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Q64727

- VINC_MOUSE

UniProt

Q64727 - VINC_MOUSE

Protein

Vinculin

Gene

Vcl

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. structural molecule activity Source: InterPro

    GO - Biological processi

    1. adherens junction assembly Source: Ensembl
    2. apical junction assembly Source: Ensembl
    3. cell adhesion Source: MGI
    4. epithelial cell-cell adhesion Source: Ensembl
    5. lamellipodium assembly Source: MGI
    6. morphogenesis of an epithelium Source: Ensembl
    7. protein localization to cell surface Source: Ensembl
    8. regulation of cell migration Source: MGI

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vinculin
    Alternative name(s):
    Metavinculin
    Gene namesi
    Name:Vcl
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:98927. Vcl.

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity. Cell junctionadherens junction By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell junctionfocal adhesion By similarity
    Note: Cytoplasmic face of adhesion plaques. Recruitment to cell-cell junctions occurs in a myosin II-dependent manner. Interaction with CTNNB1 is necessary for its localization to the cell-cell junctions. Co-localizes with LIMD1 in the focal adhesions By similarity.By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: InterPro
    2. adherens junction Source: MGI
    3. cell-cell junction Source: MGI
    4. costamere Source: MGI
    5. fascia adherens Source: MGI
    6. focal adhesion Source: UniProtKB
    7. plasma membrane Source: MGI
    8. protein complex Source: Ensembl

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 10661065VinculinPRO_0000064253Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei173 – 1731N6-acetyllysineBy similarity
    Modified residuei290 – 2901Phosphoserine2 Publications
    Modified residuei346 – 3461PhosphoserineBy similarity
    Modified residuei434 – 4341PhosphoserineBy similarity
    Modified residuei496 – 4961N6-acetyllysineBy similarity
    Modified residuei537 – 5371PhosphotyrosineSequence Analysis
    Modified residuei721 – 7211Phosphoserine1 Publication
    Modified residuei822 – 8221PhosphotyrosineBy similarity
    Modified residuei1065 – 10651Phosphotyrosine; by SRC-type Tyr-kinasesBy similarity

    Post-translational modificationi

    Phosphorylated; on serines, threonines and tyrosines. Phosphorylation on Tyr-1065 in activated platelets affects head-tail interactions and cell spreading but has no effect on actin binding nor on localization to focal adhesion plaques By similarity.By similarity
    Acetylated; mainly by myristic acid but also by a small amount of palmitic acid.By similarity

    Keywords - PTMi

    Acetylation, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiQ64727.
    PaxDbiQ64727.
    PRIDEiQ64727.

    2D gel databases

    REPRODUCTION-2DPAGEQ64727.

    PTM databases

    PhosphoSiteiQ64727.

    Miscellaneous databases

    PMAP-CutDBQ64727.

    Expressioni

    Gene expression databases

    BgeeiQ64727.
    CleanExiMM_VCL.
    GenevestigatoriQ64727.

    Interactioni

    Subunit structurei

    Exhibits self-association properties. Interacts with APBB1IP, NRAP and TLN1. Interacts with SYNM. Interacts with CTNNB1 and this interaction is necessary for its localization to the cell-cell junctions and for its function in regulating cell surface expression of E-cadherin By similarity. Interacts with SORBS1.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Arhgef1Q612103EBI-432047,EBI-641821
    PXNP490244EBI-432047,EBI-2896280From a different organism.
    PxnQ8VI363EBI-432047,EBI-983394
    Tln1P260392EBI-432047,EBI-1039593

    Protein-protein interaction databases

    BioGridi204506. 6 interactions.
    IntActiQ64727. 11 interactions.
    MINTiMINT-1634466.

    Structurei

    3D structure databases

    ProteinModelPortaliQ64727.
    SMRiQ64727. Positions 1-258, 882-1063.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati259 – 3691111Add
    BLAST
    Repeati370 – 4791102Add
    BLAST
    Repeati480 – 5891103Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 835834N-terminal globular headBy similarityAdd
    BLAST
    Regioni168 – 20841Talin-interactionBy similarityAdd
    BLAST
    Regioni259 – 5893313 X 112 AA tandem repeatsAdd
    BLAST
    Regioni836 – 87843Linker (Pro-rich)By similarityAdd
    BLAST
    Regioni879 – 1066188C-terminal tailBy similarityAdd
    BLAST
    Regioni935 – 97844Facilitates phospholipid membrane insertionAdd
    BLAST
    Regioni1052 – 106615Facilitates phospholipid membrane insertionAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi837 – 87842Pro-richAdd
    BLAST

    Domaini

    Exists in at least two conformations. When in the closed, 'inactive' conformation, extensive interactions between the head and tail domains prevent detectable binding to most of its ligands. It takes on an 'active' conformation after cooperative and simultaneous binding of two different ligands. This activation involves displacement of the head-tail interactions and leads to a significant accumulation of ternary complexes. The active form then binds a number of proteins that have both signaling and structural roles that are essential for cell adhesion By similarity.By similarity
    The N-terminal globular head (Vh) comprises of subdomains D1-D4. The C-terminal tail (Vt) binds F-actin and cross-links actin filaments into bundles. An intramolecular interaction between Vh and Vt masks the F-actin-binding domain located in Vt. The binding of talin and alpha-actinin to the D1 subdomain of vinculin induces a helical bundle conversion of this subdomain, leading to the disruption of the intramolecular interaction and the exposure of the cryptic F-actin-binding domain of Vt. Vt inhibits actin filament barbed end elongation without affecting the critical concentration of actin assembly By similarity.By similarity

    Sequence similaritiesi

    Belongs to the vinculin/alpha-catenin family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG329927.
    GeneTreeiENSGT00550000074411.
    HOGENOMiHOG000007828.
    HOVERGENiHBG079758.
    InParanoidiQ64727.
    KOiK05700.
    OMAiLTHQVHR.
    OrthoDBiEOG73NG2V.
    PhylomeDBiQ64727.
    TreeFamiTF313686.

    Family and domain databases

    InterProiIPR017997. Vinculin.
    IPR006077. Vinculin/catenin.
    IPR000633. Vinculin_CS.
    [Graphical view]
    PANTHERiPTHR18914. PTHR18914. 1 hit.
    PfamiPF01044. Vinculin. 2 hits.
    [Graphical view]
    PRINTSiPR00806. VINCULIN.
    SUPFAMiSSF47220. SSF47220. 6 hits.
    PROSITEiPS00663. VINCULIN_1. 1 hit.
    PS00664. VINCULIN_2. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q64727-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVAAVQAA     50
    VSNLVRVGKE TVQTTEDQIL KRDMPPAFIK VENACTKLVQ AAQMLQSDPY 100
    SVPARDYLID GSRGILSGTS DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV 150
    VETMEDLVTY TKNLGPGMTK MAKMIDERQQ ELTHQEHRVM LVNSMNTVKE 200
    LLPVLISAMK IFVTTKNSKN QGIEEALKNR NFTVEKMSAE INEIIRVLQL 250
    TSWDEDAWAS KDTEAMKRAL ASIDSKLNQA KGWLRDPNAS PGDAGEQAIR 300
    QILDEAGKVG ELCAGKERRE ILGTCKMLGQ MTDQVADLRA RGQGASPVAM 350
    QKAQQVSQGL DVLTAKVENA ARKLEAMTNS KQSIAKKIDA AQNWLADPNG 400
    GPEGEEQIRG ALAEARKIAE LCDDPKERDD ILRSLGEIAA LTSKLGDLRR 450
    QGKGDSPEAR ALAKQVATAL QNLQTKTNRA VANSRPAKAA VHLEGKIEQA 500
    QRWIDNPTVD DRGVGQAAIR GLVAEGHRLA NVMMGPYRQD LLAKCDRVDQ 550
    LTAQLADLAA RGEGESPQAR ALASQLQDSL KDLKAQMQEA MTQEVSDVFS 600
    DTTTPIKLLA VAATAPPDAP NREEVFDERA ANFENHSGRL GATAEKAAAV 650
    GTANKSTVEG IQASVKTARE LTPQVISAAR ILLRNPGNQA AYEHFETMKN 700
    QWIDNVEKMT GLVDEAIDTK SLLDASEEAI KKDLDKCKVA MANIQPQMLV 750
    AGATSIARRA NRILLVAKRE VENSEDPKFR EAVKAASDEL SKTISPMVMD 800
    AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP DFPPPPPDLE 850
    QLRLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEVINQPMMM 900
    AARQLHDEAR KWSSKGNDII AAAKRMALLM AEMSRLVRGG SGTKRALIQC 950
    AKDIAKASDE VTRLAKEVAK QCTDKRIRTN LLQVCERIPT ISTQLKILST 1000
    VKATMLGRTN ISDEESEQAT EMLVHNAQNL MQSVKETVRE AEAASIKIRT 1050
    DAGFTLRWVR KTPWYQ 1066
    Length:1,066
    Mass (Da):116,717
    Last modified:January 23, 2007 - v4
    Checksum:i067F1B16A5285859
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 161V → E in AAB96843. (PubMed:7568093)Curated
    Sequence conflicti215 – 2151T → S in AAB96843. (PubMed:7568093)Curated
    Sequence conflicti363 – 3631L → V in AAB96843. (PubMed:7568093)Curated
    Sequence conflicti499 – 4991Q → K in BAC37033. (PubMed:16141072)Curated
    Sequence conflicti501 – 5011Q → R in AAB96843. (PubMed:7568093)Curated
    Sequence conflicti799 – 7991M → K in BAC37033. (PubMed:16141072)Curated
    Sequence conflicti812 – 8121G → D in AAB96843. (PubMed:7568093)Curated
    Sequence conflicti1044 – 10441A → T in BAC37033. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L13300, L13299 Genomic DNA. Translation: AAA40557.1.
    L18880 mRNA. Translation: AAB96843.1.
    AK035184 mRNA. Translation: BAC28973.1.
    AK077850 mRNA. Translation: BAC37033.1.
    BC008520 mRNA. Translation: AAH08520.1.
    BC008554 mRNA. Translation: AAH08554.1.
    CCDSiCCDS26860.1.
    PIRiA60965.
    T10108.
    RefSeqiNP_033528.3. NM_009502.4.
    UniGeneiMm.279361.

    Genome annotation databases

    EnsembliENSMUST00000022369; ENSMUSP00000022369; ENSMUSG00000021823.
    GeneIDi22330.
    KEGGimmu:22330.
    UCSCiuc007skz.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L13300 , L13299 Genomic DNA. Translation: AAA40557.1 .
    L18880 mRNA. Translation: AAB96843.1 .
    AK035184 mRNA. Translation: BAC28973.1 .
    AK077850 mRNA. Translation: BAC37033.1 .
    BC008520 mRNA. Translation: AAH08520.1 .
    BC008554 mRNA. Translation: AAH08554.1 .
    CCDSi CCDS26860.1.
    PIRi A60965.
    T10108.
    RefSeqi NP_033528.3. NM_009502.4.
    UniGenei Mm.279361.

    3D structure databases

    ProteinModelPortali Q64727.
    SMRi Q64727. Positions 1-258, 882-1063.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204506. 6 interactions.
    IntActi Q64727. 11 interactions.
    MINTi MINT-1634466.

    PTM databases

    PhosphoSitei Q64727.

    2D gel databases

    REPRODUCTION-2DPAGE Q64727.

    Proteomic databases

    MaxQBi Q64727.
    PaxDbi Q64727.
    PRIDEi Q64727.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022369 ; ENSMUSP00000022369 ; ENSMUSG00000021823 .
    GeneIDi 22330.
    KEGGi mmu:22330.
    UCSCi uc007skz.1. mouse.

    Organism-specific databases

    CTDi 7414.
    MGIi MGI:98927. Vcl.

    Phylogenomic databases

    eggNOGi NOG329927.
    GeneTreei ENSGT00550000074411.
    HOGENOMi HOG000007828.
    HOVERGENi HBG079758.
    InParanoidi Q64727.
    KOi K05700.
    OMAi LTHQVHR.
    OrthoDBi EOG73NG2V.
    PhylomeDBi Q64727.
    TreeFami TF313686.

    Miscellaneous databases

    ChiTaRSi VCL. mouse.
    NextBioi 302571.
    PMAP-CutDB Q64727.
    PROi Q64727.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q64727.
    CleanExi MM_VCL.
    Genevestigatori Q64727.

    Family and domain databases

    InterProi IPR017997. Vinculin.
    IPR006077. Vinculin/catenin.
    IPR000633. Vinculin_CS.
    [Graphical view ]
    PANTHERi PTHR18914. PTHR18914. 1 hit.
    Pfami PF01044. Vinculin. 2 hits.
    [Graphical view ]
    PRINTSi PR00806. VINCULIN.
    SUPFAMi SSF47220. SSF47220. 6 hits.
    PROSITEi PS00663. VINCULIN_1. 1 hit.
    PS00664. VINCULIN_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Targeted disruption of vinculin genes in F9 and embryonic stem cells changes cell morphology, adhesion, and locomotion."
      Coll J.-L., Ben-Ze'ev A., Ezzell R.M., Rodriguez Fernandez J.L., Baribault H., Oshima R.G., Adamson E.D.
      Proc. Natl. Acad. Sci. U.S.A. 92:9161-9165(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: 129/SvJ.
      Tissue: Embryo.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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].
      Strain: C57BL/6J.
      Tissue: Embryo and Forelimb.
    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].
    5. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 286-300; 656-666 AND 916-924, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    6. "Ponsin/SH3P12: an l-afadin- and vinculin-binding protein localized at cell-cell and cell-matrix adherens junctions."
      Mandai K., Nakanishi H., Satoh A., Takahashi K., Satoh K., Nishioka H., Mizoguchi A., Takai Y.
      J. Cell Biol. 144:1001-1017(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SORBS1.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
      Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
      J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    9. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290 AND SER-721, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    10. "Vinculin's C-terminal region facilitates phospholipid membrane insertion."
      Wirth V.F., List F., Diez G., Goldmann W.H.
      Biochem. Biophys. Res. Commun. 398:433-437(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REGION INVOLVED IN PHOSPHOLIPID MEMBRANE INSERTION.

    Entry informationi

    Entry nameiVINC_MOUSE
    AccessioniPrimary (citable) accession number: Q64727
    Secondary accession number(s): Q8BP32
    , Q8BS46, Q922C5, Q922D9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 132 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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