proteomic databases

MaxQBi P52298.
PaxDbi P52298.
PRIDEi P52298.

Protocols and materials databases

DNASUi 22916.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000321256 ; ENSP00000326806 ; ENSG00000114503 . [P52298-1 ]
ENST00000427641 ; ENSP00000397619 ; ENSG00000114503 .
ENST00000452404 ; ENSP00000412785 ; ENSG00000114503 . [P52298-2 ]
GeneIDi 22916.
KEGGi hsa:22916.
UCSCi uc003fxb.1. human. [P52298-1 ]
uc011btz.1. human. [P52298-2 ]

Organism-specific databases

CTDi 22916.
GeneCardsi GC03M196662.
HGNCi HGNC:7659. NCBP2.
HPAi HPA044850.
MIMi 605133. gene.
neXtProti NX_P52298.
PharmGKBi PA31462.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0724.
HOGENOMi HOG000217589.
HOVERGENi HBG052581.
InParanoidi P52298.
KOi K12883.
OMAi GNRYEQE.
PhylomeDBi P52298.
TreeFami TF313897.

Enzyme and pathway databases

Reactomei REACT_1096. Processing of Intronless Pre-mRNAs.
REACT_11066. snRNP Assembly.
REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_1364. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
REACT_1470. mRNA Capping.
REACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
REACT_1753. mRNA Splicing - Minor Pathway.
REACT_1835. Transport of Mature mRNA Derived from an Intronless Transcript.
REACT_1849. mRNA 3'-end processing.
REACT_185. SLBP independent Processing of Histone Pre-mRNAs.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_405. Transport of the SLBP Dependant Mature mRNA.
REACT_424. Transport of the SLBP independent Mature mRNA.
REACT_467. mRNA Splicing - Major Pathway.
REACT_6261. Abortive elongation of HIV-1 transcript in the absence of Tat.
REACT_6319. Formation of the HIV-1 Early Elongation Complex.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_846. Formation of the Early Elongation Complex.

Miscellaneous databases

ChiTaRSi NCBP2. human.
EvolutionaryTracei P52298.
GenomeRNAii 22916.
NextBioi 43603.
PROi P52298.
SOURCEi Search...

Gene expression databases

ArrayExpressi P52298.
Bgeei P52298.
CleanExi HS_NCBP2.
Genevestigatori P52298.

Family and domain databases

Gene3Di 3.30.70.330. 1 hit.
InterProi IPR027157. NCBP2.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
PANTHERi PTHR18847. PTHR18847. 1 hit.
Pfami PF00076. RRM_1. 1 hit.
[Graphical view ]
SMARTi SM00360. RRM. 1 hit.
[Graphical view ]
PROSITEi PS50102. RRM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 9-25 AND 113-145.
  2. "Identification of the factors that interact with NCBP, an 80 kDa nuclear cap binding protein."
    Kataoka N., Ohno M., Moda I., Shimura Y.
    Nucleic Acids Res. 23:3638-3641(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Cervix carcinoma.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain.
  4. "Identification of a human cell proliferation gene."
    Kim J.W.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Cervix.
  9. "A nuclear cap-binding complex binds Balbiani ring pre-mRNA cotranscriptionally and accompanies the ribonucleoprotein particle during nuclear export."
    Visa N., Izaurralde E., Ferreira J., Daneholt B., Mattaj I.W.
    J. Cell Biol. 133:5-14(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "Interaction between the human nuclear cap-binding protein complex and hnRNP F."
    Gamberi C., Izaurralde E., Beisel C., Mattaj I.W.
    Mol. Cell. Biol. 17:2587-2597(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HNRNPF AND HNRNPH1.
  11. "Evidence for a pioneer round of mRNA translation: mRNAs subject to nonsense-mediated decay in mammalian cells are bound by CBP80 and CBP20."
    Ishigaki Y., Li X., Serin G., Maquat L.E.
    Cell 106:607-617(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION.
  12. "eIF4G is required for the pioneer round of translation in mammalian cells."
    Lejeune F., Ranganathan A.C., Maquat L.E.
    Nat. Struct. Mol. Biol. 11:992-1000(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PIONEER ROUND OF MRNA TRANSLATION, INTERACTION WITH EIF4G1.
  13. "Human mRNA export machinery recruited to the 5' end of mRNA."
    Cheng H., Dufu K., Lee C.-S., Hsu J.L., Dias A., Reed R.
    Cell 127:1389-1400(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MRNA EXPORT.
  14. "The interaction between cap-binding complex and RNA export factor is required for intronless mRNA export."
    Nojima T., Hirose T., Kimura H., Hagiwara M.
    J. Biol. Chem. 282:15645-15651(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MRNA EXPORT, INTERACTION WITH ALYREF/THOC4.
  15. "Failsafe nonsense-mediated mRNA decay does not detectably target eIF4E-bound mRNA."
    Matsuda D., Hosoda N., Kim Y.K., Maquat L.E.
    Nat. Struct. Mol. Biol. 14:974-979(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  17. "NMD resulting from encephalomyocarditis virus IRES-directed translation initiation seems to be restricted to CBP80/20-bound mRNA."
    Woeller C.F., Gaspari M., Isken O., Maquat L.E.
    EMBO Rep. 9:446-451(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY.
  18. "Ars2 links the nuclear cap-binding complex to RNA interference and cell proliferation."
    Gruber J.J., Zatechka D.S., Sabin L.R., Yong J., Lum J.J., Kong M., Zong W.-X., Zhang Z., Lau C.-K., Rawlings J., Cherry S., Ihle J.N., Dreyfuss G., Thompson C.B.
    Cell 138:328-339(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MIRNAS BIOGENESIS.
  19. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  22. "Crystal structure of the human nuclear cap binding complex."
    Mazza C., Ohno M., Segref A., Mattaj I.W., Cusack S.
    Mol. Cell 8:383-396(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-790 IN COMPLEX WITH NCBP1, RNA-BINDING, MUTAGENESIS OF PHE-25; TYR-43; ASN-46; PHE-83; ASP-114; ASP-116 AND PHE-119.
  23. "Large-scale induced fit recognition of an m(7)GpppG cap analogue by the human nuclear cap-binding complex."
    Mazza C., Segref A., Mattaj I.W., Cusack S.
    EMBO J. 21:5548-5557(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 20-790 IN COMPLEX WITH NCBP1 AND MRNA CAP, RNA-BINDING, MUTAGENESIS OF TYR-20; TYR-43; ARG-112 AND TYR-138.
  24. "Structural basis of m7GpppG binding to the nuclear cap-binding protein complex."
    Calero G., Wilson K.F., Ly T., Rios-Steiner J.L., Clardy J.C., Cerione R.A.
    Nat. Struct. Biol. 9:912-917(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) IN COMPLEX WITH NCBP1 AND MRNA CAP, RNA-BINDING.

Entry informationi

Entry nameiNCBP2_HUMAN
AccessioniPrimary (citable) accession number: P52298
Secondary accession number(s): B2RE91
, B4DMK7, E9PAR5, Q14924, Q2TS50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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