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Protein

Protein phosphatase Slingshot homolog 1

Gene

SSH1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.10 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei393 – 3931Phosphocysteine intermediateCurated

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • DNA binding Source: InterPro
  • phosphoprotein phosphatase activity Source: UniProtKB
  • protein tyrosine/serine/threonine phosphatase activity Source: GO_Central
  • protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  • actin cytoskeleton organization Source: UniProtKB
  • cell morphogenesis Source: UniProtKB
  • cellular response to ATP Source: MGI
  • protein dephosphorylation Source: UniProtKB
  • regulation of actin polymerization or depolymerization Source: GO_Central
  • regulation of axonogenesis Source: GO_Central
  • regulation of cellular protein metabolic process Source: MGI
  • regulation of lamellipodium assembly Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:SSH1
Synonyms:KIAA1298, SSH1L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:30579. SSH1.

Subcellular locationi

GO - Cellular componenti

  • cleavage furrow Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • cytoskeleton Source: UniProtKB-SubCell
  • lamellipodium Source: UniProtKB-SubCell
  • midbody Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi393 – 3931C → S: Abrogates phosphatase activity. 8 Publications
Mutagenesisi458 – 4581W → A: Impairs stimulation of phosphatase activity by actin but does not affect basal activity. 1 Publication
Mutagenesisi937 – 9371S → 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. 1 Publication
Mutagenesisi978 – 9781S → 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. 1 Publication

Organism-specific databases

PharmGKBiPA134941788.

Polymorphism and mutation databases

BioMutaiSSH1.
DMDMi82582267.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 10491048Protein phosphatase Slingshot homolog 1PRO_0000094841Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei37 – 371Phosphoserine1 Publication
Modified residuei57 – 571Phosphoserine1 Publication
Modified residuei978 – 9781Phosphoserine1 Publication

Post-translational modificationi

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.4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8WYL5.
PaxDbiQ8WYL5.
PRIDEiQ8WYL5.

PTM databases

DEPODiQ8WYL5.
PhosphoSiteiQ8WYL5.

Expressioni

Gene expression databases

BgeeiQ8WYL5.
CleanExiHS_SSH1.
ExpressionAtlasiQ8WYL5. baseline and differential.
GenevisibleiQ8WYL5. HS.

Organism-specific databases

HPAiHPA019845.

Interactioni

Subunit structurei

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.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CFL1P235282EBI-1222387,EBI-352733
CORO1BQ9BR763EBI-1222387,EBI-351152
LIMK1P536677EBI-1222387,EBI-444403
YWHABP319463EBI-1222387,EBI-359815
YWHAQP273482EBI-1222387,EBI-359854

Protein-protein interaction databases

BioGridi119950. 5 interactions.
IntActiQ8WYL5. 12 interactions.
MINTiMINT-1788740.
STRINGi9606.ENSP00000315713.

Structurei

3D structure databases

ProteinModelPortaliQ8WYL5.
SMRiQ8WYL5. Positions 309-449.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini308 – 448141Tyrosine-protein phosphataseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni897 – 1049153Interaction with YWHAGAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000154427.
HOVERGENiHBG094001.
InParanoidiQ8WYL5.
KOiK05766.
OMAiTTNSYLM.
OrthoDBiEOG7B8S33.
PhylomeDBiQ8WYL5.
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.
IPR027233. SSH1.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PTHR10159:SF138. PTHR10159:SF138. 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 (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8WYL5-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MALVTLQRSP TPSAASSSAS NSELEAGSEE DRKLNLSLSE SFFMVKGAAL
60 70 80 90 100
FLQQGSSPQG QRSLQHPHKH AGDLPQHLQV MINLLRCEDR IKLAVRLESA
110 120 130 140 150
WADRVRYMVV VYSSGRQDTE ENILLGVDFS SKESKSCTIG MVLRLWSDTK
160 170 180 190 200
IHLDGDGGFS VSTAGRMHIF KPVSVQAMWS ALQVLHKACE VARRHNYFPG
210 220 230 240 250
GVALIWATYY ESCISSEQSC INEWNAMQDL ESTRPDSPAL FVDKPTEGER
260 270 280 290 300
TERLIKAKLR SIMMSQDLEN VTSKEIRNEL EKQMNCNLKE LKEFIDNEML
310 320 330 340 350
LILGQMDKPS LIFDHLYLGS EWNASNLEEL QGSGVDYILN VTREIDNFFP
360 370 380 390 400
GLFAYHNIRV YDEETTDLLA HWNEAYHFIN KAKRNHSKCL VHCKMGVSRS
410 420 430 440 450
ASTVIAYAMK EFGWPLEKAY NYVKQKRSIT RPNAGFMRQL SEYEGILDAS
460 470 480 490 500
KQRHNKLWRQ QTDSSLQQPV DDPAGPGDFL PETPDGTPES QLPFLDDAAQ
510 520 530 540 550
PGLGPPLPCC FRRLSDPLLP SPEDETGSLV HLEDPEREAL LEEAAPPAEV
560 570 580 590 600
HRPARQPQQG SGLCEKDVKK KLEFGSPKGR SGSLLQVEET EREEGLGAGR
610 620 630 640 650
WGQLPTQLDQ NLLNSENLNN NSKRSCPNGM EDDAIFGILN KVKPSYKSCA
660 670 680 690 700
DCMYPTASGA PEASRERCED PNAPAICTQP AFLPHITSSP VAHLASRSRV
710 720 730 740 750
PEKPASGPTE PPPFLPPAGS RRADTSGPGA GAALEPPASL LEPSRETPKV
760 770 780 790 800
LPKSLLLKNS HCDKNPPSTE VVIKEESSPK KDMKPAKDLR LLFSNESEKP
810 820 830 840 850
TTNSYLMQHQ ESIIQLQKAG LVRKHTKELE RLKSVPADPA PPSRDGPASR
860 870 880 890 900
LEASIPEESQ DPAALHELGP LVMPSQAGSD EKSEAAPASL EGGSLKSPPP
910 920 930 940 950
FFYRLDHTSS FSKDFLKTIC YTPTSSSMSS NLTRSSSSDS IHSVRGKPGL
960 970 980 990 1000
VKQRTQEIET RLRLAGLTVS SPLKRSHSLA KLGSLTFSTE DLSSEADPST
1010 1020 1030 1040
VADSQDTTLS ESSFLHEPQG TPRDPAATSK PSGKPAPENL KSPSWMSKS
Length:1,049
Mass (Da):115,511
Last modified:November 22, 2005 - v2
Checksum:i0600B9690F0E6F9C
GO
Isoform 2 (identifier: Q8WYL5-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:692
Mass (Da):77,430
Checksum:i9DC1FF2FC8984384
GO
Isoform 3 (identifier: Q8WYL5-3) [UniParc]FASTAAdd to basket

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.
Show »
Length:148
Mass (Da):16,695
Checksum:i3EF171D933E3424D
GO
Isoform 4 (identifier: Q8WYL5-4) [UniParc]FASTAAdd to basket

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

Show »
Length:737
Mass (Da):80,684
Checksum:iE3825E2328B088D2
GO
Isoform 5 (identifier: Q8WYL5-5) [UniParc]FASTAAdd to basket

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.
Show »
Length:703
Mass (Da):78,978
Checksum:i3ACFAB4B97CBDF7A
GO

Sequence cautioni

The sequence BAA92536.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → V in AAH62341 (PubMed:15489334).Curated
Sequence conflicti230 – 2301L → P in BAB84116 (PubMed:11832213).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 312312Missing in isoform 4. 1 PublicationVSP_016311Add
BLAST
Alternative sequencei1 – 7373Missing in isoform 3. 1 PublicationVSP_016312Add
BLAST
Alternative sequencei1 – 3737MALVT…KLNLS → MARARRAVVGSVRDVSTAAT NLFYFTDFCIFLQPTHCFCC PEVSSSNY in isoform 5. 1 PublicationVSP_016313Add
BLAST
Alternative sequencei74 – 9320LPQHL…DRIKL → MGGRHHLQRQVSESMSALFQ in isoform 3. 1 PublicationVSP_016314Add
BLAST
Alternative sequencei135 – 15723Missing in isoform 3. 1 PublicationVSP_016315Add
BLAST
Alternative sequencei245 – 1049805Missing in isoform 3. 1 PublicationVSP_016316Add
BLAST
Alternative sequencei313 – 33422FDHLY…LQGSG → MRCYLSWDRWTSPPLSSIIF IS in isoform 4. 1 PublicationVSP_016317Add
BLAST
Alternative sequencei632 – 69261DDAIF…SSPVA → VGRARPAGWHTPSLPSHSNW PTSASVVGTTGTRHHTQLIF FYCLLWAPSSHLQGPEGSFT G in isoform 2 and isoform 5. 2 PublicationsVSP_016318Add
BLAST
Alternative sequencei693 – 1049357Missing in isoform 2 and isoform 5. 2 PublicationsVSP_016319Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS53825.1. [Q8WYL5-5]
CCDS55882.1. [Q8WYL5-2]
CCDS9121.1. [Q8WYL5-1]
RefSeqiNP_001154802.1. NM_001161330.1. [Q8WYL5-2]
NP_001154803.1. NM_001161331.1. [Q8WYL5-5]
NP_061857.3. NM_018984.3. [Q8WYL5-1]
XP_005269043.1. XM_005268986.2. [Q8WYL5-4]
UniGeneiHs.199763.

Genome annotation databases

EnsembliENST00000326470; ENSP00000326107; ENSG00000084112. [Q8WYL5-5]
ENST00000326495; ENSP00000315713; ENSG00000084112. [Q8WYL5-1]
ENST00000551165; ENSP00000448824; ENSG00000084112. [Q8WYL5-2]
GeneIDi54434.
KEGGihsa:54434.
UCSCiuc001tnl.3. human. [Q8WYL5-4]
uc001tnm.3. human. [Q8WYL5-1]
uc001tnn.4. human. [Q8WYL5-2]
uc001tno.1. human. [Q8WYL5-3]
uc010sxg.2. human. [Q8WYL5-5]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS53825.1. [Q8WYL5-5]
CCDS55882.1. [Q8WYL5-2]
CCDS9121.1. [Q8WYL5-1]
RefSeqiNP_001154802.1. NM_001161330.1. [Q8WYL5-2]
NP_001154803.1. NM_001161331.1. [Q8WYL5-5]
NP_061857.3. NM_018984.3. [Q8WYL5-1]
XP_005269043.1. XM_005268986.2. [Q8WYL5-4]
UniGeneiHs.199763.

3D structure databases

ProteinModelPortaliQ8WYL5.
SMRiQ8WYL5. Positions 309-449.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119950. 5 interactions.
IntActiQ8WYL5. 12 interactions.
MINTiMINT-1788740.
STRINGi9606.ENSP00000315713.

PTM databases

DEPODiQ8WYL5.
PhosphoSiteiQ8WYL5.

Polymorphism and mutation databases

BioMutaiSSH1.
DMDMi82582267.

Proteomic databases

MaxQBiQ8WYL5.
PaxDbiQ8WYL5.
PRIDEiQ8WYL5.

Protocols and materials databases

DNASUi54434.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000326470; ENSP00000326107; ENSG00000084112. [Q8WYL5-5]
ENST00000326495; ENSP00000315713; ENSG00000084112. [Q8WYL5-1]
ENST00000551165; ENSP00000448824; ENSG00000084112. [Q8WYL5-2]
GeneIDi54434.
KEGGihsa:54434.
UCSCiuc001tnl.3. human. [Q8WYL5-4]
uc001tnm.3. human. [Q8WYL5-1]
uc001tnn.4. human. [Q8WYL5-2]
uc001tno.1. human. [Q8WYL5-3]
uc010sxg.2. human. [Q8WYL5-5]

Organism-specific databases

CTDi54434.
GeneCardsiGC12M109180.
HGNCiHGNC:30579. SSH1.
HPAiHPA019845.
MIMi606778. gene.
neXtProtiNX_Q8WYL5.
PharmGKBiPA134941788.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000154427.
HOVERGENiHBG094001.
InParanoidiQ8WYL5.
KOiK05766.
OMAiTTNSYLM.
OrthoDBiEOG7B8S33.
PhylomeDBiQ8WYL5.
TreeFamiTF319444.

Miscellaneous databases

ChiTaRSiSSH1. human.
GeneWikiiSSH1.
GenomeRNAii54434.
NextBioi56643.
PROiQ8WYL5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8WYL5.
CleanExiHS_SSH1.
ExpressionAtlasiQ8WYL5. baseline and differential.
GenevisibleiQ8WYL5. HS.

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.
IPR027233. SSH1.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PTHR10159:SF138. PTHR10159:SF138. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSSH1_HUMAN
AccessioniPrimary (citable) accession number: Q8WYL5
Secondary accession number(s): Q6P6C0
, Q8N9A7, Q8WYL3, Q8WYL4, Q9P2P8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: June 24, 2015
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Miscellaneous

Tyrosine phosphatase activity has not been demonstrated for this protein to date.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.