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UniProtKB/Swiss-Prot entry P48809


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RB27C_DROME
Primary accession number P48809
Secondary accession numbers Q7JPT5 Q9TY67 Q9VM68
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on September 27, 2005 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 67)
Name and origin of the protein
Protein name Heterogeneous nuclear ribonucleoprotein 27C
Synonyms Hrb27-C
hnRNP 48
HRP48.1
Gene name
Name: Hrb27C
Synonyms: hrp48, Rbp7
ORFNames: CG10377
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
STRAIN=Canton-S;
TISSUE=Embryo;
DOI=10.1083/jcb.116.2.257; PubMed=1730754 [NCBI, ExPASy, EBI, Israel, Japan]
Matunis E.L., Matunis M.J., Dreyfuss G.;
"Characterization of the major hnRNP proteins from Drosophila melanogaster.";
J. Cell Biol. 116:257-269(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
TISSUE=Ovary;
DOI=10.1093/molbev/msi175; PubMed=15917496 [NCBI, ExPASy, EBI, Israel, Japan]
Jagadeeshan S., Singh R.S.;
"Rapidly evolving genes of Drosophila: differing levels of selective pressure in testis, ovary, and head tissues between sibling species.";
Mol. Biol. Evol. 22:1793-1801(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=Berkeley;
TISSUE=Embryo, and Ovary;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 10-53.
PubMed=8417324 [NCBI, ExPASy, EBI, Israel, Japan]
Kim Y.J., Baker B.S.;
"Isolation of RRM-type RNA-binding protein genes and the analysis of their relatedness by using a numerical approach.";
Mol. Cell. Biol. 13:174-183(1993).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-366; SER-368; SER-370; TYR-372 AND SER-379, AND MASS SPECTROMETRY.
TISSUE=Embryo;
DOI=10.1021/pr700696a; PubMed=18327897 [NCBI, ExPASy, EBI, Israel, Japan]
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X62639; CAA44505.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ062784; AAY56657.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014134; AAF52456.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY069699; AAL39844.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY128430; AAM75023.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S51720; AAB24628.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D41732; D41732.
RefSeq NP_476869.1; -.
NP_723228.1; -.
NP_723229.1; -.
UniGene Dm.1997
3D structure databases
HSSP P09651; 1L3K. [HSSP ENTRY / PDB]
ModBase P48809.
Protein-protein interaction databases
IntAct P48809; -.
Organism-specific databases
FlyBase FBgn0004838; Hrb27C.
Gene expression databases
ArrayExpress P48809; -.
GermOnline CG10377; Drosophila melanogaster.
Ontologies
GO
GO:0005654; Cellular component: nucleoplasm (inferred from direct assay from FlyBase).
GO:0030529; Cellular component: ribonucleoprotein complex (inferred from direct assay from FlyBase).
GO:0003730; Molecular function: mRNA 3'-UTR binding (inferred from direct assay from FlyBase).
GO:0048027; Molecular function: mRNA 5'-UTR binding (traceable author statement from FlyBase).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0003697; Molecular function: single-stranded DNA binding (inferred from direct assay from FlyBase).
GO:0007298; Biological process: border follicle cell migration (inferred from mutant phenotype from FlyBase).
GO:0007319; Biological process: negative regulation of oskar mRNA translation (traceable author statement from FlyBase).
GO:0045451; Biological process: pole plasm oskar mRNA localization (inferred from mutant phenotype from FlyBase).
GO:0045727; Biological process: positive regulation of translation (inferred from direct assay from FlyBase).
GO:0048024; Biological process: regulation of nuclear mRNA splicing, via spliceosome (inferred from mutant phenotype from FlyBase).
QuickGo view.
Family and domain databases
InterPro IPR012677; a_b_plait_nuc_bd.
IPR000504; RRM_RNP1.
Graphical view of domain structure.
Gene3D G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
Pfam PF00076; RRM_1; 2.
Pfam graphical view of domain structure.
SMART SM00360; RRM; 2.
SMART graphical view of domain structure.
PROSITE PS50102; RRM; 2.
PROSITE graphical view of domain structure (profiles).
BLOCKS P48809.
Genome annotation databases
Ensembl CG10377; Drosophila melanogaster. [Contig view]
GeneID 33968; -.
KEGG dme:Dmel_CG10377; -.
Phylogenomic databases
HOGENOM P48809; -.
Other
ProtoNet P48809.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein; Repeat; Ribonucleoprotein; RNA-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   421  421     Heterogeneous nuclear ribonucleoprotein 27C. PRO_0000081748
DOMAIN   7    88  82     RRM 1. 
DOMAIN   96   173  78     RRM 2. 
MOD_RES   177   177        Phosphoserine. 
MOD_RES   366   366        Phosphoserine. 
MOD_RES   368   368        Phosphoserine. 
MOD_RES   370   370        Phosphoserine. 
MOD_RES   372   372        Phosphotyrosine. 
MOD_RES   379   379        Phosphoserine. 
VAR_SEQ   262   297        Missing (in isoform B). VSP_015738
Sequence information
Length: 421 AA [This is the length of the unprocessed precursor] Molecular weight: 44770 Da [This is the MW of the unprocessed precursor] CRC64: D59DD2A647CE23F5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEEDERGKLF VGGLSWETTQ ENLSRYFCRF GDIIDCVVMK NNESGRSRGF GFVTFADPTN 

        70         80         90        100        110        120 
VNHVLQNGPH TLDGRTIDPK PCNPRTLQKP KKGGGYKVFL GGLPSNVTET DLRTFFNRYG 

       130        140        150        160        170        180 
KVTEVVIMYD QEKKKSRGFG FLSFEEESSV EHVTNERYIN LNGKQVEIKK AEPRDGSGGQ 

       190        200        210        220        230        240 
NSNNSTVGGA YGKLGNECSH WGPHHAPINM MQGQNGQMGG PPLNMPIGAP NMMPGYQGWG 

       250        260        270        280        290        300 
TSPQQQQYGY GNSGPGSYQG WGAPPGPQGP PPQWSNYAGP QQTQGYGGYD MYNSTSTGAP 

       310        320        330        340        350        360 
SGPSGGGSWN SWNMPPNSAG PTGAPGAGAG TATDMYSRAQ AWATGGPSTT GPVGGMPRTG 

       370        380        390        400        410        420 
PGNSASKSGS EYDYGGYGSG YDYDYSNYVK QEGASNYGAG PRSAYGNDSS TQPPYATSQA 


V 

P48809 in FASTA format

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