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NCBP2_RAT
ID   NCBP2_RAT               Reviewed;         156 AA.
AC   B1WC40;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Nuclear cap-binding protein subunit 2;
DE   AltName: Full=20 kDa nuclear cap-binding protein;
DE   AltName: Full=NCBP 20 kDa subunit;
DE            Short=CBP20;
GN   Name=Ncbp2; Synonyms=Cbp20;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Component of the cap-binding complex (CBC), which binds co-
CC       transcriptionally to the 5' cap of pre-mRNAs and is involved in various
CC       processes such as pre-mRNA splicing, translation regulation, nonsense-
CC       mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs
CC       (miRNAs) and mRNA export. The CBC complex is involved in mRNA export
CC       from the nucleus via its interaction with ALYREF/THOC4/ALY, leading to
CC       the recruitment of the mRNA export machinery to the 5' end of mRNA and
CC       to mRNA export in a 5' to 3' direction through the nuclear pore. The
CC       CBC complex is also involved in mediating U snRNA and intronless mRNAs
CC       export from the nucleus. The CBC complex is essential for a pioneer
CC       round of mRNA translation, before steady state translation when the CBC
CC       complex is replaced by cytoplasmic cap-binding protein eIF4E. The
CC       pioneer round of mRNA translation mediated by the CBC complex plays a
CC       central role in nonsense-mediated mRNA decay (NMD), NMD only taking
CC       place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs.
CC       The CBC complex enhances NMD in mRNAs containing at least one exon-
CC       junction complex (EJC) via its interaction with UPF1, promoting the
CC       interaction between UPF1 and UPF2. The CBC complex is also involved in
CC       'failsafe' NMD, which is independent of the EJC complex, while it does
CC       not participate in Staufen-mediated mRNA decay (SMD). During cell
CC       proliferation, the CBC complex is also involved in microRNAs (miRNAs)
CC       biogenesis via its interaction with SRRT/ARS2, thereby being required
CC       for miRNA-mediated RNA interference. The CBC complex also acts as a
CC       negative regulator of PARN, thereby acting as an inhibitor of mRNA
CC       deadenylation. In the CBC complex, NCBP2/CBP20 recognizes and binds
CC       capped RNAs (m7GpppG-capped RNA) but requires NCBP1/CBP80 to stabilize
CC       the movement of its N-terminal loop and lock the CBC into a high
CC       affinity cap-binding state with the cap structure. The conventional
CC       cap-binding complex with NCBP2 binds both small nuclear RNA (snRNA) and
CC       messenger (mRNA) and is involved in their export from the nucleus (By
CC       similarity). {ECO:0000250|UniProtKB:P52298}.
CC   -!- SUBUNIT: Component of the nuclear cap-binding complex (CBC), a
CC       heterodimer composed of NCBP1/CBP80 and NCBP2/CBP20 that interacts with
CC       m7GpppG-capped RNA. Found in a U snRNA export complex with PHAX/RNUXA,
CC       NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA. Interacts with
CC       PHAX/RNUXA, EIF4G1, HNRNPF, HNRNPH1 and ALYREF/THOC4/ALY. Interacts
CC       with SRRT/ARS2 and KPNA3 (By similarity).
CC       {ECO:0000250|UniProtKB:P52298}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P52298}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P52298}.
CC   -!- SIMILARITY: Belongs to the RRM NCBP2 family. {ECO:0000305}.
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DR   EMBL; BC161994; AAI61994.1; -; mRNA.
DR   RefSeq; NP_001102995.1; NM_001109525.1.
DR   AlphaFoldDB; B1WC40; -.
DR   SMR; B1WC40; -.
DR   STRING; 10116.ENSRNOP00000002381; -.
DR   iPTMnet; B1WC40; -.
DR   PhosphoSitePlus; B1WC40; -.
DR   jPOST; B1WC40; -.
DR   PaxDb; B1WC40; -.
DR   PeptideAtlas; B1WC40; -.
DR   PRIDE; B1WC40; -.
DR   GeneID; 689116; -.
DR   KEGG; rno:689116; -.
DR   UCSC; RGD:1596188; rat.
DR   CTD; 22916; -.
DR   RGD; 1596188; Ncbp2.
DR   VEuPathDB; HostDB:ENSRNOG00000001746; -.
DR   eggNOG; KOG0121; Eukaryota.
DR   HOGENOM; CLU_070952_2_0_1; -.
DR   InParanoid; B1WC40; -.
DR   OMA; AENCMRY; -.
DR   OrthoDB; 1298409at2759; -.
DR   PhylomeDB; B1WC40; -.
DR   TreeFam; TF313897; -.
DR   Reactome; R-RNO-111367; SLBP independent Processing of Histone Pre-mRNAs.
DR   Reactome; R-RNO-112382; Formation of RNA Pol II elongation complex.
DR   Reactome; R-RNO-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-RNO-159227; Transport of the SLBP independent Mature mRNA.
DR   Reactome; R-RNO-159230; Transport of the SLBP Dependant Mature mRNA.
DR   Reactome; R-RNO-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR   Reactome; R-RNO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-RNO-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-RNO-6803529; FGFR2 alternative splicing.
DR   Reactome; R-RNO-6807505; RNA polymerase II transcribes snRNA genes.
DR   Reactome; R-RNO-72086; mRNA Capping.
DR   Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-RNO-72165; mRNA Splicing - Minor Pathway.
DR   Reactome; R-RNO-72187; mRNA 3'-end processing.
DR   Reactome; R-RNO-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR   Reactome; R-RNO-73856; RNA Polymerase II Transcription Termination.
DR   Reactome; R-RNO-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
DR   Reactome; R-RNO-77595; Processing of Intronless Pre-mRNAs.
DR   Reactome; R-RNO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-RNO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   PRO; PR:B1WC40; -.
DR   Proteomes; UP000002494; Chromosome 11.
DR   Bgee; ENSRNOG00000001746; Expressed in thymus and 19 other tissues.
DR   Genevisible; B1WC40; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005845; C:mRNA cap binding complex; ISO:RGD.
DR   GO; GO:0005846; C:nuclear cap binding complex; IDA:RGD.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0034518; C:RNA cap binding complex; ISO:RGD.
DR   GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR   GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IDA:RGD.
DR   GO; GO:0000339; F:RNA cap binding; IBA:GO_Central.
DR   GO; GO:0017069; F:snRNA binding; ISS:UniProtKB.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0008334; P:histone mRNA metabolic process; ISO:RGD.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0006406; P:mRNA export from nucleus; ISO:RGD.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR   GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISO:RGD.
DR   GO; GO:0031442; P:positive regulation of mRNA 3'-end processing; ISO:RGD.
DR   GO; GO:0046833; P:positive regulation of RNA export from nucleus; ISS:UniProtKB.
DR   GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; ISO:RGD.
DR   GO; GO:0006446; P:regulation of translational initiation; ISO:RGD.
DR   GO; GO:0008380; P:RNA splicing; ISS:UniProtKB.
DR   GO; GO:0006408; P:snRNA export from nucleus; ISS:UniProtKB.
DR   CDD; cd12240; RRM_NCBP2; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR027157; NCBP2.
DR   InterPro; IPR034148; NCBP2_RRM.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR18847; PTHR18847; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Methylation; mRNA processing; mRNA splicing;
KW   mRNA transport; Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein;
KW   Reference proteome; RNA-binding; RNA-mediated gene silencing;
KW   Translation regulation; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P52298"
FT   CHAIN           2..156
FT                   /note="Nuclear cap-binding protein subunit 2"
FT                   /id="PRO_0000385248"
FT   DOMAIN          40..118
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          124..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         20
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="mRNA cap"
FT                   /evidence="ECO:0000250"
FT   BINDING         43
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="mRNA cap"
FT                   /evidence="ECO:0000250"
FT   BINDING         112..116
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="mRNA cap"
FT                   /evidence="ECO:0000250"
FT   BINDING         123..127
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="mRNA cap"
FT                   /evidence="ECO:0000250"
FT   BINDING         133..134
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="mRNA cap"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52298"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52298"
FT   MOD_RES         146
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P52298"
SQ   SEQUENCE   156 AA;  18017 MW;  C6DF61E0C6A2CC2C CRC64;
     MSGGLLKALR SDSYVELSEY RDQHFRGDNE EQEKLLKKSC TLYVGNLSFY TTEEQIYELF
     SKSGDIKKII MGLDKMKKTA CGFCFVEYYS RADAENAMRY INGTRLDDRI IRTDWDAGFK
     EGRQYGRGRS GGQVRDEYRE DYDAGRGGYG KLAQKQ
 
 
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