BASP1_MOUSE
ID BASP1_MOUSE Reviewed; 226 AA.
AC Q91XV3;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Brain acid soluble protein 1;
DE AltName: Full=22 kDa neuronal tissue-enriched acidic protein;
DE AltName: Full=Neuronal axonal membrane protein NAP-22;
GN Name=Basp1; Synonyms=Nap22;
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 [GENOMIC DNA].
RC STRAIN=C57BL/6J X CBA/J; TISSUE=Spleen;
RA Hamada K., Sokawa Y., Maekawa S.;
RT "Mouse NAP-22 (22 kDa neuronal tissue-enriched acidic protein) gene.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 26-52; 92-123 AND 147-225, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36 AND SER-92, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31; THR-36; SER-40; SER-92;
RP SER-128; SER-169; SER-173 AND SER-192, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC 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 -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Cell projection,
CC growth cone. Note=Associated with the membranes of growth cones that
CC form the tips of elongating axons.
CC -!- SIMILARITY: Belongs to the BASP1 family. {ECO:0000305}.
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DR EMBL; AB046714; BAB62404.1; -; Genomic_DNA.
DR CCDS; CCDS27398.1; -.
DR RefSeq; NP_081671.1; NM_027395.2.
DR AlphaFoldDB; Q91XV3; -.
DR BioGRID; 213993; 17.
DR IntAct; Q91XV3; 7.
DR MINT; Q91XV3; -.
DR STRING; 10090.ENSMUSP00000053943; -.
DR iPTMnet; Q91XV3; -.
DR PhosphoSitePlus; Q91XV3; -.
DR SwissPalm; Q91XV3; -.
DR EPD; Q91XV3; -.
DR jPOST; Q91XV3; -.
DR MaxQB; Q91XV3; -.
DR PaxDb; Q91XV3; -.
DR PeptideAtlas; Q91XV3; -.
DR PRIDE; Q91XV3; -.
DR ProteomicsDB; 273598; -.
DR Antibodypedia; 54132; 162 antibodies from 26 providers.
DR DNASU; 70350; -.
DR Ensembl; ENSMUST00000058845; ENSMUSP00000053943; ENSMUSG00000045763.
DR GeneID; 70350; -.
DR KEGG; mmu:70350; -.
DR UCSC; uc007vix.2; mouse.
DR CTD; 10409; -.
DR MGI; MGI:1917600; Basp1.
DR VEuPathDB; HostDB:ENSMUSG00000045763; -.
DR eggNOG; ENOG502RXJZ; Eukaryota.
DR GeneTree; ENSGT00730000111450; -.
DR HOGENOM; CLU_093511_0_0_1; -.
DR InParanoid; Q91XV3; -.
DR OMA; QLKRGFK; -.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR BioGRID-ORCS; 70350; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Basp1; mouse.
DR PRO; PR:Q91XV3; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q91XV3; protein.
DR Bgee; ENSMUSG00000045763; Expressed in perirhinal cortex and 252 other tissues.
DR ExpressionAtlas; Q91XV3; baseline and differential.
DR Genevisible; Q91XV3; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0008180; C:COP9 signalosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0016363; C:nuclear matrix; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0016605; C:PML body; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0072112; P:podocyte differentiation; IDA:UniProtKB.
DR InterPro; IPR008408; BASP1.
DR PANTHER; PTHR23212; PTHR23212; 1.
DR Pfam; PF05466; BASP1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Direct protein sequencing; Isopeptide bond;
KW Lipoprotein; Membrane; Myristate; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P80724"
FT CHAIN 2..226
FT /note="Brain acid soluble protein 1"
FT /id="PRO_0000142896"
FT REGION 1..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 36
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05175"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P80723"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P80723"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P80723"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P80723"
FT CROSSLNK 25
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P80723"
FT CROSSLNK 86
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P80723"
FT CROSSLNK 159
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P80723"
SQ SEQUENCE 226 AA; 22087 MW; B41CCAAB447C705D CRC64;
MGGKLSKKKK GYNVNDEKAK DKDKKAEGAG TEEEGTPKES EPQAAADATE VKESTEEKPK
DAADGEAKAE EKEADKAAAA KEEAPKAEPE KSEGAAEEQP EPAPAPEQEA AAPGPAAGGE
APKAGEASAE STGAADGAAP EEGEAKKTEA PAAAGPEAKS DAAPAASDSK PSSAEPAPSS
KETPAASEAP SSAAKAPAPA APAAAEPQAE APAAAASSEQ SVAVKE
