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 27-MAR-2024, entry version 194. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 132. DR DIP; DIP-53820N; -. DR IntAct; Q9UHR4; 66. DR MINT; Q9UHR4; -. DR STRING; 9606.ENSP00000005260; -. DR GlyGen; Q9UHR4; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q9UHR4; -. DR MetOSite; Q9UHR4; -. DR PhosphoSitePlus; Q9UHR4; -. DR SwissPalm; Q9UHR4; -. DR BioMuta; BAIAP2L1; -. DR DMDM; 74735022; -. DR EPD; Q9UHR4; -. DR jPOST; Q9UHR4; -. DR MassIVE; Q9UHR4; -. DR MaxQB; Q9UHR4; -. DR PaxDb; 9606-ENSP00000005260; -. DR PeptideAtlas; Q9UHR4; -. DR ProteomicsDB; 84402; -. DR Pumba; Q9UHR4; -. DR Antibodypedia; 16001; 232 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 AGR; HGNC:21649; -. 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; KNTSTFR; -. DR OrthoDB; 3059844at2759; -. 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; 20 hits in 1164 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 182 other cell types or tissues. 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:0030838; P:positive regulation of actin filament polymerization; IDA:UniProtKB. DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB. DR CDD; cd07645; I-BAR_IMD_BAIAP2L1; 1. DR CDD; cd11913; SH3_BAIAP2L1; 1. DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR IDEAL; IID00331; -. DR InterPro; IPR027267; AH/BAR_dom_sf. DR InterPro; IPR030060; Baiap2l1_I-BAR_dom. DR InterPro; IPR013606; I-BAR_dom. DR InterPro; IPR027681; IRSp53/IRTKS/Pinkbar. DR InterPro; IPR035592; IRTKS_SH3. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR14206; BRAIN-SPECIFIC ANGIOGENESIS INHIBITOR 1-ASSOCIATED PROTEIN 2; 1. DR PANTHER; PTHR14206:SF4; BRAIN-SPECIFIC ANGIOGENESIS INHIBITOR 1-ASSOCIATED PROTEIN 2-LIKE PROTEIN 1; 1. DR Pfam; PF08397; IMD; 1. DR Pfam; PF14604; SH3_9; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF103657; BAR/IMD domain-like; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS51338; IMD; 1. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q9UHR4; HS. 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 //