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Q6IVY4

- SSH_XENLA

UniProt

Q6IVY4 - SSH_XENLA

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Protein
Protein phosphatase Slingshot homolog
Gene
ssh
Organism
Xenopus laevis (African clawed frog)
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 cofilin, which subsequently binds to actin filaments and stimulates their disassembly. Required for completion of the gastrulation movement and for cytokinesis.2 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 sitei380 – 3801Phosphocysteine intermediate Inferred

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. protein tyrosine phosphatase activity Source: UniProtKB-EC
  3. protein tyrosine/serine/threonine phosphatase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase Slingshot homolog (EC:3.1.3.16, EC:3.1.3.48)
Short name:
xSSH
Alternative name(s):
Slingshot-related protein
Gene namesi
Name:ssh
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-5816852. ssh3.

Subcellular locationi

Cytoplasmcytoskeleton. Cleavage furrow. Midbody
Note: Also localizes to the cleavage furrow and the midbody during cytokinesis.1 Publication

GO - Cellular componenti

  1. cleavage furrow Source: UniProtKB-SubCell
  2. cytoplasm Source: UniProtKB-KW
  3. cytoskeleton Source: UniProtKB-SubCell
  4. midbody Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi380 – 3801C → S: Abrogates phosphatase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 691691Protein phosphatase Slingshot homolog
PRO_0000094848Add
BLAST

Expressioni

Developmental stagei

Maternally expressed in the early blastomere. Expressed in the involuting mesodermal cells and ectodermal cells of early gastrula stage embryos. Expression increases from stage 10.5, when the gastrulation movement occurs. Expression is concentrated at blastopore lips and the dorsal site of stage 11 embryos. Present in head structures and the trunk at the neurula and tailbud stages.1 Publication

Interactioni

Subunit structurei

Interacts with actin and this stimulates phosphatase activity.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ6IVY4.
SMRiQ6IVY4. Positions 296-436.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini295 – 435141Tyrosine-protein phosphatase
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili532 – 58049 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

KOiK05766.

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.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 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: Q6IVY4-1) [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

MALVTLQVSS LDVGSNITPV QDDEKSRRKR MQRRQSFVMV KGAALLLQDE    50
GEPIDTREPL SSSGPNEQQI HLQSMLRLLR EEDTLTLAVR LEPVRSCLTR 100
YLLVVSSTGK SNVEETLLLG VDFPHDGSLC CTIGTVLPIW SNTQVFLDGD 150
GGFTVTSGMD IRTFKPISVQ TMWSLLQMLH KACESALSNN VISSSLYSGL 200
IYYQSNRSSP QVCLNAWTAS PDIESARRDP ATPEREETER IIKLKLRDIL 250
RESDLENITS KEVRSALEQH TLCALQDYKE FIDNEMIIIL AQMDRPSEIF 300
PYLYLGSEWN ASNLEELQKN KVSHILNVTR EIDNFFPELF MYLNIRVLDE 350
ENTNLMQYWK ETHAFITTAR HQGSRVLVHC KMGVSRSAST VIAYAMKEYE 400
WTLETAIRHV KERRSIVQPN AGFMRQLQTY QGILGASKQR HSYLWDPSSA 450
PSLPLMSPPP KNFSSPTTSP LTPRLQKMNL RTLMRSISEM EAADTISEEK 500
ESTVVLEETT LKQNFNVLES SSNNLQVTPK RNEHVLSKEQ IIQEEKKVME 550
LEKGPEWVVK NNVLEEMKET EERELPNFEL PMSLNQSRER DQETIKESSV 600
ITQGSSSLDE VFESSTPTRS PEMASYACQK IQYFEQHSEG YSKVCFVDNL 650
QSVSEEEKVT LVSKQLQTDE HGERKARITR QQNVIDTHEE L 691
Length:691
Mass (Da):78,904
Last modified:November 22, 2005 - v2
Checksum:iC0EB36F3830AC20E
GO
Isoform 2 (identifier: Q6IVY4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: Missing.

Show »
Length:653
Mass (Da):74,545
Checksum:iF20DDABDF36494A2
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3838Missing in isoform 2.
VSP_016338Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651P → R in AAT39429. 1 Publication
Sequence conflicti624 – 6241A → V in AAH80117. 1 Publication
Sequence conflicti627 – 6271A → K in AAH80117. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY233266 mRNA. Translation: AAP57715.1.
AY618876 mRNA. Translation: AAT39429.1.
BC080117 mRNA. Translation: AAH80117.2.
BC094472 mRNA. Translation: AAH94472.1.
RefSeqiNP_001082641.1. NM_001089172.1.
UniGeneiXl.2010.

Genome annotation databases

GeneIDi398618.
KEGGixla:398618.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY233266 mRNA. Translation: AAP57715.1 .
AY618876 mRNA. Translation: AAT39429.1 .
BC080117 mRNA. Translation: AAH80117.2 .
BC094472 mRNA. Translation: AAH94472.1 .
RefSeqi NP_001082641.1. NM_001089172.1.
UniGenei Xl.2010.

3D structure databases

ProteinModelPortali Q6IVY4.
SMRi Q6IVY4. Positions 296-436.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 398618.
KEGGi xla:398618.

Organism-specific databases

CTDi 54961.
Xenbasei XB-GENE-5816852. ssh3.

Phylogenomic databases

KOi K05766.

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.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view ]
PANTHERi PTHR10159. PTHR10159. 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. "Functional involvement of Xenopus homologue of ADF/cofilin phosphatase, Slingshot (XSSH), in the gastrulation movement."
    Tanaka K., Nishio R., Haneda K., Abe H.
    Zool. Sci. 22:955-969(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, DEVELOPMENTAL STAGE, MUTAGENESIS OF CYS-380.
  2. NIH - Xenopus Gene Collection (XGC) project
    Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Eye and Oocyte.
  3. "Involvement of slingshot in the Rho-mediated dephosphorylation of ADF/cofilin during Xenopus cleavage."
    Tanaka K., Okubo Y., Abe H.
    Zool. Sci. 22:971-984(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ACTIN, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiSSH_XENLA
AccessioniPrimary (citable) accession number: Q6IVY4
Secondary accession number(s): Q505N4, Q68ET3, Q7T2T3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: June 11, 2014
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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