Q8WYL5 (SSH1_HUMAN) 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=hSSH-1L

Gene names

Name:	SSH1
Synonyms:	KIAA1298, SSH1L

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1049 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 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. A phosphoprotein + H2O = a protein + phosphate.
Subunit structure	Interacts with actin and this stimulates phosphatase activity. Also interacts with LIMK1 and 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. Ref.1 Ref.5 Ref.10 Ref.11
Subcellular location	Cytoplasm › cytoskeleton. Cell projection › lamellipodium. Cleavage furrow. Midbody. Note: Also recruited to actin rich membrane protrusions such as lamellipodia, which may allow local control of actin dynamics at sites of cell locomotion. Also localized to the cleavage furrow and the midbody during cytokinesis. Ref.6 Ref.8 Ref.9 Ref.10 Ref.13
Post-translational modification	Phosphorylated. Inhibitory phosphorylation by PAK4 promotes binding to YWHAZ. Phosphorylation at Ser-978 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. Ref.6 Ref.10 Ref.11 Ref.12
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 BAA92536.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cell projection 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 mutant phenotype Ref.1. Source: UniProtKB cell morphogenesis Inferred from mutant phenotype Ref.9. Source: UniProtKB cellular response to ATP Inferred from direct assay 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 direct assay 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 direct assay Ref.9. Source: UniProtKB cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell lamellipodium Inferred from electronic annotation. Source: UniProtKB-SubCell midbody Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay Ref.9. Source: UniProtKB
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro actin binding Inferred from direct assay Ref.1. Source: UniProtKB 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CORO1B	Q9BR76	3	EBI-1222387,EBI-351152

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8WYL5-1)

Also known as: L;

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: Q8WYL5-2)

Also known as: S;

The sequence of this isoform differs from the canonical sequence as follows:
     632-692: DDAIFGILNK...LPHITSSPVA → VGRARPAGWH...LQGPEGSFTG
     693-1049: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Isoform 3 (identifier: Q8WYL5-3)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: Missing.
     74-93: LPQHLQVMINLLRCEDRIKL → MGGRHHLQRQVSESMSALFQ
     135-157: Missing.
     245-1049: Missing.

Note: Due to intron retention. No experimental confirmation available.

Isoform 4 (identifier: Q8WYL5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-312: Missing.
     313-334: FDHLYLGSEWNASNLEELQGSG → MRCYLSWDRWTSPPLSSIIFIS

Isoform 5 (identifier: Q8WYL5-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: MALVTLQRSP...SEEDRKLNLS → MARARRAVVG...CCPEVSSSNY
     632-692: DDAIFGILNK...LPHITSSPVA → VGRARPAGWH...LQGPEGSFTG
     693-1049: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1049	1049	Protein phosphatase Slingshot homolog 1		PRO_0000094841
Regions
	Domain	308 – 448	141	Tyrosine-protein phosphatase
	Region	897 – 1049	153	Interaction with YWHAG
Sites
	Active site	393	1	Phosphocysteine intermediate Probable
Amino acid modifications
	Modified residue	37	1	Phosphoserine Ref.15
	Modified residue	57	1	Phosphoserine Ref.15
	Modified residue	978	1	Phosphoserine Ref.10
Natural variations
	Alternative sequence	1 – 312	312	Missing in isoform 4.		VSP_016311
	Alternative sequence	1 – 73	73	Missing in isoform 3.		VSP_016312
	Alternative sequence	1 – 37	37	MALVT…KLNLS → MARARRAVVGSVRDVSTAAT NLFYFTDFCIFLQPTHCFCC PEVSSSNY in isoform 5.		VSP_016313
	Alternative sequence	74 – 93	20	LPQHL…DRIKL → MGGRHHLQRQVSESMSALFQ in isoform 3.		VSP_016314
	Alternative sequence	135 – 157	23	Missing in isoform 3.		VSP_016315
	Alternative sequence	245 – 1049	805	Missing in isoform 3.		VSP_016316
	Alternative sequence	313 – 334	22	FDHLY…LQGSG → MRCYLSWDRWTSPPLSSIIF IS in isoform 4.		VSP_016317
	Alternative sequence	632 – 692	61	DDAIF…SSPVA → VGRARPAGWHTPSLPSHSNW PTSASVVGTTGTRHHTQLIF FYCLLWAPSSHLQGPEGSFT G in isoform 2 and isoform 5.		VSP_016318
	Alternative sequence	693 – 1049	357	Missing in isoform 2 and isoform 5.		VSP_016319
Experimental info
	Mutagenesis	393	1	C → S: Abrogates phosphatase activity. Ref.1 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13
	Mutagenesis	458	1	W → A: Impairs stimulation of phosphatase activity by actin but does not affect basal activity. Ref.13
	Mutagenesis	937	1	S → A: Reduces binding to YWHAB, YWHAG, YWHAQ and YWHAZ. Abolishes binding to YWHAB, YWHAG, YWHAQ and YWHAZ and increases association with F-actin; when associated with A-978. Ref.10
	Mutagenesis	978	1	S → A: Reduces binding to YWHAB, YWHAG, YWHAQ and YWHAZ. Abolishes binding to YWHAB, YWHAG, YWHAQ and YWHAZ and increases association with F-actin; when associated with A-937. Ref.10
	Sequence conflict	2	1	A → V in AAH62341. Ref.4
	Sequence conflict	230	1	L → P in BAB84116. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (L) [UniParc]. Last modified November 22, 2005. Version 2. Checksum: 0600B9690F0E6F9C	FASTA	1,049	115,511
	10 20 30 40 50 60 MALVTLQRSP TPSAASSSAS NSELEAGSEE DRKLNLSLSE SFFMVKGAAL FLQQGSSPQG 70 80 90 100 110 120 QRSLQHPHKH AGDLPQHLQV MINLLRCEDR IKLAVRLESA WADRVRYMVV VYSSGRQDTE 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 LKEFIDNEML 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 QTDSSLQQPV DDPAGPGDFL 490 500 510 520 530 540 PETPDGTPES QLPFLDDAAQ PGLGPPLPCC FRRLSDPLLP SPEDETGSLV HLEDPEREAL 550 560 570 580 590 600 LEEAAPPAEV HRPARQPQQG SGLCEKDVKK KLEFGSPKGR SGSLLQVEET EREEGLGAGR 610 620 630 640 650 660 WGQLPTQLDQ NLLNSENLNN NSKRSCPNGM EDDAIFGILN KVKPSYKSCA DCMYPTASGA 670 680 690 700 710 720 PEASRERCED PNAPAICTQP AFLPHITSSP VAHLASRSRV PEKPASGPTE PPPFLPPAGS 730 740 750 760 770 780 RRADTSGPGA GAALEPPASL LEPSRETPKV LPKSLLLKNS HCDKNPPSTE VVIKEESSPK 790 800 810 820 830 840 KDMKPAKDLR LLFSNESEKP TTNSYLMQHQ ESIIQLQKAG LVRKHTKELE RLKSVPADPA 850 860 870 880 890 900 PPSRDGPASR LEASIPEESQ DPAALHELGP LVMPSQAGSD EKSEAAPASL EGGSLKSPPP 910 920 930 940 950 960 FFYRLDHTSS FSKDFLKTIC YTPTSSSMSS NLTRSSSSDS IHSVRGKPGL VKQRTQEIET 970 980 990 1000 1010 1020 RLRLAGLTVS SPLKRSHSLA KLGSLTFSTE DLSSEADPST VADSQDTTLS ESSFLHEPQG 1030 1040 TPRDPAATSK PSGKPAPENL KSPSWMSKS
	Isoform 2 (S) [UniParc]. Checksum: 9DC1FF2FC8984384	FASTA	692	77,430
	10 20 30 40 50 60 MALVTLQRSP TPSAASSSAS NSELEAGSEE DRKLNLSLSE SFFMVKGAAL FLQQGSSPQG 70 80 90 100 110 120 QRSLQHPHKH AGDLPQHLQV MINLLRCEDR IKLAVRLESA WADRVRYMVV VYSSGRQDTE 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 LKEFIDNEML 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 QTDSSLQQPV DDPAGPGDFL 490 500 510 520 530 540 PETPDGTPES QLPFLDDAAQ PGLGPPLPCC FRRLSDPLLP SPEDETGSLV HLEDPEREAL 550 560 570 580 590 600 LEEAAPPAEV HRPARQPQQG SGLCEKDVKK KLEFGSPKGR SGSLLQVEET EREEGLGAGR 610 620 630 640 650 660 WGQLPTQLDQ NLLNSENLNN NSKRSCPNGM EVGRARPAGW HTPSLPSHSN WPTSASVVGT 670 680 690 TGTRHHTQLI FFYCLLWAPS SHLQGPEGSF TG
	Isoform 3 (B) [UniParc]. Checksum: 3EF171D933E3424D	FASTA	148	16,695
	10 20 30 40 50 60 MGGRHHLQRQ VSESMSALFQ AVRLESAWAD RVRYMVVVYS SGRQDTEENI LLGVDFSSKE 70 80 90 100 110 120 SGFSVSTAGR MHIFKPVSVQ AMWSALQVLH KACEVARRHN YFPGGVALIW ATYYESCISS 130 140 EQSCINEWNA MQDLESTRPD SPALFVDK
	Isoform 4 [UniParc]. Checksum: E3825E2328B088D2	FASTA	737	80,684
	10 20 30 40 50 60 MRCYLSWDRW TSPPLSSIIF ISVDYILNVT REIDNFFPGL FAYHNIRVYD EETTDLLAHW 70 80 90 100 110 120 NEAYHFINKA KRNHSKCLVH CKMGVSRSAS TVIAYAMKEF GWPLEKAYNY VKQKRSITRP 130 140 150 160 170 180 NAGFMRQLSE YEGILDASKQ RHNKLWRQQT DSSLQQPVDD PAGPGDFLPE TPDGTPESQL 190 200 210 220 230 240 PFLDDAAQPG LGPPLPCCFR RLSDPLLPSP EDETGSLVHL EDPEREALLE EAAPPAEVHR 250 260 270 280 290 300 PARQPQQGSG LCEKDVKKKL EFGSPKGRSG SLLQVEETER EEGLGAGRWG QLPTQLDQNL 310 320 330 340 350 360 LNSENLNNNS KRSCPNGMED DAIFGILNKV KPSYKSCADC MYPTASGAPE ASRERCEDPN 370 380 390 400 410 420 APAICTQPAF LPHITSSPVA HLASRSRVPE KPASGPTEPP PFLPPAGSRR ADTSGPGAGA 430 440 450 460 470 480 ALEPPASLLE PSRETPKVLP KSLLLKNSHC DKNPPSTEVV IKEESSPKKD MKPAKDLRLL 490 500 510 520 530 540 FSNESEKPTT NSYLMQHQES IIQLQKAGLV RKHTKELERL KSVPADPAPP SRDGPASRLE 550 560 570 580 590 600 ASIPEESQDP AALHELGPLV MPSQAGSDEK SEAAPASLEG GSLKSPPPFF YRLDHTSSFS 610 620 630 640 650 660 KDFLKTICYT PTSSSMSSNL TRSSSSDSIH SVRGKPGLVK QRTQEIETRL RLAGLTVSSP 670 680 690 700 710 720 LKRSHSLAKL GSLTFSTEDL SSEADPSTVA DSQDTTLSES SFLHEPQGTP RDPAATSKPS 730 GKPAPENLKS PSWMSKS
	Isoform 5 [UniParc]. Checksum: 3ACFAB4B97CBDF7A	FASTA	703	78,978
	10 20 30 40 50 60 MARARRAVVG SVRDVSTAAT NLFYFTDFCI FLQPTHCFCC PEVSSSNYLS ESFFMVKGAA 70 80 90 100 110 120 LFLQQGSSPQ GQRSLQHPHK HAGDLPQHLQ VMINLLRCED RIKLAVRLES AWADRVRYMV 130 140 150 160 170 180 VVYSSGRQDT EENILLGVDF SSKESKSCTI GMVLRLWSDT KIHLDGDGGF SVSTAGRMHI 190 200 210 220 230 240 FKPVSVQAMW SALQVLHKAC EVARRHNYFP GGVALIWATY YESCISSEQS CINEWNAMQD 250 260 270 280 290 300 LESTRPDSPA LFVDKPTEGE RTERLIKAKL RSIMMSQDLE NVTSKEIRNE LEKQMNCNLK 310 320 330 340 350 360 ELKEFIDNEM LLILGQMDKP SLIFDHLYLG SEWNASNLEE LQGSGVDYIL NVTREIDNFF 370 380 390 400 410 420 PGLFAYHNIR VYDEETTDLL AHWNEAYHFI NKAKRNHSKC LVHCKMGVSR SASTVIAYAM 430 440 450 460 470 480 KEFGWPLEKA YNYVKQKRSI TRPNAGFMRQ LSEYEGILDA SKQRHNKLWR QQTDSSLQQP 490 500 510 520 530 540 VDDPAGPGDF LPETPDGTPE SQLPFLDDAA QPGLGPPLPC CFRRLSDPLL PSPEDETGSL 550 560 570 580 590 600 VHLEDPEREA LLEEAAPPAE VHRPARQPQQ GSGLCEKDVK KKLEFGSPKG RSGSLLQVEE 610 620 630 640 650 660 TEREEGLGAG RWGQLPTQLD QNLLNSENLN NNSKRSCPNG MEVGRARPAG WHTPSLPSHS 670 680 690 700 NWPTSASVVG TTGTRHHTQL IFFYCLLWAP SSHLQGPEGS FTG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin." Niwa R., Nagata-Ohashi K., Takeichi M., Mizuno K., Uemura T. Cell 108:233-246(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, INTERACTION WITH ACTIN, MUTAGENESIS OF CYS-393.
[2]	"Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O. DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Brain.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
[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: Eye.
[5]	"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: FUNCTION, INTERACTION WITH ACTIN.
[6]	"Cell cycle-associated changes in Slingshot phosphatase activity and roles in cytokinesis in animal cells." Kaji N., Ohashi K., Shuin M., Niwa R., Uemura T., Mizuno K. J. Biol. Chem. 278:33450-33455(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, MUTAGENESIS OF CYS-393.
[7]	"Control of growth cone motility and morphology by LIM kinase and Slingshot via phosphorylation and dephosphorylation of cofilin." Endo M., Ohashi K., Sasaki Y., Goshima Y., Niwa R., Uemura T., Mizuno K. J. Neurosci. 23:2527-2537(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF CYS-393.
[8]	"Efficient Salmonella entry requires activity cycles of host ADF and cofilin." Dai S., Sarmiere P.D., Wiggan O., Bamburg J.R., Zhou D. Cell. Microbiol. 6:459-471(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-393.
[9]	"Phosphoinositide 3-kinase-mediated activation of cofilin phosphatase Slingshot and its role for insulin-induced membrane protrusion." Nishita M., Wang Y., Tomizawa C., Suzuki A., Niwa R., Uemura T., Mizuno K. J. Biol. Chem. 279:7193-7198(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]	"A pathway of neuregulin-induced activation of cofilin-phosphatase Slingshot and cofilin in lamellipodia." Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M., Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K. J. Cell Biol. 165:465-471(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH YWHAB; YWHAG; YWHAQ AND YWHAZ, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-978, MUTAGENESIS OF CYS-393; SER-937 AND SER-978.
[11]	"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: FUNCTION, INTERACTION WITH ACTIN; LIMK1 AND YWHAZ, PHOSPHORYLATION, MUTAGENESIS OF CYS-393.
[12]	"Calcium signal-induced cofilin dephosphorylation is mediated by Slingshot via calcineurin." Wang Y., Shibasaki F., Mizuno K. J. Biol. Chem. 280:12683-12689(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION, DEPHOSPHORYLATION BY PPP3CA, MUTAGENESIS OF CYS-393.
[13]	"Spatial and temporal regulation of cofilin activity by LIM kinase and Slingshot is critical for directional cell migration." Nishita M., Tomizawa C., Yamamoto M., Horita Y., Ohashi K., Mizuno K. J. Cell Biol. 171:349-359(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-393 AND TRP-458.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[15]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37 AND SER-57, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB072355 mRNA. Translation: BAB84114.1. AB072356 mRNA. Translation: BAB84115.1. AB072357 mRNA. Translation: BAB84116.1. AB037719 mRNA. Translation: BAA92536.1. Different initiation. AK095421 mRNA. Translation: BAC04546.1. BC062341 mRNA. Translation: AAH62341.1.
IPI	IPI00103741. IPI00103742. IPI00167670. IPI00383250. IPI00478191.
RefSeq	NP_001154802.1. NM_001161330.1. NP_001154803.1. NM_001161331.1. NP_061857.3. NM_018984.3.
UniGene	Hs.199763.
3D structure databases
ProteinModelPortal	Q8WYL5.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8WYL5. 5 interactions.
MINT	MINT-1788740.
STRING	9606.ENSP00000315713.
PTM databases
PhosphoSite	Q8WYL5.
Polymorphism databases
DMDM	82582267.
Proteomic databases
PaxDb	Q8WYL5.
PRIDE	Q8WYL5.
Protocols and materials databases
DNASU	54434.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000326470; ENSP00000326107; ENSG00000084112. ENST00000326495; ENSP00000315713; ENSG00000084112. ENST00000360239; ENSP00000353374; ENSG00000084112. ENST00000551165; ENSP00000448824; ENSG00000084112.
GeneID	54434.
KEGG	hsa:54434.
UCSC	uc001tnl.3. human. uc001tnm.3. human. uc001tnn.4. human. uc001tno.1. human. uc010sxg.2. human.
Organism-specific databases
CTD	54434.
GeneCards	GC12M109180.
HGNC	HGNC:30579. SSH1.
HPA	HPA019845.
MIM	606778. gene.
neXtProt	NX_Q8WYL5.
PharmGKB	PA134941788.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2453.
HOGENOM	HOG000154427.
HOVERGEN	HBG094001.
InParanoid	Q8WYL5.
KO	K05766.
OMA	NSHCDKN.
OrthoDB	EOG480HVX.
PhylomeDB	Q8WYL5.
Enzyme and pathway databases
Pathway_Interaction_DB	fgf_pathway. FGF signaling pathway.
Gene expression databases
ArrayExpress	Q8WYL5.
Bgee	Q8WYL5.
CleanEx	HS_SSH1.
Genevestigator	Q8WYL5.
GermOnline	ENSG00000084112. Homo sapiens.
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
GenomeRNAi	54434.
NextBio	56643.
SOURCE	Search...

Entry information

Entry name

SSH1_HUMAN

Accession

Primary (citable) accession number: Q8WYL5
Secondary accession number(s): Q6P6C0 , Q8N9A7, Q8WYL3, Q8WYL4, Q9P2P8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	November 22, 2005
Last modified:	May 1, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.