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P19339 (SXL_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Protein sex-lethal
Gene names
Name:Sxl
Synonyms:Sx1
ORF Names:CG18350
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Sex determination switch protein which controls sexual development by sex-specific splicing. Regulates dosage compensation in females by suppressing hyperactivation of X-linked genes. Expression of the embryo-specific isoform is under the control of primary sex-determining signal, which depends on the ratio of X chromosomes relative to autosomes (X:A ratio). Expression occurs in 2X:2A cells, but not in X:2A cells. The X:A ratio seems to be signaled by the relative concentration of the X-linked transcription factors SIS-A and SIS-B. As a result, the embryo-specific product is expressed early only in female embryos and specifies female-adult specific splicing; in the male where it is not expressed, the default splicing gives rise to a truncated non-functional protein. The female-specific isoform specifies the splicing of its own transcript, thereby initiating a positive autoregulatory feedback loop leading to female development pathway. The female-specific isoform controls the sex-specific splicing of transformer (TRA); acts as a translational repressor for male-specific lethal-2 (MSL-2) and prevents male-less (MLE), MSL-1 and MSL-3 proteins from associating with the female X chromosome. Ref.1 Ref.2 Ref.6

Subunit structure

Part of a complex containing fl2d, Sxl and vir.

Tissue specificity

Expressed in somatic tissues, but not in the pole cells, which are the precursors of the germline.

Developmental stage

Isoform 1 is embryo-specific. Isoform CM1 is male-specific. Isoforms MS3, MS11 and MS16 are female specific. Isoform 1 is expressed for a brief period during the syncytial blastoderm stage. Isoform MS11 is expressed in 4-7 hours embryo. Ref.1 Ref.2

Domain

The Gly-Asn rich domain is required for the cooperative interaction with RNA and for regulating the splicing activity.

Sequence similarities

Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
   Biological processDifferentiation
Sexual differentiation
Transcription
Transcription regulation
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandRNA-binding
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processalternative nuclear mRNA splicing, via spliceosome

Traceable author statement Ref.9. Source: FlyBase

dosage compensation

Non-traceable author statement. Source: FlyBase

female germ-line sex determination

Traceable author statement. Source: FlyBase

female somatic sex determination

Traceable author statement. Source: FlyBase

germ cell development

Traceable author statement. Source: FlyBase

imaginal disc growth

Inferred from mutant phenotype. Source: FlyBase

negative regulation of nuclear mRNA splicing, via spliceosome

Traceable author statement. Source: FlyBase

oocyte differentiation

Inferred from direct assay. Source: FlyBase

reciprocal meiotic recombination

Traceable author statement. Source: FlyBase

regulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

sex determination, primary response to X:A ratio

Traceable author statement. Source: FlyBase

sex differentiation

Non-traceable author statement. Source: FlyBase

smoothened signaling pathway

Inferred from direct assay. Source: FlyBase

transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentprotein complex

Inferred from physical interaction. Source: FlyBase

   Molecular functiongrowth factor activity

Inferred from direct assay. Source: FlyBase

mRNA 3'-UTR binding

Inferred from direct assay. Source: FlyBase

mRNA 5'-UTR binding

Inferred from direct assay. Source: FlyBase

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(U) RNA binding

Inferred from direct assay. Source: FlyBase

translation repressor activity, nucleic acid binding

Traceable author statement. Source: FlyBase

Complete GO annotation...

Alternative products

This entry describes 14 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform MS3 (identifier: P19339-1)

Also known as: CF1; D; female-specific; L; T;

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 1 (identifier: P19339-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MYGNNNPGSNNNNGGYPPYGYNNKS → MDFNFDTVTPCSTMSSYYNFKMA

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Sequence conflict151S → C in AAB21845. Ref.6
Isoform A (identifier: P19339-10)

Also known as: E; U;

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: Missing.
     42-49: Missing.
Note: No experimental confirmation available.
Isoform C (identifier: P19339-8)

Also known as: N;

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MYGNNNPGSNNNNGGYPPYGYNNKS → MDFNFDTVTPCSTMSSYYNFKMA
     42-49: Missing.
Note: No experimental confirmation available.
Isoform CM1 (identifier: P19339-3)

Also known as: B; F; M;

The sequence of this isoform differs from the canonical sequence as follows:
     26-48: SGGRGFGMSHSLPSGMSRYAFSP → RHIFFHSPERSSHHYHRKAKDTH
     49-354: Missing.
Isoform G (identifier: P19339-7)

Also known as: J;

The sequence of this isoform differs from the canonical sequence as follows:
     42-49: Missing.
Note: No experimental confirmation available.
Isoform I (identifier: P19339-9)

The sequence of this isoform differs from the canonical sequence as follows:
     3-25: GNNNPGSNNNNGGYPPYGYNNKS → RNGIDSSY
Note: No experimental confirmation available.
Isoform K (identifier: P19339-11)

Also known as: Q;

The sequence of this isoform differs from the canonical sequence as follows:
     27-42: GGRGFGMSHSLPSGMS → PERSSHHYHRKAKDTH
     43-354: Missing.
Note: No experimental confirmation available.
Isoform MS11 (identifier: P19339-4)

Also known as: H;

The sequence of this isoform differs from the canonical sequence as follows:
     42-49: Missing.
     332-354: GRSIKSQQRFQNSHPYFDAKKFI → DGAMEKLRSLFDAICDAIFGLDSENFADLLDGLYRRKYHYPYL
Isoform MS16 (identifier: P19339-5)

Also known as: P;

The sequence of this isoform differs from the canonical sequence as follows:
     333-354: RSIKSQQRFQNSHPYFDAKKFI → ENFADLLDGLYRRKYHYPYL
Isoform O (identifier: P19339-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MYGNNNPGSNNNNGGYPPYGYNNKS → MDFNFDTVTPCSTMSSYYNFKMA
     42-49: Missing.
     332-354: GRSIKSQQRFQNSHPYFDAKKFI → DGAMEKLRSLFDAICDAIFGLDSENFADLLDGLYRRKYHYPYL
Note: No experimental confirmation available.
Isoform R (identifier: P19339-12)

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MYGNNNPGSNNNNGGYPPYGYNNKS → MDFNFDTVTPCSTMSSYYNFKMA
     42-49: Missing.
     333-354: RSIKSQQRFQNSHPYFDAKKFI → ENFADLLDGLYRRKYHYPYL
Note: No experimental confirmation available.
Isoform S (identifier: P19339-13)

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: Missing.
Note: No experimental confirmation available.
Isoform V (identifier: P19339-14)

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MYGNNNPGSNNNNGGYPPYGYNNKS → MDFNFDTVTPCSTMSSYYNFKMARNGIDSSY
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 354354Protein sex-lethal
PRO_0000081967

Regions

Domain125 – 20379RRM 1
Domain211 – 29181RRM 2
Compositional bias1 – 3232Asn/Gly-rich
Compositional bias57 – 604Poly-Ser
Compositional bias312 – 3198Poly-Pro

Natural variations

Alternative sequence1 – 3232Missing in isoform A and isoform S.
VSP_019287
Alternative sequence1 – 2525MYGNN…YNNKS → MDFNFDTVTPCSTMSSYYNF KMA in isoform 1, isoform C, isoform O and isoform R.
VSP_005881
Alternative sequence1 – 2525MYGNN…YNNKS → MDFNFDTVTPCSTMSSYYNF KMARNGIDSSY in isoform V.
VSP_040526
Alternative sequence3 – 2523GNNNP…YNNKS → RNGIDSSY in isoform I.
VSP_019288
Alternative sequence26 – 4823SGGRG…YAFSP → RHIFFHSPERSSHHYHRKAK DTH in isoform CM1.
VSP_005882
Alternative sequence27 – 4216GGRGF…PSGMS → PERSSHHYHRKAKDTH in isoform K.
VSP_019289
Alternative sequence42 – 498Missing in isoform A, isoform C, isoform G, isoform MS11, isoform O and isoform R.
VSP_005883
Alternative sequence43 – 354312Missing in isoform K.
VSP_019290
Alternative sequence49 – 354306Missing in isoform CM1.
VSP_005884
Alternative sequence332 – 35423GRSIK…AKKFI → DGAMEKLRSLFDAICDAIFG LDSENFADLLDGLYRRKYHY PYL in isoform MS11 and isoform O.
VSP_005885
Alternative sequence333 – 35422RSIKS…AKKFI → ENFADLLDGLYRRKYHYPYL in isoform MS16 and isoform R.
VSP_005886

Experimental info

Sequence conflict931P → S in AAA28921. Ref.2
Sequence conflict961S → G in AAA28921. Ref.2
Sequence conflict961S → G in ACY56908. Ref.5
Sequence conflict961S → G in ADD20766. Ref.5
Sequence conflict2731N → K in ACY56908. Ref.5

Secondary structure

............................... 354
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform MS3 (CF1) (D) (female-specific) (L) (T) [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 4E443D3BC88B134E

FASTA35438,549
        10         20         30         40         50         60 
MYGNNNPGSN NNNGGYPPYG YNNKSSGGRG FGMSHSLPSG MSRYAFSPQD TEFSFPSSSS 

        70         80         90        100        110        120 
RRGYNDFPGC GGSGGNGGSA NNLGGGNMCH LPPMASNNSL NNLCGLSLGS GGSDDLMNDP 

       130        140        150        160        170        180 
RASNTNLIVN YLPQDMTDRE LYALFRAIGP INTCRIMRDY KTGYSFGYAF VDFTSEMDSQ 

       190        200        210        220        230        240 
RAIKVLNGIT VRNKRLKVSY ARPGGESIKD TNLYVTNLPR TITDDQLDTI FGKYGSIVQK 

       250        260        270        280        290        300 
NILRDKLTGR PRGVAFVRYN KREEAQEAIS ALNNVIPEGG SQPLSVRLAE EHGKAKAAHF 

       310        320        330        340        350 
MSQMGVVPAN VPPPPPQPPA HMAAAFNMMH RGRSIKSQQR FQNSHPYFDA KKFI 

« Hide

Isoform 1 [UniParc].

Checksum: FD5C0EE4F86C8A29
Show »

FASTA35238,542
Isoform A (E) (U) [UniParc].

Checksum: 8CB2DCA31C482659
Show »

FASTA31434,304
Isoform C (N) [UniParc].

Checksum: 98D4D7D547D4D55D
Show »

FASTA34437,605
Isoform CM1 (B) (F) (M) [UniParc].

Checksum: 0900E728FB154B24
Show »

FASTA485,601
Isoform G (J) [UniParc].

Checksum: DD93EDFA9C166C35
Show »

FASTA34637,612
Isoform I [UniParc].

Checksum: D1129FB38DE66614
Show »

FASTA33937,047
Isoform K (Q) [UniParc].

Checksum: 7AFD03F36F4BEA11
Show »

FASTA424,763
Isoform MS11 (H) [UniParc].

Checksum: E7202AB9FFD0772B
Show »

FASTA36639,846
Isoform MS16 (P) [UniParc].

Checksum: 30528D103AEA1523
Show »

FASTA35238,370
Isoform O [UniParc].

Checksum: 180D2C7B3316D85D
Show »

FASTA36439,839
Isoform R [UniParc].

Checksum: AABC024FFCF99F76
Show »

FASTA34237,426
Isoform S [UniParc].

Checksum: 54C3A1F020F451FF
Show »

FASTA32235,241
Isoform V [UniParc].

Checksum: A56D6D64FB33528B
Show »

FASTA36039,435

References

« Hide 'large scale' references
[1]"Sex-lethal, a Drosophila sex determination switch gene, exhibits sex-specific RNA splicing and sequence similarity to RNA binding proteins."
Bell L.R., Maine E.M., Schedl P., Cline T.W.
Cell 55:1037-1046(1988) [PubMed: 3144435] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MS3 AND CM1), FUNCTION, DEVELOPMENTAL STAGE.
Strain: Oregon-R.
[2]"The complex set of late transcripts from the Drosophila sex determination gene sex-lethal encodes multiple related polypeptides."
Samuels M.E., Schedl P., Cline T.W.
Mol. Cell. Biol. 11:3584-3602(1991) [PubMed: 1710769] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MS3; MS11 AND MS16), FUNCTION, DEVELOPMENTAL STAGE.
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]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 (MAR-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A; I; MS16 AND V).
Strain: Berkeley.
Tissue: Embryo and Head.
[6]"The primary sex determination signal of Drosophila acts at the level of transcription."
Keyes L.N., Cline T.W., Schedl P.
Cell 68:933-943(1992) [PubMed: 1547493] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26 (ISOFORM 1), FUNCTION.
Tissue: Embryo.
[7]"Regulation of the gene Sex-lethal: a comparative analysis of Drosophila melanogaster and Drosophila subobscura."
Penalva L.O.F., Sakamoto H., Navarro-Sabate A., Sakashita E., Granadino B., Segarra C., Sanchez L.
Genetics 144:1653-1664(1996) [PubMed: 8978052] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41 (ISOFORM MS3).
[8]"Control of Drosophila Sex-lethal pre-mRNA splicing by its own female-specific product."
Sakamoto H., Inoue K., Higuchi I., Ono Y., Shimura Y.
Nucleic Acids Res. 20:5533-5540(1992) [PubMed: 1454517] [Abstract]
Cited for: ALTERNATIVE SPLICING.
[9]"Biochemical function of female-lethal (2)D/Wilms' tumor suppressor-1-associated proteins in alternative pre-mRNA splicing."
Ortega A., Niksic M., Bachi A., Wilm M., Sanchez L., Hastie N., Valcarcel J.
J. Biol. Chem. 278:3040-3047(2003) [PubMed: 12444081] [Abstract]
Cited for: IDENTIFICATION IN COMPLEX WITH FL(2)D AND VIR.
[10]"Resonance assignments and solution structure of the second RNA-binding domain of sex-lethal determined by multidimensional heteronuclear magnetic resonance."
Lee A.L., Kanaar R., Rio D.C., Wemmer D.E.
Biochemistry 33:13775-13786(1994) [PubMed: 7524663] [Abstract]
Cited for: STRUCTURE BY NMR OF 199-294.
[11]"A characteristic arrangement of aromatic amino acid residues in the solution structure of the amino-terminal RNA-binding domain of Drosophila sex-lethal."
Inoue M., Muto Y., Sakamoto H., Kigawa T., Takio K., Shimura Y., Yokoyama S.
J. Mol. Biol. 272:82-94(1997) [PubMed: 9299339] [Abstract]
Cited for: STRUCTURE BY NMR OF 122-209.
[12]"Structural basis for recognition of the tra mRNA precursor by the Sex-lethal protein."
Handa N., Nureki O., Kurimoto K., Kim I., Sakamoto H., Shimura Y., Muto Y., Yokoyama S.
Nature 398:579-585(1999) [PubMed: 10217141] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 122-289, RNA-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M23635 mRNA. Translation: AAA28885.1.
M23636 mRNA. Translation: AAA28884.1.
M59447 mRNA. Translation: AAA28922.1.
M59448 mRNA. Translation: AAA28921.1.
AE014298 Genomic DNA. Translation: AAF46240.2.
AE014298 Genomic DNA. Translation: AAF46241.3.
AE014298 Genomic DNA. Translation: AAG22410.1.
AE014298 Genomic DNA. Translation: AAG22411.1.
AE014298 Genomic DNA. Translation: AAN09197.1.
AE014298 Genomic DNA. Translation: AAN09198.1.
AE014298 Genomic DNA. Translation: AAN09200.2.
AE014298 Genomic DNA. Translation: AAN09201.2.
AE014298 Genomic DNA. Translation: AAO41638.2.
AE014298 Genomic DNA. Translation: AAZ52509.1.
AE014298 Genomic DNA. Translation: AAZ52510.1.
AE014298 Genomic DNA. Translation: AAZ52511.1.
AE014298 Genomic DNA. Translation: AAZ52512.1.
AE014298 Genomic DNA. Translation: AAZ52513.1.
AE014298 Genomic DNA. Translation: AAZ52514.1.
AE014298 Genomic DNA. Translation: ACZ95222.1.
AE014298 Genomic DNA. Translation: ACZ95223.1.
AE014298 Genomic DNA. Translation: ACZ95224.1.
AE014298 Genomic DNA. Translation: ACZ95225.1.
AE014298 Genomic DNA. Translation: ACZ95226.1.
AE014298 Genomic DNA. Translation: ACZ95227.1.
BT003583 mRNA. Translation: AAO39587.1.
BT099922 mRNA. Translation: ACX32993.1.
BT100240 mRNA. Translation: ACY56908.1.
BT120392 mRNA. Translation: ADD20766.1.
S88324 Genomic DNA. Translation: AAB21845.1.
D84425 Genomic DNA. Translation: BAA20294.1.
PIRA31639.
B31639. A39725.
RefSeqNP_001027062.1. NM_001031891.2.
NP_001027063.1. NM_001031892.1.
NP_001027064.1. NM_001031893.2.
NP_001027065.1. NM_001031894.1.
NP_001027066.1. NM_001031895.1.
NP_001162686.1. NM_001169215.1.
NP_001162687.1. NM_001169216.1.
NP_001162688.1. NM_001169217.1.
NP_001162689.1. NM_001169218.1.
NP_001162690.1. NM_001169219.1.
NP_001162691.1. NM_001169220.1.
NP_524791.3. NM_080052.3.
NP_727160.2. NM_167110.3.
NP_727161.2. NM_167111.2.
NP_727162.2. NM_167112.2.
NP_727163.2. NM_167113.2.
NP_727164.2. NM_167114.2.
NP_727165.2. NM_167115.2.
NP_727166.2. NM_167116.2.
NP_727167.2. NM_167117.2.
NP_727168.1. NM_167118.2.
UniGeneDm.4502.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B7FX-ray2.60A/B122-289[»]
1SXLNMR-A199-294[»]
2SXLNMR-A122-209[»]
3SXLX-ray2.70A/B/C113-294[»]
ProteinModelPortalP19339.
SMRP19339. Positions 123-289.
ModBaseSearch...

Protein-protein interaction databases

IntActP19339. 8 interactions.
MINTMINT-276991.
STRINGP19339.

Proteomic databases

PRIDEP19339.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0100203; FBpp0099573; FBgn0003659.
FBtr0100212; FBpp0099582; FBgn0003659.
FBtr0300842; FBpp0290066; FBgn0003659.
GeneID3772180.
KEGGdme:Dmel_CG18350.

Organism-specific databases

CTD3772180.
FlyBaseFBgn0003659. Sxl.

Phylogenomic databases

eggNOGinNOG07181.
InParanoidP19339.
OMATEFTFPS.
OrthoDBEOG4F4QSS.
PhylomeDBP19339.

Gene expression databases

BgeeP19339.
GermOnlineCG18350. Drosophila melanogaster.

Family and domain databases

InterProIPR002343. Hud_Sxl_RNA.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR006546. Sex_lethal_SF.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits.
PfamPF00076. RRM_1. 2 hits.
[Graphical view]
PRINTSPR00961. HUDSXLRNA.
SMARTSM00360. RRM. 2 hits.
[Graphical view]
TIGRFAMsTIGR01659. Sex-lethal. 1 hit.
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio852740.

Entry information

Entry nameSXL_DROME
AccessionPrimary (citable) accession number: P19339
Secondary accession number(s): A4V434 expand/collapse secondary AC list , A4V435, A4V436, A4V437, C9QP40, D0IQK2, D3PFI6, E1JJI8, E1JJI9, E1JJJ0, E1JJJ2, E1JJJ3, P19340, Q0KHV2, Q26466, Q2MGN7, Q2MGN8, Q2MGN9, Q2MGP1, Q7KVU6, Q7YZ92, Q8IRQ1, Q99141, Q9TYF5, Q9W3S6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: January 25, 2012
This is version 131 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families