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Protein

Nuclear cap-binding protein subunit 1

Gene

NCBP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).14 Publications

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: ProtInc
  • RNA cap binding Source: ProtInc

GO - Biological processi

  • 7-methylguanosine mRNA capping Source: UniProtKB
  • fibroblast growth factor receptor signaling pathway Source: Reactome
  • gene expression Source: Reactome
  • gene silencing by RNA Source: UniProtKB-KW
  • histone mRNA metabolic process Source: Reactome
  • mRNA 3'-end processing Source: Reactome
  • mRNA cis splicing, via spliceosome Source: InterPro
  • mRNA export from nucleus Source: UniProtKB
  • mRNA splicing, via spliceosome Source: Reactome
  • nuclear export Source: Reactome
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
  • positive regulation of cell growth Source: UniProtKB
  • positive regulation of mRNA 3'-end processing Source: UniProtKB
  • pre-mRNA cleavage required for polyadenylation Source: UniProtKB
  • regulation of translational initiation Source: UniProtKB
  • RNA export from nucleus Source: Reactome
  • RNA splicing Source: ProtInc
  • snRNA transcription from RNA polymerase II promoter Source: Reactome
  • termination of RNA polymerase II transcription Source: Reactome
  • transcription elongation from RNA polymerase II promoter Source: Reactome
  • transcription from RNA polymerase II promoter 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

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-111367. SLBP independent Processing of Histone Pre-mRNAs.
R-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-159227. Transport of the SLBP independent Mature mRNA.
R-HSA-159230. Transport of the SLBP Dependant Mature mRNA.
R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167242. Abortive elongation of HIV-1 transcript in the absence of Tat.
R-HSA-191859. snRNP Assembly.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6803529. FGFR2 alternative splicing.
R-HSA-6807505. RNA polymerase II transcribes snRNA genes.
R-HSA-72086. mRNA Capping.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72165. mRNA Splicing - Minor Pathway.
R-HSA-72187. mRNA 3'-end processing.
R-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA.
R-HSA-77588. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
R-HSA-77595. Processing of Intronless Pre-mRNAs.
R-HSA-8851708. Signaling by FGFR2 IIIa TM.
R-HSA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SIGNORiQ09161.

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 1
Alternative name(s):
80 kDa nuclear cap-binding protein
Short name:
CBP80
Short name:
NCBP 80 kDa subunit
Gene namesi
Name:NCBP1
Synonyms:CBP80, NCBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:7658. NCBP1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • intracellular ribonucleoprotein complex Source: UniProtKB
  • mitochondrion Source: HPA
  • mRNA cap binding complex Source: UniProtKB
  • nuclear cap binding complex Source: Ensembl
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • RNA cap binding complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 71S → A: Reduced phosphorylation by RPS6KB1. Abolishes phosphorylation by RPS6KB1; when associated with 21-A-A-22. 1 Publication
Mutagenesisi17 – 182KR → AA: Abolishes nuclear localization and phosphorylation by RPS6KB1. 1 Publication
Mutagenesisi21 – 222TS → A: Reduced phosphorylation by RPS6KB1. Abolishes phosphorylation by RPS6KB1; when associated with A-7. 1 Publication

Organism-specific databases

PharmGKBiPA31461.

Polymorphism and mutation databases

BioMutaiNCBP1.
DMDMi1705654.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 790790Nuclear cap-binding protein subunit 1PRO_0000089364Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 71Phosphoserine; by RPS6KB11 Publication
Modified residuei21 – 211Phosphothreonine; by RPS6KB1Combined sources1 Publication
Modified residuei22 – 221Phosphoserine; by RPS6KB1Combined sources1 Publication
Modified residuei201 – 2011PhosphoserineCombined sources
Modified residuei204 – 2041N6-acetyllysineCombined sources
Modified residuei698 – 6981N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ09161.
MaxQBiQ09161.
PaxDbiQ09161.
PeptideAtlasiQ09161.
PRIDEiQ09161.

PTM databases

iPTMnetiQ09161.
PhosphoSiteiQ09161.
SwissPalmiQ09161.

Expressioni

Gene expression databases

BgeeiENSG00000136937.
CleanExiHS_NCBP1.
ExpressionAtlasiQ09161. baseline and differential.
GenevisibleiQ09161. HS.

Organism-specific databases

HPAiHPA042411.
HPA049031.

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 containing PHAX/RNUXA, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with PHAX/RNUXA, SRRT/ARS2, EIF4G2, IGF2BP1, HNRNPF, HNRNPH1, KIAA0427/CTIF, PARN, DROSHA, UPF1 and ALYREF/THOC4. May interact with EIF4G1; the interaction is however controversial since it is reported by PubMed:11340157, PubMed:15059963 and PubMed:15361857, but is not observed by PubMed:19648179. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1/CBP80 and POLR2A. Component of an alternative nuclear cap-binding complex (CBC) composed of NCBP1/CBP80 and NCBP3 (PubMed:26382858). Interacts with METTL3 (PubMed:27117702).14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NCBP2P522988EBI-464743,EBI-464729
PARNO954532EBI-464743,EBI-372832
POLDIP3Q9BY773EBI-464743,EBI-1776152
RPS6P627533EBI-464743,EBI-356625

Protein-protein interaction databases

BioGridi110766. 133 interactions.
DIPiDIP-33244N.
IntActiQ09161. 81 interactions.
MINTiMINT-248693.
STRINGi9606.ENSP00000364289.

Structurei

Secondary structure

1
790
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 367Combined sources
Turni37 – 393Combined sources
Helixi46 – 5914Combined sources
Helixi61 – 7818Combined sources
Helixi80 – 823Combined sources
Helixi83 – 9412Combined sources
Helixi98 – 11720Combined sources
Helixi121 – 13616Combined sources
Beta strandi138 – 1403Combined sources
Helixi142 – 15413Combined sources
Helixi155 – 1573Combined sources
Helixi163 – 17412Combined sources
Helixi177 – 20428Combined sources
Helixi211 – 2144Combined sources
Beta strandi216 – 2183Combined sources
Beta strandi221 – 2233Combined sources
Helixi228 – 24114Combined sources
Turni242 – 2443Combined sources
Beta strandi247 – 2493Combined sources
Helixi252 – 2565Combined sources
Turni257 – 2593Combined sources
Helixi262 – 2643Combined sources
Helixi294 – 2963Combined sources
Beta strandi298 – 3014Combined sources
Helixi309 – 32517Combined sources
Helixi329 – 3379Combined sources
Helixi347 – 35913Combined sources
Helixi369 – 38214Combined sources
Turni384 – 3863Combined sources
Helixi387 – 40014Combined sources
Helixi402 – 4043Combined sources
Helixi407 – 42115Combined sources
Turni422 – 4265Combined sources
Helixi430 – 4367Combined sources
Helixi444 – 45815Combined sources
Helixi462 – 4687Combined sources
Helixi471 – 4766Combined sources
Beta strandi488 – 4903Combined sources
Beta strandi493 – 4953Combined sources
Helixi498 – 50912Combined sources
Helixi514 – 5207Combined sources
Helixi521 – 5233Combined sources
Helixi541 – 55414Combined sources
Turni555 – 5573Combined sources
Helixi559 – 56810Combined sources
Helixi570 – 5767Combined sources
Helixi580 – 59415Combined sources
Helixi598 – 61013Combined sources
Helixi616 – 6238Combined sources
Helixi626 – 6283Combined sources
Turni629 – 6335Combined sources
Helixi635 – 66127Combined sources
Helixi693 – 73139Combined sources
Helixi738 – 75316Combined sources
Helixi755 – 7584Combined sources
Helixi759 – 7613Combined sources
Helixi762 – 7687Combined sources
Helixi776 – 78712Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H2TX-ray2.10C20-652[»]
C702-790[»]
1H2UX-ray2.40A/B20-652[»]
A/B702-790[»]
1H2VX-ray2.00C20-790[»]
1H6KX-ray2.00A/B/C20-790[»]
1N52X-ray2.11A1-790[»]
1N54X-ray2.72A1-790[»]
3FEXX-ray3.55A1-790[»]
3FEYX-ray2.20A1-790[»]
DisProtiDP00392.
ProteinModelPortaliQ09161.
SMRiQ09161. Positions 2-790.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ09161.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 240213MIF4GAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili643 – 71371Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi3 – 2018Nuclear localization signalSequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the NCBP1 family.Curated
Contains 1 MIF4G domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1104. Eukaryota.
ENOG410XR7H. LUCA.
GeneTreeiENSGT00390000001733.
HOGENOMiHOG000007990.
HOVERGENiHBG080328.
InParanoidiQ09161.
KOiK12882.
OMAiIMLLTEH.
OrthoDBiEOG091G02OT.
PhylomeDBiQ09161.
TreeFamiTF313400.

Family and domain databases

Gene3Di1.25.40.180. 4 hits.
InterProiIPR016024. ARM-type_fold.
IPR027159. CBP80.
IPR016021. MIF4-like.
IPR015172. MIF4G-like_typ-1.
IPR015174. MIF4G-like_typ-2.
IPR003890. MIF4G-like_typ-3.
[Graphical view]
PANTHERiPTHR12412. PTHR12412. 1 hit.
PfamiPF02854. MIF4G. 1 hit.
PF09088. MIF4G_like. 1 hit.
PF09090. MIF4G_like_2. 1 hit.
[Graphical view]
SMARTiSM00543. MIF4G. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.

Sequencei

Sequence statusi: Complete.

Q09161-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRRRHSDEN DGGQPHKRRK TSDANETEDH LESLICKVGE KSACSLESNL
60 70 80 90 100
EGLAGVLEAD LPNYKSKILR LLCTVARLLP EKLTIYTTLV GLLNARNYNF
110 120 130 140 150
GGEFVEAMIR QLKESLKANN YNEAVYLVRF LSDLVNCHVI AAPSMVAMFE
160 170 180 190 200
NFVSVTQEED VPQVRRDWYV YAFLSSLPWV GKELYEKKDA EMDRIFANTE
210 220 230 240 250
SYLKRRQKTH VPMLQVWTAD KPHPQEEYLD CLWAQIQKLK KDRWQERHIL
260 270 280 290 300
RPYLAFDSIL CEALQHNLPP FTPPPHTEDS VYPMPRVIFR MFDYTDDPEG
310 320 330 340 350
PVMPGSHSVE RFVIEENLHC IIKSHWKERK TCAAQLVSYP GKNKIPLNYH
360 370 380 390 400
IVEVIFAELF QLPAPPHIDV MYTTLLIELC KLQPGSLPQV LAQATEMLYM
410 420 430 440 450
RLDTMNTTCV DRFINWFSHH LSNFQFRWSW EDWSDCLSQD PESPKPKFVR
460 470 480 490 500
EVLEKCMRLS YHQRILDIVP PTFSALCPAN PTCIYKYGDE SSNSLPGHSV
510 520 530 540 550
ALCLAVAFKS KATNDEIFSI LKDVPNPNQD DDDDEGFSFN PLKIEVFVQT
560 570 580 590 600
LLHLAAKSFS HSFSALAKFH EVFKTLAESD EGKLHVLRVM FEVWRNHPQM
610 620 630 640 650
IAVLVDKMIR TQIVDCAAVA NWIFSSELSR DFTRLFVWEI LHSTIRKMNK
660 670 680 690 700
HVLKIQKELE EAKEKLARQH KRRSDDDDRS SDRKDGVLEE QIERLQEKVE
710 720 730 740 750
SAQSEQKNLF LVIFQRFIMI LTEHLVRCET DGTSVLTPWY KNCIERLQQI
760 770 780 790
FLQHHQIIQQ YMVTLENLLF TAELDPHILA VFQQFCALQA
Length:790
Mass (Da):91,839
Last modified:October 1, 1996 - v1
Checksum:iF10DE7B9D16FDA0B
GO

Sequence cautioni

The sequence BAD92470 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAI12863 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801P → S in BAG35665 (PubMed:14702039).Curated
Sequence conflicti159 – 1591E → D in BAD92470 (Ref. 4) Curated
Sequence conflicti674 – 6741S → G in BAG35665 (PubMed:14702039).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80030 mRNA. Translation: CAA56334.1.
D32002 mRNA. Translation: BAA06769.1.
AK312807 mRNA. Translation: BAG35665.1.
AB209233 mRNA. Translation: BAD92470.1. Different initiation.
AL445531, AL162385 Genomic DNA. Translation: CAI15431.1.
AL162385, AL445531 Genomic DNA. Translation: CAI12861.1.
AL162385 Genomic DNA. Translation: CAI12863.1. Sequence problems.
BC001450 mRNA. Translation: AAH01450.1.
CCDSiCCDS6728.1.
PIRiS50082.
RefSeqiNP_002477.1. NM_002486.4.
UniGeneiHs.595669.
Hs.686479.

Genome annotation databases

EnsembliENST00000375147; ENSP00000364289; ENSG00000136937.
GeneIDi4686.
KEGGihsa:4686.
UCSCiuc004axq.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80030 mRNA. Translation: CAA56334.1.
D32002 mRNA. Translation: BAA06769.1.
AK312807 mRNA. Translation: BAG35665.1.
AB209233 mRNA. Translation: BAD92470.1. Different initiation.
AL445531, AL162385 Genomic DNA. Translation: CAI15431.1.
AL162385, AL445531 Genomic DNA. Translation: CAI12861.1.
AL162385 Genomic DNA. Translation: CAI12863.1. Sequence problems.
BC001450 mRNA. Translation: AAH01450.1.
CCDSiCCDS6728.1.
PIRiS50082.
RefSeqiNP_002477.1. NM_002486.4.
UniGeneiHs.595669.
Hs.686479.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H2TX-ray2.10C20-652[»]
C702-790[»]
1H2UX-ray2.40A/B20-652[»]
A/B702-790[»]
1H2VX-ray2.00C20-790[»]
1H6KX-ray2.00A/B/C20-790[»]
1N52X-ray2.11A1-790[»]
1N54X-ray2.72A1-790[»]
3FEXX-ray3.55A1-790[»]
3FEYX-ray2.20A1-790[»]
DisProtiDP00392.
ProteinModelPortaliQ09161.
SMRiQ09161. Positions 2-790.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110766. 133 interactions.
DIPiDIP-33244N.
IntActiQ09161. 81 interactions.
MINTiMINT-248693.
STRINGi9606.ENSP00000364289.

Protein family/group databases

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

PTM databases

iPTMnetiQ09161.
PhosphoSiteiQ09161.
SwissPalmiQ09161.

Polymorphism and mutation databases

BioMutaiNCBP1.
DMDMi1705654.

Proteomic databases

EPDiQ09161.
MaxQBiQ09161.
PaxDbiQ09161.
PeptideAtlasiQ09161.
PRIDEiQ09161.

Protocols and materials databases

DNASUi4686.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375147; ENSP00000364289; ENSG00000136937.
GeneIDi4686.
KEGGihsa:4686.
UCSCiuc004axq.4. human.

Organism-specific databases

CTDi4686.
GeneCardsiNCBP1.
HGNCiHGNC:7658. NCBP1.
HPAiHPA042411.
HPA049031.
MIMi600469. gene.
neXtProtiNX_Q09161.
PharmGKBiPA31461.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1104. Eukaryota.
ENOG410XR7H. LUCA.
GeneTreeiENSGT00390000001733.
HOGENOMiHOG000007990.
HOVERGENiHBG080328.
InParanoidiQ09161.
KOiK12882.
OMAiIMLLTEH.
OrthoDBiEOG091G02OT.
PhylomeDBiQ09161.
TreeFamiTF313400.

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
R-HSA-111367. SLBP independent Processing of Histone Pre-mRNAs.
R-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-159227. Transport of the SLBP independent Mature mRNA.
R-HSA-159230. Transport of the SLBP Dependant Mature mRNA.
R-HSA-159231. Transport of Mature mRNA Derived from an Intronless Transcript.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167242. Abortive elongation of HIV-1 transcript in the absence of Tat.
R-HSA-191859. snRNP Assembly.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6803529. FGFR2 alternative splicing.
R-HSA-6807505. RNA polymerase II transcribes snRNA genes.
R-HSA-72086. mRNA Capping.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72165. mRNA Splicing - Minor Pathway.
R-HSA-72187. mRNA 3'-end processing.
R-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA.
R-HSA-77588. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
R-HSA-77595. Processing of Intronless Pre-mRNAs.
R-HSA-8851708. Signaling by FGFR2 IIIa TM.
R-HSA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SIGNORiQ09161.

Miscellaneous databases

ChiTaRSiNCBP1. human.
EvolutionaryTraceiQ09161.
GenomeRNAii4686.
PROiQ09161.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000136937.
CleanExiHS_NCBP1.
ExpressionAtlasiQ09161. baseline and differential.
GenevisibleiQ09161. HS.

Family and domain databases

Gene3Di1.25.40.180. 4 hits.
InterProiIPR016024. ARM-type_fold.
IPR027159. CBP80.
IPR016021. MIF4-like.
IPR015172. MIF4G-like_typ-1.
IPR015174. MIF4G-like_typ-2.
IPR003890. MIF4G-like_typ-3.
[Graphical view]
PANTHERiPTHR12412. PTHR12412. 1 hit.
PfamiPF02854. MIF4G. 1 hit.
PF09088. MIF4G_like. 1 hit.
PF09090. MIF4G_like_2. 1 hit.
[Graphical view]
SMARTiSM00543. MIF4G. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 3 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiNCBP1_HUMAN
AccessioniPrimary (citable) accession number: Q09161
Secondary accession number(s): B2R718
, Q59G76, Q5T1V0, Q5T7X2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 7, 2016
This is version 170 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 9
    Human chromosome 9: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.