NRBP_HUMAN
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 03-AUG-2022, entry version 183.
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},
RC Placenta {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 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 [20]
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 [21]
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: May play a role in subcellular trafficking between the
CC endoplasmic reticulum and Golgi apparatus through interactions with the
CC Rho-type GTPases. 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
CC replication. {ECO:0000269|PubMed:11956649, ECO:0000269|PubMed:15084397,
CC ECO:0000303|PubMed:11956649}.
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 (By similarity). {ECO:0000250}.
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.
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}.
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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; 87.
DR IntAct; Q9UHY1; 49.
DR MINT; Q9UHY1; -.
DR STRING; 9606.ENSP00000233557; -.
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; Q9UHY1; -.
DR PeptideAtlas; Q9UHY1; -.
DR PRIDE; Q9UHY1; -.
DR ProteomicsDB; 84439; -.
DR Antibodypedia; 28488; 407 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 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; 695382at2759; -.
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; 664 hits in 1135 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 195 other tissues.
DR ExpressionAtlas; Q9UHY1; baseline and differential.
DR Genevisible; Q9UHY1; HS.
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:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA: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: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
