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NCBP2_DICDI
ID   NCBP2_DICDI             Reviewed;         234 AA.
AC   Q54KR9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
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; ORFNames=DDB_G0287197;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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 and RNA-mediated gene silencing
CC       (RNAi). The CBC complex is involved in miRNA-mediated RNA interference
CC       and is required for primary microRNAs (miRNAs) processing. In the CBC
CC       complex, ncbp2 recognizes and binds capped RNAs (m7GpppG-capped RNA)
CC       but requires ncbp1 to stabilize the movement of its N-terminal loop and
CC       lock the CBC into a high affinity cap-binding state with the cap
CC       structure (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the nuclear cap-binding complex (CBC), a
CC       heterodimer composed of ncbp1 and ncbp2 that interacts with m7GpppG-
CC       capped RNA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RRM NCBP2 family. {ECO:0000305}.
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DR   EMBL; AAFI02000098; EAL63873.1; -; Genomic_DNA.
DR   RefSeq; XP_637361.1; XM_632269.1.
DR   AlphaFoldDB; Q54KR9; -.
DR   SMR; Q54KR9; -.
DR   STRING; 44689.DDB0233456; -.
DR   PaxDb; Q54KR9; -.
DR   EnsemblProtists; EAL63873; EAL63873; DDB_G0287197.
DR   GeneID; 8625983; -.
DR   KEGG; ddi:DDB_G0287197; -.
DR   dictyBase; DDB_G0287197; ncbp2.
DR   eggNOG; KOG0121; Eukaryota.
DR   HOGENOM; CLU_070952_0_2_1; -.
DR   InParanoid; Q54KR9; -.
DR   OMA; IRCDWDY; -.
DR   PhylomeDB; Q54KR9; -.
DR   Reactome; R-DDI-111367; SLBP independent Processing of Histone Pre-mRNAs.
DR   Reactome; R-DDI-113418; Formation of the Early Elongation Complex.
DR   Reactome; R-DDI-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-DDI-6803529; FGFR2 alternative splicing.
DR   Reactome; R-DDI-72086; mRNA Capping.
DR   Reactome; R-DDI-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-DDI-72165; mRNA Splicing - Minor Pathway.
DR   Reactome; R-DDI-73856; RNA Polymerase II Transcription Termination.
DR   Reactome; R-DDI-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
DR   Reactome; R-DDI-77595; Processing of Intronless Pre-mRNAs.
DR   Reactome; R-DDI-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-DDI-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   PRO; PR:Q54KR9; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005846; C:nuclear cap binding complex; ISS:dictyBase.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000339; F:RNA cap binding; ISS:dictyBase.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:dictyBase.
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   3: Inferred from homology;
KW   mRNA processing; mRNA splicing; Nucleus; Reference proteome; RNA-binding;
KW   RNA-mediated gene silencing.
FT   CHAIN           1..234
FT                   /note="Nuclear cap-binding protein subunit 2"
FT                   /id="PRO_0000385276"
FT   DOMAIN          32..110
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          122..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          177..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..208
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         12
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="mRNA cap"
FT                   /evidence="ECO:0000250"
FT   BINDING         35
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="mRNA cap"
FT                   /evidence="ECO:0000250"
FT   BINDING         104..108
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="mRNA cap"
FT                   /evidence="ECO:0000250"
FT   BINDING         115..119
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="mRNA cap"
FT                   /evidence="ECO:0000250"
FT   BINDING         125..126
FT                   /ligand="mRNA"
FT                   /ligand_id="ChEBI:CHEBI:33699"
FT                   /ligand_part="mRNA cap"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   234 AA;  27124 MW;  5512BCE3E41ADDBD CRC64;
     MSELYSTPQP FYYDKKSGFT QDEFKHAIDK SSTIYVGYLS FYTTEEQLYE LFSKCGEIKR
     IIMGLDRNQK TPCGFCFVEY YSKEDAADCI KYINGSKLDE RLIRCDWDYG FKEGRQYGRG
     LSGGQVRDEY RTDYDPGRGG YGKQRQFEMD QFSDVNGGDI TYQQQILQLQ QSQQQHQLYQ
     QANAGGPQNY SGKRNRGADD DSDSFKRQRD NNGSISAGNT PNKGRFRERD EEDD
 
 
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