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Q9DBJ3

- BI2L1_MOUSE

UniProt

Q9DBJ3 - BI2L1_MOUSE

Protein

Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1

Gene

Baiap2l1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    May function as adapter protein. Involved in the formation of clusters of actin bundles. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection By similarity.By similarity

    GO - Molecular functioni

    1. proline-rich region binding Source: UniProtKB

    GO - Biological processi

    1. filopodium assembly Source: InterPro
    2. positive regulation of actin cytoskeleton reorganization Source: UniProtKB
    3. positive regulation of actin filament polymerization Source: UniProtKB
    4. response to bacterium Source: UniProtKB
    5. signal transduction Source: InterPro

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1
    Short name:
    BAI1-associated protein 2-like protein 1
    Alternative name(s):
    Insulin receptor tyrosine kinase substrate
    Gene namesi
    Name:Baiap2l1
    Synonyms:Irtks
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:1914148. Baiap2l1.

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity
    Note: Recruited to actin pedestals that are formed upon infection by bacteria at bacterial attachment sites.By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: Ensembl
    2. cell junction Source: Ensembl
    3. cytosol Source: UniProtKB
    4. nucleus Source: Ensembl
    5. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 514514Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1PRO_0000247855Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei248 – 2481PhosphothreonineBy similarity
    Modified residuei257 – 2571PhosphothreonineBy similarity
    Modified residuei261 – 2611Phosphoserine1 Publication
    Modified residuei281 – 2811PhosphoserineBy similarity
    Modified residuei332 – 3321PhosphoserineBy similarity
    Modified residuei411 – 4111PhosphothreonineBy similarity
    Modified residuei421 – 4211Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated on tyrosine in response to insulin.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9DBJ3.
    PaxDbiQ9DBJ3.
    PRIDEiQ9DBJ3.

    PTM databases

    PhosphoSiteiQ9DBJ3.

    Expressioni

    Tissue specificityi

    Detected in bladder, liver, testes, heart, lung, spleen, brain and skeletal muscle (at protein level).1 Publication

    Gene expression databases

    BgeeiQ9DBJ3.
    CleanExiMM_BAIAP2L1.
    GenevestigatoriQ9DBJ3.

    Interactioni

    Subunit structurei

    Interacts with RAC1. Binds to F-actin. Interacts with FASLG By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ9DBJ3. 2 interactions.
    MINTiMINT-4128274.
    STRINGi10090.ENSMUSP00000053129.

    Structurei

    Secondary structure

    1
    514
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi344 – 3463
    Beta strandi357 – 3593
    Beta strandi367 – 3704
    Beta strandi379 – 3846
    Turni385 – 3873
    Beta strandi390 – 3945
    Helixi395 – 3973

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SPKNMR-A343-401[»]
    ProteinModelPortaliQ9DBJ3.
    SMRiQ9DBJ3. Positions 6-227, 343-401.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9DBJ3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 249249IMDPROSITE-ProRule annotationAdd
    BLAST
    Domaini340 – 40364SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni486 – 51429Binds F-actinBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili115 – 14834Sequence AnalysisAdd
    BLAST

    Domaini

    The IMD domain is predicted to have a helical structure. It may induce actin bundling and filopodia formation By similarity.By similarity

    Sequence similaritiesi

    Contains 1 IMD (IRSp53/MIM homology) domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, SH3 domain

    Phylogenomic databases

    eggNOGiNOG71665.
    GeneTreeiENSGT00390000005995.
    HOGENOMiHOG000038005.
    HOVERGENiHBG054462.
    InParanoidiQ9DBJ3.
    OMAiYRNVMEQ.
    OrthoDBiEOG7N0C3W.
    PhylomeDBiQ9DBJ3.
    TreeFamiTF325648.

    Family and domain databases

    InterProiIPR027681. BAIAP2.
    IPR013606. IRSp53/MIM_homology_IMD.
    IPR001452. SH3_domain.
    [Graphical view]
    PANTHERiPTHR14206. PTHR14206. 1 hit.
    PfamiPF08397. IMD. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view]
    SMARTiSM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS51338. IMD. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9DBJ3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRGPEEVNR LTENTYRNVM EQFNPGLRNL INLGKNYEKA VNAMILAGKA    50
    YYDGVAKIGE IATGSPVSTE LGHVLIEISS THKKLNETLD ENFKKFHKDI 100
    IHELEKKTEL DVKYMNATLK RYQAEHRNKL DSLEKSQAEL KKIRRKSQGG 150
    RNALKYEHKE IEYVETVTSR QSEIQKFIAD GCKEALLEEK RRFCFLVDKH 200
    CSFASHIHYY HMQSAELLNS KLPRWQETCC DATKVPEKIM NMIEEIKTPI 250
    STPVSGTPQP SPMIERSKMI GKDYDTLSKY SPKMPPAPSV KAYTSPLIDM 300
    FNNPATAAQS SEKTNNSTAN TGEDPSLQRS VSVATGLNMM KKQKVKTIFP 350
    HTAGNNKTLL SFAQGDVLTL LIPEEKDGWL YGEHDTTKAR GWFPSSYTKL 400
    LEENEAMSVP TPSPAPVRSI STVDLTEKSS VVIPPPDYLE CLSMGATSDK 450
    KAGAPKVPSA STFRAPVSRP DATSTSPSDA NGTAKPPFLS GENPFATVKL 500
    RPTVTNDRSA PIIR 514
    Length:514
    Mass (Da):57,188
    Last modified:June 1, 2001 - v1
    Checksum:iAF9974A0696812EC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK004918 mRNA. Translation: BAB23669.1.
    BC015459 mRNA. Translation: AAH15459.1.
    CCDSiCCDS39378.1.
    RefSeqiNP_080109.1. NM_025833.3.
    UniGeneiMm.18814.

    Genome annotation databases

    EnsembliENSMUST00000055190; ENSMUSP00000053129; ENSMUSG00000038859.
    GeneIDi66898.
    KEGGimmu:66898.
    UCSCiuc009alq.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK004918 mRNA. Translation: BAB23669.1 .
    BC015459 mRNA. Translation: AAH15459.1 .
    CCDSi CCDS39378.1.
    RefSeqi NP_080109.1. NM_025833.3.
    UniGenei Mm.18814.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SPK NMR - A 343-401 [» ]
    ProteinModelPortali Q9DBJ3.
    SMRi Q9DBJ3. Positions 6-227, 343-401.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9DBJ3. 2 interactions.
    MINTi MINT-4128274.
    STRINGi 10090.ENSMUSP00000053129.

    PTM databases

    PhosphoSitei Q9DBJ3.

    Proteomic databases

    MaxQBi Q9DBJ3.
    PaxDbi Q9DBJ3.
    PRIDEi Q9DBJ3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000055190 ; ENSMUSP00000053129 ; ENSMUSG00000038859 .
    GeneIDi 66898.
    KEGGi mmu:66898.
    UCSCi uc009alq.1. mouse.

    Organism-specific databases

    CTDi 55971.
    MGIi MGI:1914148. Baiap2l1.

    Phylogenomic databases

    eggNOGi NOG71665.
    GeneTreei ENSGT00390000005995.
    HOGENOMi HOG000038005.
    HOVERGENi HBG054462.
    InParanoidi Q9DBJ3.
    OMAi YRNVMEQ.
    OrthoDBi EOG7N0C3W.
    PhylomeDBi Q9DBJ3.
    TreeFami TF325648.

    Miscellaneous databases

    EvolutionaryTracei Q9DBJ3.
    NextBioi 322961.
    PROi Q9DBJ3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9DBJ3.
    CleanExi MM_BAIAP2L1.
    Genevestigatori Q9DBJ3.

    Family and domain databases

    InterProi IPR027681. BAIAP2.
    IPR013606. IRSp53/MIM_homology_IMD.
    IPR001452. SH3_domain.
    [Graphical view ]
    PANTHERi PTHR14206. PTHR14206. 1 hit.
    Pfami PF08397. IMD. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view ]
    SMARTi SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS51338. IMD. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: Liver.
    2. "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].
      Strain: FVB/N.
      Tissue: Mammary tumor.
    3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261 AND SER-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    4. "Solution structure of RSGI RUH-010, an SH3 domain from mouse cDNA."
      RIKEN structural genomics initiative (RSGI)
      Submitted (SEP-2004) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 343-401.
    5. "Characterisation of IRTKS, a novel IRSp53/MIM family actin regulator with distinct filament bundling properties."
      Millard T.H., Dawson J., Machesky L.M.
      J. Cell Sci. 120:1663-1672(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiBI2L1_MOUSE
    AccessioniPrimary (citable) accession number: Q9DBJ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 102 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3