BI2L1_HUMAN
ID BI2L1_HUMAN Reviewed; 511 AA.
AC Q9UHR4; A4D268; Q75L21; Q75L22; Q96CV4; Q9H5F5; Q9Y2M8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1;
DE Short=BAI1-associated protein 2-like protein 1;
DE AltName: Full=Insulin receptor tyrosine kinase substrate;
GN Name=BAIAP2L1; Synonyms=IRTKS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 317-511.
RC TISSUE=Lung;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP FUNCTION, INTERACTION WITH RAC1 AND F-ACTIN, PHOSPHORYLATION, AND
RP MUTAGENESIS OF LYS-141; LYS-142; ARG-145; LYS-146 AND 488-GLY--ARG-511.
RX PubMed=17430976; DOI=10.1242/jcs.001776;
RA Millard T.H., Dawson J., Machesky L.M.;
RT "Characterisation of IRTKS, a novel IRSp53/MIM family actin regulator with
RT distinct filament bundling properties.";
RL J. Cell Sci. 120:1663-1672(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248; THR-257; SER-261;
RP SER-281; SER-331 AND THR-412, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP INTERACTION WITH FASLG.
RX PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA Voss M., Lettau M., Janssen O.;
RT "Identification of SH3 domain interaction partners of human FasL (CD178) by
RT phage display screening.";
RL BMC Immunol. 10:53-53(2009).
RN [13]
RP FUNCTION, INTERACTION WITH E.COLI EFFECTOR PROTEIN ESPF(U), IDENTIFICATION
RP IN A COMPLEX WITH WASL AND E.COLI EFFECTOR PROTEIN ESPF(U), INTERACTION
RP WITH E.COLI INTIMIN RECEPTOR TIR, AND SUBCELLULAR LOCATION.
RX PubMed=19366662; DOI=10.1073/pnas.0809131106;
RA Vingadassalom D., Kazlauskas A., Skehan B., Cheng H.C., Magoun L.,
RA Robbins D., Rosen M.K., Saksela K., Leong J.M.;
RT "Insulin receptor tyrosine kinase substrate links the E. coli O157:H7 actin
RT assembly effectors Tir and EspF(U) during pedestal formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:6754-6759(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248; THR-257; SER-261 AND
RP THR-412, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257; SER-261; SER-281;
RP SER-331 AND SER-354, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331; SER-414 AND SER-420, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP STRUCTURE BY NMR OF 339-402 IN COMPLEX WITH E.COLI EFFECTOR PROTEIN
RP ESPF(U), AND SUBUNIT.
RX PubMed=21098279; DOI=10.1073/pnas.1010243107;
RA Aitio O., Hellman M., Kazlauskas A., Vingadassalom D.F., Leong J.M.,
RA Saksela K., Permi P.;
RT "Recognition of tandem PxxP motifs as a unique Src homology 3-binding mode
RT triggers pathogen-driven actin assembly.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:21743-21748(2010).
RN [19]
RP STRUCTURE BY NMR OF 339-402 IN COMPLEX WITH WASL AND E.COLI ESPF(U),
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH WASL AND E.COLI ESPF(U).
RX PubMed=22921828; DOI=10.1016/j.str.2012.07.015;
RA Aitio O., Hellman M., Skehan B., Kesti T., Leong J.M., Saksela K.,
RA Permi P.;
RT "Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack
RT host f-actin assembly.";
RL Structure 20:1692-1703(2012).
CC -!- FUNCTION: May function as adapter protein. Involved in the formation of
CC clusters of actin bundles. Plays a role in the reorganization of the
CC actin cytoskeleton in response to bacterial infection.
CC {ECO:0000269|PubMed:17430976, ECO:0000269|PubMed:19366662,
CC ECO:0000269|PubMed:22921828}.
CC -!- SUBUNIT: Interacts with RAC1. Binds to F-actin. Interacts with FASLG.
CC Interacts (via SH3 domain) with E.coli effector protein EspF(U) (via
CC PXXP motifs). Identified in a complex containing at least WASL,
CC BAIAP2L1 and E.coli EspF(U). Interacts with E.coli intimin receptor
CC Tir. {ECO:0000269|PubMed:17430976, ECO:0000269|PubMed:19366662,
CC ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:21098279,
CC ECO:0000269|PubMed:22921828}.
CC -!- INTERACTION:
CC Q9UHR4; O95817: BAG3; NbExp=3; IntAct=EBI-2483278, EBI-747185;
CC Q9UHR4; Q9UQB8-6: BAIAP2; NbExp=3; IntAct=EBI-2483278, EBI-9092016;
CC Q9UHR4; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2483278, EBI-3867333;
CC Q9UHR4; Q12929: EPS8; NbExp=4; IntAct=EBI-2483278, EBI-375576;
CC Q9UHR4; O43813: LANCL1; NbExp=3; IntAct=EBI-2483278, EBI-3046631;
CC Q9UHR4; P0DJ88: espF(U); Xeno; NbExp=9; IntAct=EBI-2483278, EBI-10039462;
CC Q9UHR4; Q7DB77: tir; Xeno; NbExp=3; IntAct=EBI-2483278, EBI-6480811;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19366662}. Note=Recruited to actin pedestals that
CC are formed upon infection by bacteria at bacterial attachment sites.
CC -!- DOMAIN: The IMD domain is predicted to have a helical structure. It may
CC induce actin bundling and filopodia formation (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine in response to insulin.
CC {ECO:0000269|PubMed:17430976}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD20937.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAS07549.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB15671.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF119666; AAF17223.2; -; mRNA.
DR EMBL; AC004841; AAD20937.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC093169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093799; AAS07549.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC093799; AAS07550.1; -; Genomic_DNA.
DR EMBL; CH236956; EAL23890.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76706.1; -; Genomic_DNA.
DR EMBL; BC013888; AAH13888.1; -; mRNA.
DR EMBL; AK027142; BAB15671.1; ALT_INIT; mRNA.
DR CCDS; CCDS34687.1; -.
DR RefSeq; NP_061330.2; NM_018842.4.
DR PDB; 2KXC; NMR; -; A=339-402.
DR PDB; 2LNH; NMR; -; B=339-402.
DR PDBsum; 2KXC; -.
DR PDBsum; 2LNH; -.
DR AlphaFoldDB; Q9UHR4; -.
DR BMRB; Q9UHR4; -.
DR SMR; Q9UHR4; -.
DR BioGRID; 121017; 104.
DR DIP; DIP-53820N; -.
DR IntAct; Q9UHR4; 52.
DR MINT; Q9UHR4; -.
DR STRING; 9606.ENSP00000005260; -.
DR GlyGen; Q9UHR4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UHR4; -.
DR MetOSite; Q9UHR4; -.
DR PhosphoSitePlus; Q9UHR4; -.
DR BioMuta; BAIAP2L1; -.
DR DMDM; 74735022; -.
DR EPD; Q9UHR4; -.
DR jPOST; Q9UHR4; -.
DR MassIVE; Q9UHR4; -.
DR MaxQB; Q9UHR4; -.
DR PaxDb; Q9UHR4; -.
DR PeptideAtlas; Q9UHR4; -.
DR PRIDE; Q9UHR4; -.
DR ProteomicsDB; 84402; -.
DR Antibodypedia; 16001; 206 antibodies from 31 providers.
DR DNASU; 55971; -.
DR Ensembl; ENST00000005260.9; ENSP00000005260.8; ENSG00000006453.14.
DR GeneID; 55971; -.
DR KEGG; hsa:55971; -.
DR MANE-Select; ENST00000005260.9; ENSP00000005260.8; NM_018842.5; NP_061330.2.
DR UCSC; uc003upj.4; human.
DR CTD; 55971; -.
DR DisGeNET; 55971; -.
DR GeneCards; BAIAP2L1; -.
DR HGNC; HGNC:21649; BAIAP2L1.
DR HPA; ENSG00000006453; Tissue enhanced (stomach).
DR MIM; 611877; gene.
DR neXtProt; NX_Q9UHR4; -.
DR OpenTargets; ENSG00000006453; -.
DR PharmGKB; PA142672562; -.
DR VEuPathDB; HostDB:ENSG00000006453; -.
DR eggNOG; ENOG502QQC6; Eukaryota.
DR GeneTree; ENSGT00940000153560; -.
DR HOGENOM; CLU_025877_0_1_1; -.
DR InParanoid; Q9UHR4; -.
DR OMA; HIHHYHL; -.
DR OrthoDB; 457637at2759; -.
DR PhylomeDB; Q9UHR4; -.
DR TreeFam; TF325648; -.
DR PathwayCommons; Q9UHR4; -.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR SignaLink; Q9UHR4; -.
DR SIGNOR; Q9UHR4; -.
DR BioGRID-ORCS; 55971; 19 hits in 1086 CRISPR screens.
DR ChiTaRS; BAIAP2L1; human.
DR GeneWiki; BAIAP2L1; -.
DR GenomeRNAi; 55971; -.
DR Pharos; Q9UHR4; Tbio.
DR PRO; PR:Q9UHR4; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UHR4; protein.
DR Bgee; ENSG00000006453; Expressed in pancreatic ductal cell and 181 other tissues.
DR Genevisible; Q9UHR4; HS.
DR GO; GO:0005912; C:adherens junction; HDA:BHF-UCL.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; HDA:BHF-UCL.
DR GO; GO:0070064; F:proline-rich region binding; IDA:UniProtKB.
DR GO; GO:0051764; P:actin crosslink formation; IBA:GO_Central.
DR GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IMP:UniProtKB.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:UniProtKB.
DR GO; GO:0046626; P:regulation of insulin receptor signaling pathway; IEA:InterPro.
DR GO; GO:0009617; P:response to bacterium; IDA:UniProtKB.
DR CDD; cd11913; SH3_BAIAP2L1; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR IDEAL; IID00331; -.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR013606; I-BAR_dom.
DR InterPro; IPR027681; IRSp53/IRTKS/Pinkbar.
DR InterPro; IPR030060; IRTKS.
DR InterPro; IPR035592; IRTKS_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14206; PTHR14206; 1.
DR PANTHER; PTHR14206:SF4; PTHR14206:SF4; 1.
DR Pfam; PF08397; IMD; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51338; IMD; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..511
FT /note="Brain-specific angiogenesis inhibitor 1-associated
FT protein 2-like protein 1"
FT /id="PRO_0000247854"
FT DOMAIN 1..249
FT /note="IMD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00668"
FT DOMAIN 339..402
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 302..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..511
FT /note="Binds F-actin"
FT COILED 115..154
FT /evidence="ECO:0000255"
FT MOD_RES 248
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 257
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 412
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBJ3"
FT VARIANT 460
FT /note="S -> T (in dbSNP:rs2269966)"
FT /id="VAR_033515"
FT MUTAGEN 141
FT /note="K->E: Loss ability to induce the formation of actin
FT clusters; when associated with K-142; R-145 and K-146."
FT /evidence="ECO:0000269|PubMed:17430976"
FT MUTAGEN 142
FT /note="K->E: Loss ability to induce the formation of actin
FT clusters; when associated with K-141; R-145 and K-146."
FT /evidence="ECO:0000269|PubMed:17430976"
FT MUTAGEN 145
FT /note="R->E: Loss ability to induce the formation of actin
FT clusters; when associated with K-141; K-142 and K-146."
FT /evidence="ECO:0000269|PubMed:17430976"
FT MUTAGEN 146
FT /note="K->E: Loss ability to induce the formation of actin
FT clusters; when associated with K-141; K-142 and R-145."
FT /evidence="ECO:0000269|PubMed:17430976"
FT MUTAGEN 488..511
FT /note="Missing: Loss ability to induce the formation of
FT actin clusters; induce the formation of long filopodia."
FT /evidence="ECO:0000269|PubMed:17430976"
FT CONFLICT 456
FT /note="A -> V (in Ref. 6; BAB15671)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="S -> F (in Ref. 6; BAB15671)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="A -> V (in Ref. 6; BAB15671)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="A -> V (in Ref. 6; BAB15671)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="S -> F (in Ref. 6; BAB15671)"
FT /evidence="ECO:0000305"
FT STRAND 343..348
FT /evidence="ECO:0007829|PDB:2KXC"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:2KXC"
FT STRAND 366..373
FT /evidence="ECO:0007829|PDB:2KXC"
FT STRAND 378..386
FT /evidence="ECO:0007829|PDB:2KXC"
FT STRAND 389..393
FT /evidence="ECO:0007829|PDB:2KXC"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:2KXC"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:2KXC"
SQ SEQUENCE 511 AA; 56883 MW; C2304C4444B02F02 CRC64;
MSRGPEEVNR LTESTYRNVM EQFNPGLRNL INLGKNYEKA VNAMILAGKA YYDGVAKIGE
IATGSPVSTE LGHVLIEISS THKKLNESLD ENFKKFHKEI IHELEKKIEL DVKYMNATLK
RYQTEHKNKL ESLEKSQAEL KKIRRKSQGS RNALKYEHKE IEYVETVTSR QSEIQKFIAD
GCKEALLEEK RRFCFLVDKH CGFANHIHYY HLQSAELLNS KLPRWQETCV DAIKVPEKIM
NMIEEIKTPA STPVSGTPQA SPMIERSNVV RKDYDTLSKC SPKMPPAPSG RAYTSPLIDM
FNNPATAAPN SQRVNNSTGT SEDPSLQRSV SVATGLNMMK KQKVKTIFPH TAGSNKTLLS
FAQGDVITLL IPEEKDGWLY GEHDVSKARG WFPSSYTKLL EENETEAVTV PTPSPTPVRS
ISTVNLSENS SVVIPPPDYL ECLSMGAAAD RRADSARTTS TFKAPASKPE TAAPNDANGT
AKPPFLSGEN PFATVKLRPT VTNDRSAPII R
