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Q76I79

- SSH1_MOUSE

UniProt

Q76I79 - SSH1_MOUSE

Protein

Protein phosphatase Slingshot homolog 1

Gene

Ssh1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      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.1 Publication

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

    GO - Biological processi

    1. actin cytoskeleton organization Source: Ensembl
    2. cell morphogenesis Source: Ensembl
    3. cellular response to ATP Source: MGI
    4. protein dephosphorylation Source: RefGenome
    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:
    mSSH-1L
    Gene namesi
    Name:Ssh1
    Synonyms:Kiaa1298, Ssh1l
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:2686240. Ssh1.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication. Cleavage furrow By similarity. Midbody By similarity
    Note: Localized to the cleavage furrow and the midbody during cytokinesis By similarity. Also colocalizes with F-actin in the cytoplasm and the cell periphery, which may allow local control of actin dynamics at sites of cell locomotion.By similarity

    GO - Cellular componenti

    1. cleavage furrow Source: UniProtKB-SubCell
    2. cytoplasm Source: RefGenome
    3. cytoskeleton Source: UniProtKB-SubCell
    4. midbody Source: UniProtKB-SubCell
    5. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi393 – 3931C → S: Abrogates phosphatase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 10421041Protein phosphatase Slingshot homolog 1PRO_0000094842Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei37 – 371PhosphoserineBy similarity
    Modified residuei57 – 571PhosphoserineBy similarity
    Modified residuei970 – 9701PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated. Inhibitory phosphorylation by PAK4 promotes binding to YWHAZ. Phosphorylation at Ser-970 is decreased by stimuli which promote actin reorganization and lamellipodia formation. Can be dephosphorylated and activated by PPP3CA/calcineurin A. Phosphorylation decreases immediately prior to telophase By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiQ76I79.
    PRIDEiQ76I79.

    PTM databases

    PhosphoSiteiQ76I79.

    Expressioni

    Tissue specificityi

    Expressed in brain, heart, kidney and thymus. Also expressed at lower levels in liver, skeletal muscle, small intestine and spleen.1 Publication

    Developmental stagei

    Ubiquitously expressed in the embryo at E14.5.1 Publication

    Gene expression databases

    ArrayExpressiQ76I79.
    BgeeiQ76I79.
    CleanExiMM_SSH1.
    GenevestigatoriQ76I79.

    Interactioni

    Subunit structurei

    Interacts with the 14-3-3 proteins YWHAB, YWHAG, YWHAQ, and YWHAZ. Interaction with 14-3-3 proteins inhibits phosphatase activity and also blocks recruitment to lamellipodia and stimulation by actin By similarity. Interacts with actin and this stimulates phosphatase activity. Interacts with LIMK1.By similarity2 Publications

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000076873.

    Structurei

    3D structure databases

    ProteinModelPortaliQ76I79.
    SMRiQ76I79. 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
    Regioni889 – 1042154Interaction with YWHAGBy similarityAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2453.
    GeneTreeiENSGT00750000117282.
    HOGENOMiHOG000154427.
    HOVERGENiHBG094001.
    InParanoidiQ76I79.
    KOiK05766.
    OMAiNSHCDKN.
    OrthoDBiEOG7B8S33.
    PhylomeDBiQ76I79.
    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 (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q76I79-1) [UniParc]FASTAAdd to Basket

    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 NSELEAGSDE ERKLNLSLSE SFFMVKGAAL     50
    FLQQGNSPQG QRSLQHPHKH AGDLPQHLQV MINLLRCEDR IKLAVRLESV 100
    WTDRVRYMVV VYTSGRQDTE ENILLGVDFS SKESKSCTIG MVLRLWSDTK 150
    IHLDGDGGFS VSTAGRMHIF KPVSVQAMWS ALQVLHKACE VARRHNYFPG 200
    GVALIWATYY ESCISSEQSC INEWNAMQDL ESTRPDSPAL FVDKPTEGER 250
    TERLIKAKLR SIMMSQDLEN VTSKEIRNEL EKQMNCNLKE FKEFIDNEML 300
    LILGQMDKPS LIFDHLYLGS EWNASNLEEL QGSGVDYILN VTREIDNFFP 350
    GLFAYHNIRV YDEETTDLLA HWNEAYHFIN KAKRNHSKCL VHCKMGVSRS 400
    ASTVIAYAMK EFGWPLEKAY NYVKQKRSIT RPNAGFMRQL SEYEGILDAS 450
    KQRHNKLWRQ QPTDDTIAEP SEFLPETLDG ALDAQLPCLD DTTHPGLPRS 500
    LAPGGPALPC CFRRLSDPLL LPHHDETGGL VHLEDLEKDA LLEEEESQPV 550
    EVHKLVQHPQ EGARLCEKDV KRKLEFGNSK PRSDSLPQVE ELEKDGSPRT 600
    GRWRRASTQL DRSLLDQENL NNNNSKRSCP DDLERDAMFG ILSKVKPPYT 650
    SCADCMYPTA GGTPEAYMER HEDPSSSAIC TQPTFLPHVT SSPMAHASSR 700
    SRAPERPASG PANTSPFLLP AGSRKPDVSG SGAGAAPEPP ASLLEPSRET 750
    SKALPKSLQL KNPHCDKNAA NMEVSAKEEP SPKKDPKPAK DLRLLFSNEA 800
    EKPTTNSYLM QHQESIIQLQ KAGLVRKHTK ELERLKSLPS DSPAACRDSA 850
    TCRLEASIPE EGSQEPAHPA LCSQAGSEEQ PVGGTLQKSP TSTLPRLDHT 900
    SNFSKDFLKT VCYTPTSSSI SSNLTRSSSS DSIHSVRGKP GLVKQRAQEI 950
    ETRLRLAGLT VSSPLKRSHS LAKLGSLNFS TEDLSSEADT STIADSQDAK 1000
    CGLSSSFLPE PQSAPRDPAA TSKSSGKSAP EHLKSPSRVN KS 1042
    Length:1,042
    Mass (Da):115,297
    Last modified:July 5, 2004 - v1
    Checksum:i19A34E4937FA48FA
    GO
    Isoform 2 (identifier: Q76I79-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,020
    Mass (Da):112,878
    Checksum:i553EF13BEE0F0AF6
    GO

    Sequence cautioni

    The sequence BAD32422.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti526 – 5261E → D in AAH46529. (PubMed:15489334)Curated
    Sequence conflicti550 – 5501V → A in BAE41639. (PubMed:16141072)Curated
    Sequence conflicti569 – 5691D → E in BAE41639. (PubMed:16141072)Curated
    Sequence conflicti867 – 8671A → V in AAH46529. (PubMed:15489334)Curated
    Sequence conflicti1010 – 10101E → G in BAE41639. (PubMed:16141072)Curated
    Sequence conflicti1035 – 10351S → N in AAH46529. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei158 – 17922Missing in isoform 2. 1 PublicationVSP_016320Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB099287 mRNA. Translation: BAC97810.1.
    AK173144 mRNA. Translation: BAD32422.1. Different initiation.
    AK155557 mRNA. Translation: BAE33323.1.
    AK170212 mRNA. Translation: BAE41639.1.
    AK171556 mRNA. Translation: BAE42524.1.
    BC046529 mRNA. Translation: AAH46529.1.
    CCDSiCCDS19556.1. [Q76I79-1]
    RefSeqiNP_932777.2. NM_198109.4. [Q76I79-1]
    UniGeneiMm.389682.

    Genome annotation databases

    EnsembliENSMUST00000112298; ENSMUSP00000107917; ENSMUSG00000042121. [Q76I79-2]
    ENSMUST00000159592; ENSMUSP00000124312; ENSMUSG00000042121. [Q76I79-1]
    GeneIDi231637.
    KEGGimmu:231637.
    UCSCiuc008yyx.1. mouse. [Q76I79-1]
    uc008yyz.1. mouse. [Q76I79-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB099287 mRNA. Translation: BAC97810.1 .
    AK173144 mRNA. Translation: BAD32422.1 . Different initiation.
    AK155557 mRNA. Translation: BAE33323.1 .
    AK170212 mRNA. Translation: BAE41639.1 .
    AK171556 mRNA. Translation: BAE42524.1 .
    BC046529 mRNA. Translation: AAH46529.1 .
    CCDSi CCDS19556.1. [Q76I79-1 ]
    RefSeqi NP_932777.2. NM_198109.4. [Q76I79-1 ]
    UniGenei Mm.389682.

    3D structure databases

    ProteinModelPortali Q76I79.
    SMRi Q76I79. Positions 309-449.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000076873.

    PTM databases

    PhosphoSitei Q76I79.

    Proteomic databases

    PaxDbi Q76I79.
    PRIDEi Q76I79.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000112298 ; ENSMUSP00000107917 ; ENSMUSG00000042121 . [Q76I79-2 ]
    ENSMUST00000159592 ; ENSMUSP00000124312 ; ENSMUSG00000042121 . [Q76I79-1 ]
    GeneIDi 231637.
    KEGGi mmu:231637.
    UCSCi uc008yyx.1. mouse. [Q76I79-1 ]
    uc008yyz.1. mouse. [Q76I79-2 ]

    Organism-specific databases

    CTDi 54434.
    MGIi MGI:2686240. Ssh1.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG2453.
    GeneTreei ENSGT00750000117282.
    HOGENOMi HOG000154427.
    HOVERGENi HBG094001.
    InParanoidi Q76I79.
    KOi K05766.
    OMAi NSHCDKN.
    OrthoDBi EOG7B8S33.
    PhylomeDBi Q76I79.
    TreeFami TF319444.

    Miscellaneous databases

    NextBioi 380673.
    PROi Q76I79.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q76I79.
    Bgeei Q76I79.
    CleanExi MM_SSH1.
    Genevestigatori Q76I79.

    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. "Differential activities, subcellular distribution and tissue expression patterns of three members of Slingshot family phosphatases that dephosphorylate cofilin."
      Ohta Y., Kousaka K., Nagata-Ohashi K., Ohashi K., Muramoto A., Shima Y., Niwa R., Uemura T., Mizuno K.
      Genes Cells 8:811-824(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ACTIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF CYS-393.
    2. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
      DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Embryonic tail.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 539-1042 (ISOFORMS 1/2).
      Strain: C57BL/6J.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 166-1042 (ISOFORM 1).
      Strain: FVB/N.
      Tissue: Liver.
    5. "Interplay between components of a novel LIM kinase-slingshot phosphatase complex regulates cofilin."
      Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N., Sarcevic B., Sampath R., Bamburg J.R., Bernard O.
      EMBO J. 24:473-486(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LIMK1.

    Entry informationi

    Entry nameiSSH1_MOUSE
    AccessioniPrimary (citable) accession number: Q76I79
    Secondary accession number(s): Q3TDG3, Q69ZM4, Q811E5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 96 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3