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Q6NN85

- SSH_DROME

UniProt

Q6NN85 - SSH_DROME

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Protein

Protein phosphatase Slingshot

Gene
ssh, CG6238
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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

Sites

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

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
Complete GO annotation...

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
Complete GO annotation...

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.

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. VSP_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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 88 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

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