Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q76I79

- SSH1_MOUSE

UniProt

Q76I79 - SSH1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Protein phosphatase Slingshot homolog 1

Gene

Ssh1

Organism
Mus musculus (Mouse)
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. Inhibitory phosphorylation of cofilin is mediated by LIMK1, which may also be dephosphorylated and inactivated by this protein.1 Publication

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 sitei393 – 3931Phosphocysteine intermediateCurated

GO - Molecular functioni

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

GO - Biological processi

  1. actin cytoskeleton organization Source: Ensembl
  2. cell morphogenesis Source: Ensembl
  3. cellular response to ATP Source: MGI
  4. protein dephosphorylation Source: RefGenome
  5. regulation of actin polymerization or depolymerization Source: RefGenome
  6. regulation of axonogenesis Source: RefGenome
  7. regulation of cellular protein metabolic process Source: MGI
  8. regulation of lamellipodium assembly Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Ssh1
Synonyms:Kiaa1298, Ssh1l
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:2686240. Ssh1.

Subcellular locationi

Cytoplasmcytoskeleton 1 Publication. 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.By similarity

GO - Cellular componenti

  1. cytoplasm Source: RefGenome
  2. cytoskeleton Source: UniProtKB-KW
  3. nucleus Source: Ensembl
  4. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi393 – 3931C → S: Abrogates phosphatase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 10421041Protein phosphatase Slingshot homolog 1PRO_0000094842Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei37 – 371PhosphoserineBy similarity
Modified residuei57 – 571PhosphoserineBy similarity
Modified residuei970 – 9701PhosphoserineBy similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ76I79.
PaxDbiQ76I79.
PRIDEiQ76I79.

PTM databases

PhosphoSiteiQ76I79.

Expressioni

Tissue specificityi

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

Developmental stagei

Ubiquitously expressed in the embryo at E14.5.1 Publication

Gene expression databases

BgeeiQ76I79.
CleanExiMM_SSH1.
ExpressionAtlasiQ76I79. baseline and differential.
GenevestigatoriQ76I79.

Interactioni

Subunit structurei

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.By similarity2 Publications

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000076873.

Structurei

3D structure databases

ProteinModelPortaliQ76I79.
SMRiQ76I79. Positions 309-449.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini308 – 448141Tyrosine-protein phosphataseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni889 – 1042154Interaction with YWHAGBy similarityAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000154427.
HOVERGENiHBG094001.
InParanoidiQ76I79.
KOiK05766.
OMAiNSHCDKN.
OrthoDBiEOG7B8S33.
PhylomeDBiQ76I79.
TreeFamiTF319444.

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.
IPR027233. SSH1.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PTHR10159:SF138. PTHR10159:SF138. 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q76I79-1) [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

        10         20         30         40         50
MALVTLQRSP TPSAASSSAS NSELEAGSDE ERKLNLSLSE SFFMVKGAAL
60 70 80 90 100
FLQQGNSPQG QRSLQHPHKH AGDLPQHLQV MINLLRCEDR IKLAVRLESV
110 120 130 140 150
WTDRVRYMVV VYTSGRQDTE ENILLGVDFS SKESKSCTIG MVLRLWSDTK
160 170 180 190 200
IHLDGDGGFS VSTAGRMHIF KPVSVQAMWS ALQVLHKACE VARRHNYFPG
210 220 230 240 250
GVALIWATYY ESCISSEQSC INEWNAMQDL ESTRPDSPAL FVDKPTEGER
260 270 280 290 300
TERLIKAKLR SIMMSQDLEN VTSKEIRNEL EKQMNCNLKE FKEFIDNEML
310 320 330 340 350
LILGQMDKPS LIFDHLYLGS EWNASNLEEL QGSGVDYILN VTREIDNFFP
360 370 380 390 400
GLFAYHNIRV YDEETTDLLA HWNEAYHFIN KAKRNHSKCL VHCKMGVSRS
410 420 430 440 450
ASTVIAYAMK EFGWPLEKAY NYVKQKRSIT RPNAGFMRQL SEYEGILDAS
460 470 480 490 500
KQRHNKLWRQ QPTDDTIAEP SEFLPETLDG ALDAQLPCLD DTTHPGLPRS
510 520 530 540 550
LAPGGPALPC CFRRLSDPLL LPHHDETGGL VHLEDLEKDA LLEEEESQPV
560 570 580 590 600
EVHKLVQHPQ EGARLCEKDV KRKLEFGNSK PRSDSLPQVE ELEKDGSPRT
610 620 630 640 650
GRWRRASTQL DRSLLDQENL NNNNSKRSCP DDLERDAMFG ILSKVKPPYT
660 670 680 690 700
SCADCMYPTA GGTPEAYMER HEDPSSSAIC TQPTFLPHVT SSPMAHASSR
710 720 730 740 750
SRAPERPASG PANTSPFLLP AGSRKPDVSG SGAGAAPEPP ASLLEPSRET
760 770 780 790 800
SKALPKSLQL KNPHCDKNAA NMEVSAKEEP SPKKDPKPAK DLRLLFSNEA
810 820 830 840 850
EKPTTNSYLM QHQESIIQLQ KAGLVRKHTK ELERLKSLPS DSPAACRDSA
860 870 880 890 900
TCRLEASIPE EGSQEPAHPA LCSQAGSEEQ PVGGTLQKSP TSTLPRLDHT
910 920 930 940 950
SNFSKDFLKT VCYTPTSSSI SSNLTRSSSS DSIHSVRGKP GLVKQRAQEI
960 970 980 990 1000
ETRLRLAGLT VSSPLKRSHS LAKLGSLNFS TEDLSSEADT STIADSQDAK
1010 1020 1030 1040
CGLSSSFLPE PQSAPRDPAA TSKSSGKSAP EHLKSPSRVN KS
Length:1,042
Mass (Da):115,297
Last modified:July 5, 2004 - v1
Checksum:i19A34E4937FA48FA
GO
Isoform 2 (identifier: Q76I79-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,020
Mass (Da):112,878
Checksum:i553EF13BEE0F0AF6
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti526 – 5261E → D in AAH46529. (PubMed:15489334)Curated
Sequence conflicti550 – 5501V → A in BAE41639. (PubMed:16141072)Curated
Sequence conflicti569 – 5691D → E in BAE41639. (PubMed:16141072)Curated
Sequence conflicti867 – 8671A → V in AAH46529. (PubMed:15489334)Curated
Sequence conflicti1010 – 10101E → G in BAE41639. (PubMed:16141072)Curated
Sequence conflicti1035 – 10351S → N in AAH46529. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei158 – 17922Missing in isoform 2. 1 PublicationVSP_016320Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS19556.1. [Q76I79-1]
RefSeqiNP_932777.2. NM_198109.4. [Q76I79-1]
UniGeneiMm.389682.

Genome annotation databases

EnsembliENSMUST00000112298; ENSMUSP00000107917; ENSMUSG00000042121. [Q76I79-2]
ENSMUST00000159592; ENSMUSP00000124312; ENSMUSG00000042121. [Q76I79-1]
GeneIDi231637.
KEGGimmu:231637.
UCSCiuc008yyx.1. mouse. [Q76I79-1]
uc008yyz.1. mouse. [Q76I79-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS19556.1. [Q76I79-1 ]
RefSeqi NP_932777.2. NM_198109.4. [Q76I79-1 ]
UniGenei Mm.389682.

3D structure databases

ProteinModelPortali Q76I79.
SMRi Q76I79. Positions 309-449.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000076873.

PTM databases

PhosphoSitei Q76I79.

Proteomic databases

MaxQBi Q76I79.
PaxDbi Q76I79.
PRIDEi Q76I79.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000112298 ; ENSMUSP00000107917 ; ENSMUSG00000042121 . [Q76I79-2 ]
ENSMUST00000159592 ; ENSMUSP00000124312 ; ENSMUSG00000042121 . [Q76I79-1 ]
GeneIDi 231637.
KEGGi mmu:231637.
UCSCi uc008yyx.1. mouse. [Q76I79-1 ]
uc008yyz.1. mouse. [Q76I79-2 ]

Organism-specific databases

CTDi 54434.
MGIi MGI:2686240. Ssh1.
Rougei Search...

Phylogenomic databases

eggNOGi COG2453.
GeneTreei ENSGT00760000118902.
HOGENOMi HOG000154427.
HOVERGENi HBG094001.
InParanoidi Q76I79.
KOi K05766.
OMAi NSHCDKN.
OrthoDBi EOG7B8S33.
PhylomeDBi Q76I79.
TreeFami TF319444.

Miscellaneous databases

NextBioi 380673.
PROi Q76I79.
SOURCEi Search...

Gene expression databases

Bgeei Q76I79.
CleanExi MM_SSH1.
ExpressionAtlasi Q76I79. baseline and differential.
Genevestigatori Q76I79.

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

Entry informationi

Entry nameiSSH1_MOUSE
AccessioniPrimary (citable) accession number: Q76I79
Secondary accession number(s): Q3TDG3, Q69ZM4, Q811E5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 97 of the entry and version 1 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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3