Q76I79 (SSH1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein phosphatase Slingshot homolog 1
EC=3.1.3.16
EC=3.1.3.48

Alternative name(s):
SSH-like protein 1
Short name=SSH-1L
Short name=mSSH-1L

Gene names

Name:	Ssh1
Synonyms:	Kiaa1298, Ssh1l

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1042 AA.
Sequence status	Complete.
Protein existence	Evidence 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 phosphoprotein + H2O = a protein + phosphate.
Subunit structure	Interacts with the 14-3-3 proteins YWHAB, YWHAG, YWHAQ, and YWHAZ. Interaction with 14-3-3 proteins inhibits phosphatase activity and also blocks recruitment to lamellipodia and stimulation by actin By similarity. Interacts with actin and this stimulates phosphatase activity. Interacts with LIMK1. Ref.1 Ref.5
Subcellular location	Cytoplasm › cytoskeleton. Cleavage furrow By similarity. Midbody By similarity. Note: Localized to the cleavage furrow and the midbody during cytokinesis By similarity. Also colocalizes with F-actin in the cytoplasm and the cell periphery, which may allow local control of actin dynamics at sites of cell locomotion. Ref.1
Tissue specificity	Expressed in brain, heart, kidney and thymus. Also expressed at lower levels in liver, skeletal muscle, small intestine and spleen. Ref.1
Developmental stage	Ubiquitously expressed in the embryo at E14.5. Ref.1
Post-translational modification	Phosphorylated. Inhibitory phosphorylation by PAK4 promotes binding to YWHAZ. Phosphorylation at Ser-970 is decreased by stimuli which promote actin reorganization and lamellipodia formation. Can be dephosphorylated and activated by PPP3CA/calcineurin A. Phosphorylation decreases immediately prior to telophase By similarity.
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 BAD32422.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing
Ligand	Actin-binding
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization Inferred from electronic annotation. Source: Compara cell morphogenesis Inferred from electronic annotation. Source: Compara cellular response to ATP Inferred from sequence orthology PubMed 19000834. Source: MGI 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 cellular protein metabolic process Inferred from sequence orthology PubMed 19000834. Source: MGI regulation of lamellipodium assembly Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	cleavage furrow Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasm Inferred from Biological aspect of Ancestor. Source: RefGenome cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell midbody Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: Compara
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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q76I79-1)

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: Q76I79-2)

The sequence of this isoform differs from the canonical sequence as follows:
     158-179: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1042	1042	Protein phosphatase Slingshot homolog 1		PRO_0000094842
Regions
	Domain	308 – 448	141	Tyrosine-protein phosphatase
	Region	889 – 1042	154	Interaction with YWHAG By similarity
Sites
	Active site	393	1	Phosphocysteine intermediate Probable
Amino acid modifications
	Modified residue	37	1	Phosphoserine By similarity
	Modified residue	57	1	Phosphoserine By similarity
	Modified residue	970	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	158 – 179	22	Missing in isoform 2.		VSP_016320
Experimental info
	Mutagenesis	393	1	C → S: Abrogates phosphatase activity. Ref.1
	Sequence conflict	526	1	E → D in AAH46529. Ref.4
	Sequence conflict	550	1	V → A in BAE41639. Ref.3
	Sequence conflict	569	1	D → E in BAE41639. Ref.3
	Sequence conflict	867	1	A → V in AAH46529. Ref.4
	Sequence conflict	1010	1	E → G in BAE41639. Ref.3
	Sequence conflict	1035	1	S → N in AAH46529. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 19A34E4937FA48FA	FASTA	1,042	115,297
	10 20 30 40 50 60 MALVTLQRSP TPSAASSSAS NSELEAGSDE ERKLNLSLSE SFFMVKGAAL FLQQGNSPQG 70 80 90 100 110 120 QRSLQHPHKH AGDLPQHLQV MINLLRCEDR IKLAVRLESV WTDRVRYMVV VYTSGRQDTE 130 140 150 160 170 180 ENILLGVDFS SKESKSCTIG MVLRLWSDTK IHLDGDGGFS VSTAGRMHIF KPVSVQAMWS 190 200 210 220 230 240 ALQVLHKACE VARRHNYFPG GVALIWATYY ESCISSEQSC INEWNAMQDL ESTRPDSPAL 250 260 270 280 290 300 FVDKPTEGER TERLIKAKLR SIMMSQDLEN VTSKEIRNEL EKQMNCNLKE FKEFIDNEML 310 320 330 340 350 360 LILGQMDKPS LIFDHLYLGS EWNASNLEEL QGSGVDYILN VTREIDNFFP GLFAYHNIRV 370 380 390 400 410 420 YDEETTDLLA HWNEAYHFIN KAKRNHSKCL VHCKMGVSRS ASTVIAYAMK EFGWPLEKAY 430 440 450 460 470 480 NYVKQKRSIT RPNAGFMRQL SEYEGILDAS KQRHNKLWRQ QPTDDTIAEP SEFLPETLDG 490 500 510 520 530 540 ALDAQLPCLD DTTHPGLPRS LAPGGPALPC CFRRLSDPLL LPHHDETGGL VHLEDLEKDA 550 560 570 580 590 600 LLEEEESQPV EVHKLVQHPQ EGARLCEKDV KRKLEFGNSK PRSDSLPQVE ELEKDGSPRT 610 620 630 640 650 660 GRWRRASTQL DRSLLDQENL NNNNSKRSCP DDLERDAMFG ILSKVKPPYT SCADCMYPTA 670 680 690 700 710 720 GGTPEAYMER HEDPSSSAIC TQPTFLPHVT SSPMAHASSR SRAPERPASG PANTSPFLLP 730 740 750 760 770 780 AGSRKPDVSG SGAGAAPEPP ASLLEPSRET SKALPKSLQL KNPHCDKNAA NMEVSAKEEP 790 800 810 820 830 840 SPKKDPKPAK DLRLLFSNEA EKPTTNSYLM QHQESIIQLQ KAGLVRKHTK ELERLKSLPS 850 860 870 880 890 900 DSPAACRDSA TCRLEASIPE EGSQEPAHPA LCSQAGSEEQ PVGGTLQKSP TSTLPRLDHT 910 920 930 940 950 960 SNFSKDFLKT VCYTPTSSSI SSNLTRSSSS DSIHSVRGKP GLVKQRAQEI ETRLRLAGLT 970 980 990 1000 1010 1020 VSSPLKRSHS LAKLGSLNFS TEDLSSEADT STIADSQDAK CGLSSSFLPE PQSAPRDPAA 1030 1040 TSKSSGKSAP EHLKSPSRVN KS
	Isoform 2 [UniParc]. Checksum: 553EF13BEE0F0AF6	FASTA	1,020	112,878
	10 20 30 40 50 60 MALVTLQRSP TPSAASSSAS NSELEAGSDE ERKLNLSLSE SFFMVKGAAL FLQQGNSPQG 70 80 90 100 110 120 QRSLQHPHKH AGDLPQHLQV MINLLRCEDR IKLAVRLESV WTDRVRYMVV VYTSGRQDTE 130 140 150 160 170 180 ENILLGVDFS SKESKSCTIG MVLRLWSDTK IHLDGDGSAL QVLHKACEVA RRHNYFPGGV 190 200 210 220 230 240 ALIWATYYES CISSEQSCIN EWNAMQDLES TRPDSPALFV DKPTEGERTE RLIKAKLRSI 250 260 270 280 290 300 MMSQDLENVT SKEIRNELEK QMNCNLKEFK EFIDNEMLLI LGQMDKPSLI FDHLYLGSEW 310 320 330 340 350 360 NASNLEELQG SGVDYILNVT REIDNFFPGL FAYHNIRVYD EETTDLLAHW NEAYHFINKA 370 380 390 400 410 420 KRNHSKCLVH CKMGVSRSAS TVIAYAMKEF GWPLEKAYNY VKQKRSITRP NAGFMRQLSE 430 440 450 460 470 480 YEGILDASKQ RHNKLWRQQP TDDTIAEPSE FLPETLDGAL DAQLPCLDDT THPGLPRSLA 490 500 510 520 530 540 PGGPALPCCF RRLSDPLLLP HHDETGGLVH LEDLEKDALL EEEESQPVEV HKLVQHPQEG 550 560 570 580 590 600 ARLCEKDVKR KLEFGNSKPR SDSLPQVEEL EKDGSPRTGR WRRASTQLDR SLLDQENLNN 610 620 630 640 650 660 NNSKRSCPDD LERDAMFGIL SKVKPPYTSC ADCMYPTAGG TPEAYMERHE DPSSSAICTQ 670 680 690 700 710 720 PTFLPHVTSS PMAHASSRSR APERPASGPA NTSPFLLPAG SRKPDVSGSG AGAAPEPPAS 730 740 750 760 770 780 LLEPSRETSK ALPKSLQLKN PHCDKNAANM EVSAKEEPSP KKDPKPAKDL RLLFSNEAEK 790 800 810 820 830 840 PTTNSYLMQH QESIIQLQKA GLVRKHTKEL ERLKSLPSDS PAACRDSATC RLEASIPEEG 850 860 870 880 890 900 SQEPAHPALC SQAGSEEQPV GGTLQKSPTS TLPRLDHTSN FSKDFLKTVC YTPTSSSISS 910 920 930 940 950 960 NLTRSSSSDS IHSVRGKPGL VKQRAQEIET RLRLAGLTVS SPLKRSHSLA KLGSLNFSTE 970 980 990 1000 1010 1020 DLSSEADTST IADSQDAKCG LSSSFLPEPQ SAPRDPAATS KSSGKSAPEH LKSPSRVNKS

References

	« 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, INTERACTION WITH ACTIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF CYS-393.
[2]	"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] (ISOFORM 2). Tissue: Embryonic tail.
[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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 539-1042 (ISOFORMS 1/2). 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] OF 166-1042 (ISOFORM 1). Strain: FVB/N. Tissue: Liver.
[5]	"Interplay between components of a novel LIM kinase-slingshot phosphatase complex regulates cofilin." Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N., Sarcevic B., Sampath R., Bamburg J.R., Bernard O. EMBO J. 24:473-486(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LIMK1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB099287 mRNA. Translation: BAC97810.1. AK173144 mRNA. Translation: BAD32422.1. Different initiation. AK155557 mRNA. Translation: BAE33323.1. AK170212 mRNA. Translation: BAE41639.1. AK171556 mRNA. Translation: BAE42524.1. BC046529 mRNA. Translation: AAH46529.1.
IPI	IPI00467332. IPI00625071.
RefSeq	NP_932777.2. NM_198109.4.
UniGene	Mm.389682.
3D structure databases
ProteinModelPortal	Q76I79.
SMR	Q76I79. Positions 309-449.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000076873.
PTM databases
PhosphoSite	Q76I79.
Proteomic databases
PaxDb	Q76I79.
PRIDE	Q76I79.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000112298; ENSMUSP00000107917; ENSMUSG00000042121. ENSMUST00000159592; ENSMUSP00000124312; ENSMUSG00000042121.
GeneID	231637.
KEGG	mmu:231637.
UCSC	uc008yyx.1. mouse. uc008yyz.1. mouse.
Organism-specific databases
CTD	54434.
MGI	MGI:2686240. Ssh1.
Rouge	Search...
Phylogenomic databases
eggNOG	COG2453.
GeneTree	ENSGT00700000104026.
HOGENOM	HOG000154427.
HOVERGEN	HBG094001.
InParanoid	Q76I79.
KO	K05766.
OMA	NSHCDKN.
OrthoDB	EOG480HVX.
Gene expression databases
ArrayExpress	Q76I79.
Bgee	Q76I79.
CleanEx	MM_SSH1.
Genevestigator	Q76I79.
GermOnline	ENSMUSG00000042121. 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. IPR027233. SSH1. IPR000387. Tyr/Dual-sp_Pase. IPR016130. Tyr_Pase_AS. [Graphical view]
PANTHER	PTHR10159. PTHR10159. 1 hit. PTHR10159:SF138. PTHR10159:SF138. 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	380673.
SOURCE	Search...

Entry information

Entry name

SSH1_MOUSE

Accession

Primary (citable) accession number: Q76I79
Secondary accession number(s): Q3TDG3, Q69ZM4, Q811E5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program