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Protein

Protein phosphatase Slingshot homolog 3

Gene

Ssh3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protein phosphatase which may play a role in the regulation of actin filament dynamics. Can dephosphorylate and activate the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly.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 sitei410 – 4101Phosphocysteine intermediateCurated

GO - Molecular functioni

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

GO - Biological processi

  1. protein dephosphorylation Source: GO_Central
  2. regulation of actin polymerization or depolymerization Source: GO_Central
  3. regulation of axonogenesis Source: GO_Central
  4. regulation of lamellipodium assembly Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase Slingshot homolog 3 (EC:3.1.3.16, EC:3.1.3.48)
Alternative name(s):
SSH-like protein 3
Short name:
SSH-3L
Short name:
mSSH-3L
Gene namesi
Name:Ssh3
Synonyms:Ssh3l
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:2683546. Ssh3.

Subcellular locationi

Cytoplasmcytoskeleton 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: GO_Central
  2. cytoskeleton Source: UniProtKB-SubCell
  3. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi410 – 4101C → S: Abrogates phosphatase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 649648Protein phosphatase Slingshot homolog 3PRO_0000094846Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei88 – 881PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ8K330.
PRIDEiQ8K330.

PTM databases

PhosphoSiteiQ8K330.

Expressioni

Tissue specificityi

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

Developmental stagei

Expressed in the nervous system and epithelial tissues of the trachea at E14.5.1 Publication

Gene expression databases

BgeeiQ8K330.
CleanExiMM_SSH3.
GenevestigatoriQ8K330.

Interactioni

Subunit structurei

Does not bind to, or colocalize with, filamentous actin.

Structurei

3D structure databases

ProteinModelPortaliQ8K330.
SMRiQ8K330. Positions 327-466.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini325 – 465141Tyrosine-protein phosphataseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000154428.
HOVERGENiHBG089321.
InParanoidiQ8K330.
KOiK05766.
OMAiPHWKETH.
OrthoDBiEOG7B8S33.
PhylomeDBiQ8K330.
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.
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.

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: Q8K330-1) [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
MALVTVSRSP PASGHSTPVG PTQDRVVRRR GRLQRRQSFA VLRGAVLGLQ
60 70 80 90 100
DGGDSNVASE ADSEPMEEPS GEEQPTEDQT DKGQGLQSPW KQVQKRHLHL
110 120 130 140 150
MVELLRPQDD IRLAAQLEAA RPPRLRYLLV VSTGEELSEE AILLGVDFPD
160 170 180 190 200
SSSHSCTLGL VLPLWSDTQV YLDGDGGFSV TSGGQSRIFK PVSIQTMWAT
210 220 230 240 250
LQVLHQACEV ALGSGLVPGG SALAWATYYQ EKLNSDQGCL NEWMAMSDLE
260 270 280 290 300
SFRPPNAEPG QASEQEKMEQ AILAELWQVL DTSDLDSVTS KEIRQALELR
310 320 330 340 350
LGCPLQQYRD FIDNQMLLLM AQQDRASRIF PHLYLGSEWN AANLEELQKN
360 370 380 390 400
RVSHILNMAR EIDNFFPERF TYYNVRVWDE ESAQLLPHWK ETHRFIEDAR
410 420 430 440 450
AQGTRVLVHC KMGVSRSAAT VLAYAMKQYG WDLEQALIHV QELRPIVRPN
460 470 480 490 500
HGFLRQLRTY QGILTASRQS HVWEQKVGVV SPEEPLAPEV STPLPPLPPE
510 520 530 540 550
PGGSGEVMVM GLEGSQETPK EELGLRPRIN LRGVMRSISL LEPSESESTP
560 570 580 590 600
EAGGLPEVFS SDEEPLHPFS QLSRAKGGQR VRKGPWPALK SRQSVVALHS
610 620 630 640
AALVASRTRA FQEQGQGQEQ SEPGMSSTPR LRKVMRQASV DDSREEDKA
Length:649
Mass (Da):72,227
Last modified:October 1, 2002 - v1
Checksum:iDF8628B5E007E6F0
GO
Isoform 2 (identifier: Q8K330-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     261-261: Q → QITTR

Note: No experimental confirmation available.

Show »
Length:653
Mass (Da):72,699
Checksum:iA9674B3180E0648A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741Q → R in BAE29141. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei261 – 2611Q → QITTR in isoform 2. 1 PublicationVSP_016337

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB099289 mRNA. Translation: BAC97812.1.
BC028922 mRNA. Translation: AAH28922.1.
AK149880 mRNA. Translation: BAE29141.1.
CCDSiCCDS29425.1. [Q8K330-1]
RefSeqiNP_932781.1. NM_198113.2. [Q8K330-1]
XP_006531811.1. XM_006531748.1. [Q8K330-2]
UniGeneiMm.248388.

Genome annotation databases

EnsembliENSMUST00000037992; ENSMUSP00000047718; ENSMUSG00000034616. [Q8K330-1]
ENSMUST00000113852; ENSMUSP00000109483; ENSMUSG00000034616. [Q8K330-2]
GeneIDi245857.
KEGGimmu:245857.
UCSCiuc008fzo.2. mouse. [Q8K330-1]
uc012bgi.2. mouse. [Q8K330-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB099289 mRNA. Translation: BAC97812.1.
BC028922 mRNA. Translation: AAH28922.1.
AK149880 mRNA. Translation: BAE29141.1.
CCDSiCCDS29425.1. [Q8K330-1]
RefSeqiNP_932781.1. NM_198113.2. [Q8K330-1]
XP_006531811.1. XM_006531748.1. [Q8K330-2]
UniGeneiMm.248388.

3D structure databases

ProteinModelPortaliQ8K330.
SMRiQ8K330. Positions 327-466.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ8K330.

Proteomic databases

PaxDbiQ8K330.
PRIDEiQ8K330.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000037992; ENSMUSP00000047718; ENSMUSG00000034616. [Q8K330-1]
ENSMUST00000113852; ENSMUSP00000109483; ENSMUSG00000034616. [Q8K330-2]
GeneIDi245857.
KEGGimmu:245857.
UCSCiuc008fzo.2. mouse. [Q8K330-1]
uc012bgi.2. mouse. [Q8K330-2]

Organism-specific databases

CTDi54961.
MGIiMGI:2683546. Ssh3.

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000154428.
HOVERGENiHBG089321.
InParanoidiQ8K330.
KOiK05766.
OMAiPHWKETH.
OrthoDBiEOG7B8S33.
PhylomeDBiQ8K330.
TreeFamiTF319444.

Miscellaneous databases

NextBioi386960.
PROiQ8K330.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K330.
CleanExiMM_SSH3.
GenevestigatoriQ8K330.

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]
ProtoNetiSearch...

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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF CYS-410.
    Tissue: Brain.
  2. "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] (ISOFORM 1).
    Strain: Czech II.
    Tissue: Mammary tumor.
  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] OF 1-582 (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Bone marrow.
  4. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSSH3_MOUSE
AccessioniPrimary (citable) accession number: Q8K330
Secondary accession number(s): Q3UDX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: October 1, 2002
Last modified: February 4, 2015
This is version 108 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.