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Q5SW75 (SSH2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. 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 2

EC=3.1.3.16
EC=3.1.3.48
Alternative name(s):
SSH-like protein 2
Short name=SSH-2L
Short name=mSSH-2L
Gene names
Name:Ssh2
Synonyms:Kiaa1725, Ssh2l
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1423 AA.
Sequence statusComplete.
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 filamentous actin. Ref.1

Subcellular location

Cytoplasmcytoskeleton. Cell junctionfocal adhesion. Note: Colocalizes with filamentous actin in the cytoplasm and the cell periphery. Also localizes to focal adhesions. Ref.1

Tissue specificity

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

Developmental stage

Expressed in the nervous system 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.

Sequence caution

The sequence BAE41593.1 differs from that shown. Reason: Intron retention.

The sequence CAI24907.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI35940.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI51882.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5SW75-1)

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: Q5SW75-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MALVTVQRSP...EEECRSQPRS → MTLSTLAGER...VISQNAINQL
Isoform 3 (identifier: Q5SW75-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MALVTVQRSP...EEECRSQPRS → MTLSTLAGER...VISQNAINQL
     133-133: S → R
     134-1423: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q5SW75-4)

The sequence of this isoform differs from the canonical sequence as follows:
     21-21: S → SSSYLEDSESAALLCCEYGESEIFSDFN
Note: Gene prediction based on EST data. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14231423Protein phosphatase Slingshot homolog 2
PRO_0000094844

Regions

Domain307 – 447141Tyrosine-protein phosphatase

Sites

Active site3921Phosphocysteine intermediate Probable

Amino acid modifications

Modified residue361Phosphoserine By similarity
Modified residue4871Phosphoserine By similarity
Modified residue14221Phosphothreonine By similarity

Natural variations

Alternative sequence1 – 3636MALVT…SQPRS → MTLSTLAGERKALPASTCSL GGPDMIPYFSANAVISQNAI NQL in isoform 2 and isoform 3.
VSP_016326
Alternative sequence211S → SSSYLEDSESAALLCCEYGE SEIFSDFN in isoform 4.
VSP_016327
Alternative sequence1331S → R in isoform 3.
VSP_016328
Alternative sequence134 – 14231290Missing in isoform 3.
VSP_016329

Experimental info

Mutagenesis3921C → S: Abrogates phosphatase activity. Ref.1
Sequence conflict1331Missing in BAE33137. Ref.2
Sequence conflict3251N → D in BAE41593. Ref.2

Sequences

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

Last modified March 15, 2005. Version 2.
Checksum: 7F2608E87A72BAFD

FASTA1,423158,230
        10         20         30         40         50         60 
MALVTVQRSP TPSTTSSPCA SEADSGEEEC RSQPRSISES FLTVKGAALF LPRGNGSSTP 

        70         80         90        100        110        120 
RVSHRRNKHA GDLQQHLQAM FILLRPEDNI RLAVRLESTY QNRTRYMVVV STNGRQDTEE 

       130        140        150        160        170        180 
SIVLGMDFSS NDSSTCTMGL VLPLWSDTLI HLDGDGGFSV STDNRVHIFK PVSVQAMWSA 

       190        200        210        220        230        240 
LQSLHKACEV ARMHNYYPGS LFLTWVSYYE SHINSDQSSV NEWNAMQDVQ SHRPDSPALF 

       250        260        270        280        290        300 
TDIPTERERT ERLIKTKLRE IMMQKDLENI TSKEIRTELE MQMVCNLREF KEFIDNEMIV 

       310        320        330        340        350        360 
ILGQMDSPTQ IFEHVFLGSE WNASNLEDLQ NRGVRYILNV TREIDNFFPG VFEYHNIRVY 

       370        380        390        400        410        420 
DEEATDLLAY WNDTYKFISK AKKHGSKCLV HCKMGVSRSA STVIAYAMKE YGWNLDRAYD 

       430        440        450        460        470        480 
YVKERRTVTK PNPSFMRQLE EYQGILLASK QRHNKLWRSH SDSDLSDHHE PICKPGLELN 

       490        500        510        520        530        540 
KKEMTTSADQ IAEVKTVENL AAMPTVFMEH VVPQDANQKG LHTKERVICL EFSSQEFRAG 

       550        560        570        580        590        600 
QIEDELNLND INGCSSGCCL SESKLPLDNC HASKALLQPG QAPDIANKFP DLAVEDLETD 

       610        620        630        640        650        660 
ALKADMNVHL LPMEELTSRL KDLPMSPDLE SPSPQASCQA AISDFSTDRI DFFSALEKFV 

       670        680        690        700        710        720 
ELSQETRSRS FSHSRIEELG GGRSEGCRLS VIEVAASEMA ADDQRSSSLS NTPHASEESS 

       730        740        750        760        770        780 
VDEDQSKAIT ELVSPDIIMQ SHSENAISVK EIVTEIESIS QGVGQVQLKG DILSNPCHTP 

       790        800        810        820        830        840 
KKSTIHELPL ERVPAPESKP GHWEQDESFC SVQPELARDS GKCAPEEGCL TTHSSTADLE 

       850        860        870        880        890        900 
EEEPVEGEHD WGPGMHSGAK WCPGSVRRAT LEFEERLRQE QENHGTASAG PTLSNRKNSK 

       910        920        930        940        950        960 
NDSSVADLMP KWKSDETTPE HSFFLKEAEP SKGKGKCSGS EAGSLSHCER NPTMPDCELL 

       970        980        990       1000       1010       1020 
EHHSLPAPQD CLGSDSRSKK QEGDLKKQRA VVPNQECDTQ AILLPLPKKI EIIEYTPTVT 

      1030       1040       1050       1060       1070       1080 
SLGHTEPGGE ATPSKEGEKQ GLRKVKMEQS ITMFCALDEN LNRTLEPSQV SLHPQVLPLP 

      1090       1100       1110       1120       1130       1140 
HSSSECDRPA DPNPMLSSPQ DKGDCPSTPF KTAAPFVSCS TQGASFSLDY LLPHSVVHLE 

      1150       1160       1170       1180       1190       1200 
GCTEQSSATD NELSPEQASW EDSRGHFLSS GSGMAHTSSP LTNEDLSLIN KLGDSVGVLQ 

      1210       1220       1230       1240       1250       1260 
KKLDPSPEAC RIPHSSSSEN IRDLSHSRGV VKEHAKEIES RVIFQAGFSK TSQMKRSASL 

      1270       1280       1290       1300       1310       1320 
AKLGYLDLCK DYLPDRELVS SESPHLKLLQ PFLRTDSGMH ALMAHEPSES AGAQQNPQPT 

      1330       1340       1350       1360       1370       1380 
KYSVEQLKTS ECIVQSKPVE RPSVQYAKEF GYSQQCLLPK ARPELTSSEG GLPLLQTQGL 

      1390       1400       1410       1420 
QYTGPSPGLA VAPRQQHGRT HPLRRLKRAN DKKRTTNPFY NTM 

« Hide

Isoform 2 [UniParc].

Checksum: DC554069F95CD99D
Show »

FASTA1,430158,900
Isoform 3 [UniParc].

Checksum: 05F40C9021BA2B9D
Show »

FASTA14015,439
Isoform 4 [UniParc].

Checksum: A76802D4C70636BF
Show »

FASTA1,450161,221

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-392.
Tissue: Kidney.
[2]"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] (ISOFORMS 2 AND 3).
Strain: NOD.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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] (ISOFORM 1).
Tissue: Brain.
[5]"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] OF 371-1423 (ISOFORMS 1/2).
Tissue: Brain.
[6]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB099288 mRNA. Translation: BAC97811.1.
AK155232 mRNA. Translation: BAE33137.1.
AK158449 mRNA. Translation: BAE34514.1.
AK170142 mRNA. Translation: BAE41593.1. Sequence problems.
AL606724, AL607072, AL663066 Genomic DNA. Translation: CAI24906.2.
AL606724, AL663066 Genomic DNA. Translation: CAI24907.1. Sequence problems.
AL663066, AL606724, AL607072 Genomic DNA. Translation: CAI35939.2.
AL663066, AL606724 Genomic DNA. Translation: CAI35940.1. Sequence problems.
AL606724 Genomic DNA. Translation: CAI51882.1. Sequence problems.
AL607072, AL606724, AL663066 Genomic DNA. Translation: CAI52040.1.
BC141392 mRNA. Translation: AAI41393.1.
BC141393 mRNA. Translation: AAI41394.1.
AK173243 mRNA. Translation: BAD32521.1.
RefSeqNP_808378.2. NM_177710.4.
XP_006533290.1. XM_006533227.1.
XP_006533292.1. XM_006533229.1.
XP_006533293.1. XM_006533230.1.
UniGeneMm.440381.

3D structure databases

ProteinModelPortalQ5SW75.
SMRQ5SW75. Positions 253-302, 307-448.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000104034.

PTM databases

PhosphoSiteQ5SW75.

Proteomic databases

PaxDbQ5SW75.
PRIDEQ5SW75.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000037912; ENSMUSP00000042625; ENSMUSG00000037926. [Q5SW75-1]
ENSMUST00000181283; ENSMUSP00000137933; ENSMUSG00000037926.
GeneID237860.
KEGGmmu:237860.
UCSCuc007kgl.2. mouse. [Q5SW75-1]
uc007kgo.2. mouse. [Q5SW75-2]

Organism-specific databases

CTD85464.
MGIMGI:2679255. Ssh2.
RougeSearch...

Phylogenomic databases

eggNOGCOG2453.
GeneTreeENSGT00750000117282.
HOVERGENHBG094002.
KOK05766.
OrthoDBEOG7B8S33.
PhylomeDBQ5SW75.
TreeFamTF319444.

Gene expression databases

BgeeQ5SW75.
CleanExMM_SSH2.
GenevestigatorQ5SW75.

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

NextBio383532.
PROQ5SW75.
SOURCESearch...

Entry information

Entry nameSSH2_MOUSE
AccessionPrimary (citable) accession number: Q5SW75
Secondary accession number(s): B9EJ94 expand/collapse secondary AC list , Q3TDK8, Q3TYP8, Q3U2K3, Q5F268, Q5SW74, Q69ZC3, Q76I78
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: March 15, 2005
Last modified: April 16, 2014
This is version 92 of the entry and version 2 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