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Q6NN85

- SSH_DROME

UniProt

Q6NN85 - SSH_DROME

Protein

Protein phosphatase Slingshot

Gene

ssh

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 2 (22 Nov 2005)
      Previous versions | rss
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    Functioni

    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.3 Publications

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation
    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei468 – 4681Phosphocysteine intermediateCurated

    GO - Molecular functioni

    1. actin binding Source: UniProtKB
    2. DNA binding Source: InterPro
    3. phosphoprotein phosphatase activity Source: UniProtKB
    4. protein tyrosine/serine/threonine phosphatase activity Source: FlyBase
    5. protein tyrosine phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. axonogenesis Source: UniProtKB
    2. cell morphogenesis Source: UniProtKB
    3. compound eye development Source: FlyBase
    4. establishment of nucleus localization Source: UniProtKB
    5. mitotic cell cycle Source: FlyBase
    6. mushroom body development Source: FlyBase
    7. negative regulation of actin filament polymerization Source: UniProtKB
    8. protein dephosphorylation Source: UniProtKB
    9. regulation of actin filament polymerization Source: UniProtKB
    10. regulation of actin polymerization or depolymerization Source: FlyBase
    11. regulation of axonogenesis Source: FlyBase
    12. regulation of lamellipodium assembly Source: FlyBase

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein phosphatase Slingshot (EC:3.1.3.16, EC:3.1.3.48)
    Gene namesi
    Name:ssh
    ORF Names:CG6238
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0029157. ssh.

    Subcellular locationi

    GO - Cellular componenti

    1. apical part of cell Source: UniProtKB
    2. cytoplasm Source: RefGenome
    3. cytoskeleton Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi468 – 4681C → S: Abrogates phosphatase activity. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10451045Protein phosphatase SlingshotPRO_0000094849Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei719 – 7191Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ6NN85.

    Expressioni

    Developmental stagei

    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.1 Publication

    Gene expression databases

    BgeeiQ6NN85.

    Interactioni

    Subunit structurei

    Interacts with actin.1 Publication

    Protein-protein interaction databases

    BioGridi67907. 5 interactions.
    MINTiMINT-965230.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6NN85.
    SMRiQ6NN85. Positions 383-524.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini383 – 523141Tyrosine-protein phosphataseAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi985 – 104561Ser-richAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2453.
    GeneTreeiENSGT00750000117282.
    InParanoidiQ6NN85.
    KOiK05766.
    OrthoDBiEOG7B8S33.
    PhylomeDBiQ6NN85.

    Family and domain databases

    Gene3Di1.10.10.60. 1 hit.
    3.90.190.10. 1 hit.
    InterProiIPR014876. 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]
    PANTHERiPTHR10159. PTHR10159. 1 hit.
    PTHR10159:SF317. PTHR10159:SF317. 1 hit.
    PfamiPF08766. DEK_C. 1 hit.
    PF00782. DSPc. 1 hit.
    [Graphical view]
    SMARTiSM00195. DSPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 1 hit.
    PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6NN85-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MALVTVQRSP SVAGSCSNSD GESEDDEGNS KGNDRSECFF AGKGTALVLA     50
    LKDIPPLTQS ERRLSTDSTR SSNSTQSNNS DIQLHLQSMF YLLQREDTLK 100
    MAVKLESQRS NRTRYLVIAS RSCCRSGTSD RRRHRIMRHH SVKVGGSAGT 150
    KSSTSPAVPT QRQLSVEQTA TEASSKCDKT ADKENATAAG DNKNTSGMEE 200
    SCLLGIDCNE RTTIGLVVPI LADTTIHLDG DGGFSVKVYE KTHIFKPVSV 250
    QAMWSALQTL HKVSKKAREN NFYASGPSHD WLSSYERRIE SDQSCLNEWN 300
    AMDALESRRP PSPDAIRNKP PEKEETESVI KMKLKAIMMS VDLDEVTSKY 350
    IRGRLEEILD MDLGEYKSFI DAEMLVILGQ MDAPTKIFEH VYLGSEWNAS 400
    NLEELQKNGV RHILNVTREI DNFFPGTFEY FNVRVYDDEK TNLLKYWDDT 450
    FRYITRAKAE GSKVLVHCKM GVSRSASVVI AYAMKAYQWE FQQALEHVKK 500
    RRSCIKPNKN FLNQLETYSG MLDAMKNKEK LQRSKSETNL KSTKDARLLP 550
    GSEPTPLIQA LNQAKSKSTG EAGVTPDGEE EDGSRMHRRS IAQKSQRRMV 600
    RRSSSTSPKT QTAVVTKQQS QSMENLTPER SVAEEPKNMR FPGSNGENYS 650
    VTQNQVLHIQ KHTPLSVRTR IHDLEAHRAD QLPQQPVWTS LTKLITQTSH 700
    LGKSVSGSSS GNIDSRRDSS CSDVFSSQVD SVFAKDEGEK RQRRKTHSWT 750
    ESLGPSGGIV LDPTPQQQKQ QSNAILRPRG TRQRELPSRH ASWGSGDNRC 800
    CLPQRTSSGS YYDSNRNTTA IFEGVIQDLK RSSNCNVIEG VAVAVEPIVG 850
    VGEGTVKRTK QKLEESTSLK KRCQEESQEL LLEAVDAGQR RCPSLYRSAS 900
    SAHSPRQRQP LRCNSEELMH TSDIENKNTT PGDHEATVVL RVQGQTLADD 950
    QRISGNVQIL KQNFEAKAGV VGTGGGGGGG TAAGSGSSST IATSVSAVAG 1000
    ACSANPGKKT TSHQSLPSSP VAQHANHVSA ASNSNSSASN SSDSS 1045
    Length:1,045
    Mass (Da):114,997
    Last modified:November 22, 2005 - v2
    Checksum:i76620BB63EE58A8B
    GO
    Isoform 2 (identifier: Q6NN85-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-19: MALVTVQRSPSVAGSCSNS → MSMQVCSLPDDILIFSLTPR

    Note: No experimental confirmation available.

    Show »
    Length:1,046
    Mass (Da):115,370
    Checksum:i9E34B1FF5DAF14D8
    GO

    Sequence cautioni

    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.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1919MALVT…SCSNS → MSMQVCSLPDDILIFSLTPR in isoform 2. 1 PublicationVSP_016339Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    RefSeqiNP_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.
    UniGeneiDm.1518.

    Genome annotation databases

    EnsemblMetazoaiFBtr0301613; FBpp0290828; FBgn0029157. [Q6NN85-1]
    GeneIDi42986.
    KEGGidme:Dmel_CG6238.
    UCSCiCG6238-RA. d. melanogaster. [Q6NN85-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    RefSeqi NP_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.
    UniGenei Dm.1518.

    3D structure databases

    ProteinModelPortali Q6NN85.
    SMRi Q6NN85. Positions 383-524.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 67907. 5 interactions.
    MINTi MINT-965230.

    Proteomic databases

    PaxDbi Q6NN85.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0301613 ; FBpp0290828 ; FBgn0029157 . [Q6NN85-1 ]
    GeneIDi 42986.
    KEGGi dme:Dmel_CG6238.
    UCSCi CG6238-RA. d. melanogaster. [Q6NN85-1 ]

    Organism-specific databases

    CTDi 42986.
    FlyBasei FBgn0029157. ssh.

    Phylogenomic databases

    eggNOGi COG2453.
    GeneTreei ENSGT00750000117282.
    InParanoidi Q6NN85.
    KOi K05766.
    OrthoDBi EOG7B8S33.
    PhylomeDBi Q6NN85.

    Miscellaneous databases

    GenomeRNAii 42986.
    NextBioi 831661.
    PROi Q6NN85.

    Gene expression databases

    Bgeei Q6NN85.

    Family and domain databases

    Gene3Di 1.10.10.60. 1 hit.
    3.90.190.10. 1 hit.
    InterProi IPR014876. 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 ]
    PANTHERi PTHR10159. PTHR10159. 1 hit.
    PTHR10159:SF317. PTHR10159:SF317. 1 hit.
    Pfami PF08766. DEK_C. 1 hit.
    PF00782. DSPc. 1 hit.
    [Graphical view ]
    SMARTi SM00195. DSPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 1 hit.
    PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.

    Entry informationi

    Entry nameiSSH_DROME
    AccessioniPrimary (citable) accession number: Q6NN85
    Secondary accession number(s): Q7KS05
    , Q8IMU8, Q9NKY1, Q9VC04
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: November 22, 2005
    Last modified: October 1, 2014
    This is version 89 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3