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Q8WYL5

- SSH1_HUMAN

UniProt

Q8WYL5 - SSH1_HUMAN

Protein

Protein phosphatase Slingshot homolog 1

Gene

SSH1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (22 Nov 2005)
      Previous versions | rss
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    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

    1. actin binding Source: UniProtKB
    2. DNA binding Source: InterPro
    3. phosphoprotein phosphatase activity Source: UniProtKB
    4. protein binding Source: IntAct
    5. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
    6. protein tyrosine phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. actin cytoskeleton organization Source: UniProtKB
    2. cell morphogenesis Source: UniProtKB
    3. cellular response to ATP Source: MGI
    4. protein dephosphorylation Source: UniProtKB
    5. regulation of actin polymerization or depolymerization Source: RefGenome
    6. regulation of axonogenesis Source: RefGenome
    7. regulation of cellular protein metabolic process Source: MGI
    8. regulation of lamellipodium assembly Source: RefGenome

    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: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:30579. SSH1.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cell projectionlamellipodium. 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.

    GO - Cellular componenti

    1. cleavage furrow Source: UniProtKB-SubCell
    2. cytoplasm Source: UniProtKB
    3. cytoskeleton Source: UniProtKB-SubCell
    4. lamellipodium Source: UniProtKB-SubCell
    5. midbody Source: UniProtKB-SubCell
    6. nucleus Source: HPA
    7. plasma membrane Source: UniProtKB

    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.

    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.5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8WYL5.
    PaxDbiQ8WYL5.
    PRIDEiQ8WYL5.

    PTM databases

    PhosphoSiteiQ8WYL5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8WYL5.
    BgeeiQ8WYL5.
    CleanExiHS_SSH1.
    GenevestigatoriQ8WYL5.

    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. 6 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.
    HOGENOMiHOG000154427.
    HOVERGENiHBG094001.
    InParanoidiQ8WYL5.
    KOiK05766.
    OMAiNSHCDKN.
    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. Align

    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

    MALVTLQRSP TPSAASSSAS NSELEAGSEE DRKLNLSLSE SFFMVKGAAL     50
    FLQQGSSPQG QRSLQHPHKH AGDLPQHLQV MINLLRCEDR IKLAVRLESA 100
    WADRVRYMVV VYSSGRQDTE ENILLGVDFS SKESKSCTIG MVLRLWSDTK 150
    IHLDGDGGFS VSTAGRMHIF KPVSVQAMWS ALQVLHKACE VARRHNYFPG 200
    GVALIWATYY ESCISSEQSC INEWNAMQDL ESTRPDSPAL FVDKPTEGER 250
    TERLIKAKLR SIMMSQDLEN VTSKEIRNEL EKQMNCNLKE LKEFIDNEML 300
    LILGQMDKPS LIFDHLYLGS EWNASNLEEL QGSGVDYILN VTREIDNFFP 350
    GLFAYHNIRV YDEETTDLLA HWNEAYHFIN KAKRNHSKCL VHCKMGVSRS 400
    ASTVIAYAMK EFGWPLEKAY NYVKQKRSIT RPNAGFMRQL SEYEGILDAS 450
    KQRHNKLWRQ QTDSSLQQPV DDPAGPGDFL PETPDGTPES QLPFLDDAAQ 500
    PGLGPPLPCC FRRLSDPLLP SPEDETGSLV HLEDPEREAL LEEAAPPAEV 550
    HRPARQPQQG SGLCEKDVKK KLEFGSPKGR SGSLLQVEET EREEGLGAGR 600
    WGQLPTQLDQ NLLNSENLNN NSKRSCPNGM EDDAIFGILN KVKPSYKSCA 650
    DCMYPTASGA PEASRERCED PNAPAICTQP AFLPHITSSP VAHLASRSRV 700
    PEKPASGPTE PPPFLPPAGS RRADTSGPGA GAALEPPASL LEPSRETPKV 750
    LPKSLLLKNS HCDKNPPSTE VVIKEESSPK KDMKPAKDLR LLFSNESEKP 800
    TTNSYLMQHQ ESIIQLQKAG LVRKHTKELE RLKSVPADPA PPSRDGPASR 850
    LEASIPEESQ DPAALHELGP LVMPSQAGSD EKSEAAPASL EGGSLKSPPP 900
    FFYRLDHTSS FSKDFLKTIC YTPTSSSMSS NLTRSSSSDS IHSVRGKPGL 950
    VKQRTQEIET RLRLAGLTVS SPLKRSHSLA KLGSLTFSTE DLSSEADPST 1000
    VADSQDTTLS ESSFLHEPQG TPRDPAATSK PSGKPAPENL KSPSWMSKS 1049
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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_005268986.1. [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]

    Polymorphism databases

    DMDMi82582267.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS53825.1. [Q8WYL5-5 ]
    CCDS55882.1. [Q8WYL5-2 ]
    CCDS9121.1. [Q8WYL5-1 ]
    RefSeqi NP_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_005268986.1. [Q8WYL5-4 ]
    UniGenei Hs.199763.

    3D structure databases

    ProteinModelPortali Q8WYL5.
    SMRi Q8WYL5. Positions 309-449.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119950. 6 interactions.
    IntActi Q8WYL5. 12 interactions.
    MINTi MINT-1788740.
    STRINGi 9606.ENSP00000315713.

    PTM databases

    PhosphoSitei Q8WYL5.

    Polymorphism databases

    DMDMi 82582267.

    Proteomic databases

    MaxQBi Q8WYL5.
    PaxDbi Q8WYL5.
    PRIDEi Q8WYL5.

    Protocols and materials databases

    DNASUi 54434.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000326470 ; ENSP00000326107 ; ENSG00000084112 . [Q8WYL5-5 ]
    ENST00000326495 ; ENSP00000315713 ; ENSG00000084112 . [Q8WYL5-1 ]
    ENST00000551165 ; ENSP00000448824 ; ENSG00000084112 . [Q8WYL5-2 ]
    GeneIDi 54434.
    KEGGi hsa:54434.
    UCSCi uc001tnl.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

    CTDi 54434.
    GeneCardsi GC12M109180.
    HGNCi HGNC:30579. SSH1.
    HPAi HPA019845.
    MIMi 606778. gene.
    neXtProti NX_Q8WYL5.
    PharmGKBi PA134941788.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2453.
    HOGENOMi HOG000154427.
    HOVERGENi HBG094001.
    InParanoidi Q8WYL5.
    KOi K05766.
    OMAi NSHCDKN.
    OrthoDBi EOG7B8S33.
    PhylomeDBi Q8WYL5.
    TreeFami TF319444.

    Miscellaneous databases

    GeneWikii SSH1.
    GenomeRNAii 54434.
    NextBioi 56643.
    PROi Q8WYL5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8WYL5.
    Bgeei Q8WYL5.
    CleanExi HS_SSH1.
    Genevestigatori Q8WYL5.

    Family and domain databases

    Gene3Di 1.10.10.60. 1 hit.
    3.90.190.10. 1 hit.
    InterProi IPR014876. 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 ]
    PANTHERi PTHR10159. PTHR10159. 1 hit.
    PTHR10159:SF138. PTHR10159:SF138. 1 hit.
    Pfami PF08766. DEK_C. 1 hit.
    PF00782. DSPc. 1 hit.
    [Graphical view ]
    SMARTi SM00195. DSPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 1 hit.
    PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    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: October 1, 2014
    This is version 116 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