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Q6NN85 (SSH_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. 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:
Protein phosphatase Slingshot

EC=3.1.3.16
EC=3.1.3.48
Gene names
Name:ssh
ORF Names:CG6238
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1045 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protein phosphatase which regulates actin filament dynamics. Dephosphorylates and activates the actin binding/depolymerizing factor tsr/cofilin, which subsequently binds to actin filaments and stimulates their disassembly. Ref.1 Ref.5 Ref.6

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Subunit structure

Interacts with actin. Ref.1

Subcellular location

Cytoplasmcytoskeleton.

Developmental stage

Strongly expressed in apical regions of the assembling ommatidia of the eye-imaginal disk. Apical expression requires the receptor tyrosine kinases Egfr and sev/sevenless. Ref.6

Miscellaneous

Tyrosine phosphatase activity has not been demonstrated for this protein to date.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family.

Contains 1 tyrosine-protein phosphatase domain.

Sequence caution

The sequence AAF56372.3 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAN14027.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   LigandActin-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxonogenesis

Inferred from mutant phenotype Ref.5. Source: UniProtKB

cell morphogenesis

Inferred from mutant phenotype Ref.1. Source: UniProtKB

compound eye development

Inferred from genetic interaction PubMed 17097274. Source: FlyBase

establishment of nucleus localization

Inferred from mutant phenotype Ref.6. Source: UniProtKB

mitotic cell cycle

Inferred from mutant phenotype PubMed 17306545. Source: FlyBase

mushroom body development

Inferred from mutant phenotype Ref.5. Source: FlyBase

negative regulation of actin filament polymerization

Inferred from direct assay Ref.1. Source: UniProtKB

protein dephosphorylation

Inferred from mutant phenotype Ref.1Ref.5. Source: UniProtKB

regulation of actin filament polymerization

Inferred from mutant phenotype Ref.6. Source: UniProtKB

regulation of actin polymerization or depolymerization

Inferred from mutant phenotype Ref.1. Source: FlyBase

regulation of axonogenesis

Inferred from mutant phenotype Ref.5. Source: FlyBase

regulation of lamellipodium assembly

Inferred from mutant phenotype PubMed 17331727. Source: FlyBase

   Cellular_componentapical part of cell

Inferred from direct assay Ref.6. Source: UniProtKB

cytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

actin binding

Inferred from direct assay Ref.1. Source: UniProtKB

phosphoprotein phosphatase activity

Inferred from direct assay Ref.1. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein tyrosine/serine/threonine phosphatase activity

Non-traceable author statement PubMed 10908587. Source: FlyBase

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6NN85-1)

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 2 (identifier: Q6NN85-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MALVTVQRSPSVAGSCSNS → MSMQVCSLPDDILIFSLTPR
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10451045Protein phosphatase Slingshot
PRO_0000094849

Regions

Domain383 – 523141Tyrosine-protein phosphatase
Compositional bias985 – 104561Ser-rich

Sites

Active site4681Phosphocysteine intermediate Probable

Amino acid modifications

Modified residue7191Phosphoserine Ref.7

Natural variations

Alternative sequence1 – 1919MALVT…SCSNS → MSMQVCSLPDDILIFSLTPR in isoform 2.
VSP_016339

Experimental info

Mutagenesis4681C → S: Abrogates phosphatase activity. Ref.1 Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 22, 2005. Version 2.
Checksum: 76620BB63EE58A8B

FASTA1,045114,997
        10         20         30         40         50         60 
MALVTVQRSP SVAGSCSNSD GESEDDEGNS KGNDRSECFF AGKGTALVLA LKDIPPLTQS 

        70         80         90        100        110        120 
ERRLSTDSTR SSNSTQSNNS DIQLHLQSMF YLLQREDTLK MAVKLESQRS NRTRYLVIAS 

       130        140        150        160        170        180 
RSCCRSGTSD RRRHRIMRHH SVKVGGSAGT KSSTSPAVPT QRQLSVEQTA TEASSKCDKT 

       190        200        210        220        230        240 
ADKENATAAG DNKNTSGMEE SCLLGIDCNE RTTIGLVVPI LADTTIHLDG DGGFSVKVYE 

       250        260        270        280        290        300 
KTHIFKPVSV QAMWSALQTL HKVSKKAREN NFYASGPSHD WLSSYERRIE SDQSCLNEWN 

       310        320        330        340        350        360 
AMDALESRRP PSPDAIRNKP PEKEETESVI KMKLKAIMMS VDLDEVTSKY IRGRLEEILD 

       370        380        390        400        410        420 
MDLGEYKSFI DAEMLVILGQ MDAPTKIFEH VYLGSEWNAS NLEELQKNGV RHILNVTREI 

       430        440        450        460        470        480 
DNFFPGTFEY FNVRVYDDEK TNLLKYWDDT FRYITRAKAE GSKVLVHCKM GVSRSASVVI 

       490        500        510        520        530        540 
AYAMKAYQWE FQQALEHVKK RRSCIKPNKN FLNQLETYSG MLDAMKNKEK LQRSKSETNL 

       550        560        570        580        590        600 
KSTKDARLLP GSEPTPLIQA LNQAKSKSTG EAGVTPDGEE EDGSRMHRRS IAQKSQRRMV 

       610        620        630        640        650        660 
RRSSSTSPKT QTAVVTKQQS QSMENLTPER SVAEEPKNMR FPGSNGENYS VTQNQVLHIQ 

       670        680        690        700        710        720 
KHTPLSVRTR IHDLEAHRAD QLPQQPVWTS LTKLITQTSH LGKSVSGSSS GNIDSRRDSS 

       730        740        750        760        770        780 
CSDVFSSQVD SVFAKDEGEK RQRRKTHSWT ESLGPSGGIV LDPTPQQQKQ QSNAILRPRG 

       790        800        810        820        830        840 
TRQRELPSRH ASWGSGDNRC CLPQRTSSGS YYDSNRNTTA IFEGVIQDLK RSSNCNVIEG 

       850        860        870        880        890        900 
VAVAVEPIVG VGEGTVKRTK QKLEESTSLK KRCQEESQEL LLEAVDAGQR RCPSLYRSAS 

       910        920        930        940        950        960 
SAHSPRQRQP LRCNSEELMH TSDIENKNTT PGDHEATVVL RVQGQTLADD QRISGNVQIL 

       970        980        990       1000       1010       1020 
KQNFEAKAGV VGTGGGGGGG TAAGSGSSST IATSVSAVAG ACSANPGKKT TSHQSLPSSP 

      1030       1040 
VAQHANHVSA ASNSNSSASN SSDSS 

« Hide

Isoform 2 [UniParc].

Checksum: 9E34B1FF5DAF14D8
Show »

FASTA1,046115,370

References

« Hide 'large scale' references
[1]"Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin."
Niwa R., Nagata-Ohashi K., Takeichi M., Mizuno K., Uemura T.
Cell 108:233-246(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ACTIN, MUTAGENESIS OF CYS-468.
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"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] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: Berkeley.
Tissue: Testis.
[5]"Rho GTPases regulate axon growth through convergent and divergent signaling pathways."
Ng J., Luo L.
Neuron 44:779-793(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-468.
[6]"Slingshot cofilin phosphatase localization is regulated by receptor tyrosine kinases and regulates cytoskeletal structure in the developing Drosophila eye."
Rogers E.M., Hsiung F., Rodrigues A.B., Moses K.
Mech. Dev. 122:1194-1205(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEVELOPMENTAL STAGE.
[7]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-719, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB036834 mRNA. Translation: BAA89534.1.
AE014297 Genomic DNA. Translation: AAF56372.3. Sequence problems.
AE014297 Genomic DNA. Translation: AAN14027.1. Sequence problems.
BT011408 mRNA. Translation: AAR96200.1.
RefSeqNP_001163716.1. NM_001170245.1. [Q6NN85-2]
NP_001163717.1. NM_001170246.1. [Q6NN85-1]
NP_524492.2. NM_079768.4.
NP_733063.1. NM_170184.2.
UniGeneDm.1518.

3D structure databases

ProteinModelPortalQ6NN85.
SMRQ6NN85. Positions 383-524.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid67907. 5 interactions.
MINTMINT-965230.

Proteomic databases

PaxDbQ6NN85.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0301613; FBpp0290828; FBgn0029157. [Q6NN85-1]
GeneID42986.
KEGGdme:Dmel_CG6238.
UCSCCG6238-RA. d. melanogaster. [Q6NN85-1]

Organism-specific databases

CTD42986.
FlyBaseFBgn0029157. ssh.

Phylogenomic databases

eggNOGCOG2453.
GeneTreeENSGT00750000117282.
InParanoidQ6NN85.
KOK05766.
OrthoDBEOG7B8S33.
PhylomeDBQ6NN85.

Gene expression databases

BgeeQ6NN85.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
3.90.190.10. 1 hit.
InterProIPR014876. DEK_C.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR009057. Homeodomain-like.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR027232. Ssh.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PTHR10159:SF317. PTHR10159:SF317. 1 hit.
PfamPF08766. DEK_C. 1 hit.
PF00782. DSPc. 1 hit.
[Graphical view]
SMARTSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 1 hit.
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi42986.
NextBio831661.
PROQ6NN85.

Entry information

Entry nameSSH_DROME
AccessionPrimary (citable) accession number: Q6NN85
Secondary accession number(s): Q7KS05 expand/collapse secondary AC list , Q8IMU8, Q9NKY1, Q9VC04
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: July 9, 2014
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

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