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Q9UHR4

- BI2L1_HUMAN

UniProt

Q9UHR4 - BI2L1_HUMAN

Protein

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

Gene

BAIAP2L1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (01 Mar 2004)
      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.3 Publications

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:21649. BAIAP2L1.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication
    Note: Recruited to actin pedestals that are formed upon infection by bacteria at bacterial attachment sites.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytoskeleton Source: UniProtKB-SubCell
    3. cytosol Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. nucleus Source: HPA
    6. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi141 – 1411K → E: Loss ability to induce the formation of actin clusters; when associated with K-142; R-145 and K-146. 1 Publication
    Mutagenesisi142 – 1421K → E: Loss ability to induce the formation of actin clusters; when associated with K-141; R-145 and K-146. 1 Publication
    Mutagenesisi145 – 1451R → E: Loss ability to induce the formation of actin clusters; when associated with K-141; K-142 and K-146. 1 Publication
    Mutagenesisi146 – 1461K → E: Loss ability to induce the formation of actin clusters; when associated with K-141; K-142 and R-145. 1 Publication
    Mutagenesisi488 – 51124Missing: Loss ability to induce the formation of actin clusters; induce the formation of long filopodia. Add
    BLAST

    Organism-specific databases

    PharmGKBiPA142672562.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 511511Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1PRO_0000247854Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei248 – 2481Phosphothreonine3 Publications
    Modified residuei257 – 2571Phosphothreonine3 Publications
    Modified residuei261 – 2611Phosphoserine4 Publications
    Modified residuei281 – 2811Phosphoserine2 Publications
    Modified residuei331 – 3311Phosphoserine2 Publications
    Modified residuei412 – 4121Phosphothreonine3 Publications
    Modified residuei422 – 4221PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated on tyrosine in response to insulin.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UHR4.
    PaxDbiQ9UHR4.
    PeptideAtlasiQ9UHR4.
    PRIDEiQ9UHR4.

    PTM databases

    PhosphoSiteiQ9UHR4.

    Expressioni

    Gene expression databases

    BgeeiQ9UHR4.
    CleanExiHS_BAIAP2L1.
    GenevestigatoriQ9UHR4.

    Organism-specific databases

    HPAiHPA019484.
    HPA021257.
    HPA023874.
    HPA029503.

    Interactioni

    Subunit structurei

    Interacts with RAC1. Binds to F-actin. Interacts with FASLG. Interacts (via SH3 domain) with E.coli effector protein EspF(U) (via PXXP motifs). Identified in a complex containing at least WASL, BAIAP2L1 and E.coli EspF(U). Interacts with E.coli intimin receptor Tir.5 Publications

    Protein-protein interaction databases

    BioGridi121017. 13 interactions.
    DIPiDIP-53820N.
    IntActiQ9UHR4. 5 interactions.
    MINTiMINT-5006683.
    STRINGi9606.ENSP00000005260.

    Structurei

    Secondary structure

    1
    511
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi343 – 3486
    Beta strandi356 – 3583
    Beta strandi366 – 3738
    Beta strandi378 – 3869
    Beta strandi389 – 3935
    Helixi394 – 3963
    Beta strandi397 – 4004

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KXCNMR-A339-402[»]
    2LNHNMR-B339-402[»]
    ProteinModelPortaliQ9UHR4.
    SMRiQ9UHR4. Positions 6-227, 339-402.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 249249IMDPROSITE-ProRule annotationAdd
    BLAST
    Domaini339 – 40264SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni483 – 51129Binds F-actinAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili115 – 15440Sequence 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.
    HOVERGENiHBG054462.
    InParanoidiQ9UHR4.
    OMAiYRNVMEQ.
    OrthoDBiEOG7N0C3W.
    PhylomeDBiQ9UHR4.
    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.

    Q9UHR4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRGPEEVNR LTESTYRNVM EQFNPGLRNL INLGKNYEKA VNAMILAGKA    50
    YYDGVAKIGE IATGSPVSTE LGHVLIEISS THKKLNESLD ENFKKFHKEI 100
    IHELEKKIEL DVKYMNATLK RYQTEHKNKL ESLEKSQAEL KKIRRKSQGS 150
    RNALKYEHKE IEYVETVTSR QSEIQKFIAD GCKEALLEEK RRFCFLVDKH 200
    CGFANHIHYY HLQSAELLNS KLPRWQETCV DAIKVPEKIM NMIEEIKTPA 250
    STPVSGTPQA SPMIERSNVV RKDYDTLSKC SPKMPPAPSG RAYTSPLIDM 300
    FNNPATAAPN SQRVNNSTGT SEDPSLQRSV SVATGLNMMK KQKVKTIFPH 350
    TAGSNKTLLS FAQGDVITLL IPEEKDGWLY GEHDVSKARG WFPSSYTKLL 400
    EENETEAVTV PTPSPTPVRS ISTVNLSENS SVVIPPPDYL ECLSMGAAAD 450
    RRADSARTTS TFKAPASKPE TAAPNDANGT AKPPFLSGEN PFATVKLRPT 500
    VTNDRSAPII R 511
    Length:511
    Mass (Da):56,883
    Last modified:March 1, 2004 - v2
    Checksum:iC2304C4444B02F02
    GO

    Sequence cautioni

    The sequence AAS07549.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB15671.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAD20937.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti456 – 4561A → V in BAB15671. (PubMed:14702039)Curated
    Sequence conflicti460 – 4601S → F in BAB15671. (PubMed:14702039)Curated
    Sequence conflicti464 – 4641A → V in BAB15671. (PubMed:14702039)Curated
    Sequence conflicti466 – 4661A → V in BAB15671. (PubMed:14702039)Curated
    Sequence conflicti467 – 4671S → F in BAB15671. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti460 – 4601S → T.
    Corresponds to variant rs2269966 [ dbSNP | Ensembl ].
    VAR_033515

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF119666 mRNA. Translation: AAF17223.2.
    AC004841 Genomic DNA. Translation: AAD20937.1. Sequence problems.
    AC093169 Genomic DNA. No translation available.
    AC093799 Genomic DNA. Translation: AAS07549.1. Different initiation.
    AC093799 Genomic DNA. Translation: AAS07550.1.
    CH236956 Genomic DNA. Translation: EAL23890.1.
    CH471091 Genomic DNA. Translation: EAW76706.1.
    BC013888 mRNA. Translation: AAH13888.1.
    AK027142 mRNA. Translation: BAB15671.1. Different initiation.
    CCDSiCCDS34687.1.
    RefSeqiNP_061330.2. NM_018842.4.
    UniGeneiHs.656063.

    Genome annotation databases

    EnsembliENST00000005260; ENSP00000005260; ENSG00000006453.
    GeneIDi55971.
    KEGGihsa:55971.
    UCSCiuc003upj.3. human.

    Polymorphism databases

    DMDMi74735022.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF119666 mRNA. Translation: AAF17223.2 .
    AC004841 Genomic DNA. Translation: AAD20937.1 . Sequence problems.
    AC093169 Genomic DNA. No translation available.
    AC093799 Genomic DNA. Translation: AAS07549.1 . Different initiation.
    AC093799 Genomic DNA. Translation: AAS07550.1 .
    CH236956 Genomic DNA. Translation: EAL23890.1 .
    CH471091 Genomic DNA. Translation: EAW76706.1 .
    BC013888 mRNA. Translation: AAH13888.1 .
    AK027142 mRNA. Translation: BAB15671.1 . Different initiation.
    CCDSi CCDS34687.1.
    RefSeqi NP_061330.2. NM_018842.4.
    UniGenei Hs.656063.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KXC NMR - A 339-402 [» ]
    2LNH NMR - B 339-402 [» ]
    ProteinModelPortali Q9UHR4.
    SMRi Q9UHR4. Positions 6-227, 339-402.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121017. 13 interactions.
    DIPi DIP-53820N.
    IntActi Q9UHR4. 5 interactions.
    MINTi MINT-5006683.
    STRINGi 9606.ENSP00000005260.

    PTM databases

    PhosphoSitei Q9UHR4.

    Polymorphism databases

    DMDMi 74735022.

    Proteomic databases

    MaxQBi Q9UHR4.
    PaxDbi Q9UHR4.
    PeptideAtlasi Q9UHR4.
    PRIDEi Q9UHR4.

    Protocols and materials databases

    DNASUi 55971.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000005260 ; ENSP00000005260 ; ENSG00000006453 .
    GeneIDi 55971.
    KEGGi hsa:55971.
    UCSCi uc003upj.3. human.

    Organism-specific databases

    CTDi 55971.
    GeneCardsi GC07M097920.
    H-InvDB HIX0167837.
    HGNCi HGNC:21649. BAIAP2L1.
    HPAi HPA019484.
    HPA021257.
    HPA023874.
    HPA029503.
    MIMi 611877. gene.
    neXtProti NX_Q9UHR4.
    PharmGKBi PA142672562.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG71665.
    HOVERGENi HBG054462.
    InParanoidi Q9UHR4.
    OMAi YRNVMEQ.
    OrthoDBi EOG7N0C3W.
    PhylomeDBi Q9UHR4.
    TreeFami TF325648.

    Miscellaneous databases

    ChiTaRSi BAIAP2L1. human.
    GeneWikii BAIAP2L1.
    GenomeRNAii 55971.
    NextBioi 61407.
    PROi Q9UHR4.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UHR4.
    CleanExi HS_BAIAP2L1.
    Genevestigatori Q9UHR4.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Adrenal gland.
    2. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
      Tissue: Placenta.
    6. "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] OF 317-511.
      Tissue: Lung.
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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: FUNCTION, INTERACTION WITH RAC1 AND F-ACTIN, PHOSPHORYLATION, MUTAGENESIS OF LYS-141; LYS-142; ARG-145; LYS-146 AND 488-GLY--ARG-511.
    9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248; THR-257; SER-261; SER-281; SER-331 AND THR-412, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
      Voss M., Lettau M., Janssen O.
      BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FASLG.
    13. "Insulin receptor tyrosine kinase substrate links the E. coli O157:H7 actin assembly effectors Tir and EspF(U) during pedestal formation."
      Vingadassalom D., Kazlauskas A., Skehan B., Cheng H.C., Magoun L., Robbins D., Rosen M.K., Saksela K., Leong J.M.
      Proc. Natl. Acad. Sci. U.S.A. 106:6754-6759(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH E.COLI EFFECTOR PROTEIN ESPF(U), IDENTIFICATION IN A COMPLEX WITH WASL AND E.COLI EFFECTOR PROTEIN ESPF(U), INTERACTION WITH E.COLI INTIMIN RECEPTOR TIR, SUBCELLULAR LOCATION.
    14. "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 THR-248; THR-257; SER-261 AND THR-412, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Recognition of tandem PxxP motifs as a unique Src homology 3-binding mode triggers pathogen-driven actin assembly."
      Aitio O., Hellman M., Kazlauskas A., Vingadassalom D.F., Leong J.M., Saksela K., Permi P.
      Proc. Natl. Acad. Sci. U.S.A. 107:21743-21748(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 339-402 IN COMPLEX WITH E.COLI EFFECTOR PROTEIN ESPF(U), SUBUNIT.
    17. "Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly."
      Aitio O., Hellman M., Skehan B., Kesti T., Leong J.M., Saksela K., Permi P.
      Structure 20:1692-1703(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 339-402 IN COMPLEX WITH WASL AND E.COLI ESPF(U), FUNCTION, IDENTIFICATION IN A COMPLEX WITH WASL AND E.COLI ESPF(U).

    Entry informationi

    Entry nameiBI2L1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UHR4
    Secondary accession number(s): A4D268
    , Q75L21, Q75L22, Q96CV4, Q9H5F5, Q9Y2M8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: March 1, 2004
    Last modified: October 1, 2014
    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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3