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Q8K330

- SSH3_MOUSE

UniProt

Q8K330 - SSH3_MOUSE

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Protein
Protein phosphatase Slingshot homolog 3
Gene
Ssh3, Ssh3l
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei410 – 4101Phosphocysteine intermediate Inferred

GO - Molecular functioni

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

GO - Biological processi

  1. protein dephosphorylation Source: RefGenome
  2. regulation of actin polymerization or depolymerization Source: RefGenome
  3. regulation of axonogenesis Source: RefGenome
  4. regulation of lamellipodium assembly Source: RefGenome
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. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: RefGenome
  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 3
PRO_0000094846Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei88 – 881Phosphoserine By 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.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00750000117282.
HOGENOMiHOG000154428.
HOVERGENiHBG089321.
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

MALVTVSRSP PASGHSTPVG PTQDRVVRRR GRLQRRQSFA VLRGAVLGLQ    50
DGGDSNVASE ADSEPMEEPS GEEQPTEDQT DKGQGLQSPW KQVQKRHLHL 100
MVELLRPQDD IRLAAQLEAA RPPRLRYLLV VSTGEELSEE AILLGVDFPD 150
SSSHSCTLGL VLPLWSDTQV YLDGDGGFSV TSGGQSRIFK PVSIQTMWAT 200
LQVLHQACEV ALGSGLVPGG SALAWATYYQ EKLNSDQGCL NEWMAMSDLE 250
SFRPPNAEPG QASEQEKMEQ AILAELWQVL DTSDLDSVTS KEIRQALELR 300
LGCPLQQYRD FIDNQMLLLM AQQDRASRIF PHLYLGSEWN AANLEELQKN 350
RVSHILNMAR EIDNFFPERF TYYNVRVWDE ESAQLLPHWK ETHRFIEDAR 400
AQGTRVLVHC KMGVSRSAAT VLAYAMKQYG WDLEQALIHV QELRPIVRPN 450
HGFLRQLRTY QGILTASRQS HVWEQKVGVV SPEEPLAPEV STPLPPLPPE 500
PGGSGEVMVM GLEGSQETPK EELGLRPRIN LRGVMRSISL LEPSESESTP 550
EAGGLPEVFS SDEEPLHPFS QLSRAKGGQR VRKGPWPALK SRQSVVALHS 600
AALVASRTRA FQEQGQGQEQ SEPGMSSTPR LRKVMRQASV DDSREEDKA 649
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei261 – 2611Q → QITTR in isoform 2.
VSP_016337

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741Q → R in BAE29141. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AB099289 mRNA. Translation: BAC97812.1 .
BC028922 mRNA. Translation: AAH28922.1 .
AK149880 mRNA. Translation: BAE29141.1 .
CCDSi CCDS29425.1. [Q8K330-1 ]
RefSeqi NP_932781.1. NM_198113.2. [Q8K330-1 ]
XP_006531811.1. XM_006531748.1. [Q8K330-2 ]
UniGenei Mm.248388.

3D structure databases

ProteinModelPortali Q8K330.
SMRi Q8K330. Positions 327-466.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q8K330.

Proteomic databases

PaxDbi Q8K330.
PRIDEi Q8K330.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000037992 ; ENSMUSP00000047718 ; ENSMUSG00000034616 . [Q8K330-1 ]
ENSMUST00000113852 ; ENSMUSP00000109483 ; ENSMUSG00000034616 . [Q8K330-2 ]
GeneIDi 245857.
KEGGi mmu:245857.
UCSCi uc008fzo.2. mouse. [Q8K330-1 ]
uc012bgi.2. mouse. [Q8K330-2 ]

Organism-specific databases

CTDi 54961.
MGIi MGI:2683546. Ssh3.

Phylogenomic databases

eggNOGi COG2453.
GeneTreei ENSGT00750000117282.
HOGENOMi HOG000154428.
HOVERGENi HBG089321.
KOi K05766.
OMAi PHWKETH.
OrthoDBi EOG7B8S33.
PhylomeDBi Q8K330.
TreeFami TF319444.

Miscellaneous databases

NextBioi 386960.
PROi Q8K330.
SOURCEi Search...

Gene expression databases

Bgeei Q8K330.
CleanExi MM_SSH3.
Genevestigatori Q8K330.

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.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view ]
PANTHERi PTHR10159. PTHR10159. 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, 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: July 9, 2014
This is version 104 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

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