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Nuclear receptor subfamily 4 group A member 1 (Early response protein NAK1) (Nuclear hormone receptor NUR/77) (Nur77) (Orphan nuclear receptor HMR) (Orphan nuclear receptor TR3) (ST-59) (Testicular receptor 3)

 NR4A1_HUMAN             Reviewed;         598 AA.
P22736; B4DML7; Q15627; Q53Y00; Q6IBU8;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-AUG-1991, sequence version 1.
10-OCT-2018, entry version 203.
RecName: Full=Nuclear receptor subfamily 4 group A member 1;
AltName: Full=Early response protein NAK1;
AltName: Full=Nuclear hormone receptor NUR/77;
Short=Nur77;
AltName: Full=Orphan nuclear receptor HMR;
AltName: Full=Orphan nuclear receptor TR3;
AltName: Full=ST-59;
AltName: Full=Testicular receptor 3;
Name=NR4A1; Synonyms=GFRP1, HMR, NAK1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal skeletal muscle;
PubMed=2283997; DOI=10.1210/mend-4-10-1438;
Nakai A., Kartha S., Sakurai A., Toback F.G., Degroot L.J.;
"A human early response gene homologous to murine nur77 and rat NGFI-
B, and related to the nuclear receptor superfamily.";
Mol. Endocrinol. 4:1438-1443(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2626032; DOI=10.1016/0022-4731(89)90114-3;
Chang C., Kokontis J., Liao S., Chang Y.;
"Isolation and characterization of human TR3 receptor: a member of
steroid receptor superfamily.";
J. Steroid Biochem. 34:391-395(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Skeletal muscle;
Ohkura N., Ito M., Tsukada T., Sasaki K., Yamaguchi K., Miki K.;
"Identification of an isoform of human TR3 (NGFI-B, Nur77).";
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Kobayashi T., Kodani Y., Sawasaki T., Endo Y.;
"Comprehensive DNA-binding analysis of human hormone nuclear receptors
by fluorescence correlation spectroscopy based on cell-free system.";
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Heart;
Kaighin V.A., Martin A.L., Aronstam R.S.;
"Isolation of cDNA coding for multiple human nuclear receptor
clones.";
Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Brain, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 35-398 (ISOFORM 1).
TISSUE=Colon adenocarcinoma;
PubMed=1651101;
Bondy G.P.;
"Phorbol ester, forskolin, and serum induction of a human colon
nuclear hormone receptor gene related to the NUR 77/NGFI-B genes.";
Cell Growth Differ. 2:203-208(1991).
[13]
FUNCTION.
PubMed=15466594; DOI=10.1093/nar/gkh856;
Harant H., Lindley I.J.;
"Negative cross-talk between the human orphan nuclear receptor
Nur77/NAK-1/TR3 and nuclear factor-kappaB.";
Nucleic Acids Res. 32:5280-5290(2004).
[14]
INTERACTION WITH GADD45GIP1.
PubMed=15459248; DOI=10.1210/me.2004-0107;
Park K.C., Song K.-H., Chung H.K., Kim H., Kim D.W., Song J.H.,
Hwang E.S., Jung H.S., Park S.-H., Bae I., Lee I.K., Choi H.-S.,
Shong M.;
"CR6-interacting factor 1 interacts with orphan nuclear receptor Nur77
and inhibits its transactivation.";
Mol. Endocrinol. 19:12-24(2005).
[15]
PHOSPHORYLATION AT SER-351.
PubMed=17360704; DOI=10.1074/jbc.M700906200;
Roux P.P., Shahbazian D., Vu H., Holz M.K., Cohen M.S., Taunton J.,
Sonenberg N., Blenis J.;
"RAS/ERK signaling promotes site-specific ribosomal protein S6
phosphorylation via RSK and stimulates cap-dependent translation.";
J. Biol. Chem. 282:14056-14064(2007).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
ACETYLATION, AND SUBCELLULAR LOCATION.
PubMed=20438716; DOI=10.1016/j.bcp.2010.04.026;
Kang S.A., Na H., Kang H.J., Kim S.H., Lee M.H., Lee M.O.;
"Regulation of Nur77 protein turnover through acetylation and
deacetylation induced by p300 and HDAC1.";
Biochem. Pharmacol. 80:867-873(2010).
[19]
INTERACTION WITH IFI27, AND SUBCELLULAR LOCATION.
PubMed=22427340; DOI=10.1161/CIRCRESAHA.111.258814;
Papac-Milicevic N., Breuss J.M., Zaujec J., Ryban L., Plyushch T.,
Wagner G.A., Fenzl S., Dremsek P., Cabaravdic M., Steiner M.,
Glass C.K., Binder C.J., Uhrin P., Binder B.R.;
"The interferon stimulated gene 12 inactivates vasculoprotective
functions of NR4A nuclear receptors.";
Circ. Res. 110:E50-E63(2012).
[20]
X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 351-598 ALONE AND IN COMPLEX
WITH ANTAGONIST, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH
STK11, AND MUTAGENESIS OF THR-595.
PubMed=22983157; DOI=10.1038/nchembio.1069;
Zhan Y.Y., Chen Y., Zhang Q., Zhuang J.J., Tian M., Chen H.Z.,
Zhang L.R., Zhang H.K., He J.P., Wang W.J., Wu R., Wang Y., Shi C.,
Yang K., Li A.Z., Xin Y.Z., Li T.Y., Yang J.Y., Zheng Z.H., Yu C.D.,
Lin S.C., Chang C., Huang P.Q., Lin T., Wu Q.;
"The orphan nuclear receptor Nur77 regulates LKB1 localization and
activates AMPK.";
Nat. Chem. Biol. 8:897-904(2012).
-!- FUNCTION: Orphan nuclear receptor. May act concomitantly with
NURR1 in regulating the expression of delayed-early genes during
liver regeneration. Binds the NGFI-B response element (NBRE) 5'-
AAAAGGTCA-3' (By similarity). May inhibit NF-kappa-B
transactivation of IL2. Participates in energy homeostasis by
sequestrating the kinase STK11 in the nucleus, thereby attenuating
cytoplasmic AMPK activation. Plays a role in the vascular response
to injury (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P12813, ECO:0000269|PubMed:15466594,
ECO:0000269|PubMed:22983157}.
-!- SUBUNIT: Binds DNA as a monomer (By similarity). Interacts with
GADD45GIP1 (PubMed:15459248). Interacts with STK11
(PubMed:22983157). Interacts with IFI27 (PubMed:22427340).
{ECO:0000250|UniProtKB:P22829, ECO:0000269|PubMed:15459248,
ECO:0000269|PubMed:22427340, ECO:0000269|PubMed:22983157}.
-!- INTERACTION:
Q9WMX2:- (xeno); NbExp=2; IntAct=EBI-721550, EBI-9028517;
Q9P2G1:ANKIB1; NbExp=2; IntAct=EBI-721550, EBI-2687890;
P10415:BCL2; NbExp=7; IntAct=EBI-721550, EBI-77694;
O60238:BNIP3L; NbExp=4; IntAct=EBI-16085263, EBI-849893;
P55273:CDKN2D; NbExp=3; IntAct=EBI-721550, EBI-745859;
O60888:CUTA; NbExp=2; IntAct=EBI-721550, EBI-1051556;
P03120:E2 (xeno); NbExp=3; IntAct=EBI-721550, EBI-1779322;
P32189:GK; NbExp=3; IntAct=EBI-721550, EBI-3926629;
P60370:KRTAP10-5; NbExp=3; IntAct=EBI-721550, EBI-10172150;
Q17RB8:LONRF1; NbExp=3; IntAct=EBI-721550, EBI-2341787;
Q16539-1:MAPK14; NbExp=5; IntAct=EBI-16085263, EBI-15834191;
P43243:MATR3; NbExp=2; IntAct=EBI-721550, EBI-352602;
Q96JS3:PGBD1; NbExp=3; IntAct=EBI-12697871, EBI-10290053;
Q9Y4D7:PLXND1; NbExp=2; IntAct=EBI-721550, EBI-310731;
Q99873:PRMT1; NbExp=6; IntAct=EBI-721550, EBI-78738;
Q04206:RELA; NbExp=3; IntAct=EBI-16085263, EBI-73886;
P12235:SLC25A4; NbExp=2; IntAct=EBI-16085263, EBI-359074;
P40763:STAT3; NbExp=3; IntAct=EBI-721550, EBI-518675;
P04637:TP53; NbExp=6; IntAct=EBI-721550, EBI-366083;
P04350:TUBB4A; NbExp=2; IntAct=EBI-721550, EBI-355007;
P50552:VASP; NbExp=2; IntAct=EBI-721550, EBI-748201;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20438716,
ECO:0000269|PubMed:22427340, ECO:0000269|PubMed:22983157}.
Cytoplasm {ECO:0000269|PubMed:20438716,
ECO:0000269|PubMed:22427340}. Note=Nuclear export to the cytoplasm
is XPO1-mediated and positively regulated by IFI27.
{ECO:0000269|PubMed:22427340}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P22736-1; Sequence=Displayed;
Name=2;
IsoId=P22736-2; Sequence=VSP_043086;
Note=No experimental confirmation available.;
Name=3;
IsoId=P22736-3; Sequence=VSP_047769, VSP_047770;
-!- TISSUE SPECIFICITY: Fetal muscle and adult liver, brain and
thyroid.
-!- INDUCTION: By growth-stimulating agents.
-!- PTM: Phosphorylated at Ser-351 by RPS6KA1 and RPS6KA3 in response
to mitogenic or stress stimuli. {ECO:0000269|PubMed:17360704}.
-!- PTM: Acetylated by p300/CBP, acetylation increases stability.
Deacetylated by HDAC1. {ECO:0000269|PubMed:20438716}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR4
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/NR4A1ID41573ch12q13.html";
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EMBL; D49728; BAA08565.1; -; mRNA.
EMBL; L13740; AAA36763.1; -; mRNA.
EMBL; D85245; BAA12746.1; -; mRNA.
EMBL; AK297526; BAG59929.1; -; mRNA.
EMBL; HQ692855; ADZ17366.1; -; mRNA.
EMBL; AB307717; BAH02308.1; -; mRNA.
EMBL; BT007144; AAP35808.1; -; mRNA.
EMBL; AK314437; BAG37048.1; -; mRNA.
EMBL; CR456704; CAG32985.1; -; mRNA.
EMBL; AC025259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471111; EAW58222.1; -; Genomic_DNA.
EMBL; CH471111; EAW58224.1; -; Genomic_DNA.
EMBL; CH471111; EAW58225.1; -; Genomic_DNA.
EMBL; BC016147; AAH16147.1; -; mRNA.
CCDS; CCDS55828.1; -. [P22736-2]
CCDS; CCDS8818.1; -. [P22736-1]
PIR; A37251; A37251.
RefSeq; NP_001189162.1; NM_001202233.1. [P22736-2]
RefSeq; NP_002126.2; NM_002135.4. [P22736-1]
RefSeq; NP_775180.1; NM_173157.2. [P22736-1]
RefSeq; XP_005268881.1; XM_005268824.3. [P22736-1]
RefSeq; XP_006719426.1; XM_006719363.1. [P22736-1]
RefSeq; XP_006719427.1; XM_006719364.3. [P22736-1]
UniGene; Hs.524430; -.
UniGene; Hs.670088; -.
PDB; 2QW4; X-ray; 2.80 A; A/B/C/D=347-598.
PDB; 3V3E; X-ray; 2.06 A; A/B=351-598.
PDB; 3V3Q; X-ray; 2.22 A; A/B=351-598.
PDB; 4JGV; X-ray; 3.01 A; A/B=351-598.
PDB; 4KZI; X-ray; 2.41 A; A/B=351-598.
PDB; 4KZJ; X-ray; 2.12 A; A/B=351-598.
PDB; 4KZM; X-ray; 2.30 A; A/B=351-598.
PDB; 4RE8; X-ray; 2.16 A; A/B=351-598.
PDB; 4REE; X-ray; 2.37 A; A/B=351-598.
PDB; 4REF; X-ray; 2.10 A; A/B=351-598.
PDB; 4RZE; X-ray; 2.49 A; A/B=351-598.
PDB; 4RZF; X-ray; 1.99 A; A/B=351-598.
PDB; 4RZG; X-ray; 2.70 A; A/B=351-598.
PDB; 4WHF; X-ray; 2.27 A; A/B=351-598.
PDB; 4WHG; X-ray; 2.18 A; A/B=351-598.
PDBsum; 2QW4; -.
PDBsum; 3V3E; -.
PDBsum; 3V3Q; -.
PDBsum; 4JGV; -.
PDBsum; 4KZI; -.
PDBsum; 4KZJ; -.
PDBsum; 4KZM; -.
PDBsum; 4RE8; -.
PDBsum; 4REE; -.
PDBsum; 4REF; -.
PDBsum; 4RZE; -.
PDBsum; 4RZF; -.
PDBsum; 4RZG; -.
PDBsum; 4WHF; -.
PDBsum; 4WHG; -.
ProteinModelPortal; P22736; -.
SMR; P22736; -.
BioGrid; 109407; 100.
DIP; DIP-40392N; -.
IntAct; P22736; 107.
MINT; P22736; -.
STRING; 9606.ENSP00000353427; -.
BindingDB; P22736; -.
ChEMBL; CHEMBL1293229; -.
MoonDB; P22736; Predicted.
iPTMnet; P22736; -.
PhosphoSitePlus; P22736; -.
BioMuta; NR4A1; -.
DMDM; 127819; -.
EPD; P22736; -.
PaxDb; P22736; -.
PeptideAtlas; P22736; -.
PRIDE; P22736; -.
ProteomicsDB; 54032; -.
ProteomicsDB; 54033; -. [P22736-2]
DNASU; 3164; -.
Ensembl; ENST00000243050; ENSP00000243050; ENSG00000123358. [P22736-1]
Ensembl; ENST00000360284; ENSP00000353427; ENSG00000123358. [P22736-2]
Ensembl; ENST00000394824; ENSP00000378301; ENSG00000123358. [P22736-1]
Ensembl; ENST00000394825; ENSP00000378302; ENSG00000123358. [P22736-1]
Ensembl; ENST00000548232; ENSP00000449587; ENSG00000123358. [P22736-3]
Ensembl; ENST00000550082; ENSP00000449539; ENSG00000123358. [P22736-2]
GeneID; 3164; -.
KEGG; hsa:3164; -.
UCSC; uc001rzs.4; human. [P22736-1]
CTD; 3164; -.
DisGeNET; 3164; -.
EuPathDB; HostDB:ENSG00000123358.19; -.
GeneCards; NR4A1; -.
H-InvDB; HIX0171621; -.
HGNC; HGNC:7980; NR4A1.
HPA; HPA059742; -.
HPA; HPA070142; -.
MIM; 139139; gene.
neXtProt; NX_P22736; -.
OpenTargets; ENSG00000123358; -.
PharmGKB; PA31761; -.
eggNOG; KOG4217; Eukaryota.
eggNOG; ENOG410YWNC; LUCA.
GeneTree; ENSGT00760000118887; -.
HOGENOM; HOG000230925; -.
HOVERGEN; HBG052663; -.
InParanoid; P22736; -.
KO; K04465; -.
PhylomeDB; P22736; -.
TreeFam; TF315430; -.
Reactome; R-HSA-198693; AKT phosphorylates targets in the nucleus.
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer.
SignaLink; P22736; -.
SIGNOR; P22736; -.
ChiTaRS; NR4A1; human.
EvolutionaryTrace; P22736; -.
GeneWiki; Nerve_Growth_factor_IB; -.
GenomeRNAi; 3164; -.
PRO; PR:P22736; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000123358; Expressed in 221 organ(s), highest expression level in right adrenal gland.
CleanEx; HS_NR4A1; -.
ExpressionAtlas; P22736; baseline and differential.
Genevisible; P22736; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0003677; F:DNA binding; ISS:BHF-UCL.
GO; GO:0004879; F:nuclear receptor activity; TAS:ProtInc.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IDA:BHF-UCL.
GO; GO:0071376; P:cellular response to corticotropin-releasing hormone stimulus; ISS:UniProtKB.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IMP:BHF-UCL.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IMP:BHF-UCL.
GO; GO:0035767; P:endothelial cell chemotaxis; IMP:BHF-UCL.
GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
GO; GO:0045786; P:negative regulation of cell cycle; ISS:UniProtKB.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0061469; P:regulation of type B pancreatic cell proliferation; ISS:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR003071; Nuc_orp_HMR_rcpt.
InterPro; IPR003070; Nuc_orph_rcpt.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR01285; HMRNUCRECPTR.
PRINTS; PR01284; NUCLEARECPTR.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS51843; NR_LBD; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Transcription;
Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 598 Nuclear receptor subfamily 4 group A
member 1.
/FTId=PRO_0000053715.
DOMAIN 360 595 NR LBD. {ECO:0000255|PROSITE-
ProRule:PRU01189}.
DNA_BIND 264 339 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 267 287 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 303 327 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
COMPBIAS 82 92 Poly-Ser.
COMPBIAS 583 586 Poly-Pro.
MOD_RES 341 341 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P22829}.
MOD_RES 351 351 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:17360704}.
VAR_SEQ 1 1 M -> MWLAKACWSIQSEM (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043086.
VAR_SEQ 293 325 RTVQKNAKYICLANKDCPVDKRRRNRCQFCRFQ -> VPRS
PRWGLLLEMERGWPHPIGTCGLPLGSPPS (in isoform
3). {ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.3}.
/FTId=VSP_047769.
VAR_SEQ 326 598 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.3}.
/FTId=VSP_047770.
VARIANT 26 26 L -> V (in dbSNP:rs1882118).
/FTId=VAR_061534.
MUTAGEN 595 595 T->E: Strongly weakens interaction with
STK11. {ECO:0000269|PubMed:22983157}.
CONFLICT 253 253 T -> I (in Ref. 12). {ECO:0000305}.
CONFLICT 262 262 G -> P (in Ref. 2; AAA36763).
{ECO:0000305}.
CONFLICT 360 360 S -> F (in Ref. 8; CAG32985).
{ECO:0000305}.
CONFLICT 370 370 R -> L (in Ref. 2; AAA36763).
{ECO:0000305}.
HELIX 364 373 {ECO:0000244|PDB:4RZF}.
HELIX 379 381 {ECO:0000244|PDB:4RZF}.
STRAND 395 397 {ECO:0000244|PDB:4REF}.
HELIX 400 422 {ECO:0000244|PDB:4RZF}.
HELIX 427 429 {ECO:0000244|PDB:4RZF}.
HELIX 432 454 {ECO:0000244|PDB:4RZF}.
HELIX 457 459 {ECO:0000244|PDB:4RZF}.
STRAND 461 463 {ECO:0000244|PDB:4RZF}.
STRAND 467 471 {ECO:0000244|PDB:4RZF}.
HELIX 472 479 {ECO:0000244|PDB:4RZF}.
HELIX 482 495 {ECO:0000244|PDB:4RZF}.
HELIX 500 511 {ECO:0000244|PDB:4RZF}.
HELIX 521 541 {ECO:0000244|PDB:4RZF}.
TURN 544 546 {ECO:0000244|PDB:3V3Q}.
HELIX 550 556 {ECO:0000244|PDB:4RZF}.
HELIX 558 579 {ECO:0000244|PDB:4RZF}.
HELIX 586 594 {ECO:0000244|PDB:4RZF}.
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


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