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P26686 (SRR55_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine-arginine protein 55

Short name=SRP55
Alternative name(s):
52 kDa bracketing protein
B52 protein
Protein enhancer of deformed
Gene names
Name:B52
Synonyms:E(Dfd), RS55, SR55
ORF Names:CG10851
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length376 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential for development. May have a critical role in splicing or in controlling alternative splice site use of at least some pre-mRNA in vivo. Not required for all splicing. May play a general role in the condensation or decondensation of chromatin. Ref.1 Ref.8 Ref.9

Subcellular location

Nucleus. Note: Associated with boundaries of transcriptionally active chromatin. Ref.1 Ref.2 Ref.8

Developmental stage

Expressed throughout development. Ref.9

Post-translational modification

Extensively phosphorylated on serine residues in the RS domain. Ref.1 Ref.10

Sequence similarities

Belongs to the splicing factor SR family.

Contains 2 RRM (RNA recognition motif) domains.

Sequence caution

The sequence AAN71237.1 differs from that shown. Reason: Frameshift at position 78.

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P26686-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform A (identifier: P26686-2)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     103-107: Missing.
     319-339: Missing.
Isoform B (identifier: P26686-3)

Also known as: I;

The sequence of this isoform differs from the canonical sequence as follows:
     323-376: SFKSSFYKFTTMPFFCSDRSASAENKSRSRSRSRSASPKNGNASPDRNNESMDD → VVQKLVL
Note: No experimental confirmation available.
Isoform D (identifier: P26686-4)

The sequence of this isoform differs from the canonical sequence as follows:
     103-107: Missing.
     135-140: DLKDYM → SLMCFD
     141-376: Missing.
Note: No experimental confirmation available.
Isoform E (identifier: P26686-5)

The sequence of this isoform differs from the canonical sequence as follows:
     319-339: Missing.
Note: No experimental confirmation available.
Isoform F (identifier: P26686-6)

Also known as: K;

The sequence of this isoform differs from the canonical sequence as follows:
     103-107: Missing.
     135-152: DLKDYMRQAGEVTYADAH → VSEHGSMYRALGVVYTVA
     153-376: Missing.
Note: No experimental confirmation available.
Isoform G (identifier: P26686-7)

Also known as: H;

The sequence of this isoform differs from the canonical sequence as follows:
     1-139: Missing.
     319-339: Missing.
Note: No experimental confirmation available.
Isoform J (identifier: P26686-8)

The sequence of this isoform differs from the canonical sequence as follows:
     78-261: Missing.
     319-339: Missing.
Note: No experimental confirmation available.
Isoform L (identifier: P26686-9)

The sequence of this isoform differs from the canonical sequence as follows:
     103-107: Missing.
     132-154: SWQDLKDYMRQAGEVTYADAHKQ → RSQGLHAPGWRGHLCRCPQAASQ
     155-376: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 376375Serine-arginine protein 55
PRO_0000081961

Regions

Domain4 – 7471RRM 1
Domain120 – 19374RRM 2
Compositional bias89 – 979Gly-rich (hinge region)
Compositional bias184 – 359176Arg/Ser-rich (RS domain)

Amino acid modifications

Modified residue1651Phosphoserine Ref.10

Natural variations

Alternative sequence1 – 139139Missing in isoform G.
VSP_015924
Alternative sequence78 – 261184Missing in isoform J.
VSP_015925
Alternative sequence103 – 1075Missing in isoform A, isoform D, isoform F and isoform L.
VSP_015926
Alternative sequence132 – 15423SWQDL…DAHKQ → RSQGLHAPGWRGHLCRCPQA ASQ in isoform L.
VSP_041738
Alternative sequence135 – 15218DLKDY…YADAH → VSEHGSMYRALGVVYTVA in isoform F.
VSP_015928
Alternative sequence135 – 1406DLKDYM → SLMCFD in isoform D.
VSP_015929
Alternative sequence141 – 376236Missing in isoform D.
VSP_015930
Alternative sequence153 – 376224Missing in isoform F.
VSP_015931
Alternative sequence155 – 376222Missing in isoform L.
VSP_041739
Alternative sequence319 – 33921Missing in isoform A, isoform E, isoform G and isoform J.
VSP_005878
Alternative sequence323 – 37654SFKSS…ESMDD → VVQKLVL in isoform B.
VSP_015932

Experimental info

Sequence conflict71Y → F in AAB24629. Ref.7
Sequence conflict17 – 182ER → AA in AAB24629. Ref.7
Sequence conflict40 – 423GFV → AFM in AAB24629. Ref.7
Sequence conflict751T → S in CAA41556. Ref.1
Sequence conflict1961R → A in CAA44483. Ref.2
Sequence conflict2291S → T in CAA44483. Ref.2
Sequence conflict2611R → A in CAA44483. Ref.2
Sequence conflict280 – 2823RSR → APV in CAA44483. Ref.2
Sequence conflict2941S → T in CAA41556. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: B35CEDA034933019

FASTA37642,813
        10         20         30         40         50         60 
MVGSRVYVGG LPYGVRERDL ERFFKGYGRT RDILIKNGYG FVEFEDYRDA DDAVYELNGK 

        70         80         90        100        110        120 
ELLGERVVVE PARGTARGSN RDRYDDRYGG RRGGGGGRYN EKNKNSRSSS RYGPPLRTEY 

       130        140        150        160        170        180 
RLIVENLSSR VSWQDLKDYM RQAGEVTYAD AHKQRRNEGV VEFASLSDMK TAIEKLDDTE 

       190        200        210        220        230        240 
LNGRRIHLVE DRRGGRSGGG GGSGRGRSRS SSSRSRSRSR RRSRSRRSSH SRSKSRSRSK 

       250        260        270        280        290        300 
SRGGRSKSKS PVKSRSRSRS RSNKSRDVSK SKSKSHSRTR SRSPKRERDS RSRSRSVSKR 

       310        320        330        340        350        360 
ESRSRSRSKS IHRDSRSRPP TVSFKSSFYK FTTMPFFCSD RSASAENKSR SRSRSRSASP 

       370 
KNGNASPDRN NESMDD 

« Hide

Isoform A (C) [UniParc].

Checksum: 7EDD2BC7FC52F865
Show »

FASTA35039,782
Isoform B (I) [UniParc].

Checksum: 7BD8602770AEF24A
Show »

FASTA32937,536
Isoform D [UniParc].

Checksum: CF9FEC836310B725
Show »

FASTA13515,469
Isoform E [UniParc].

Checksum: 54A1776E1F85A095
Show »

FASTA35540,381
Isoform F (K) [UniParc].

Checksum: A951ABAE25029D00
Show »

FASTA14716,694
Isoform G (H) [UniParc].

Checksum: 8A372A38D2E8D51C
Show »

FASTA21624,393
Isoform J [UniParc].

Checksum: F94FBC33C8A00A14
Show »

FASTA17119,554
Isoform L [UniParc].

Checksum: 9779F973085E8639
Show »

FASTA14916,870

References

« Hide 'large scale' references
[1]"A conserved family of nuclear phosphoproteins localized to sites of polymerase II transcription."
Roth M.B., Zahler A.M., Stolk J.A.
J. Cell Biol. 115:587-596(1991) [PubMed: 1717489] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROTEIN SEQUENCE OF 2-15; 126-132 AND 137-148, FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
Strain: CL.
Tissue: Embryo.
[2]"Characterization of a Drosophila protein associated with boundaries of transcriptionally active chromatin."
Champlin D.T., Frasch M., Saumweber H., Lis J.T.
Genes Dev. 5:1611-1621(1991) [PubMed: 1885003] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), SUBCELLULAR LOCATION.
Tissue: Embryo.
[3]"The genome sequence of Drosophila melanogaster."
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. expand/collapse author list , 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.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
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. expand/collapse author list , 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.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[5]"A Drosophila full-length cDNA resource."
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.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND G), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-376 (ISOFORM J).
Strain: Berkeley.
Tissue: Embryo, Head and Testis.
[6]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Booth B., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G. expand/collapse author list , Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A; E; G AND J).
Strain: Berkeley.
Tissue: Head and Ovary.
[7]"Isolation of RRM-type RNA-binding protein genes and the analysis of their relatedness by using a numerical approach."
Kim Y.-J., Baker B.S.
Mol. Cell. Biol. 13:174-183(1993) [PubMed: 8417324] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-42.
[8]"Two members of a conserved family of nuclear phosphoproteins are involved in pre-mRNA splicing."
Mayeda A., Zahler A.M., Krainer A.R., Roth M.B.
Proc. Natl. Acad. Sci. U.S.A. 89:1301-1304(1992) [PubMed: 1741384] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]"The SR protein B52/SRp55 is essential for Drosophila development."
Ring H.Z., Lis J.T.
Mol. Cell. Biol. 14:7499-7506(1994) [PubMed: 7935465] [Abstract]
Cited for: FUNCTION, DEVELOPMENTAL STAGE.
[10]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X58720 mRNA. Translation: CAA41556.1.
X62599 mRNA. Translation: CAA44483.1.
AE014297 Genomic DNA. Translation: AAF54968.1.
AE014297 Genomic DNA. Translation: AAF54969.2.
AE014297 Genomic DNA. Translation: AAN13575.1.
AE014297 Genomic DNA. Translation: AAN13577.1.
AE014297 Genomic DNA. Translation: AAN13578.1.
AE014297 Genomic DNA. Translation: ACZ94900.1.
AE014297 Genomic DNA. Translation: ACZ94901.1.
AE014297 Genomic DNA. Translation: ACZ94902.1.
AY069302 mRNA. Translation: AAL39447.1.
AY113327 mRNA. Translation: AAM29332.1.
BT001417 mRNA. Translation: AAN71172.1.
BT001482 mRNA. Translation: AAN71237.1. Frameshift.
BT001495 mRNA. Translation: AAN71250.1.
BT001750 mRNA. Translation: AAN71505.1.
BT003286 mRNA. Translation: AAO25044.1.
BT004500 mRNA. Translation: AAO42664.1.
BT125783 mRNA. Translation: ADQ89797.1.
S51722 mRNA. Translation: AAB24629.1.
PIRA37282.
A40459.
H48110.
RefSeqNP_001163603.1. NM_001170132.1.
NP_001163604.1. NM_001170133.1.
NP_001163605.1. NM_001170134.1.
NP_788665.1. NM_176488.2.
NP_788666.1. NM_176489.2.
NP_788668.1. NM_176491.2.
NP_788669.1. NM_176492.3.
NP_788670.1. NM_176493.3.
UniGeneDm.2188.

3D structure databases

ProteinModelPortalP26686.
SMRP26686. Positions 4-192.
ModBaseSearch...

Protein-protein interaction databases

IntActP26686. 3 interactions.
MINTMINT-934286.
STRINGP26686.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID41670.
KEGGdme:Dmel_CG10851.

Organism-specific databases

CTD41670.
FlyBaseFBgn0004587. B52.

Phylogenomic databases

eggNOGinNOG06535.
GeneTreeEMGT00050000000447.
InParanoidP26686.
OMADRNNESM.
OrthoDBEOG4NK9C3.
PhylomeDBP26686.

Gene expression databases

BgeeP26686.
GermOnlineCG10851. Drosophila melanogaster.

Family and domain databases

InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits.
KOK12893.
PfamPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio824942.

Entry information

Entry nameSRR55_DROME
AccessionPrimary (citable) accession number: P26686
Secondary accession number(s): A4V2U2 expand/collapse secondary AC list , E1JIK1, E1JIK2, E1JIK3, E4NKI6, Q24252, Q26277, Q8IH12, Q8ING7, Q8ING8, Q8ING9, Q8MZ66, Q8T0I0, Q9VFT0, Q9VFT1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 118 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families