ID NRBP_HUMAN Reviewed; 535 AA. AC Q9UHY1; B3KV40; D6W558; Q53FZ5; Q96SU3; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 192. DE RecName: Full=Nuclear receptor-binding protein; GN Name=NRBP1; Synonyms=BCON3 {ECO:0000312|EMBL:AAF21967.1}, NRBP; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF21967.1} RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX PubMed=10843813; DOI=10.1006/geno.2000.6167; RA Hooper J.D., Baker E., Ogbourne S.M., Sutherland G.R., Antalis T.M.; RT "Cloning of the cDNA and localization of the gene encoding human NRBP, a RT ubiquitously expressed, multidomain putative adapter protein."; RL Genomics 66:113-118(2000). RN [2] {ECO:0000312|EMBL:BAA91993.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Neuron {ECO:0000312|EMBL:BAB55185.1}, Placenta RC {ECO:0000312|EMBL:BAA91993.1}, and Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [4] {ECO:0000312|EMBL:CAB66617.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney {ECO:0000312|EMBL:BAD96856.1}; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000305, ECO:0000312|EMBL:AAY14847.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [6] {ECO:0000312|EMBL:CAB66617.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000312|EMBL:AAH01221.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung {ECO:0000312|EMBL:AAH01221.1}; 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 [8] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-426, FUNCTION, SUBCELLULAR LOCATION, RP PHOSPHORYLATION, AND INTERACTION WITH RAC3. RX PubMed=11956649; RA De Langhe S., Haataja L., Senadheera D., Groffen J., Heisterkamp N.; RT "Interaction of the small GTPase Rac3 with NRBP, a protein with a kinase- RT homology domain."; RL Int. J. Mol. Med. 9:451-459(2002). RN [9] {ECO:0000305} RP FUNCTION, AND INTERACTION WITH DENGUE VIRUS TYPE 2 NS3. RX PubMed=15084397; DOI=10.1016/j.virusres.2004.01.025; RA Chua J.J.E., Ng M.M.L., Chow V.T.K.; RT "The non-structural 3 (NS3) protein of dengue virus type 2 interacts with RT human nuclear receptor binding protein and is associated with alterations RT in membrane structure."; RL Virus Res. 102:151-163(2004). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-433, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-433, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-433, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [19] RP INTERACTION WITH ELOB; ELOC; TSC22D2; TSC22D4 AND SALL4. RX PubMed=22510880; DOI=10.1038/emboj.2012.91; RA Wilson C.H., Crombie C., van der Weyden L., Poulogiannis G., Rust A.G., RA Pardo M., Gracia T., Yu L., Choudhary J., Poulin G.B., McIntyre R.E., RA Winton D.J., March H.N., Arends M.J., Fraser A.G., Adams D.J.; RT "Nuclear receptor binding protein 1 regulates intestinal progenitor cell RT homeostasis and tumour formation."; RL EMBO J. 31:2486-2497(2012). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-433, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [22] RP VARIANTS [LARGE SCALE ANALYSIS] ILE-365; LEU-432 AND ARG-460. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Required for embryonic development (By similarity). Plays a CC role in intestinal epithelial cell fate and proliferation, thereby CC involved in the architectural development of the intestine potentially CC via the regulation of Wnt-responsive genes (By similarity). May play a CC role in subcellular trafficking between the endoplasmic reticulum and CC Golgi apparatus through interactions with the Rho-type GTPases CC (PubMed:11956649). Binding to the NS3 protein of dengue virus type 2 CC appears to subvert this activity into the alteration of the CC intracellular membrane structure associated with flaviviral replication CC (PubMed:15084397). {ECO:0000250|UniProtKB:Q99J45, CC ECO:0000269|PubMed:11956649, ECO:0000269|PubMed:15084397}. CC -!- SUBUNIT: Homodimer (By similarity). Binds to MLF1, recruiting a serine CC kinase which phosphorylates both itself and MLF1 (By similarity). CC Phosphorylated MLF1 binds to YWHAZ and is retained in the cytoplasm (By CC similarity). Interacts with ELOC/TCEB1, ELOB/TCEB2, TSC22D2 and TSC22D4 CC (PubMed:22510880). Interacts with the Elongin BC E3 ubiquitin ligase CC complex via its interaction with ELOB/TCEB2 and ELOC/TCEB1 CC (PubMed:22510880). Interacts with SALL4 (PubMed:22510880). CC {ECO:0000250|UniProtKB:Q99J45, ECO:0000269|PubMed:22510880}. CC -!- INTERACTION: CC Q9UHY1; Q96LR7: C2orf50; NbExp=3; IntAct=EBI-749731, EBI-10290932; CC Q9UHY1; P60763: RAC3; NbExp=3; IntAct=EBI-749731, EBI-767084; CC Q9UHY1; Q8N9S9-2: SNX31; NbExp=3; IntAct=EBI-749731, EBI-11745060; CC Q9UHY1; O60504: SORBS3; NbExp=3; IntAct=EBI-749731, EBI-741237; CC Q9UHY1; Q8IV54: TSC22D4; NbExp=5; IntAct=EBI-749731, EBI-10261521; CC Q9UHY1; Q9Y3Q8: TSC22D4; NbExp=7; IntAct=EBI-749731, EBI-739485; CC Q9UHY1; Q8BX22: Sall4; Xeno; NbExp=2; IntAct=EBI-749731, EBI-2312582; CC Q9UHY1; P14340; Xeno; NbExp=4; IntAct=EBI-749731, EBI-465733; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex CC {ECO:0000269|PubMed:11956649}. Endomembrane system CC {ECO:0000269|PubMed:11956649}. Cell projection, lamellipodium CC {ECO:0000269|PubMed:11956649}. Note=Colocalizes with activated RAC3 to CC endomembranes and at the cell periphery in lamellipodia. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined with CC high levels in the testis. {ECO:0000269|PubMed:10843813}. CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- MISCELLANEOUS: May act as a tumor suppressor to decrease tumor CC incidence and improve survival (PubMed:22510880). Expression levels CC have also been found to be reduced in a range of tumor types, such as CC leukemia, lymphoma, colorectal, breast, brain, esophageal, renal cell, CC prostate and lung (PubMed:22510880). {ECO:0000269|PubMed:22510880}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- CAUTION: Author states that kinase activity observed in PubMed:11956649 CC may be due to sample contamination. This protein is predicted to be CC catalytically inactive. {ECO:0000305}. 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; AF113249; AAF21967.1; -; mRNA. DR EMBL; AK001946; BAA91993.1; -; mRNA. DR EMBL; AK027538; BAB55185.1; -; mRNA. DR EMBL; AK122664; BAG53652.1; -; mRNA. DR EMBL; AL136682; CAB66617.1; -; mRNA. DR EMBL; AK223136; BAD96856.1; -; mRNA. DR EMBL; AC074117; AAY14847.1; -; Genomic_DNA. DR EMBL; CH471053; EAX00578.1; -; Genomic_DNA. DR EMBL; CH471053; EAX00579.1; -; Genomic_DNA. DR EMBL; CH471053; EAX00580.1; -; Genomic_DNA. DR EMBL; BC001221; AAH01221.1; -; mRNA. DR CCDS; CCDS1753.1; -. DR RefSeq; NP_001308286.1; NM_001321357.1. DR RefSeq; NP_001308287.1; NM_001321358.1. DR RefSeq; NP_001308288.1; NM_001321359.1. DR RefSeq; NP_001308290.1; NM_001321361.1. DR RefSeq; NP_001308291.1; NM_001321362.1. DR RefSeq; NP_001308292.1; NM_001321363.1. DR RefSeq; NP_037524.1; NM_013392.3. DR AlphaFoldDB; Q9UHY1; -. DR SMR; Q9UHY1; -. DR BioGRID; 118995; 141. DR IntAct; Q9UHY1; 54. DR MINT; Q9UHY1; -. DR STRING; 9606.ENSP00000369192; -. DR GlyCosmos; Q9UHY1; 4 sites, 1 glycan. DR GlyGen; Q9UHY1; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q9UHY1; -. DR PhosphoSitePlus; Q9UHY1; -. DR BioMuta; NRBP1; -. DR DMDM; 74761962; -. DR EPD; Q9UHY1; -. DR jPOST; Q9UHY1; -. DR MassIVE; Q9UHY1; -. DR MaxQB; Q9UHY1; -. DR PaxDb; 9606-ENSP00000233557; -. DR PeptideAtlas; Q9UHY1; -. DR ProteomicsDB; 84439; -. DR Pumba; Q9UHY1; -. DR Antibodypedia; 28488; 452 antibodies from 29 providers. DR DNASU; 29959; -. DR Ensembl; ENST00000233557.7; ENSP00000233557.3; ENSG00000115216.14. DR Ensembl; ENST00000379852.8; ENSP00000369181.3; ENSG00000115216.14. DR GeneID; 29959; -. DR KEGG; hsa:29959; -. DR MANE-Select; ENST00000379852.8; ENSP00000369181.3; NM_013392.4; NP_037524.1. DR UCSC; uc002rko.4; human. DR AGR; HGNC:7993; -. DR CTD; 29959; -. DR DisGeNET; 29959; -. DR GeneCards; NRBP1; -. DR HGNC; HGNC:7993; NRBP1. DR HPA; ENSG00000115216; Low tissue specificity. DR MIM; 606010; gene. DR neXtProt; NX_Q9UHY1; -. DR OpenTargets; ENSG00000115216; -. DR PharmGKB; PA31772; -. DR VEuPathDB; HostDB:ENSG00000115216; -. DR eggNOG; KOG1266; Eukaryota. DR GeneTree; ENSGT00940000155605; -. DR HOGENOM; CLU_024273_0_0_1; -. DR InParanoid; Q9UHY1; -. DR OrthoDB; 5478852at2759; -. DR PhylomeDB; Q9UHY1; -. DR TreeFam; TF315519; -. DR PathwayCommons; Q9UHY1; -. DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway. DR SignaLink; Q9UHY1; -. DR BioGRID-ORCS; 29959; 680 hits in 1222 CRISPR screens. DR ChiTaRS; NRBP1; human. DR GeneWiki; NRBP1; -. DR GenomeRNAi; 29959; -. DR Pharos; Q9UHY1; Tbio. DR PRO; PR:Q9UHY1; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q9UHY1; Protein. DR Bgee; ENSG00000115216; Expressed in lower esophagus mucosa and 197 other cell types or tissues. DR ExpressionAtlas; Q9UHY1; baseline and differential. 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; IDA:UniProtKB. DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. 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; IDA:UniProtKB. DR CDD; cd14034; PK_NRBP1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR PANTHER; PTHR13902:SF48; NUCLEAR RECEPTOR-BINDING PROTEIN; 1. DR PANTHER; PTHR13902; SERINE/THREONINE-PROTEIN KINASE WNK WITH NO LYSINE -RELATED; 1. DR Pfam; PF00069; Pkinase; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR Genevisible; Q9UHY1; HS. 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:0007744|PubMed:19413330, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:22223895" FT CHAIN 2..535 FT /note="Nuclear receptor-binding protein" FT /id="PRO_0000086449" 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:0007744|PubMed:19413330, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:22223895" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 431 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q99J45" FT MOD_RES 433 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT VARIANT 365 FT /note="V -> I (in dbSNP:rs56004639)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041359" FT VARIANT 432 FT /note="P -> L (in an ovarian mucinous carcinoma sample; FT somatic mutation; dbSNP:rs753734841)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041360" FT VARIANT 460 FT /note="H -> R (in dbSNP:rs34260196)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041361" FT CONFLICT 63 FT /note="R -> G (in Ref. 4; BAD96856)" FT /evidence="ECO:0000305" FT CONFLICT 95 FT /note="V -> M (in Ref. 2; BAB55185)" FT /evidence="ECO:0000305" FT CONFLICT 473 FT /note="N -> S (in Ref. 2; BAB55185)" FT /evidence="ECO:0000305" SQ SEQUENCE 535 AA; 59845 MW; 398078661547EDD0 CRC64; MSEGESQTVL SSGSDPKVES SSSAPGLTSV SPPVTSTTSA ASPEEEEESE DESEILEESP CGRWQKRREE VNQRNVPGID SAYLAMDTEE GVEVVWNEVQ FSERKNYKLQ EEKVRAVFDN LIQLEHLNIV KFHKYWADIK ENKARVIFIT EYMSSGSLKQ FLKKTKKNHK TMNEKAWKRW CTQILSALSY LHSCDPPIIH GNLTCDTIFI QHNGLIKIGS VAPDTINNHV KTCREEQKNL HFFAPEYGEV TNVTTAVDIY SFGMCALEMA VLEIQGNGES SYVPQEAISS AIQLLEDPLQ REFIQKCLQS EPARRPTARE LLFHPALFEV PSLKLLAAHC IVGHQHMIPE NALEEITKNM DTSAVLAEIP AGPGREPVQT LYSQSPALEL DKFLEDVRNG IYPLTAFGLP RPQQPQQEEV TSPVVPPSVK TPTPEPAEVE TRKVVLMQCN IESVEEGVKH HLTLLLKLED KLNRHLSCDL MPNENIPELA AELVQLGFIS EADQSRLTSL LEETLNKFNF ARNSTLNSAA VTVSS //