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Q8K330 (SSH3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. 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 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 names
Name:Ssh3
Synonyms:Ssh3l
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length649 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 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. Ref.1

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

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

Subunit structure

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

Subcellular location

Cytoplasmcytoskeleton. Nucleus Ref.1.

Tissue specificity

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

Developmental stage

Expressed in the nervous system and epithelial tissues of the trachea at E14.5. Ref.1

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.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8K330-1)

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: Q8K330-2)

The sequence of this isoform differs from the canonical sequence as follows:
     261-261: Q → QITTR
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 649648Protein phosphatase Slingshot homolog 3
PRO_0000094846

Regions

Domain325 – 465141Tyrosine-protein phosphatase

Sites

Active site4101Phosphocysteine intermediate Probable

Amino acid modifications

Modified residue21N-acetylalanine Ref.4
Modified residue881Phosphoserine By similarity

Natural variations

Alternative sequence2611Q → QITTR in isoform 2.
VSP_016337

Experimental info

Mutagenesis4101C → S: Abrogates phosphatase activity. Ref.1
Sequence conflict741Q → R in BAE29141. Ref.3

Sequences

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

Last modified October 1, 2002. Version 1.
Checksum: DF8628B5E007E6F0

FASTA64972,227
        10         20         30         40         50         60 
MALVTVSRSP PASGHSTPVG PTQDRVVRRR GRLQRRQSFA VLRGAVLGLQ DGGDSNVASE 

        70         80         90        100        110        120 
ADSEPMEEPS GEEQPTEDQT DKGQGLQSPW KQVQKRHLHL MVELLRPQDD IRLAAQLEAA 

       130        140        150        160        170        180 
RPPRLRYLLV VSTGEELSEE AILLGVDFPD SSSHSCTLGL VLPLWSDTQV YLDGDGGFSV 

       190        200        210        220        230        240 
TSGGQSRIFK PVSIQTMWAT LQVLHQACEV ALGSGLVPGG SALAWATYYQ EKLNSDQGCL 

       250        260        270        280        290        300 
NEWMAMSDLE SFRPPNAEPG QASEQEKMEQ AILAELWQVL DTSDLDSVTS KEIRQALELR 

       310        320        330        340        350        360 
LGCPLQQYRD FIDNQMLLLM AQQDRASRIF PHLYLGSEWN AANLEELQKN RVSHILNMAR 

       370        380        390        400        410        420 
EIDNFFPERF TYYNVRVWDE ESAQLLPHWK ETHRFIEDAR AQGTRVLVHC KMGVSRSAAT 

       430        440        450        460        470        480 
VLAYAMKQYG WDLEQALIHV QELRPIVRPN HGFLRQLRTY QGILTASRQS HVWEQKVGVV 

       490        500        510        520        530        540 
SPEEPLAPEV STPLPPLPPE PGGSGEVMVM GLEGSQETPK EELGLRPRIN LRGVMRSISL 

       550        560        570        580        590        600 
LEPSESESTP EAGGLPEVFS SDEEPLHPFS QLSRAKGGQR VRKGPWPALK SRQSVVALHS 

       610        620        630        640 
AALVASRTRA FQEQGQGQEQ SEPGMSSTPR LRKVMRQASV DDSREEDKA 

« Hide

Isoform 2 [UniParc].

Checksum: A9674B3180E0648A
Show »

FASTA65372,699

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, 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. 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] OF 1-582 (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Bone marrow.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB099289 mRNA. Translation: BAC97812.1.
BC028922 mRNA. Translation: AAH28922.1.
AK149880 mRNA. Translation: BAE29141.1.
RefSeqNP_932781.1. NM_198113.2.
XP_006531811.1. XM_006531748.1.
UniGeneMm.248388.

3D structure databases

ProteinModelPortalQ8K330.
SMRQ8K330. Positions 327-466.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8K330.

Proteomic databases

PaxDbQ8K330.
PRIDEQ8K330.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000037992; ENSMUSP00000047718; ENSMUSG00000034616. [Q8K330-1]
ENSMUST00000113852; ENSMUSP00000109483; ENSMUSG00000034616. [Q8K330-2]
GeneID245857.
KEGGmmu:245857.
UCSCuc008fzo.2. mouse. [Q8K330-1]
uc012bgi.2. mouse. [Q8K330-2]

Organism-specific databases

CTD54961.
MGIMGI:2683546. Ssh3.

Phylogenomic databases

eggNOGCOG2453.
GeneTreeENSGT00750000117282.
HOGENOMHOG000154428.
HOVERGENHBG089321.
KOK05766.
OMAPHWKETH.
OrthoDBEOG7B8S33.
PhylomeDBQ8K330.
TreeFamTF319444.

Gene expression databases

BgeeQ8K330.
CleanExMM_SSH3.
GenevestigatorQ8K330.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
InterProIPR014876. DEK_C.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR009057. Homeodomain-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF08766. DEK_C. 1 hit.
PF00782. DSPc. 1 hit.
[Graphical view]
SMARTSM00195. DSPc. 1 hit.
[Graphical view]
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio386960.
PROQ8K330.
SOURCESearch...

Entry information

Entry nameSSH3_MOUSE
AccessionPrimary (citable) accession number: Q8K330
Secondary accession number(s): Q3UDX0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 101 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