NUPR1_HUMAN
ID NUPR1_HUMAN Reviewed; 82 AA.
AC O60356; B2R5C4; O60357; Q6FGG3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Nuclear protein 1 {ECO:0000305};
DE AltName: Full=Candidate of metastasis 1 {ECO:0000303|PubMed:10493524};
DE AltName: Full=Protein p8 {ECO:0000303|PubMed:10092851};
GN Name=NUPR1 {ECO:0000312|HGNC:HGNC:29990}; Synonyms=COM1;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Pancreas;
RX PubMed=10092851; DOI=10.1046/j.1432-1327.1999.00092.x;
RA Vasseur S., Mallo G.V., Fiedler F., Boedeker H., Canepa E., Moreno S.,
RA Iovanna J.L.;
RT "Cloning and expression of the human p8, a nuclear protein with mitogenic
RT activity.";
RL Eur. J. Biochem. 259:670-675(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Mammary cancer;
RX PubMed=10493524;
RA Ree A.H., Tvermyr M., Engebraaten O., Rooman M., Rosok O., Hovig E.,
RA Meza-Zepeda L.A., Bruland O.S., Fodstad O.;
RT "Expression of a novel factor in human breast cancer cells with metastatic
RT potential.";
RL Cancer Res. 59:4675-4680(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=16341674; DOI=10.1007/s00335-005-0075-2;
RA Oh J.H., Yang J.O., Hahn Y., Kim M.R., Byun S.S., Jeon Y.J., Kim J.M.,
RA Song K.S., Noh S.M., Kim S., Yoo H.S., Kim Y.S., Kim N.S.;
RT "Transcriptome analysis of human gastric cancer.";
RL Mamm. Genome 16:942-954(2005).
RN [5]
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 vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from human
RT chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 [10]
RP DNA-BINDING, MONOMER, PHOSPHORYLATION, AND FUNCTION.
RX PubMed=11056169; DOI=10.1074/jbc.m008594200;
RA Encinar J.A., Mallo G.V., Mizyrycki C., Giono L., Gonzalez-Ros J.M.,
RA Rico M., Canepa E., Moreno S., Neira J.L., Iovanna J.L.;
RT "Human p8 is a HMG-I/Y-like protein with DNA binding activity enhanced by
RT phosphorylation.";
RL J. Biol. Chem. 276:2742-2751(2001).
RN [11]
RP INTERACTION WITH EP300 AND PAXIP1, ACETYLATION, AND FUNCTION.
RX PubMed=11940591; DOI=10.1074/jbc.m201657200;
RA Hoffmeister A., Ropolo A., Vasseur S., Mallo G.V., Bodeker H.,
RA Ritz-Laser B., Dressler G.R., Vaccaro M.I., Dagorn J.C., Moreno S.,
RA Iovanna J.L.;
RT "The HMG-I/Y-related protein p8 binds to p300 and Pax2 trans-activation
RT domain-interacting protein to regulate the trans-activation activity of the
RT Pax2A and Pax2B transcription factors on the glucagon gene promoter.";
RL J. Biol. Chem. 277:22314-22319(2002).
RN [12]
RP INTERACTION WITH COPS5, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16300740; DOI=10.1016/j.bbrc.2005.11.018;
RA Malicet C., Hoffmeister A., Moreno S., Closa D., Dagorn J.C., Vasseur S.,
RA Iovanna J.L.;
RT "Interaction of the stress protein p8 with Jab1 is required for Jab1-
RT dependent p27 nuclear-to-cytoplasm translocation.";
RL Biochem. Biophys. Res. Commun. 339:284-289(2006).
RN [13]
RP INTERACTION WITH PTMA, AND FUNCTION.
RX PubMed=16478804; DOI=10.1073/pnas.0508955103;
RA Malicet C., Giroux V., Vasseur S., Dagorn J.C., Neira J.L., Iovanna J.L.;
RT "Regulation of apoptosis by the p8/prothymosin alpha complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:2671-2676(2006).
RN [14]
RP INDUCTION, INTERACTION WITH TP53 AND EP300, AND FUNCTION.
RX PubMed=18690848; DOI=10.2174/156800908785133196;
RA Clark D.W., Mitra A., Fillmore R.A., Jiang W.G., Samant R.S., Fodstad O.,
RA Shevde L.A.;
RT "NUPR1 interacts with p53, transcriptionally regulates p21 and rescues
RT breast epithelial cells from doxorubicin-induced genotoxic stress.";
RL Curr. Cancer Drug Targets 8:421-430(2008).
RN [15]
RP FUNCTION, INTERACTION WITH MSL1 AND MORF4L1, AND INDUCTION BY
RP GAMMA-IRRADIATION.
RX PubMed=19650074; DOI=10.1002/jcp.21889;
RA Gironella M., Malicet C., Cano C., Sandi M.J., Hamidi T., Tauil R.M.,
RA Baston M., Valaco P., Moreno S., Lopez F., Neira J.L., Dagorn J.C.,
RA Iovanna J.L.;
RT "p8/nupr1 regulates DNA-repair activity after double-strand gamma
RT irradiation-induced DNA damage.";
RL J. Cell. Physiol. 221:594-602(2009).
RN [16]
RP INTERACTION WITH MYOD1, AND FUNCTION.
RX PubMed=19723804; DOI=10.1242/jcs.048678;
RA Sambasivan R., Cheedipudi S., Pasupuleti N., Saleh A., Pavlath G.K.,
RA Dhawan J.;
RT "The small chromatin-binding protein p8 coordinates the association of
RT anti-proliferative and pro-myogenic proteins at the myogenin promoter.";
RL J. Cell Sci. 122:3481-3491(2009).
RN [17]
RP INTERACTION WITH FOXO3, AND FUNCTION.
RX PubMed=20181828; DOI=10.1091/mbc.e09-09-0818;
RA Kong D.K., Georgescu S.P., Cano C., Aronovitz M.J., Iovanna J.L.,
RA Patten R.D., Kyriakis J.M., Goruppi S.;
RT "Deficiency of the transcriptional regulator p8 results in increased
RT autophagy and apoptosis, and causes impaired heart function.";
RL Mol. Biol. Cell 21:1335-1349(2010).
RN [18]
RP FUNCTION.
RX PubMed=22858377; DOI=10.1016/j.febslet.2012.07.063;
RA Vincent A.J., Ren S., Harris L.G., Devine D.J., Samant R.S., Fodstad O.,
RA Shevde L.A.;
RT "Cytoplasmic translocation of p21 mediates NUPR1-induced chemoresistance:
RT NUPR1 and p21 in chemoresistance.";
RL FEBS Lett. 586:3429-3434(2012).
RN [19]
RP FUNCTION, AND INDUCTION BY NUTRIENT DEPRIVATION.
RX PubMed=22565310; DOI=10.1172/jci60144;
RA Hamidi T., Algul H., Cano C.E., Sandi M.J., Molejon M.I., Riemann M.,
RA Calvo E.L., Lomberk G., Dagorn J.C., Weih F., Urrutia R., Schmid R.M.,
RA Iovanna J.L.;
RT "Nuclear protein 1 promotes pancreatic cancer development and protects
RT cells from stress by inhibiting apoptosis.";
RL J. Clin. Invest. 122:2092-2103(2012).
RN [20]
RP INTERACTION WITH RNF2, AND MUTAGENESIS OF ALA-33 AND THR-68.
RX PubMed=28720707; DOI=10.1073/pnas.1619932114;
RA Santofimia-Castano P., Rizzuti B., Pey A.L., Soubeyran P., Vidal M.,
RA Urrutia R., Iovanna J.L., Neira J.L.;
RT "Intrinsically disordered chromatin protein NUPR1 binds to the C-terminal
RT region of Polycomb RING1B.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E6332-E6341(2017).
RN [21]
RP FUNCTION.
RX PubMed=30451898; DOI=10.1038/s41598-018-35020-3;
RA Santofimia-Castano P., Lan W., Bintz J., Gayet O., Carrier A., Lomberk G.,
RA Neira J.L., Gonzalez A., Urrutia R., Soubeyran P., Iovanna J.;
RT "Inactivation of NUPR1 promotes cell death by coupling ER-stress responses
RT with necrosis.";
RL Sci. Rep. 8:16999-16999(2018).
CC -!- FUNCTION: Transcription regulator that converts stress signals into a
CC program of gene expression that empowers cells with resistance to the
CC stress induced by a change in their microenvironment. Thereby
CC participates in regulation of many process namely cell-cycle,
CC apoptosis, autophagy and DNA repair responses (PubMed:16478804,
CC PubMed:19650074, PubMed:16300740, PubMed:19723804, PubMed:11056169,
CC PubMed:22858377, PubMed:11940591, PubMed:18690848, PubMed:22565310,
CC PubMed:20181828, PubMed:30451898). Controls cell cycle progression and
CC protects cells from genotoxic stress induced by doxorubicin through the
CC complex formation with TP53 and EP300 that binds CDKN1A promoter
CC leading to transcriptional induction of CDKN1A (PubMed:18690848).
CC Protects pancreatic cancer cells from stress-induced cell death by
CC binding the RELB promoter and activating its transcription, leading to
CC IER3 transactivation (PubMed:22565310). Negatively regulates apoptosis
CC through interaction with PTMA (PubMed:16478804). Inhibits autophagy-
CC induced apoptosis in cardiac cells through FOXO3 interaction, inducing
CC cytoplasmic translocation of FOXO3 thereby preventing the FOXO3
CC association with the pro-autophagic BNIP3 promoter (PubMed:20181828).
CC Inhibits cell growth and facilitates programmed cell death by apoptosis
CC after adriamycin-induced DNA damage through transactivation of TP53 (By
CC similarity). Regulates methamphetamine-induced apoptosis and autophagy
CC through DDIT3-mediated endoplasmic reticulum stress pathway (By
CC similarity). Participates in DNA repair following gamma-irradiation by
CC facilitating DNA access of the transcription machinery through
CC interaction with MSL1 leading to inhibition of histone H4' Lys-16'
CC acetylation (H4K16ac) (PubMed:19650074). Coactivator of PAX2
CC transcription factor activity, both by recruiting EP300 to increase
CC PAX2 transcription factor activity and by binding PAXIP1 to suppress
CC PAXIP1-induced inhibition on PAX2 (PubMed:11940591). Positively
CC regulates cell cycle progression through interaction with COPS5
CC inducing cytoplasmic translocation of CDKN1B leading to the CDKN1B
CC degradation (PubMed:16300740). Coordinates, through its interaction
CC with EP300, the assiociation of MYOD1, EP300 and DDX5 to the MYOG
CC promoter, leading to inhibition of cell-cycle progression and myogenic
CC differentiation promotion (PubMed:19723804). Negatively regulates beta
CC cell proliferation via inhibition of cell-cycle regulatory genes
CC expression through the suppression of their promoter activities (By
CC similarity). Also required for LHB expression and ovarian maturation
CC (By similarity). Exacerbates CNS inflammation and demyelination upon
CC cuprizone treatment (By similarity). {ECO:0000250|UniProtKB:O54842,
CC ECO:0000250|UniProtKB:Q9WTK0, ECO:0000269|PubMed:11056169,
CC ECO:0000269|PubMed:11940591, ECO:0000269|PubMed:16300740,
CC ECO:0000269|PubMed:16478804, ECO:0000269|PubMed:18690848,
CC ECO:0000269|PubMed:19650074, ECO:0000269|PubMed:19723804,
CC ECO:0000269|PubMed:20181828, ECO:0000269|PubMed:22565310,
CC ECO:0000269|PubMed:22858377, ECO:0000269|PubMed:30451898}.
CC -!- SUBUNIT: Monomer. Directly interacts with MSL1 and binds MORF4L1, two
CC components of histone acetyltransferase complex; the interaction with
CC MORF4L1 may be mediated by MSL1 (PubMed:19650074). Interacts with
CC EP300; this interaction enhances the effect of EP300 on PAX2
CC transcription factor activity (PubMed:11940591). Interacts with PAXIP1;
CC this interaction prevents PAXIP1 inhibition of PAX2 transcription
CC factor activity (PubMed:11940591). Interacts with COPS5; this
CC interaction allows COPS5-dependent CDKN1B nuclear to cytoplasm
CC translocation (PubMed:16300740). Interacts with RNF2 (PubMed:28720707).
CC Interacts with FOXO3; this interaction represses FOXO3 transactivation
CC (PubMed:20181828). Interacts with PTMA; negatively regulates apoptotic
CC process (PubMed:16478804). Interacts with MYOD1, EP300 and DDX5; this
CC interaction coordinates the association of anti-proliferative and pro-
CC myogenic proteins at the myogenin promoter (PubMed:19723804) (By
CC similarity). Interacts with TP53; interaction is stress-dependent
CC (PubMed:18690848). Forms a complex with EP300 and TP53; this complex
CC binds CDKN1A promoter leading to transcriptional induction of CDKN1A
CC (PubMed:18690848). {ECO:0000250|UniProtKB:Q9WTK0,
CC ECO:0000269|PubMed:11940591, ECO:0000269|PubMed:16300740,
CC ECO:0000269|PubMed:16478804, ECO:0000269|PubMed:18690848,
CC ECO:0000269|PubMed:19650074, ECO:0000269|PubMed:19723804,
CC ECO:0000269|PubMed:20181828, ECO:0000269|PubMed:28720707}.
CC -!- INTERACTION:
CC O60356; P17655: CAPN2; NbExp=3; IntAct=EBI-3908808, EBI-1028956;
CC O60356; Q494V2-2: CFAP100; NbExp=3; IntAct=EBI-3908808, EBI-11953200;
CC O60356; O15534: PER1; NbExp=3; IntAct=EBI-3908808, EBI-2557276;
CC O60356; P06454: PTMA; NbExp=7; IntAct=EBI-3908808, EBI-2682091;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10092851,
CC ECO:0000269|PubMed:16300740}. Cytoplasm {ECO:0000269|PubMed:16300740}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:16300740}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60356-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60356-2; Sequence=VSP_053816;
CC -!- TISSUE SPECIFICITY: Widely expressed, with high levels in liver,
CC pancreas, prostate, ovary, colon, thyroid, spinal cord, trachea and
CC adrenal gland, moderate levels in heart, placenta, lung, skeletal
CC muscle, kidney, testis, small intestine, stomach and lymph node, and
CC low levels in brain, spleen, thymus and bone marrow. Not detected in
CC peripheral blood leukocytes. {ECO:0000269|PubMed:10092851}.
CC -!- INDUCTION: Up-regulated by stress agents, such as nutrient deprivation
CC (at protein level) (PubMed:22565310). Up-regulation by gamma-
CC irradiation is eventually followed by down-regulation
CC (PubMed:19650074). Expression increases with the tumor aggressiveness.
CC up-regulated by DNA-damaging agent such as doxorubicin
CC (PubMed:18690848). {ECO:0000269|PubMed:18690848,
CC ECO:0000269|PubMed:19650074, ECO:0000269|PubMed:22565310}.
CC -!- PTM: Phosphorylated in vitro by PKA and CK. Phosphorylation promotes
CC DNA-binding activity. {ECO:0000269|PubMed:11056169}.
CC -!- PTM: Acetylated by EP300 in vitro. {ECO:0000269|PubMed:11940591}.
CC -!- MISCELLANEOUS: Mediates resistance to anticancer drugs, namely taxol,
CC doxorubicin, gemcitabine. {ECO:0000269|PubMed:18690848,
CC ECO:0000269|PubMed:22565310, ECO:0000269|PubMed:22858377}.
CC -!- SIMILARITY: Belongs to the NUPR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC05335.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF069073; AAC19384.1; -; mRNA.
DR EMBL; AF069074; AAC19385.1; -; Genomic_DNA.
DR EMBL; AF135266; AAD49221.1; -; mRNA.
DR EMBL; AK312135; BAG35071.1; -; mRNA.
DR EMBL; BM792961; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BT006896; AAP35542.1; -; mRNA.
DR EMBL; CR542144; CAG46941.1; -; mRNA.
DR EMBL; AC002425; AAC05336.1; -; Genomic_DNA.
DR EMBL; AC002425; AAC05335.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471279; EAW52274.1; -; Genomic_DNA.
DR EMBL; BC002434; AAH02434.1; -; mRNA.
DR CCDS; CCDS10634.1; -. [O60356-1]
DR CCDS; CCDS42137.1; -. [O60356-2]
DR RefSeq; NP_001035948.1; NM_001042483.1. [O60356-2]
DR RefSeq; NP_036517.1; NM_012385.2. [O60356-1]
DR AlphaFoldDB; O60356; -.
DR BMRB; O60356; -.
DR BioGRID; 117695; 681.
DR DIP; DIP-61114N; -.
DR IntAct; O60356; 24.
DR iPTMnet; O60356; -.
DR PhosphoSitePlus; O60356; -.
DR BioMuta; NUPR1; -.
DR MassIVE; O60356; -.
DR PeptideAtlas; O60356; -.
DR PRIDE; O60356; -.
DR ProteomicsDB; 49379; -. [O60356-1]
DR Antibodypedia; 13028; 154 antibodies from 26 providers.
DR DNASU; 26471; -.
DR Ensembl; ENST00000324873.8; ENSP00000315559.7; ENSG00000176046.9. [O60356-1]
DR Ensembl; ENST00000395641.2; ENSP00000379003.2; ENSG00000176046.9. [O60356-2]
DR GeneID; 26471; -.
DR KEGG; hsa:26471; -.
DR MANE-Select; ENST00000324873.8; ENSP00000315559.7; NM_012385.3; NP_036517.1.
DR UCSC; uc002dqd.2; human. [O60356-1]
DR CTD; 26471; -.
DR DisGeNET; 26471; -.
DR GeneCards; NUPR1; -.
DR HGNC; HGNC:29990; NUPR1.
DR HPA; ENSG00000176046; Tissue enhanced (pancreas).
DR MIM; 614812; gene.
DR neXtProt; NX_O60356; -.
DR OpenTargets; ENSG00000176046; -.
DR PharmGKB; PA165450395; -.
DR VEuPathDB; HostDB:ENSG00000176046; -.
DR GeneTree; ENSGT00530000064242; -.
DR HOGENOM; CLU_180450_1_0_1; -.
DR InParanoid; O60356; -.
DR OMA; RQNPAGH; -.
DR OrthoDB; 1609352at2759; -.
DR PhylomeDB; O60356; -.
DR TreeFam; TF324649; -.
DR PathwayCommons; O60356; -.
DR SignaLink; O60356; -.
DR SIGNOR; O60356; -.
DR BioGRID-ORCS; 26471; 8 hits in 1073 CRISPR screens.
DR ChiTaRS; NUPR1; human.
DR GeneWiki; NUPR1; -.
DR GenomeRNAi; 26471; -.
DR Pharos; O60356; Tbio.
DR PRO; PR:O60356; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O60356; protein.
DR Bgee; ENSG00000176046; Expressed in left lobe of thyroid gland and 93 other tissues.
DR ExpressionAtlas; O60356; baseline and differential.
DR Genevisible; O60356; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0032993; C:protein-DNA complex; IDA:CAFA.
DR GO; GO:0010698; F:acetyltransferase activator activity; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
DR GO; GO:0002526; P:acute inflammatory response; IEA:Ensembl.
DR GO; GO:0044346; P:fibroblast apoptotic process; IEA:Ensembl.
DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:1902902; P:negative regulation of autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP:UniProtKB.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IMP:UniProtKB.
DR GO; GO:0045786; P:negative regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:1904036; P:negative regulation of epithelial cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0045820; P:negative regulation of glycolytic process; IMP:UniProtKB.
DR GO; GO:0062099; P:negative regulation of programmed necrotic cell death; IMP:UniProtKB.
DR GO; GO:1904691; P:negative regulation of type B pancreatic cell proliferation; ISS:UniProtKB.
DR GO; GO:0045787; P:positive regulation of cell cycle; IDA:UniProtKB.
DR GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; IEA:Ensembl.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0150078; P:positive regulation of neuroinflammatory response; ISS:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:1903862; P:positive regulation of oxidative phosphorylation; IMP:UniProtKB.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IMP:UniProtKB.
DR GO; GO:0031401; P:positive regulation of protein modification process; IEA:Ensembl.
DR GO; GO:0006473; P:protein acetylation; IEA:Ensembl.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
DR GO; GO:2000194; P:regulation of female gonad development; IEA:Ensembl.
DR GO; GO:1905897; P:regulation of response to endoplasmic reticulum stress; IMP:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR DisProt; DP00510; -.
DR InterPro; IPR018792; NUPR1-like.
DR PANTHER; PTHR17149; PTHR17149; 1.
DR Pfam; PF10195; Phospho_p8; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytoplasm; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..82
FT /note="Nuclear protein 1"
FT /id="PRO_0000058007"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 65..82
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT VAR_SEQ 37
FT /note="L -> LGPLIMPMPTSPLTPALVT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16341674"
FT /id="VSP_053816"
FT MUTAGEN 33
FT /note="A->Q: Impairs interaction with RNF2."
FT /evidence="ECO:0000269|PubMed:28720707"
FT MUTAGEN 68
FT /note="T->Q: Impairs interaction with RNF2."
FT /evidence="ECO:0000269|PubMed:28720707"
FT CONFLICT 47
FT /note="K -> N (in Ref. 3; BAG35071)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 82 AA; 8873 MW; 596E342D10F87AF3 CRC64;
MATFPPATSA PQQPPGPEDE DSSLDESDLY SLAHSYLGGG GRKGRTKREA AANTNRPSPG
GHERKLVTKL QNSERKKRGA RR
