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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

BioCyciZFISH:ENSG00000136937-MONOMER.
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)DescriptionActionsGraphical viewLength
Mutagenesisi7S → A: Reduced phosphorylation by RPS6KB1. Abolishes phosphorylation by RPS6KB1; when associated with 21-A-A-22. 1 Publication1
Mutagenesisi17 – 18KR → AA: Abolishes nuclear localization and phosphorylation by RPS6KB1. 1 Publication2
Mutagenesisi21 – 22TS → A: Reduced phosphorylation by RPS6KB1. Abolishes phosphorylation by RPS6KB1; when associated with A-7. 1 Publication2

Organism-specific databases

OpenTargetsiENSG00000136937.
PharmGKBiPA31461.

Polymorphism and mutation databases

BioMutaiNCBP1.
DMDMi1705654.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000893641 – 790Nuclear cap-binding protein subunit 1Add BLAST790

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei7Phosphoserine; by RPS6KB11 Publication1
Modified residuei21Phosphothreonine; by RPS6KB1Combined sources1 Publication1
Modified residuei22Phosphoserine; by RPS6KB1Combined sources1 Publication1
Modified residuei201PhosphoserineCombined sources1
Modified residuei204N6-acetyllysineCombined sources1
Modified residuei698N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ09161.
MaxQBiQ09161.
PaxDbiQ09161.
PeptideAtlasiQ09161.
PRIDEiQ09161.

PTM databases

iPTMnetiQ09161.
PhosphoSitePlusiQ09161.
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
RNF40O751503EBI-464743,EBI-744408
RPS6P627533EBI-464743,EBI-356625

Protein-protein interaction databases

BioGridi110766. 133 interactors.
DIPiDIP-33244N.
IntActiQ09161. 83 interactors.
MINTiMINT-248693.
STRINGi9606.ENSP00000364289.

Structurei

Secondary structure

1790
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi30 – 36Combined sources7
Turni37 – 39Combined sources3
Helixi46 – 59Combined sources14
Helixi61 – 78Combined sources18
Helixi80 – 82Combined sources3
Helixi83 – 94Combined sources12
Helixi98 – 117Combined sources20
Helixi121 – 136Combined sources16
Beta strandi138 – 140Combined sources3
Helixi142 – 154Combined sources13
Helixi155 – 157Combined sources3
Helixi163 – 174Combined sources12
Helixi177 – 204Combined sources28
Helixi211 – 214Combined sources4
Beta strandi216 – 218Combined sources3
Beta strandi221 – 223Combined sources3
Helixi228 – 241Combined sources14
Turni242 – 244Combined sources3
Beta strandi247 – 249Combined sources3
Helixi252 – 256Combined sources5
Turni257 – 259Combined sources3
Helixi262 – 264Combined sources3
Helixi294 – 296Combined sources3
Beta strandi298 – 301Combined sources4
Helixi309 – 325Combined sources17
Helixi329 – 337Combined sources9
Helixi347 – 359Combined sources13
Helixi369 – 382Combined sources14
Turni384 – 386Combined sources3
Helixi387 – 400Combined sources14
Helixi402 – 404Combined sources3
Helixi407 – 421Combined sources15
Turni422 – 426Combined sources5
Helixi430 – 436Combined sources7
Helixi444 – 458Combined sources15
Helixi462 – 468Combined sources7
Helixi471 – 476Combined sources6
Beta strandi488 – 490Combined sources3
Beta strandi493 – 495Combined sources3
Helixi498 – 509Combined sources12
Helixi514 – 520Combined sources7
Helixi521 – 523Combined sources3
Helixi541 – 554Combined sources14
Turni555 – 557Combined sources3
Helixi559 – 568Combined sources10
Helixi570 – 576Combined sources7
Helixi580 – 594Combined sources15
Helixi598 – 610Combined sources13
Helixi616 – 623Combined sources8
Helixi626 – 628Combined sources3
Turni629 – 633Combined sources5
Helixi635 – 661Combined sources27
Helixi693 – 731Combined sources39
Helixi738 – 753Combined sources16
Helixi755 – 758Combined sources4
Helixi759 – 761Combined sources3
Helixi762 – 768Combined sources7
Helixi776 – 787Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ09161.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 240MIF4GAdd BLAST213

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili643 – 713Sequence analysisAdd BLAST71

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi3 – 20Nuclear localization signalSequence analysisAdd BLAST18

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)DescriptionActionsGraphical viewLength
Sequence conflicti80P → S in BAG35665 (PubMed:14702039).Curated1
Sequence conflicti159E → D in BAD92470 (Ref. 4) Curated1
Sequence conflicti674S → G in BAG35665 (PubMed:14702039).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110766. 133 interactors.
DIPiDIP-33244N.
IntActiQ09161. 83 interactors.
MINTiMINT-248693.
STRINGi9606.ENSP00000364289.

Protein family/group databases

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

PTM databases

iPTMnetiQ09161.
PhosphoSitePlusiQ09161.
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.
OpenTargetsiENSG00000136937.
PharmGKBiPA31461.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000136937-MONOMER.
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: November 30, 2016
This is version 173 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.