NRBP_MOUSE
ID NRBP_MOUSE Reviewed; 535 AA.
AC Q99J45; Q8BL77;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Nuclear receptor-binding protein;
DE AltName: Full=HLS7-interacting protein kinase;
DE AltName: Full=MLF1 adapter molecule;
GN Name=Nrbp1; Synonyms=Madm, Nrbp;
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] {ECO:0000305, ECO:0000312|EMBL:AAK97260.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION,
RP PHOSPHORYLATION, HOMODIMERIZATION, AND INTERACTION WITH MLF1.
RC STRAIN=129 {ECO:0000312|EMBL:AAK97261.1}, and
RC BDF1 {ECO:0000312|EMBL:AAK97260.1};
RX PubMed=12176995; DOI=10.1074/jbc.m206041200;
RA Lim R., Winteringham L.N., Williams J.H., McCulloch R.K., Ingley E.,
RA Tiao J.Y.-H., Lalonde J.-P., Tsai S., Tilbrook P.A., Sun Y., Wu X.,
RA Morris S.W., Klinken S.P.;
RT "MADM, a novel adaptor protein that mediates phosphorylation of the 14-3-3
RT binding site of myeloid leukemia factor 1.";
RL J. Biol. Chem. 277:40997-41008(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
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] {ECO:0000312|EMBL:AAH04756.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129 {ECO:0000312|EMBL:AAH04756.1}, and
RC FVB/N {ECO:0000312|EMBL:AAH18463.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH04756.1};
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-431 AND THR-433, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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 play a role in subcellular trafficking between the
CC endoplasmic reticulum and Golgi apparatus through interactions with the
CC Rho-type GTPases. {ECO:0000250|UniProtKB:Q9UHY1}.
CC -!- SUBUNIT: Homodimer. Binds to MLF1, recruiting a serine kinase which
CC phosphorylates both itself and MLF1. Phosphorylated MLF1 binds to YWHAZ
CC and is retained in the cytoplasm. {ECO:0000269|PubMed:12176995}.
CC -!- INTERACTION:
CC Q99J45; Q9QWV4: Mlf1; NbExp=5; IntAct=EBI-767484, EBI-354765;
CC Q99J45; Q99J45: Nrbp1; NbExp=2; IntAct=EBI-767484, EBI-767484;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:12176995}. Endomembrane system
CC {ECO:0000269|PubMed:12176995}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:12176995}. Note=Colocalizes with activated RAC3 to
CC endomembranes and at the cell periphery in lamellipodia.
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 ---------------------------------------------------------------------------
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; AF302138; AAK97260.1; -; mRNA.
DR EMBL; AF302139; AAK97261.1; -; Genomic_DNA.
DR EMBL; AK046142; BAC32612.1; -; mRNA.
DR EMBL; BC004756; AAH04756.1; -; mRNA.
DR EMBL; BC018463; AAH18463.1; -; mRNA.
DR CCDS; CCDS19180.1; -.
DR RefSeq; NP_671734.1; NM_147201.2.
DR AlphaFoldDB; Q99J45; -.
DR SMR; Q99J45; -.
DR BioGRID; 228688; 7.
DR IntAct; Q99J45; 3.
DR MINT; Q99J45; -.
DR STRING; 10090.ENSMUSP00000031034; -.
DR iPTMnet; Q99J45; -.
DR PhosphoSitePlus; Q99J45; -.
DR EPD; Q99J45; -.
DR jPOST; Q99J45; -.
DR MaxQB; Q99J45; -.
DR PaxDb; Q99J45; -.
DR PRIDE; Q99J45; -.
DR ProteomicsDB; 253012; -.
DR Antibodypedia; 28488; 407 antibodies from 29 providers.
DR DNASU; 192292; -.
DR Ensembl; ENSMUST00000031034; ENSMUSP00000031034; ENSMUSG00000029148.
DR GeneID; 192292; -.
DR KEGG; mmu:192292; -.
DR UCSC; uc008wxt.1; mouse.
DR CTD; 29959; -.
DR MGI; MGI:2183436; Nrbp1.
DR VEuPathDB; HostDB:ENSMUSG00000029148; -.
DR eggNOG; KOG1266; Eukaryota.
DR GeneTree; ENSGT00940000155605; -.
DR HOGENOM; CLU_024273_0_0_1; -.
DR InParanoid; Q99J45; -.
DR PhylomeDB; Q99J45; -.
DR TreeFam; TF315519; -.
DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR BioGRID-ORCS; 192292; 18 hits in 77 CRISPR screens.
DR ChiTaRS; Nrbp1; mouse.
DR PRO; PR:Q99J45; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q99J45; protein.
DR Bgee; ENSMUSG00000029148; Expressed in embryonic post-anal tail and 267 other tissues.
DR ExpressionAtlas; Q99J45; baseline and differential.
DR Genevisible; Q99J45; MM.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0012505; C:endomembrane system; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell projection; Cytoplasm; Membrane; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UHY1"
FT CHAIN 2..535
FT /note="Nuclear receptor-binding protein"
FT /id="PRO_0000086451"
FT DOMAIN 68..327
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHY1"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHY1"
FT MOD_RES 431
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 433
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 220
FT /note="S -> SVFHRIFAN (in Ref. 2; BAC32612)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="V -> G (in Ref. 2; BAC32612)"
FT /evidence="ECO:0000305"
FT CONFLICT 508..510
FT /note="TSL -> SSV (in Ref. 2; BAC32612)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="T -> S (in Ref. 2; BAC32612)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="S -> VVELT (in Ref. 2; BAC32612)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 59866 MW; 85DD5F6FC25C5AB7 CRC64;
MSEGESQTVV SSGSDPKVES SSLAPGLTSV SPPVTSTTSA ASPEEEEESE DESEILEESP
CGRWQKRREE VNQRNVPGID SAYLAMDTEE GVEVVWNEVQ FSERKNYKLQ EEKVRAVFDN
LIQLEHLNIV KFHKYWADVK ENKARVIFIT EYMSSGSLKQ FLKKTKKNHK TMNEKAWKRW
CTQILSALSY LHSCDPPIIH GNLTCDTIFI QHNGLIKIGS VAPDTINNHV KTCREEQKNL
HFFAPEYGEV TNVTTAVDIY SFGMCALEMA VLEIQGNGES SYVPQEAISS AIQLLEDSLQ
REFIQKCLQS EPARRPTARE LLFHPALFEV PSLKLLAAHC IVGHQHMIPE NALEEITKNM
DTSAVLAEIP AGPGREPVQT LYSQSPALEL DKFLEDVRNG IYPLTAFGLP RPQQPQQEEV
TSPVVPPSVK TPTPEPAEVE TRKVVLMQCN IESVEEGVKH HLTLLLKLED KLNRHLSCDL
MPNESIPDLA AELVQLGFIS EADQSRLTSL LEETLNKFNF TRNSTLNTAT VTVSS
