BANK1_MOUSE
ID BANK1_MOUSE Reviewed; 783 AA.
AC Q80VH0; E9QMV3; Q3U178; Q8BRV6; Q8BRY8;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=B-cell scaffold protein with ankyrin repeats;
DE AltName: Full=Protein AVIEF;
GN Name=Bank1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Lymph node;
RA Vu H.L., Nguyen H.H., Mestecky J.;
RT "AVIEF sequence.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Aorta, Spleen, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=11782428; DOI=10.1093/emboj/21.1.83;
RA Yokoyama K., Su I., Tezuka T., Yasuda T., Mikoshiba K., Tarakhovsky A.,
RA Yamamoto T.;
RT "BANK regulates BCR-induced calcium mobilization by promoting tyrosine
RT phosphorylation of IP3 receptor.";
RL EMBO J. 21:83-92(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-649, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in B-cell receptor (BCR)-induced Ca(2+) mobilization
CC from intracellular stores. Promotes Lyn-mediated phosphorylation of IP3
CC receptors 1 and 2 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with LYN, ITPR1 and ITPR2. {ECO:0000250}.
CC -!- INTERACTION:
CC Q80VH0; P42227: Stat3; NbExp=4; IntAct=EBI-646949, EBI-602878;
CC -!- TISSUE SPECIFICITY: Specifically expressed in spleen. Highly expressed
CC in immature B-cells and recirculating B-cells, and at low levels in
CC pro-B and pre-B cells. {ECO:0000269|PubMed:11782428}.
CC -!- PTM: Phosphorylated on tyrosines upon BCR activation. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO13613.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE33622.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE33622.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY178734; AAO13613.1; ALT_INIT; mRNA.
DR EMBL; AK041039; BAC30794.1; -; mRNA.
DR EMBL; AK041242; BAC30875.1; -; mRNA.
DR EMBL; AK156201; BAE33622.1; ALT_SEQ; mRNA.
DR EMBL; AC101978; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC166331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS38645.1; -.
DR RefSeq; NP_001028522.2; NM_001033350.3.
DR AlphaFoldDB; Q80VH0; -.
DR SMR; Q80VH0; -.
DR BioGRID; 232385; 4.
DR IntAct; Q80VH0; 2.
DR STRING; 10090.ENSMUSP00000035484; -.
DR iPTMnet; Q80VH0; -.
DR PhosphoSitePlus; Q80VH0; -.
DR EPD; Q80VH0; -.
DR MaxQB; Q80VH0; -.
DR PaxDb; Q80VH0; -.
DR PRIDE; Q80VH0; -.
DR ProteomicsDB; 273536; -.
DR Antibodypedia; 51626; 110 antibodies from 26 providers.
DR Ensembl; ENSMUST00000041577; ENSMUSP00000035484; ENSMUSG00000037922.
DR GeneID; 242248; -.
DR KEGG; mmu:242248; -.
DR UCSC; uc008rmd.1; mouse.
DR CTD; 55024; -.
DR MGI; MGI:2442120; Bank1.
DR VEuPathDB; HostDB:ENSMUSG00000037922; -.
DR eggNOG; ENOG502REIM; Eukaryota.
DR GeneTree; ENSGT00390000008787; -.
DR HOGENOM; CLU_012993_1_0_1; -.
DR InParanoid; Q80VH0; -.
DR OMA; KINIVHH; -.
DR OrthoDB; 280243at2759; -.
DR PhylomeDB; Q80VH0; -.
DR TreeFam; TF328570; -.
DR BioGRID-ORCS; 242248; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Bank1; mouse.
DR PRO; PR:Q80VH0; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q80VH0; protein.
DR Bgee; ENSMUSG00000037922; Expressed in peripheral lymph node and 85 other tissues.
DR ExpressionAtlas; Q80VH0; baseline and differential.
DR Genevisible; Q80VH0; MM.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0043274; F:phospholipase binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
DR GO; GO:0035591; F:signaling adaptor activity; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0042113; P:B cell activation; ISO:MGI.
DR GO; GO:0000165; P:MAPK cascade; IMP:MGI.
DR GO; GO:0050869; P:negative regulation of B cell activation; IGI:MGI.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IMP:MGI.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; IGI:MGI.
DR GO; GO:0045947; P:negative regulation of translational initiation; IMP:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0043491; P:protein kinase B signaling; IGI:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR Gene3D; 3.40.50.10140; -; 1.
DR InterPro; IPR017893; DBB_domain.
DR InterPro; IPR041340; PIK3AP1_TIR.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR Pfam; PF14545; DBB; 1.
DR Pfam; PF18567; TIR_3; 1.
DR SMART; SM01282; DBB; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS51376; DBB; 1.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW ANK repeat; B-cell activation; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..783
FT /note="B-cell scaffold protein with ankyrin repeats"
FT /id="PRO_0000251928"
FT DOMAIN 25..153
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT DOMAIN 199..326
FT /note="DBB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00707"
FT REPEAT 341..370
FT /note="ANK 1"
FT REPEAT 377..407
FT /note="ANK 2"
FT REGION 1..154
FT /note="Interaction with ITPR2"
FT /evidence="ECO:0000250"
FT REGION 422..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..581
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 649
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 63
FT /note="H -> R (in Ref. 2; BAC30875)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="F -> L (in Ref. 1; AAO13613 and 2; BAE33622)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="A -> M (in Ref. 1; AAO13613 and 2; BAE33622)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="E -> V (in Ref. 2; BAC30875)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="S -> P (in Ref. 1; AAO13613)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="L -> V (in Ref. 2; BAC30875)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 783 AA; 89406 MW; 05597B51DE45C65C CRC64;
MLPVASGTRG STQDLFQVGL APPGNAKDIL LLYEEDAEEW ALYLREIFMR VVEREAILLY
PLHSFSSSHL EMLNFYAYKC KLLIISNSLL KDLTPKKCQF LEKILHSTGN VVTLLCGMES
SDPFYQLLSI PRKRWEISTE QDPDGYISVI RQILDQGPED YLEVSIPTDS RAKYPEDTSG
QKGTDVLASL RPSVPRVLVL PGEIPCEKPG EIFILLKDEL IGEILEVEFI STNKRLRARP
ARWNKSVWHM KAADFPAGSV TVNIHCDGII KATTEIKYCS AAKATESPFR VSDPGKSLCQ
KSIEELDNVL ASIFKREIPY YEFKHLQAET YPQKERTHTT ELPTLLHCAA KFGLKNLALH
LLQCSGATRA ARMKATDGSD LLHIAERHGH EELKEVFEDF LSQNTGRNSK QENDYEEDVI
SFSTYSPSMP SPASLHELRK THRRNTDRSE EPERSVEMKE EEAGAEARRS LSEGERESSE
NQYDDLYVFI PGFDTEGNSE EPLPHCRPPL LPPRPGTAAS QLERPHFTSQ GKVLEDQMER
SQNWNDLNAR PETREESSRE EKKEEAQEEE EEEENPYAFA ETEDNEYDLI LASKSVKKRT
GNRSFIINRP PAPTPRPTHI PPKEETTPYI AQVFQQKAAR RQSDGDKFYS LPKKPDKTRM
EGPTFPSTRD YLTTGQEELI LLQERVKNGK MSVDEALEKF KHWQMGKSGL EMIQQEKLRQ
LRDNIIGKRP EDENAYDKLT IVHHPSGNTA HNENMLYNSP FNSKFPARIQ VEKEFGFCCK
KDH
