ID   IGB1B_MOUSE             Reviewed;         343 AA.
AC   Q9QZ29;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Immunoglobulin-binding protein 1b;
DE   AltName: Full=Alpha 4-b protein;
DE   AltName: Full=CD79a-binding protein 1b;
DE   AltName: Full=Protein alpha-4-b;
GN   Name=Igbp1b;
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=Brain;
RX   PubMed=10491115; DOI=10.1046/j.1432-1327.1999.00571.x;
RA   Maeda K., Inui S., Tanaka H., Sakaguchi N.;
RT   "A new member of the alpha4-related molecule (alpha4-b) that binds to the
RT   protein phosphatase 2A is expressed selectively in the brain and testis.";
RL   Eur. J. Biochem. 264:702-706(1999).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
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: Associated to surface IgM-receptor; may be involved in signal
CC       transduction (By similarity). May be involved in regulation of the
CC       catalytic activity of type 2A-related serine/threonine phosphatases.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Associates with PP2A-alpha catalytic subunit.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed selectively in brain and testis.
CC   -!- SIMILARITY: Belongs to the IGBP1/TAP42 family. {ECO:0000305}.
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DR   EMBL; AJ010637; CAB60142.1; -; mRNA.
DR   CCDS; CCDS20670.1; -.
DR   AlphaFoldDB; Q9QZ29; -.
DR   SMR; Q9QZ29; -.
DR   STRING; 10090.ENSMUSP00000050818; -.
DR   iPTMnet; Q9QZ29; -.
DR   PhosphoSitePlus; Q9QZ29; -.
DR   MaxQB; Q9QZ29; -.
DR   PaxDb; Q9QZ29; -.
DR   PeptideAtlas; Q9QZ29; -.
DR   PRIDE; Q9QZ29; -.
DR   ProteomicsDB; 267290; -.
DR   UCSC; uc009enq.2; mouse.
DR   MGI; MGI:1354380; Igbp1b.
DR   eggNOG; KOG2830; Eukaryota.
DR   InParanoid; Q9QZ29; -.
DR   PhylomeDB; Q9QZ29; -.
DR   PRO; PR:Q9QZ29; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q9QZ29; protein.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0019208; F:phosphatase regulator activity; TAS:MGI.
DR   GO; GO:0051721; F:protein phosphatase 2A binding; IBA:GO_Central.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; ISO:MGI.
DR   GO; GO:0042113; P:B cell activation; IEA:UniProtKB-KW.
DR   GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR   GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0035303; P:regulation of dephosphorylation; IBA:GO_Central.
DR   GO; GO:0060632; P:regulation of microtubule-based movement; ISO:MGI.
DR   GO; GO:0070555; P:response to interleukin-1; ISO:MGI.
DR   GO; GO:0034612; P:response to tumor necrosis factor; ISO:MGI.
DR   GO; GO:0007165; P:signal transduction; TAS:MGI.
DR   Gene3D; 1.25.40.540; -; 1.
DR   InterPro; IPR038511; TAP42/TAP46-like_sf.
DR   InterPro; IPR007304; TAP46-like.
DR   PANTHER; PTHR10933; PTHR10933; 1.
DR   Pfam; PF04177; TAP42; 1.
PE   1: Evidence at protein level;
KW   B-cell activation; Cytoplasm; Reference proteome.
FT   CHAIN           1..343
FT                   /note="Immunoglobulin-binding protein 1b"
FT                   /id="PRO_0000218621"
FT   REGION          278..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..298
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   343 AA;  39246 MW;  E0834092C433F3AD CRC64;
     MASFTEEMQK PKLRELLETG IQLLEEVEAA TQPTGSKPIQ EKVREALKLL EKASDMLSQL
     DLFSRNEDWE EIASADLKYL MLPALKGALT LKLVGSSKRL GLLQDAREHF MNFLTQTHSY
     HVADFQLPWA QSSSMEGNPA ATSDAQEQNL VAMASQRQTK IQRYKQKKAV EQRLSSLKSA
     VESGQADDER VREYYLLQLR RWISISLDEI ENIEQEIEIL RERDSLGETS ASRSSPQERP
     PLKPFVLTRS VAQAQVFGAG YPSLATMTVN DWYEQRQKNE VSPTLQEAEK QAPPSETFTV
     SEKEEPDLEQ KEDEDENALH RMQEWDDWKD THPRGYGNRQ NMG