SSH1_HUMAN
ID SSH1_HUMAN Reviewed; 1049 AA.
AC Q8WYL5; Q6P6C0; Q8N9A7; Q8WYL3; Q8WYL4; Q9P2P8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Protein phosphatase Slingshot homolog 1 {ECO:0000305};
DE EC=3.1.3.16 {ECO:0000269|PubMed:11832213};
DE EC=3.1.3.48 {ECO:0000255|PROSITE-ProRule:PRU10044};
DE AltName: Full=SSH-like protein 1;
DE Short=SSH-1L;
DE Short=hSSH-1L;
GN Name=SSH1 {ECO:0000312|HGNC:HGNC:30579}; Synonyms=KIAA1298, SSH1L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, CATALYTIC
RP ACTIVITY, INTERACTION WITH ACTIN, AND MUTAGENESIS OF CYS-393.
RX PubMed=11832213; DOI=10.1016/s0092-8674(01)00638-9;
RA Niwa R., Nagata-Ohashi K., Takeichi M., Mizuno K., Uemura T.;
RT "Control of actin reorganization by Slingshot, a family of phosphatases
RT that dephosphorylate ADF/cofilin.";
RL Cell 108:233-246(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND INTERACTION WITH ACTIN.
RX PubMed=14531860; DOI=10.1046/j.1365-2443.2003.00678.x;
RA Ohta Y., Kousaka K., Nagata-Ohashi K., Ohashi K., Muramoto A., Shima Y.,
RA Niwa R., Uemura T., Mizuno K.;
RT "Differential activities, subcellular distribution and tissue expression
RT patterns of three members of Slingshot family phosphatases that
RT dephosphorylate cofilin.";
RL Genes Cells 8:811-824(2003).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF
RP CYS-393.
RX PubMed=12807904; DOI=10.1074/jbc.m305802200;
RA Kaji N., Ohashi K., Shuin M., Niwa R., Uemura T., Mizuno K.;
RT "Cell cycle-associated changes in Slingshot phosphatase activity and roles
RT in cytokinesis in animal cells.";
RL J. Biol. Chem. 278:33450-33455(2003).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF CYS-393.
RX PubMed=12684437; DOI=10.1523/jneurosci.23-07-02527.2003;
RA Endo M., Ohashi K., Sasaki Y., Goshima Y., Niwa R., Uemura T., Mizuno K.;
RT "Control of growth cone motility and morphology by LIM kinase and Slingshot
RT via phosphorylation and dephosphorylation of cofilin.";
RL J. Neurosci. 23:2527-2537(2003).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-393.
RX PubMed=15056216; DOI=10.1111/j.1462-5822.2004.00375.x;
RA Dai S., Sarmiere P.D., Wiggan O., Bamburg J.R., Zhou D.;
RT "Efficient Salmonella entry requires activity cycles of host ADF and
RT cofilin.";
RL Cell. Microbiol. 6:459-471(2004).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14645219; DOI=10.1074/jbc.m312591200;
RA Nishita M., Wang Y., Tomizawa C., Suzuki A., Niwa R., Uemura T., Mizuno K.;
RT "Phosphoinositide 3-kinase-mediated activation of cofilin phosphatase
RT Slingshot and its role for insulin-induced membrane protrusion.";
RL J. Biol. Chem. 279:7193-7198(2004).
RN [10]
RP FUNCTION, INTERACTION WITH YWHAB; YWHAG; YWHAQ AND YWHAZ, SUBCELLULAR
RP LOCATION, PHOSPHORYLATION AT SER-978, AND MUTAGENESIS OF CYS-393; SER-937
RP AND SER-978.
RX PubMed=15159416; DOI=10.1083/jcb.200401136;
RA Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M.,
RA Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.;
RT "A pathway of neuregulin-induced activation of cofilin-phosphatase
RT Slingshot and cofilin in lamellipodia.";
RL J. Cell Biol. 165:465-471(2004).
RN [11]
RP FUNCTION, INTERACTION WITH ACTIN; LIMK1 AND YWHAZ, PHOSPHORYLATION, AND
RP MUTAGENESIS OF CYS-393.
RX PubMed=15660133; DOI=10.1038/sj.emboj.7600543;
RA Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N., Sarcevic B.,
RA Sampath R., Bamburg J.R., Bernard O.;
RT "Interplay between components of a novel LIM kinase-slingshot phosphatase
RT complex regulates cofilin.";
RL EMBO J. 24:473-486(2005).
RN [12]
RP FUNCTION, PHOSPHORYLATION, DEPHOSPHORYLATION BY PPP3CA, AND MUTAGENESIS OF
RP CYS-393.
RX PubMed=15671020; DOI=10.1074/jbc.m411494200;
RA Wang Y., Shibasaki F., Mizuno K.;
RT "Calcium signal-induced cofilin dephosphorylation is mediated by Slingshot
RT via calcineurin.";
RL J. Biol. Chem. 280:12683-12689(2005).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-393 AND TRP-458.
RX PubMed=16230460; DOI=10.1083/jcb.200504029;
RA Nishita M., Tomizawa C., Yamamoto M., Horita Y., Ohashi K., Mizuno K.;
RT "Spatial and temporal regulation of cofilin activity by LIM kinase and
RT Slingshot is critical for directional cell migration.";
RL J. Cell Biol. 171:349-359(2005).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37 AND SER-57, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576 AND SER-897, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Protein phosphatase which regulates actin filament dynamics.
CC Dephosphorylates and activates the actin binding/depolymerizing factor
CC cofilin, which subsequently binds to actin filaments and stimulates
CC their disassembly. Inhibitory phosphorylation of cofilin is mediated by
CC LIMK1, which may also be dephosphorylated and inactivated by this
CC protein. {ECO:0000269|PubMed:11832213, ECO:0000269|PubMed:12684437,
CC ECO:0000269|PubMed:12807904, ECO:0000269|PubMed:14531860,
CC ECO:0000269|PubMed:14645219, ECO:0000269|PubMed:15056216,
CC ECO:0000269|PubMed:15159416, ECO:0000269|PubMed:15660133,
CC ECO:0000269|PubMed:15671020, ECO:0000269|PubMed:16230460}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:11832213};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- SUBUNIT: Interacts with actin and this stimulates phosphatase activity.
CC Also interacts with LIMK1 and with the 14-3-3 proteins YWHAB, YWHAG,
CC YWHAQ, and YWHAZ. Interaction with 14-3-3 proteins inhibits phosphatase
CC activity and also blocks recruitment to lamellipodia and stimulation by
CC actin. {ECO:0000269|PubMed:11832213, ECO:0000269|PubMed:14531860,
CC ECO:0000269|PubMed:15159416, ECO:0000269|PubMed:15660133}.
CC -!- INTERACTION:
CC Q8WYL5; P23528: CFL1; NbExp=2; IntAct=EBI-1222387, EBI-352733;
CC Q8WYL5; Q9BR76: CORO1B; NbExp=3; IntAct=EBI-1222387, EBI-351152;
CC Q8WYL5; P53667: LIMK1; NbExp=6; IntAct=EBI-1222387, EBI-444403;
CC Q8WYL5; P31946: YWHAB; NbExp=3; IntAct=EBI-1222387, EBI-359815;
CC Q8WYL5; P27348: YWHAQ; NbExp=2; IntAct=EBI-1222387, EBI-359854;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection,
CC lamellipodium. Cleavage furrow. Midbody. Note=Also recruited to actin
CC rich membrane protrusions such as lamellipodia, which may allow local
CC control of actin dynamics at sites of cell locomotion. Also localized
CC to the cleavage furrow and the midbody during cytokinesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=L;
CC IsoId=Q8WYL5-1; Sequence=Displayed;
CC Name=2; Synonyms=S;
CC IsoId=Q8WYL5-2; Sequence=VSP_016318, VSP_016319;
CC Name=3; Synonyms=B;
CC IsoId=Q8WYL5-3; Sequence=VSP_016312, VSP_016314, VSP_016315,
CC VSP_016316;
CC Name=4;
CC IsoId=Q8WYL5-4; Sequence=VSP_016311, VSP_016317;
CC Name=5;
CC IsoId=Q8WYL5-5; Sequence=VSP_016313, VSP_016318, VSP_016319;
CC -!- PTM: Phosphorylated. Inhibitory phosphorylation by PAK4 promotes
CC binding to YWHAZ. Phosphorylation at Ser-978 is decreased by stimuli
CC which promote actin reorganization and lamellipodia formation. Can be
CC dephosphorylated and activated by PPP3CA/calcineurin A. Phosphorylation
CC decreases immediately prior to telophase. {ECO:0000269|PubMed:12807904,
CC ECO:0000269|PubMed:15159416, ECO:0000269|PubMed:15660133,
CC ECO:0000269|PubMed:15671020}.
CC -!- MISCELLANEOUS: Tyrosine phosphatase activity has not been demonstrated
CC for this protein to date.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Due to intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92536.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB072355; BAB84114.1; -; mRNA.
DR EMBL; AB072356; BAB84115.1; -; mRNA.
DR EMBL; AB072357; BAB84116.1; -; mRNA.
DR EMBL; AB037719; BAA92536.1; ALT_INIT; mRNA.
DR EMBL; AK095421; BAC04546.1; -; mRNA.
DR EMBL; BC062341; AAH62341.1; -; mRNA.
DR CCDS; CCDS53825.1; -. [Q8WYL5-5]
DR CCDS; CCDS55882.1; -. [Q8WYL5-2]
DR CCDS; CCDS9121.1; -. [Q8WYL5-1]
DR RefSeq; NP_001154802.1; NM_001161330.1. [Q8WYL5-2]
DR RefSeq; NP_001154803.1; NM_001161331.1. [Q8WYL5-5]
DR RefSeq; NP_061857.3; NM_018984.3. [Q8WYL5-1]
DR RefSeq; XP_016874982.1; XM_017019493.1. [Q8WYL5-4]
DR RefSeq; XP_016874983.1; XM_017019494.1. [Q8WYL5-4]
DR AlphaFoldDB; Q8WYL5; -.
DR SMR; Q8WYL5; -.
DR BioGRID; 119950; 73.
DR IntAct; Q8WYL5; 31.
DR MINT; Q8WYL5; -.
DR STRING; 9606.ENSP00000315713; -.
DR DEPOD; SSH1; -.
DR iPTMnet; Q8WYL5; -.
DR PhosphoSitePlus; Q8WYL5; -.
DR BioMuta; SSH1; -.
DR DMDM; 82582267; -.
DR EPD; Q8WYL5; -.
DR jPOST; Q8WYL5; -.
DR MassIVE; Q8WYL5; -.
DR MaxQB; Q8WYL5; -.
DR PaxDb; Q8WYL5; -.
DR PeptideAtlas; Q8WYL5; -.
DR PRIDE; Q8WYL5; -.
DR ProteomicsDB; 75168; -. [Q8WYL5-1]
DR ProteomicsDB; 75169; -. [Q8WYL5-2]
DR ProteomicsDB; 75170; -. [Q8WYL5-3]
DR ProteomicsDB; 75171; -. [Q8WYL5-4]
DR ProteomicsDB; 75172; -. [Q8WYL5-5]
DR Antibodypedia; 18311; 208 antibodies from 24 providers.
DR DNASU; 54434; -.
DR Ensembl; ENST00000326470.9; ENSP00000326107.5; ENSG00000084112.15. [Q8WYL5-5]
DR Ensembl; ENST00000326495.10; ENSP00000315713.5; ENSG00000084112.15. [Q8WYL5-1]
DR Ensembl; ENST00000551165.5; ENSP00000448824.1; ENSG00000084112.15. [Q8WYL5-2]
DR GeneID; 54434; -.
DR KEGG; hsa:54434; -.
DR MANE-Select; ENST00000326495.10; ENSP00000315713.5; NM_018984.4; NP_061857.3.
DR UCSC; uc001tnm.4; human. [Q8WYL5-1]
DR CTD; 54434; -.
DR DisGeNET; 54434; -.
DR GeneCards; SSH1; -.
DR HGNC; HGNC:30579; SSH1.
DR HPA; ENSG00000084112; Low tissue specificity.
DR MIM; 606778; gene.
DR neXtProt; NX_Q8WYL5; -.
DR OpenTargets; ENSG00000084112; -.
DR PharmGKB; PA134941788; -.
DR VEuPathDB; HostDB:ENSG00000084112; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000156133; -.
DR HOGENOM; CLU_006650_1_0_1; -.
DR InParanoid; Q8WYL5; -.
DR OMA; KPPYKSC; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q8WYL5; -.
DR TreeFam; TF319444; -.
DR PathwayCommons; Q8WYL5; -.
DR SignaLink; Q8WYL5; -.
DR SIGNOR; Q8WYL5; -.
DR BioGRID-ORCS; 54434; 15 hits in 1078 CRISPR screens.
DR ChiTaRS; SSH1; human.
DR GeneWiki; SSH1; -.
DR GenomeRNAi; 54434; -.
DR Pharos; Q8WYL5; Tbio.
DR PRO; PR:Q8WYL5; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8WYL5; protein.
DR Bgee; ENSG00000084112; Expressed in sural nerve and 205 other tissues.
DR ExpressionAtlas; Q8WYL5; baseline and differential.
DR Genevisible; Q8WYL5; HS.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0000902; P:cell morphogenesis; IMP:UniProtKB.
DR GO; GO:0071318; P:cellular response to ATP; IDA:MGI.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:UniProtKB.
DR GO; GO:0032268; P:regulation of cellular protein metabolic process; IDA:MGI.
DR CDD; cd11652; SSH-N; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR014876; DEK_C.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR043587; Phosphatase_SSH-like.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR043588; SSH-N.
DR InterPro; IPR027233; SSH1.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR45864; PTHR45864; 1.
DR PANTHER; PTHR45864:SF5; PTHR45864:SF5; 1.
DR Pfam; PF08766; DEK_C; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51998; DEK_C; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Cell projection;
KW Cytoplasm; Cytoskeleton; Hydrolase; Phosphoprotein; Protein phosphatase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..1049
FT /note="Protein phosphatase Slingshot homolog 1"
FT /id="PRO_0000094841"
FT DOMAIN 249..304
FT /note="DEK-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01342"
FT DOMAIN 308..449
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..1049
FT /note="Interaction with YWHAG"
FT /evidence="ECO:0000269|PubMed:15159416"
FT REGION 923..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 393
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q76I79"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 897
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 978
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15159416"
FT VAR_SEQ 1..312
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10718198"
FT /id="VSP_016311"
FT VAR_SEQ 1..73
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11832213"
FT /id="VSP_016312"
FT VAR_SEQ 1..37
FT /note="MALVTLQRSPTPSAASSSASNSELEAGSEEDRKLNLS -> MARARRAVVGS
FT VRDVSTAATNLFYFTDFCIFLQPTHCFCCPEVSSSNY (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016313"
FT VAR_SEQ 74..93
FT /note="LPQHLQVMINLLRCEDRIKL -> MGGRHHLQRQVSESMSALFQ (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:11832213"
FT /id="VSP_016314"
FT VAR_SEQ 135..157
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11832213"
FT /id="VSP_016315"
FT VAR_SEQ 245..1049
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11832213"
FT /id="VSP_016316"
FT VAR_SEQ 313..334
FT /note="FDHLYLGSEWNASNLEELQGSG -> MRCYLSWDRWTSPPLSSIIFIS (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:10718198"
FT /id="VSP_016317"
FT VAR_SEQ 632..692
FT /note="DDAIFGILNKVKPSYKSCADCMYPTASGAPEASRERCEDPNAPAICTQPAFL
FT PHITSSPVA -> VGRARPAGWHTPSLPSHSNWPTSASVVGTTGTRHHTQLIFFYCLLW
FT APSSHLQGPEGSFTG (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:11832213,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_016318"
FT VAR_SEQ 693..1049
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:11832213,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_016319"
FT MUTAGEN 393
FT /note="C->S: Abrogates phosphatase activity."
FT /evidence="ECO:0000269|PubMed:11832213,
FT ECO:0000269|PubMed:12684437, ECO:0000269|PubMed:12807904,
FT ECO:0000269|PubMed:15056216, ECO:0000269|PubMed:15159416,
FT ECO:0000269|PubMed:15660133, ECO:0000269|PubMed:15671020,
FT ECO:0000269|PubMed:16230460"
FT MUTAGEN 458
FT /note="W->A: Impairs stimulation of phosphatase activity by
FT actin but does not affect basal activity."
FT /evidence="ECO:0000269|PubMed:16230460"
FT MUTAGEN 937
FT /note="S->A: Reduces binding to YWHAB, YWHAG, YWHAQ and
FT YWHAZ. Abolishes binding to YWHAB, YWHAG, YWHAQ and YWHAZ
FT and increases association with F-actin; when associated
FT with A-978."
FT /evidence="ECO:0000269|PubMed:15159416"
FT MUTAGEN 978
FT /note="S->A: Reduces binding to YWHAB, YWHAG, YWHAQ and
FT YWHAZ. Abolishes binding to YWHAB, YWHAG, YWHAQ and YWHAZ
FT and increases association with F-actin; when associated
FT with A-937."
FT /evidence="ECO:0000269|PubMed:15159416"
FT CONFLICT 2
FT /note="A -> V (in Ref. 4; AAH62341)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="L -> P (in Ref. 1; BAB84116)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1049 AA; 115511 MW; 0600B9690F0E6F9C CRC64;
MALVTLQRSP TPSAASSSAS NSELEAGSEE DRKLNLSLSE SFFMVKGAAL FLQQGSSPQG
QRSLQHPHKH AGDLPQHLQV MINLLRCEDR IKLAVRLESA WADRVRYMVV VYSSGRQDTE
ENILLGVDFS SKESKSCTIG MVLRLWSDTK IHLDGDGGFS VSTAGRMHIF KPVSVQAMWS
ALQVLHKACE VARRHNYFPG GVALIWATYY ESCISSEQSC INEWNAMQDL ESTRPDSPAL
FVDKPTEGER TERLIKAKLR SIMMSQDLEN VTSKEIRNEL EKQMNCNLKE LKEFIDNEML
LILGQMDKPS LIFDHLYLGS EWNASNLEEL QGSGVDYILN VTREIDNFFP GLFAYHNIRV
YDEETTDLLA HWNEAYHFIN KAKRNHSKCL VHCKMGVSRS ASTVIAYAMK EFGWPLEKAY
NYVKQKRSIT RPNAGFMRQL SEYEGILDAS KQRHNKLWRQ QTDSSLQQPV DDPAGPGDFL
PETPDGTPES QLPFLDDAAQ PGLGPPLPCC FRRLSDPLLP SPEDETGSLV HLEDPEREAL
LEEAAPPAEV HRPARQPQQG SGLCEKDVKK KLEFGSPKGR SGSLLQVEET EREEGLGAGR
WGQLPTQLDQ NLLNSENLNN NSKRSCPNGM EDDAIFGILN KVKPSYKSCA DCMYPTASGA
PEASRERCED PNAPAICTQP AFLPHITSSP VAHLASRSRV PEKPASGPTE PPPFLPPAGS
RRADTSGPGA GAALEPPASL LEPSRETPKV LPKSLLLKNS HCDKNPPSTE VVIKEESSPK
KDMKPAKDLR LLFSNESEKP TTNSYLMQHQ ESIIQLQKAG LVRKHTKELE RLKSVPADPA
PPSRDGPASR LEASIPEESQ DPAALHELGP LVMPSQAGSD EKSEAAPASL EGGSLKSPPP
FFYRLDHTSS FSKDFLKTIC YTPTSSSMSS NLTRSSSSDS IHSVRGKPGL VKQRTQEIET
RLRLAGLTVS SPLKRSHSLA KLGSLTFSTE DLSSEADPST VADSQDTTLS ESSFLHEPQG
TPRDPAATSK PSGKPAPENL KSPSWMSKS
