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Q76I79 (SSH1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. 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 homolog 1

EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
SSH-like protein 1
Short name=SSH-1L
Short name=mSSH-1L
Gene names
Name:Ssh1
Synonyms:Kiaa1298, Ssh1l
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1042 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Inhibitory phosphorylation of cofilin is mediated by LIMK1, which may also be dephosphorylated and inactivated by this protein. Ref.1

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

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

Subunit structure

Interacts with the 14-3-3 proteins YWHAB, YWHAG, YWHAQ, and YWHAZ. Interaction with 14-3-3 proteins inhibits phosphatase activity and also blocks recruitment to lamellipodia and stimulation by actin By similarity. Interacts with actin and this stimulates phosphatase activity. Interacts with LIMK1. Ref.1 Ref.5

Subcellular location

Cytoplasmcytoskeleton. Cleavage furrow By similarity. Midbody By similarity. Note: Localized to the cleavage furrow and the midbody during cytokinesis By similarity. Also colocalizes with F-actin in the cytoplasm and the cell periphery, which may allow local control of actin dynamics at sites of cell locomotion. Ref.1

Tissue specificity

Expressed in brain, heart, kidney and thymus. Also expressed at lower levels in liver, skeletal muscle, small intestine and spleen. Ref.1

Developmental stage

Ubiquitously expressed in the embryo at E14.5. Ref.1

Post-translational modification

Phosphorylated. Inhibitory phosphorylation by PAK4 promotes binding to YWHAZ. Phosphorylation at Ser-970 is decreased by stimuli which promote actin reorganization and lamellipodia formation. Can be dephosphorylated and activated by PPP3CA/calcineurin A. Phosphorylation decreases immediately prior to telophase By similarity.

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 BAD32422.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   LigandActin-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

cell morphogenesis

Inferred from electronic annotation. Source: Ensembl

cellular response to ATP

Inferred from sequence orthology PubMed 19000834. Source: MGI

protein dephosphorylation

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of actin polymerization or depolymerization

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of axonogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of cellular protein metabolic process

Inferred from sequence orthology PubMed 19000834. Source: MGI

regulation of lamellipodium assembly

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentcleavage furrow

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

midbody

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

actin binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

phosphoprotein phosphatase activity

Inferred from sequence orthology PubMed 19000834. Source: MGI

protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein tyrosine/serine/threonine phosphatase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q76I79-1)

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: Q76I79-2)

The sequence of this isoform differs from the canonical sequence as follows:
     158-179: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 10421041Protein phosphatase Slingshot homolog 1
PRO_0000094842

Regions

Domain308 – 448141Tyrosine-protein phosphatase
Region889 – 1042154Interaction with YWHAG By similarity

Sites

Active site3931Phosphocysteine intermediate Probable

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue371Phosphoserine By similarity
Modified residue571Phosphoserine By similarity
Modified residue9701Phosphoserine By similarity

Natural variations

Alternative sequence158 – 17922Missing in isoform 2.
VSP_016320

Experimental info

Mutagenesis3931C → S: Abrogates phosphatase activity. Ref.1
Sequence conflict5261E → D in AAH46529. Ref.4
Sequence conflict5501V → A in BAE41639. Ref.3
Sequence conflict5691D → E in BAE41639. Ref.3
Sequence conflict8671A → V in AAH46529. Ref.4
Sequence conflict10101E → G in BAE41639. Ref.3
Sequence conflict10351S → N in AAH46529. Ref.4

Sequences

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

Last modified July 5, 2004. Version 1.
Checksum: 19A34E4937FA48FA

FASTA1,042115,297
        10         20         30         40         50         60 
MALVTLQRSP TPSAASSSAS NSELEAGSDE ERKLNLSLSE SFFMVKGAAL FLQQGNSPQG 

        70         80         90        100        110        120 
QRSLQHPHKH AGDLPQHLQV MINLLRCEDR IKLAVRLESV WTDRVRYMVV VYTSGRQDTE 

       130        140        150        160        170        180 
ENILLGVDFS SKESKSCTIG MVLRLWSDTK IHLDGDGGFS VSTAGRMHIF KPVSVQAMWS 

       190        200        210        220        230        240 
ALQVLHKACE VARRHNYFPG GVALIWATYY ESCISSEQSC INEWNAMQDL ESTRPDSPAL 

       250        260        270        280        290        300 
FVDKPTEGER TERLIKAKLR SIMMSQDLEN VTSKEIRNEL EKQMNCNLKE FKEFIDNEML 

       310        320        330        340        350        360 
LILGQMDKPS LIFDHLYLGS EWNASNLEEL QGSGVDYILN VTREIDNFFP GLFAYHNIRV 

       370        380        390        400        410        420 
YDEETTDLLA HWNEAYHFIN KAKRNHSKCL VHCKMGVSRS ASTVIAYAMK EFGWPLEKAY 

       430        440        450        460        470        480 
NYVKQKRSIT RPNAGFMRQL SEYEGILDAS KQRHNKLWRQ QPTDDTIAEP SEFLPETLDG 

       490        500        510        520        530        540 
ALDAQLPCLD DTTHPGLPRS LAPGGPALPC CFRRLSDPLL LPHHDETGGL VHLEDLEKDA 

       550        560        570        580        590        600 
LLEEEESQPV EVHKLVQHPQ EGARLCEKDV KRKLEFGNSK PRSDSLPQVE ELEKDGSPRT 

       610        620        630        640        650        660 
GRWRRASTQL DRSLLDQENL NNNNSKRSCP DDLERDAMFG ILSKVKPPYT SCADCMYPTA 

       670        680        690        700        710        720 
GGTPEAYMER HEDPSSSAIC TQPTFLPHVT SSPMAHASSR SRAPERPASG PANTSPFLLP 

       730        740        750        760        770        780 
AGSRKPDVSG SGAGAAPEPP ASLLEPSRET SKALPKSLQL KNPHCDKNAA NMEVSAKEEP 

       790        800        810        820        830        840 
SPKKDPKPAK DLRLLFSNEA EKPTTNSYLM QHQESIIQLQ KAGLVRKHTK ELERLKSLPS 

       850        860        870        880        890        900 
DSPAACRDSA TCRLEASIPE EGSQEPAHPA LCSQAGSEEQ PVGGTLQKSP TSTLPRLDHT 

       910        920        930        940        950        960 
SNFSKDFLKT VCYTPTSSSI SSNLTRSSSS DSIHSVRGKP GLVKQRAQEI ETRLRLAGLT 

       970        980        990       1000       1010       1020 
VSSPLKRSHS LAKLGSLNFS TEDLSSEADT STIADSQDAK CGLSSSFLPE PQSAPRDPAA 

      1030       1040 
TSKSSGKSAP EHLKSPSRVN KS 

« Hide

Isoform 2 [UniParc].

Checksum: 553EF13BEE0F0AF6
Show »

FASTA1,020112,878

References

« Hide 'large scale' references
[1]"Differential activities, subcellular distribution and tissue expression patterns of three members of Slingshot family phosphatases that dephosphorylate cofilin."
Ohta Y., Kousaka K., Nagata-Ohashi K., Ohashi K., Muramoto A., Shima Y., Niwa R., Uemura T., Mizuno K.
Genes Cells 8:811-824(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ACTIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF CYS-393.
[2]"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Embryonic tail.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 539-1042 (ISOFORMS 1/2).
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 166-1042 (ISOFORM 1).
Strain: FVB/N.
Tissue: Liver.
[5]"Interplay between components of a novel LIM kinase-slingshot phosphatase complex regulates cofilin."
Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N., Sarcevic B., Sampath R., Bamburg J.R., Bernard O.
EMBO J. 24:473-486(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LIMK1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB099287 mRNA. Translation: BAC97810.1.
AK173144 mRNA. Translation: BAD32422.1. Different initiation.
AK155557 mRNA. Translation: BAE33323.1.
AK170212 mRNA. Translation: BAE41639.1.
AK171556 mRNA. Translation: BAE42524.1.
BC046529 mRNA. Translation: AAH46529.1.
CCDSCCDS19556.1. [Q76I79-1]
RefSeqNP_932777.2. NM_198109.4. [Q76I79-1]
UniGeneMm.389682.

3D structure databases

ProteinModelPortalQ76I79.
SMRQ76I79. Positions 309-449.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000076873.

PTM databases

PhosphoSiteQ76I79.

Proteomic databases

PaxDbQ76I79.
PRIDEQ76I79.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000112298; ENSMUSP00000107917; ENSMUSG00000042121. [Q76I79-2]
ENSMUST00000159592; ENSMUSP00000124312; ENSMUSG00000042121. [Q76I79-1]
GeneID231637.
KEGGmmu:231637.
UCSCuc008yyx.1. mouse. [Q76I79-1]
uc008yyz.1. mouse. [Q76I79-2]

Organism-specific databases

CTD54434.
MGIMGI:2686240. Ssh1.
RougeSearch...

Phylogenomic databases

eggNOGCOG2453.
GeneTreeENSGT00750000117282.
HOGENOMHOG000154427.
HOVERGENHBG094001.
InParanoidQ76I79.
KOK05766.
OMANSHCDKN.
OrthoDBEOG7B8S33.
PhylomeDBQ76I79.
TreeFamTF319444.

Gene expression databases

ArrayExpressQ76I79.
BgeeQ76I79.
CleanExMM_SSH1.
GenevestigatorQ76I79.

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.
IPR027233. SSH1.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PTHR10159:SF138. PTHR10159:SF138. 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

NextBio380673.
PROQ76I79.
SOURCESearch...

Entry information

Entry nameSSH1_MOUSE
AccessionPrimary (citable) accession number: Q76I79
Secondary accession number(s): Q3TDG3, Q69ZM4, Q811E5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot