Protein phosphatase Slingshot homolog 3

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Preferred order of sections

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Contribute

Send feedback

Read comments (?) or add your own

Q8K330 (SSH3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 92. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Protein names

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 names

Name:	Ssh3
Synonyms:	Ssh3l

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Sequence length	649 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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 phosphoprotein + H₂O = a protein + phosphate.
Subunit structure	Does not bind to, or colocalize with, filamentous actin.
Subcellular location	Cytoplasm › cytoskeleton. 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.

Keywords
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC regulation of actin polymerization or depolymerization Inferred from Biological aspect of Ancestor. Source: RefGenome regulation of axonogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome regulation of lamellipodium assembly Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	cytoplasm Inferred from Biological aspect of Ancestor. Source: RefGenome cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro actin binding Inferred from Biological aspect of Ancestor. Source: RefGenome protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine/serine/threonine phosphatase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Chain

1 – 649

649

Protein phosphatase Slingshot homolog 3

PRO_0000094846

Domain

325 – 465

141

Tyrosine-protein phosphatase

Active site

410

Phosphocysteine intermediate Probable

Modified residue

Phosphoserine Ref.4

Modified residue

Phosphoserine Ref.5

Modified residue

Phosphoserine Ref.5

Modified residue

Phosphoserine By similarity

Modified residue

639

Phosphoserine Ref.5

Alternative sequence

261

Q → QITTR in isoform 2.

VSP_016337

Mutagenesis

410

C → S: Abrogates phosphatase activity. Ref.1

Sequence conflict

Q → R in BAE29141. Ref.3

Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: DF8628B5E007E6F0 Show »	FASTA	649	72,227
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 »	FASTA	653	72,699
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 QITTRASEQE KMEQAILAEL WQVLDTSDLD SVTSKEIRQA 310 320 330 340 350 360 LELRLGCPLQ QYRDFIDNQM LLLMAQQDRA SRIFPHLYLG SEWNAANLEE LQKNRVSHIL 370 380 390 400 410 420 NMAREIDNFF PERFTYYNVR VWDEESAQLL PHWKETHRFI EDARAQGTRV LVHCKMGVSR 430 440 450 460 470 480 SAATVLAYAM KQYGWDLEQA LIHVQELRPI VRPNHGFLRQ LRTYQGILTA SRQSHVWEQK 490 500 510 520 530 540 VGVVSPEEPL APEVSTPLPP LPPEPGGSGE VMVMGLEGSQ ETPKEELGLR PRINLRGVMR 550 560 570 580 590 600 SISLLEPSES ESTPEAGGLP EVFSSDEEPL HPFSQLSRAK GGQRVRKGPW PALKSRQSVV 610 620 630 640 650 ALHSAALVAS RTRAFQEQGQ GQEQSEPGMS STPRLRKVMR QASVDDSREE DKA « Hide

	« Hide 'large scale' referencesShow '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. 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-38 AND SER-639, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Sequence databases
EMBL GenBank DDBJ	AB099289 mRNA. Translation: BAC97812.1. BC028922 mRNA. Translation: AAH28922.1. AK149880 mRNA. Translation: BAE29141.1.
IPI	IPI00356992. IPI00656268.
RefSeq	NP_932781.1. NM_198113.2.
UniGene	Mm.248388.
3D structure databases
ProteinModelPortal	Q8K330.
SMR	Q8K330. Positions 327-466.
ModBase	Search...
PTM databases
PhosphoSite	Q8K330.
Proteomic databases
PaxDb	Q8K330.
PRIDE	Q8K330.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000037992; ENSMUSP00000047718; ENSMUSG00000034616. ENSMUST00000113852; ENSMUSP00000109483; ENSMUSG00000034616.
GeneID	245857.
KEGG	mmu:245857.
UCSC	uc008fzo.1. mouse. uc012bgi.1. mouse.
Organism-specific databases
CTD	54961.
MGI	MGI:2683546. Ssh3.
Phylogenomic databases
eggNOG	COG2453.
GeneTree	ENSGT00700000104026.
HOGENOM	HOG000154428.
HOVERGEN	HBG089321.
KO	K05766.
OMA	HILNMAR.
OrthoDB	EOG4WDDBT.
Gene expression databases
Bgee	Q8K330.
CleanEx	MM_SSH3.
Genevestigator	Q8K330.
GermOnline	ENSMUSG00000034616. Mus musculus.
Family and domain databases
Gene3D	1.10.10.60. 1 hit.
InterPro	IPR014876. 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]
PANTHER	PTHR10159. PTHR10159. 1 hit.
Pfam	PF08766. DEK_C. 1 hit. PF00782. DSPc. 1 hit. [Graphical view]
SMART	SM00195. DSPc. 1 hit. [Graphical view]
PROSITE	PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50054. TYR_PHOSPHATASE_DUAL. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	386960.
SOURCE	Search...

Entry name

SSH3_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

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.