Full text data of NRBP1
NRBP1
(BCON3, NRBP)
[Confidence: low (only semi-automatic identification from reviews)]
Nuclear receptor-binding protein
Nuclear receptor-binding protein
UniProt
Q9UHY1
ID NRBP_HUMAN Reviewed; 535 AA.
AC Q9UHY1; B3KV40; D6W558; Q53FZ5; Q96SU3;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Nuclear receptor-binding protein;
GN Name=NRBP1; Synonyms=BCON3, NRBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [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,
RT a ubiquitously expressed, multidomain putative adapter protein.";
RL Genomics 66:113-118(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neuron, Placenta, 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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]
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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
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
RT kinase-homology domain.";
RL Int. J. Mol. Med. 9:451-459(2002).
RN [9]
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
RT with human nuclear receptor binding protein and is associated with
RT alterations 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-433, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation 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 MASS
RP SPECTROMETRY.
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, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-433, AND MASS
RP SPECTROMETRY.
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
RP SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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
RP SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
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.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., 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
CC with the Rho-type GTPases. Binding to the NS3 protein of dengue
CC virus type 2 appears to subvert this activity into the alteration
CC of the intracellular membrane structure associated with flaviviral
CC replication.
CC -!- SUBUNIT: Homodimer. Binds to MLF1, recruiting a serine kinase
CC which phosphorylates both itself and MLF1. Phosphorylated MLF1
CC binds to YWHAZ and is retained in the cytoplasm (By similarity).
CC -!- INTERACTION:
CC P14340:- (xeno); NbExp=4; IntAct=EBI-749731, EBI-465733;
CC P60763:RAC3; NbExp=3; IntAct=EBI-749731, EBI-767084;
CC Q8BX22:Sall4 (xeno); NbExp=2; IntAct=EBI-749731, EBI-2312582;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Endomembrane system.
CC Cell projection, lamellipodium. Note=Colocalizes with activated
CC RAC3 to endomembranes and at the cell periphery in lamellipodia.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined
CC with high levels in the testis.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC protein kinase family.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- CAUTION: Author states that kinase activity observed in
CC PubMed:11956649 may be due to sample contamination. This protein
CC is predicted to be catalytically inactive.
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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 RefSeq; NP_037524.1; NM_013392.2.
DR RefSeq; XP_005264331.1; XM_005264274.1.
DR UniGene; Hs.515876; -.
DR ProteinModelPortal; Q9UHY1; -.
DR SMR; Q9UHY1; 81-329.
DR IntAct; Q9UHY1; 19.
DR MINT; MINT-1406316; -.
DR STRING; 9606.ENSP00000233557; -.
DR PhosphoSite; Q9UHY1; -.
DR DMDM; 74761962; -.
DR PaxDb; Q9UHY1; -.
DR PeptideAtlas; Q9UHY1; -.
DR PRIDE; Q9UHY1; -.
DR DNASU; 29959; -.
DR Ensembl; ENST00000233557; ENSP00000233557; ENSG00000115216.
DR Ensembl; ENST00000379852; ENSP00000369181; ENSG00000115216.
DR GeneID; 29959; -.
DR KEGG; hsa:29959; -.
DR UCSC; uc002rko.3; human.
DR CTD; 29959; -.
DR GeneCards; GC02P027651; -.
DR HGNC; HGNC:7993; NRBP1.
DR HPA; CAB033078; -.
DR HPA; HPA029527; -.
DR MIM; 606010; gene.
DR neXtProt; NX_Q9UHY1; -.
DR PharmGKB; PA31772; -.
DR eggNOG; COG0515; -.
DR HOGENOM; HOG000267147; -.
DR HOVERGEN; HBG057400; -.
DR KO; K08875; -.
DR PhylomeDB; Q9UHY1; -.
DR Reactome; REACT_71; Gene Expression.
DR SignaLink; Q9UHY1; -.
DR GeneWiki; NRBP1; -.
DR GenomeRNAi; 29959; -.
DR NextBio; 52679; -.
DR PRO; PR:Q9UHY1; -.
DR ArrayExpress; Q9UHY1; -.
DR Bgee; Q9UHY1; -.
DR CleanEx; HS_NRBP1; -.
DR Genevestigator; Q9UHY1; -.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
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:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
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:ER to Golgi vesicle-mediated transport; IDA:UniProtKB.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
DR InterPro; IPR011009; Kinase-like_dom.
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 Acetylation; Cell projection; Complete proteome; Cytoplasm; Membrane;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 535 Nuclear receptor-binding protein.
FT /FTId=PRO_0000086449.
FT DOMAIN 68 327 Protein kinase.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 2 2 Phosphoserine.
FT MOD_RES 433 433 Phosphothreonine.
FT VARIANT 365 365 V -> I (in dbSNP:rs56004639).
FT /FTId=VAR_041359.
FT VARIANT 432 432 P -> L (in an ovarian mucinous carcinoma
FT sample; somatic mutation).
FT /FTId=VAR_041360.
FT VARIANT 460 460 H -> R (in dbSNP:rs34260196).
FT /FTId=VAR_041361.
FT CONFLICT 63 63 R -> G (in Ref. 4; BAD96856).
FT CONFLICT 95 95 V -> M (in Ref. 2; BAB55185).
FT CONFLICT 473 473 N -> S (in Ref. 2; BAB55185).
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
//
ID NRBP_HUMAN Reviewed; 535 AA.
AC Q9UHY1; B3KV40; D6W558; Q53FZ5; Q96SU3;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Nuclear receptor-binding protein;
GN Name=NRBP1; Synonyms=BCON3, NRBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [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,
RT a ubiquitously expressed, multidomain putative adapter protein.";
RL Genomics 66:113-118(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neuron, Placenta, 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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]
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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
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
RT kinase-homology domain.";
RL Int. J. Mol. Med. 9:451-459(2002).
RN [9]
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
RT with human nuclear receptor binding protein and is associated with
RT alterations 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-433, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation 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 MASS
RP SPECTROMETRY.
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, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-433, AND MASS
RP SPECTROMETRY.
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
RP SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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
RP SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
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.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., 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
CC with the Rho-type GTPases. Binding to the NS3 protein of dengue
CC virus type 2 appears to subvert this activity into the alteration
CC of the intracellular membrane structure associated with flaviviral
CC replication.
CC -!- SUBUNIT: Homodimer. Binds to MLF1, recruiting a serine kinase
CC which phosphorylates both itself and MLF1. Phosphorylated MLF1
CC binds to YWHAZ and is retained in the cytoplasm (By similarity).
CC -!- INTERACTION:
CC P14340:- (xeno); NbExp=4; IntAct=EBI-749731, EBI-465733;
CC P60763:RAC3; NbExp=3; IntAct=EBI-749731, EBI-767084;
CC Q8BX22:Sall4 (xeno); NbExp=2; IntAct=EBI-749731, EBI-2312582;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Endomembrane system.
CC Cell projection, lamellipodium. Note=Colocalizes with activated
CC RAC3 to endomembranes and at the cell periphery in lamellipodia.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined
CC with high levels in the testis.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC protein kinase family.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- CAUTION: Author states that kinase activity observed in
CC PubMed:11956649 may be due to sample contamination. This protein
CC is predicted to be catalytically inactive.
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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 RefSeq; NP_037524.1; NM_013392.2.
DR RefSeq; XP_005264331.1; XM_005264274.1.
DR UniGene; Hs.515876; -.
DR ProteinModelPortal; Q9UHY1; -.
DR SMR; Q9UHY1; 81-329.
DR IntAct; Q9UHY1; 19.
DR MINT; MINT-1406316; -.
DR STRING; 9606.ENSP00000233557; -.
DR PhosphoSite; Q9UHY1; -.
DR DMDM; 74761962; -.
DR PaxDb; Q9UHY1; -.
DR PeptideAtlas; Q9UHY1; -.
DR PRIDE; Q9UHY1; -.
DR DNASU; 29959; -.
DR Ensembl; ENST00000233557; ENSP00000233557; ENSG00000115216.
DR Ensembl; ENST00000379852; ENSP00000369181; ENSG00000115216.
DR GeneID; 29959; -.
DR KEGG; hsa:29959; -.
DR UCSC; uc002rko.3; human.
DR CTD; 29959; -.
DR GeneCards; GC02P027651; -.
DR HGNC; HGNC:7993; NRBP1.
DR HPA; CAB033078; -.
DR HPA; HPA029527; -.
DR MIM; 606010; gene.
DR neXtProt; NX_Q9UHY1; -.
DR PharmGKB; PA31772; -.
DR eggNOG; COG0515; -.
DR HOGENOM; HOG000267147; -.
DR HOVERGEN; HBG057400; -.
DR KO; K08875; -.
DR PhylomeDB; Q9UHY1; -.
DR Reactome; REACT_71; Gene Expression.
DR SignaLink; Q9UHY1; -.
DR GeneWiki; NRBP1; -.
DR GenomeRNAi; 29959; -.
DR NextBio; 52679; -.
DR PRO; PR:Q9UHY1; -.
DR ArrayExpress; Q9UHY1; -.
DR Bgee; Q9UHY1; -.
DR CleanEx; HS_NRBP1; -.
DR Genevestigator; Q9UHY1; -.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
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:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
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:ER to Golgi vesicle-mediated transport; IDA:UniProtKB.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
DR InterPro; IPR011009; Kinase-like_dom.
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 Acetylation; Cell projection; Complete proteome; Cytoplasm; Membrane;
KW Phosphoprotein; Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 535 Nuclear receptor-binding protein.
FT /FTId=PRO_0000086449.
FT DOMAIN 68 327 Protein kinase.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 2 2 Phosphoserine.
FT MOD_RES 433 433 Phosphothreonine.
FT VARIANT 365 365 V -> I (in dbSNP:rs56004639).
FT /FTId=VAR_041359.
FT VARIANT 432 432 P -> L (in an ovarian mucinous carcinoma
FT sample; somatic mutation).
FT /FTId=VAR_041360.
FT VARIANT 460 460 H -> R (in dbSNP:rs34260196).
FT /FTId=VAR_041361.
FT CONFLICT 63 63 R -> G (in Ref. 4; BAD96856).
FT CONFLICT 95 95 V -> M (in Ref. 2; BAB55185).
FT CONFLICT 473 473 N -> S (in Ref. 2; BAB55185).
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
//
MIM
606010
*RECORD*
*FIELD* NO
606010
*FIELD* TI
*606010 NUCLEAR RECEPTOR-BINDING PROTEIN 1; NRBP1
*FIELD* TX
CLONING
Adaptor proteins modulate multiple signaling pathways by regulating the
read moreaggregation of other factors into signaling complexes. By a combination
of PCR-based homology cloning, 5-prime RACE, and clones obtained from an
EST database, Hooper et al. (2000) isolated a novel human cDNA encoding
a putative adaptor protein, which they called NRBP. By EST database
searching, they also identified mouse and rat homologs of NRBP with 91%
and 89% identity, respectively. The deduced 535-amino acid human protein
has a molecular mass of 59.8 kD and contains 2 putative nuclear
receptor-binding motifs, a putative binding domain for SH2
domain-containing proteins, a kinase-like domain, a bipartite nuclear
localization signal, and 3 sequences rich in glutamic acid, serine,
proline, and threonine (PEST) residues. Northern blot analysis detected
ubiquitous expression of a 2.4-kb NRBP transcript, with highest levels
in testis and lowest levels in thymus. Dot-blot analysis showed highest
levels in testis and placenta and lowest levels in hippocampus and
thymus. NRBP mRNA was also expressed in each of 15 cultured human tumor
cell lines examined. Translation of NRBP mRNA in vitro revealed 3
translation products of 60, 51, and 43 kD, suggesting that translation
of NRBP may initiate at multiple sites.
MAPPING
By fluorescence in situ hybridization, Hooper et al. (2000) mapped the
NRBP1 gene to chromosome 2p23.
*FIELD* RF
1. Hooper, J. D.; Baker, E.; Ogbourne, S. M.; Sutherland, G. R.; Antalis,
T. M.: Cloning of the cDNA and localization of the gene encoding
human NRBP, a ubiquitously expressed, multidomain putative adapter
protein. Genomics 66: 113-118, 2000.
*FIELD* CD
Carol A. Bocchini: 6/14/2001
*FIELD* ED
alopez: 03/29/2012
alopez: 3/29/2012
mcapotos: 6/14/2001
carol: 6/14/2001
*RECORD*
*FIELD* NO
606010
*FIELD* TI
*606010 NUCLEAR RECEPTOR-BINDING PROTEIN 1; NRBP1
*FIELD* TX
CLONING
Adaptor proteins modulate multiple signaling pathways by regulating the
read moreaggregation of other factors into signaling complexes. By a combination
of PCR-based homology cloning, 5-prime RACE, and clones obtained from an
EST database, Hooper et al. (2000) isolated a novel human cDNA encoding
a putative adaptor protein, which they called NRBP. By EST database
searching, they also identified mouse and rat homologs of NRBP with 91%
and 89% identity, respectively. The deduced 535-amino acid human protein
has a molecular mass of 59.8 kD and contains 2 putative nuclear
receptor-binding motifs, a putative binding domain for SH2
domain-containing proteins, a kinase-like domain, a bipartite nuclear
localization signal, and 3 sequences rich in glutamic acid, serine,
proline, and threonine (PEST) residues. Northern blot analysis detected
ubiquitous expression of a 2.4-kb NRBP transcript, with highest levels
in testis and lowest levels in thymus. Dot-blot analysis showed highest
levels in testis and placenta and lowest levels in hippocampus and
thymus. NRBP mRNA was also expressed in each of 15 cultured human tumor
cell lines examined. Translation of NRBP mRNA in vitro revealed 3
translation products of 60, 51, and 43 kD, suggesting that translation
of NRBP may initiate at multiple sites.
MAPPING
By fluorescence in situ hybridization, Hooper et al. (2000) mapped the
NRBP1 gene to chromosome 2p23.
*FIELD* RF
1. Hooper, J. D.; Baker, E.; Ogbourne, S. M.; Sutherland, G. R.; Antalis,
T. M.: Cloning of the cDNA and localization of the gene encoding
human NRBP, a ubiquitously expressed, multidomain putative adapter
protein. Genomics 66: 113-118, 2000.
*FIELD* CD
Carol A. Bocchini: 6/14/2001
*FIELD* ED
alopez: 03/29/2012
alopez: 3/29/2012
mcapotos: 6/14/2001
carol: 6/14/2001