NRBP2_MOUSE
ID NRBP2_MOUSE Reviewed; 499 AA.
AC Q91V36; Q8R3M0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Nuclear receptor-binding protein 2;
GN Name=Nrbp2 {ECO:0000312|EMBL:AAH12437.1, ECO:0000312|MGI:MGI:2385017};
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 [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 [2] {ECO:0000312|EMBL:AAH12437.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 191-499.
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH11468.1}, and
RC FVB/N {ECO:0000312|EMBL:AAH12437.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH12437.1};
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=18619852; DOI=10.1016/j.mcn.2008.05.013;
RA Larsson J., Forsberg M., Brannvall K., Zhang X.Q., Enarsson M., Hedborg F.,
RA Forsberg-Nilsson K.;
RT "Nuclear receptor binding protein 2 is induced during neural progenitor
RT differentiation and affects cell survival.";
RL Mol. Cell. Neurosci. 39:32-39(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-407 AND THR-409, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and 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: May regulate apoptosis of neural progenitor cells during
CC their differentiation. {ECO:0000269|PubMed:18619852}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18619852}.
CC -!- TISSUE SPECIFICITY: Expressed in Purkinje cells of the cerebellum and
CC neurons in the CA3 region of the hippocampus. Also detected in non-
CC neural tissues including mesenchymal layer adjacent to epithelium in
CC developing bronchi of the lung, the epithelium of the stomach as well
CC as cells in the liver. {ECO:0000269|PubMed:18619852}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the cerebral cortex at 14 dpc (at
CC protein level). Expressed in the walls of the third and fourth
CC ventricles, and in the hippocampus during development.
CC {ECO:0000269|PubMed:18619852}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH11468.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH12437.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC116487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011468; AAH11468.1; ALT_INIT; mRNA.
DR EMBL; BC012437; AAH12437.1; ALT_INIT; mRNA.
DR EMBL; BC025042; AAH25042.1; -; mRNA.
DR CCDS; CCDS27561.2; -.
DR RefSeq; NP_659096.1; NM_144847.1.
DR RefSeq; XP_006520835.1; XM_006520772.3.
DR AlphaFoldDB; Q91V36; -.
DR SMR; Q91V36; -.
DR STRING; 10090.ENSMUSP00000019516; -.
DR iPTMnet; Q91V36; -.
DR PhosphoSitePlus; Q91V36; -.
DR jPOST; Q91V36; -.
DR MaxQB; Q91V36; -.
DR PaxDb; Q91V36; -.
DR PeptideAtlas; Q91V36; -.
DR PRIDE; Q91V36; -.
DR ProteomicsDB; 293727; -.
DR Antibodypedia; 28122; 205 antibodies from 26 providers.
DR DNASU; 223649; -.
DR Ensembl; ENSMUST00000228366; ENSMUSP00000154287; ENSMUSG00000075590.
DR UCSC; uc007wil.1; mouse.
DR MGI; MGI:2385017; Nrbp2.
DR VEuPathDB; HostDB:ENSMUSG00000075590; -.
DR eggNOG; KOG1266; Eukaryota.
DR GeneTree; ENSGT00940000160430; -.
DR InParanoid; Q91V36; -.
DR OMA; KVFKAHE; -.
DR OrthoDB; 695382at2759; -.
DR PhylomeDB; Q91V36; -.
DR BioGRID-ORCS; 223649; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Nrbp2; mouse.
DR PRO; PR:Q91V36; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q91V36; protein.
DR Bgee; ENSMUSG00000075590; Expressed in superior frontal gyrus and 206 other tissues.
DR ExpressionAtlas; Q91V36; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0016242; P:negative regulation of macroautophagy; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IEP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR CDD; cd14035; PK_MADML; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR042697; NRBP2_PK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Neurogenesis; Phosphoprotein; Reference proteome.
FT CHAIN 1..499
FT /note="Nuclear receptor-binding protein 2"
FT /id="PRO_0000225609"
FT DOMAIN 36..304
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 407
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 409
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 200
FT /note="A -> V (in Ref. 2; AAH11468)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 499 AA; 57348 MW; B46B19E047549170 CRC64;
MAAPEPAPRR GREREREDES EDESDILEES PCGRWQKRRE QVNQGNMPGI QSTFLAMDTE
EGVEVVWNEL HFGDRKAFAA HEEKIQTMFE QLALVDHPNI VKLHKYWLDA SEARARVIFI
TEYVSSGSLK QFLKKTKKNH KAMNARAWKR WCTQILSALS FLHACSPPII HGNLTSDTIF
IQHNGLIKIG SVWYRIFSNA LPDDLRSPIR AEREELRNLH FFPPEYGEVN DGTAVDIFSF
GMCALEMAVL EIQANGDTRV TEEAIARARH SLSDPNMREF ILSCLARDPA RRPSAHNLLF
HRVLFEVHSL KLLAAHCFIQ HQYLMPENVV EEKTKAMDLH AVLAEMPQPH GPPMQWRYSE
VSFLELDKFL EDVRNGIYPL MNFAAARPLG LPRVLAPPPE EAQKAKTPTP EPFDSETRKV
VQMQCNLERS EDKARWHLTL LLVLEDRLHR QLTYDLLPTD SAQDLAAELV HYGFLHEDDR
TKLAAFLETT FLKYRGTQA