ID NR4A1_HUMAN Reviewed; 598 AA. AC P22736; B4DML7; Q15627; Q53Y00; Q6IBU8; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 1. DT 09-DEC-2015, entry version 177. DE RecName: Full=Nuclear receptor subfamily 4 group A member 1; DE AltName: Full=Early response protein NAK1; DE AltName: Full=Nuclear hormone receptor NUR/77; DE Short=Nur77; DE AltName: Full=Orphan nuclear receptor HMR; DE AltName: Full=Orphan nuclear receptor TR3; DE AltName: Full=ST-59; DE AltName: Full=Testicular receptor 3; GN Name=NR4A1; Synonyms=GFRP1, HMR, NAK1; 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] (ISOFORM 1). RC TISSUE=Fetal skeletal muscle; RX PubMed=2283997; DOI=10.1210/mend-4-10-1438; RA Nakai A., Kartha S., Sakurai A., Toback F.G., Degroot L.J.; RT "A human early response gene homologous to murine nur77 and rat NGFI- RT B, and related to the nuclear receptor superfamily."; RL Mol. Endocrinol. 4:1438-1443(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2626032; DOI=10.1016/0022-4731(89)90114-3; RA Chang C., Kokontis J., Liao S., Chang Y.; RT "Isolation and characterization of human TR3 receptor: a member of RT steroid receptor superfamily."; RL J. Steroid Biochem. 34:391-395(1989). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RC TISSUE=Skeletal muscle; RA Ohkura N., Ito M., Tsukada T., Sasaki K., Yamaguchi K., Miki K.; RT "Identification of an isoform of human TR3 (NGFI-B, Nur77)."; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Kobayashi T., Kodani Y., Sawasaki T., Endo Y.; RT "Comprehensive DNA-binding analysis of human hormone nuclear receptors RT by fluorescence correlation spectroscopy based on cell-free system."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Heart; RA Kaighin V.A., Martin A.L., Aronstam R.S.; RT "Isolation of cDNA coding for multiple human nuclear receptor RT clones."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Brain, and Trachea; 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., RA Kucherlapati R., Weinstock G., Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin; 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 [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-398 (ISOFORM 1). RC TISSUE=Colon adenocarcinoma; RX PubMed=1651101; RA Bondy G.P.; RT "Phorbol ester, forskolin, and serum induction of a human colon RT nuclear hormone receptor gene related to the NUR 77/NGFI-B genes."; RL Cell Growth Differ. 2:203-208(1991). RN [13] RP FUNCTION. RX PubMed=15466594; DOI=10.1093/nar/gkh856; RA Harant H., Lindley I.J.; RT "Negative cross-talk between the human orphan nuclear receptor RT Nur77/NAK-1/TR3 and nuclear factor-kappaB."; RL Nucleic Acids Res. 32:5280-5290(2004). RN [14] RP INTERACTION WITH GADD45GIP1. RX PubMed=15459248; DOI=10.1210/me.2004-0107; RA Park K.C., Song K.-H., Chung H.K., Kim H., Kim D.W., Song J.H., RA Hwang E.S., Jung H.S., Park S.-H., Bae I., Lee I.K., Choi H.-S., RA Shong M.; RT "CR6-interacting factor 1 interacts with orphan nuclear receptor Nur77 RT and inhibits its transactivation."; RL Mol. Endocrinol. 19:12-24(2005). RN [15] RP PHOSPHORYLATION AT SER-351. RX PubMed=17360704; DOI=10.1074/jbc.M700906200; RA Roux P.P., Shahbazian D., Vu H., Holz M.K., Cohen M.S., Taunton J., RA Sonenberg N., Blenis J.; RT "RAS/ERK signaling promotes site-specific ribosomal protein S6 RT phosphorylation via RSK and stimulates cap-dependent translation."; RL J. Biol. Chem. 282:14056-14064(2007). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION RP BY 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 [18] RP ACETYLATION, AND SUBCELLULAR LOCATION. RX PubMed=20438716; DOI=10.1016/j.bcp.2010.04.026; RA Kang S.A., Na H., Kang H.J., Kim S.H., Lee M.H., Lee M.O.; RT "Regulation of Nur77 protein turnover through acetylation and RT deacetylation induced by p300 and HDAC1."; RL Biochem. Pharmacol. 80:867-873(2010). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 351-598 ALONE AND IN COMPLEX RP WITH ANTAGONIST, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RP STK11, AND MUTAGENESIS OF THR-595. RX PubMed=22983157; DOI=10.1038/nchembio.1069; RA Zhan Y.Y., Chen Y., Zhang Q., Zhuang J.J., Tian M., Chen H.Z., RA Zhang L.R., Zhang H.K., He J.P., Wang W.J., Wu R., Wang Y., Shi C., RA Yang K., Li A.Z., Xin Y.Z., Li T.Y., Yang J.Y., Zheng Z.H., Yu C.D., RA Lin S.C., Chang C., Huang P.Q., Lin T., Wu Q.; RT "The orphan nuclear receptor Nur77 regulates LKB1 localization and RT activates AMPK."; RL Nat. Chem. Biol. 8:897-904(2012). CC -!- FUNCTION: Orphan nuclear receptor. May act concomitantly with CC NURR1 in regulating the expression of delayed-early genes during CC liver regeneration. Binds the NGFI-B response element (NBRE) 5'- CC AAAAGGTCA-3' (By similarity). May inhibit NF-kappa-B CC transactivation of IL2. Participates in energy homeostasis by CC sequestrating the kinase STK11 in the nucleus, thereby attenuating CC cytoplasmic AMPK activation. {ECO:0000250, CC ECO:0000269|PubMed:15466594, ECO:0000269|PubMed:22983157}. CC -!- SUBUNIT: Binds DNA as a monomer (By similarity). Interacts with CC GADD45GIP1. Interacts with STK11. {ECO:0000250, CC ECO:0000269|PubMed:15459248, ECO:0000269|PubMed:22983157}. CC -!- INTERACTION: CC Q9WMX2:- (xeno); NbExp=2; IntAct=EBI-721550, EBI-9028517; CC Q9P2G1:ANKIB1; NbExp=2; IntAct=EBI-721550, EBI-2687890; CC P10415:BCL2; NbExp=7; IntAct=EBI-721550, EBI-77694; CC P55273:CDKN2D; NbExp=3; IntAct=EBI-721550, EBI-745859; CC O60888:CUTA; NbExp=2; IntAct=EBI-721550, EBI-1051556; CC P32189:GK; NbExp=3; IntAct=EBI-721550, EBI-3926629; CC P60370:KRTAP10-5; NbExp=3; IntAct=EBI-721550, EBI-10172150; CC Q17RB8:LONRF1; NbExp=3; IntAct=EBI-721550, EBI-2341787; CC P43243:MATR3; NbExp=2; IntAct=EBI-721550, EBI-352602; CC Q96JS3:PGBD1; NbExp=3; IntAct=EBI-721550, EBI-10290053; CC Q9Y4D7:PLXND1; NbExp=2; IntAct=EBI-721550, EBI-310731; CC P40763:STAT3; NbExp=3; IntAct=EBI-721550, EBI-518675; CC P04637:TP53; NbExp=6; IntAct=EBI-721550, EBI-366083; CC P04350:TUBB4A; NbExp=2; IntAct=EBI-721550, EBI-355007; CC P50552:VASP; NbExp=2; IntAct=EBI-721550, EBI-748201; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P22736-1; Sequence=Displayed; CC Name=2; CC IsoId=P22736-2; Sequence=VSP_043086; CC Note=No experimental confirmation available.; CC Name=3; CC IsoId=P22736-3; Sequence=VSP_047769, VSP_047770; CC -!- TISSUE SPECIFICITY: Fetal muscle and adult liver, brain and CC thyroid. CC -!- INDUCTION: By growth-stimulating agents. CC -!- PTM: Phosphorylated at Ser-351 by RPS6KA1 and RPS6KA3 in response CC to mitogenic or stress stimuli. {ECO:0000269|PubMed:17360704}. CC -!- PTM: Acetylated by p300/CBP, acetylation increases stability. CC Deacetylated by HDAC1. {ECO:0000269|PubMed:20438716}. CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR4 CC subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 nuclear receptor DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00407}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/NR4A1ID41573ch12q13.html"; 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; D49728; BAA08565.1; -; mRNA. DR EMBL; L13740; AAA36763.1; -; mRNA. DR EMBL; D85245; BAA12746.1; -; mRNA. DR EMBL; AK297526; BAG59929.1; -; mRNA. DR EMBL; HQ692855; ADZ17366.1; -; mRNA. DR EMBL; AB307717; BAH02308.1; -; mRNA. DR EMBL; BT007144; AAP35808.1; -; mRNA. DR EMBL; AK314437; BAG37048.1; -; mRNA. DR EMBL; CR456704; CAG32985.1; -; mRNA. DR EMBL; AC025259; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471111; EAW58222.1; -; Genomic_DNA. DR EMBL; CH471111; EAW58224.1; -; Genomic_DNA. DR EMBL; CH471111; EAW58225.1; -; Genomic_DNA. DR EMBL; BC016147; AAH16147.1; -; mRNA. DR CCDS; CCDS55828.1; -. [P22736-2] DR CCDS; CCDS8818.1; -. [P22736-1] DR PIR; A37251; A37251. DR RefSeq; NP_001189162.1; NM_001202233.1. [P22736-2] DR RefSeq; NP_002126.2; NM_002135.4. [P22736-1] DR RefSeq; NP_775180.1; NM_173157.2. [P22736-1] DR RefSeq; XP_005268881.1; XM_005268824.2. [P22736-1] DR RefSeq; XP_006719426.1; XM_006719363.1. [P22736-1] DR RefSeq; XP_006719427.1; XM_006719364.2. [P22736-1] DR RefSeq; XP_011536552.1; XM_011538250.1. [P22736-1] DR UniGene; Hs.524430; -. DR UniGene; Hs.670088; -. DR PDB; 2QW4; X-ray; 2.80 A; A/B/C/D=347-598. DR PDB; 3V3E; X-ray; 2.06 A; A/B=351-598. DR PDB; 3V3Q; X-ray; 2.22 A; A/B=351-598. DR PDB; 4JGV; X-ray; 3.01 A; A/B=351-598. DR PDB; 4KZI; X-ray; 2.41 A; A/B=351-598. DR PDB; 4KZJ; X-ray; 2.12 A; A/B=351-598. DR PDB; 4KZM; X-ray; 2.30 A; A/B=351-598. DR PDB; 4RE8; X-ray; 2.16 A; A/B=351-598. DR PDB; 4REE; X-ray; 2.37 A; A/B=351-598. DR PDB; 4REF; X-ray; 2.10 A; A/B=351-598. DR PDB; 4RZE; X-ray; 2.49 A; A/B=351-598. DR PDB; 4RZF; X-ray; 1.99 A; A/B=351-598. DR PDB; 4RZG; X-ray; 2.70 A; A/B=351-598. DR PDB; 4WHF; X-ray; 2.27 A; A/B=351-598. DR PDB; 4WHG; X-ray; 2.18 A; A/B=351-598. DR PDBsum; 2QW4; -. DR PDBsum; 3V3E; -. DR PDBsum; 3V3Q; -. DR PDBsum; 4JGV; -. DR PDBsum; 4KZI; -. DR PDBsum; 4KZJ; -. DR PDBsum; 4KZM; -. DR PDBsum; 4RE8; -. DR PDBsum; 4REE; -. DR PDBsum; 4REF; -. DR PDBsum; 4RZE; -. DR PDBsum; 4RZF; -. DR PDBsum; 4RZG; -. DR PDBsum; 4WHF; -. DR PDBsum; 4WHG; -. DR ProteinModelPortal; P22736; -. DR SMR; P22736; 265-598. DR BioGrid; 109407; 94. DR DIP; DIP-40392N; -. DR IntAct; P22736; 87. DR MINT; MINT-2859679; -. DR STRING; 9606.ENSP00000353427; -. DR BindingDB; P22736; -. DR ChEMBL; CHEMBL1293229; -. DR PhosphoSite; P22736; -. DR BioMuta; NR4A1; -. DR DMDM; 127819; -. DR PaxDb; P22736; -. DR PRIDE; P22736; -. DR DNASU; 3164; -. DR Ensembl; ENST00000243050; ENSP00000243050; ENSG00000123358. [P22736-1] DR Ensembl; ENST00000360284; ENSP00000353427; ENSG00000123358. [P22736-2] DR Ensembl; ENST00000394824; ENSP00000378301; ENSG00000123358. [P22736-1] DR Ensembl; ENST00000394825; ENSP00000378302; ENSG00000123358. [P22736-1] DR Ensembl; ENST00000548232; ENSP00000449587; ENSG00000123358. [P22736-3] DR Ensembl; ENST00000550082; ENSP00000449539; ENSG00000123358. [P22736-2] DR GeneID; 3164; -. DR KEGG; hsa:3164; -. DR UCSC; uc001rzr.2; human. DR UCSC; uc001rzs.3; human. [P22736-1] DR UCSC; uc010sno.2; human. [P22736-2] DR CTD; 3164; -. DR GeneCards; NR4A1; -. DR H-InvDB; HIX0171621; -. DR HGNC; HGNC:7980; NR4A1. DR MIM; 139139; gene. DR neXtProt; NX_P22736; -. DR PharmGKB; PA31761; -. DR eggNOG; KOG4217; Eukaryota. DR eggNOG; ENOG410YWNC; LUCA. DR GeneTree; ENSGT00760000118887; -. DR HOGENOM; HOG000230925; -. DR HOVERGEN; HBG052663; -. DR InParanoid; P22736; -. DR KO; K04465; -. DR PhylomeDB; P22736; -. DR TreeFam; TF315430; -. DR Reactome; R-HSA-198693; AKT phosphorylates targets in the nucleus. DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway. DR Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer. DR SignaLink; P22736; -. DR ChiTaRS; NR4A1; human. DR EvolutionaryTrace; P22736; -. DR GeneWiki; Nerve_Growth_factor_IB; -. DR GenomeRNAi; 3164; -. DR NextBio; 12546; -. DR PRO; PR:P22736; -. DR Proteomes; UP000005640; Chromosome 12. DR Bgee; P22736; -. DR CleanEx; HS_NR4A1; -. DR ExpressionAtlas; P22736; baseline and differential. DR Genevisible; P22736; HS. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0031965; C:nuclear membrane; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; ISS:BHF-UCL. DR GO; GO:0003677; F:DNA binding; ISS:BHF-UCL. DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB. DR GO; GO:0004879; F:RNA polymerase II transcription factor activity, ligand-activated sequence-specific DNA binding; TAS:ProtInc. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro. DR GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IDA:BHF-UCL. DR GO; GO:0071376; P:cellular response to corticotropin-releasing hormone stimulus; ISS:UniProtKB. DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IMP:BHF-UCL. DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IMP:BHF-UCL. DR GO; GO:0035767; P:endothelial cell chemotaxis; IMP:BHF-UCL. DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome. DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB. DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome. DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome. DR GO; GO:0010467; P:gene expression; TAS:Reactome. DR GO; GO:0045087; P:innate immune response; TAS:Reactome. DR GO; GO:0030522; P:intracellular receptor signaling pathway; TAS:GOC. DR GO; GO:0045786; P:negative regulation of cell cycle; ISS:UniProtKB. DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome. DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome. DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI. DR GO; GO:0061469; P:regulation of type B pancreatic cell proliferation; ISS:UniProtKB. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome. DR Gene3D; 1.10.565.10; -; 1. DR Gene3D; 3.30.50.10; -; 1. DR InterPro; IPR003071; Nuc_orp_HMR_rcpt. DR InterPro; IPR003070; Nuc_orph_rcpt. DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd. DR InterPro; IPR001723; Nuclear_hrmn_rcpt. DR InterPro; IPR001628; Znf_hrmn_rcpt. DR InterPro; IPR013088; Znf_NHR/GATA. DR Pfam; PF00104; Hormone_recep; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR01285; HMRNUCRECPTR. DR PRINTS; PR01284; NUCLEARECPTR. DR PRINTS; PR00398; STRDHORMONER. DR PRINTS; PR00047; STROIDFINGER. DR SMART; SM00430; HOLI; 1. DR SMART; SM00399; ZnF_C4; 1. DR SUPFAM; SSF48508; SSF48508; 1. DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1. DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Complete proteome; KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; KW Polymorphism; Receptor; Reference proteome; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 598 Nuclear receptor subfamily 4 group A FT member 1. FT /FTId=PRO_0000053715. FT DNA_BIND 264 339 Nuclear receptor. {ECO:0000255|PROSITE- FT ProRule:PRU00407}. FT ZN_FING 267 287 NR C4-type. {ECO:0000255|PROSITE- FT ProRule:PRU00407}. FT ZN_FING 303 327 NR C4-type. {ECO:0000255|PROSITE- FT ProRule:PRU00407}. FT REGION 409 459 Ligand-binding. {ECO:0000255}. FT COMPBIAS 82 92 Poly-Ser. FT COMPBIAS 583 586 Poly-Pro. FT MOD_RES 341 341 Phosphoserine; by PKA. {ECO:0000250}. FT MOD_RES 351 351 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000269|PubMed:17360704}. FT VAR_SEQ 1 1 M -> MWLAKACWSIQSEM (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_043086. FT VAR_SEQ 293 325 RTVQKNAKYICLANKDCPVDKRRRNRCQFCRFQ -> VPRS FT PRWGLLLEMERGWPHPIGTCGLPLGSPPS (in isoform FT 3). {ECO:0000303|PubMed:14702039, FT ECO:0000303|Ref.3}. FT /FTId=VSP_047769. FT VAR_SEQ 326 598 Missing (in isoform 3). FT {ECO:0000303|PubMed:14702039, FT ECO:0000303|Ref.3}. FT /FTId=VSP_047770. FT VARIANT 26 26 L -> V (in dbSNP:rs1882118). FT /FTId=VAR_061534. FT MUTAGEN 595 595 T->E: Strongly weakens interaction with FT STK11. {ECO:0000269|PubMed:22983157}. FT CONFLICT 253 253 T -> I (in Ref. 12). {ECO:0000305}. FT CONFLICT 262 262 G -> P (in Ref. 2; AAA36763). FT {ECO:0000305}. FT CONFLICT 360 360 S -> F (in Ref. 8; CAG32985). FT {ECO:0000305}. FT CONFLICT 370 370 R -> L (in Ref. 2; AAA36763). FT {ECO:0000305}. FT HELIX 364 373 {ECO:0000244|PDB:4RZF}. FT HELIX 379 381 {ECO:0000244|PDB:4RZF}. FT STRAND 395 397 {ECO:0000244|PDB:4REF}. FT HELIX 400 422 {ECO:0000244|PDB:4RZF}. FT HELIX 427 429 {ECO:0000244|PDB:4RZF}. FT HELIX 432 454 {ECO:0000244|PDB:4RZF}. FT HELIX 457 459 {ECO:0000244|PDB:4RZF}. FT STRAND 461 463 {ECO:0000244|PDB:4RZF}. FT STRAND 467 471 {ECO:0000244|PDB:4RZF}. FT HELIX 472 479 {ECO:0000244|PDB:4RZF}. FT HELIX 482 495 {ECO:0000244|PDB:4RZF}. FT HELIX 500 511 {ECO:0000244|PDB:4RZF}. FT HELIX 521 541 {ECO:0000244|PDB:4RZF}. FT TURN 544 546 {ECO:0000244|PDB:3V3Q}. FT HELIX 550 556 {ECO:0000244|PDB:4RZF}. FT HELIX 558 579 {ECO:0000244|PDB:4RZF}. FT HELIX 586 594 {ECO:0000244|PDB:4RZF}. SQ SEQUENCE 598 AA; 64463 MW; 41DAAEA7C25FDA22 CRC64; MPCIQAQYGT PAPSPGPRDH LASDPLTPEF IKPTMDLASP EAAPAAPTAL PSFSTFMDGY TGEFDTFLYQ LPGTVQPCSS ASSSASSTSS SSATSPASAS FKFEDFQVYG CYPGPLSGPV DEALSSSGSD YYGSPCSAPS PSTPSFQPPQ LSPWDGSFGH FSPSQTYEGL RAWTEQLPKA SGPPQPPAFF SFSPPTGPSP SLAQSPLKLF PSQATHQLGE GESYSMPTAF PGLAPTSPHL EGSGILDTPV TSTKARSGAP GGSEGRCAVC GDNASCQHYG VRTCEGCKGF FKRTVQKNAK YICLANKDCP VDKRRRNRCQ FCRFQKCLAV GMVKEVVRTD SLKGRRGRLP SKPKQPPDAS PANLLTSLVR AHLDSGPSTA KLDYSKFQEL VLPHFGKEDA GDVQQFYDLL SGSLEVIRKW AEKIPGFAEL SPADQDLLLE SAFLELFILR LAYRSKPGEG KLIFCSGLVL HRLQCARGFG DWIDSILAFS RSLHSLLVDV PAFACLSALV LITDRHGLQE PRRVEELQNR IASCLKEHVA AVAGEPQPAS CLSRLLGKLP ELRTLCTQGL QRIFYLKLED LVPPPPIIDK IFMDTLPF //