NMD3_HUMAN
ID NMD3_HUMAN Reviewed; 503 AA.
AC Q96D46; D3DNM7; Q9Y2Z6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=60S ribosomal export protein NMD3;
DE Short=hNMD3;
GN Name=NMD3; ORFNames=CGI-07;
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 [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LYS-6.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
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 [4]
RP FUNCTION, IDENTIFICATION IN A 60S RIBOSOMAL SUBUNIT COMPLEX WITH RAN AND
RP XPO1, INTERACTION WITH XPO1, ASSOCIATION WITH THE 60S RIBOSOMAL SUBUNIT,
RP MUTAGENESIS OF LEU-484 AND LEU-487, AND SUBCELLULAR LOCATION.
RX PubMed=12724356; DOI=10.1242/jcs.00464;
RA Thomas F., Kutay U.;
RT "Biogenesis and nuclear export of ribosomal subunits in higher eukaryotes
RT depend on the CRM1 export pathway.";
RL J. Cell Sci. 116:2409-2419(2003).
RN [5]
RP FUNCTION, ASSOCIATION WITH THE 60S RIBOSOMAL SUBUNIT, MUTAGENESIS OF
RP LYS-405; LYS-406; LEU-480; LEU-484 AND LEU-487, AND SUBCELLULAR LOCATION.
RX PubMed=12773398; DOI=10.1093/emboj/cdg249;
RA Trotta C.R., Lund E., Kahan L., Johnson A.W., Dahlberg J.E.;
RT "Coordinated nuclear export of 60S ribosomal subunits and NMD3 in
RT vertebrates.";
RL EMBO J. 22:2841-2851(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-433; SER-468 AND THR-470, AND
RP IDENTIFICATION 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468 AND THR-470, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468 AND THR-470, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-470, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-468 AND THR-470, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15] {ECO:0007744|PDB:6LQM, ECO:0007744|PDB:6LSR, ECO:0007744|PDB:6LU8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.09 ANGSTROMS) IN COMPLEX WITH PRE-60S
RP RIBOSOMAL PARTICLES, AND INTERACTION WITH PRE-60S RIBOSOMAL PARTICLES.
RX PubMed=32669547; DOI=10.1038/s41467-020-17237-x;
RA Liang X., Zuo M.Q., Zhang Y., Li N., Ma C., Dong M.Q., Gao N.;
RT "Structural snapshots of human pre-60S ribosomal particles before and after
RT nuclear export.";
RL Nat. Commun. 11:3542-3542(2020).
CC -!- FUNCTION: Acts as an adapter for the XPO1/CRM1-mediated export of the
CC 60S ribosomal subunit. {ECO:0000269|PubMed:12724356,
CC ECO:0000269|PubMed:12773398}.
CC -!- SUBUNIT: Found in a 60S ribosomal subunit export complex with RAN and
CC XPO1 (PubMed:12724356). Interacts with XPO1. Associates with pre-60S
CC ribosomal particles (PubMed:12724356, PubMed:32669547).
CC {ECO:0000269|PubMed:12724356, ECO:0000269|PubMed:32669547}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12724356,
CC ECO:0000269|PubMed:12773398}. Nucleus {ECO:0000269|PubMed:12724356,
CC ECO:0000269|PubMed:12773398}. Note=Shuttles between the
CC nucleus/nucleolus and the cytoplasm in a XPO1/CRM1-dependent manner.
CC {ECO:0000269|PubMed:12724356, ECO:0000269|PubMed:12773398}.
CC -!- SIMILARITY: Belongs to the NMD3 family. {ECO:0000305}.
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DR EMBL; AF132941; AAD27716.1; -; mRNA.
DR EMBL; CH471052; EAW78618.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78619.1; -; Genomic_DNA.
DR EMBL; BC013317; AAH13317.1; -; mRNA.
DR CCDS; CCDS3194.1; -.
DR RefSeq; NP_057022.2; NM_015938.4.
DR RefSeq; XP_005247568.1; XM_005247511.1.
DR RefSeq; XP_005247569.1; XM_005247512.1.
DR PDB; 6LQM; EM; 3.09 A; 3=1-503.
DR PDB; 6LSR; EM; 3.13 A; 3=1-503.
DR PDB; 6LU8; EM; 3.13 A; 3=1-503.
DR PDBsum; 6LQM; -.
DR PDBsum; 6LSR; -.
DR PDBsum; 6LU8; -.
DR AlphaFoldDB; Q96D46; -.
DR SMR; Q96D46; -.
DR BioGRID; 119259; 112.
DR DIP; DIP-53427N; -.
DR IntAct; Q96D46; 21.
DR MINT; Q96D46; -.
DR STRING; 9606.ENSP00000419004; -.
DR GlyGen; Q96D46; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96D46; -.
DR MetOSite; Q96D46; -.
DR PhosphoSitePlus; Q96D46; -.
DR BioMuta; NMD3; -.
DR DMDM; 74731412; -.
DR EPD; Q96D46; -.
DR jPOST; Q96D46; -.
DR MassIVE; Q96D46; -.
DR MaxQB; Q96D46; -.
DR PaxDb; Q96D46; -.
DR PeptideAtlas; Q96D46; -.
DR PRIDE; Q96D46; -.
DR ProteomicsDB; 76251; -.
DR Antibodypedia; 33677; 131 antibodies from 27 providers.
DR DNASU; 51068; -.
DR Ensembl; ENST00000351193.7; ENSP00000307525.2; ENSG00000169251.13.
DR Ensembl; ENST00000460469.1; ENSP00000419004.1; ENSG00000169251.13.
DR GeneID; 51068; -.
DR KEGG; hsa:51068; -.
DR MANE-Select; ENST00000351193.7; ENSP00000307525.2; NM_015938.5; NP_057022.2.
DR UCSC; uc003feb.2; human.
DR CTD; 51068; -.
DR DisGeNET; 51068; -.
DR GeneCards; NMD3; -.
DR HGNC; HGNC:24250; NMD3.
DR HPA; ENSG00000169251; Low tissue specificity.
DR MIM; 611021; gene.
DR neXtProt; NX_Q96D46; -.
DR OpenTargets; ENSG00000169251; -.
DR PharmGKB; PA134884140; -.
DR VEuPathDB; HostDB:ENSG00000169251; -.
DR eggNOG; KOG2613; Eukaryota.
DR GeneTree; ENSGT00390000005104; -.
DR HOGENOM; CLU_027444_2_0_1; -.
DR InParanoid; Q96D46; -.
DR OMA; ILVKKHY; -.
DR PhylomeDB; Q96D46; -.
DR TreeFam; TF105744; -.
DR PathwayCommons; Q96D46; -.
DR SignaLink; Q96D46; -.
DR BioGRID-ORCS; 51068; 725 hits in 1080 CRISPR screens.
DR ChiTaRS; NMD3; human.
DR GeneWiki; NMD3; -.
DR GenomeRNAi; 51068; -.
DR Pharos; Q96D46; Tbio.
DR PRO; PR:Q96D46; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q96D46; protein.
DR Bgee; ENSG00000169251; Expressed in endothelial cell and 202 other tissues.
DR ExpressionAtlas; Q96D46; baseline and differential.
DR Genevisible; Q96D46; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043023; F:ribosomal large subunit binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0032092; P:positive regulation of protein binding; IMP:ParkinsonsUK-UCL.
DR GO; GO:1904751; P:positive regulation of protein localization to nucleolus; IMP:ParkinsonsUK-UCL.
DR GO; GO:1902680; P:positive regulation of RNA biosynthetic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:ParkinsonsUK-UCL.
DR InterPro; IPR039768; Nmd3.
DR InterPro; IPR007064; Nmd3_N.
DR PANTHER; PTHR12746; PTHR12746; 1.
DR Pfam; PF04981; NMD3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..503
FT /note="60S ribosomal export protein NMD3"
FT /id="PRO_0000323561"
FT REGION 425..503
FT /note="Necessary for the nuclear export of the 60S
FT ribosomal subunit"
FT /evidence="ECO:0000269|PubMed:12773398"
FT MOTIF 405..422
FT /note="Nuclear and nucleolar localization signal"
FT /evidence="ECO:0000269|PubMed:12773398"
FT MOTIF 480..489
FT /note="Nuclear export signal"
FT /evidence="ECO:0000269|PubMed:12773398"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 433
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 470
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VARIANT 6
FT /note="E -> K (in dbSNP:rs12490341)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_039546"
FT MUTAGEN 405
FT /note="K->A: Reduces accumulation in the nucleus. Loss of
FT nucleolar localization; when associated with A-406."
FT /evidence="ECO:0000269|PubMed:12773398"
FT MUTAGEN 406
FT /note="K->A: Reduces accumulation in the nucleus. Loss of
FT nucleolar localization; when associated with A-405."
FT /evidence="ECO:0000269|PubMed:12773398"
FT MUTAGEN 480
FT /note="L->A: Reduces nuclear export."
FT /evidence="ECO:0000269|PubMed:12773398"
FT MUTAGEN 484
FT /note="L->A: Reduces nuclear export."
FT /evidence="ECO:0000269|PubMed:12724356,
FT ECO:0000269|PubMed:12773398"
FT MUTAGEN 487
FT /note="L->A: Reduces nuclear export."
FT /evidence="ECO:0000269|PubMed:12724356,
FT ECO:0000269|PubMed:12773398"
FT CONFLICT 319
FT /note="M -> I (in Ref. 1; AAD27716)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 57603 MW; 5CEFD4E41FE2EBC1 CRC64;
MEYMAESTDR SPGHILCCEC GVPISPNPAN ICVACLRSKV DISQGIPKQV SISFCKQCQR
YFQPPGTWIQ CALESRELLA LCLKKIKAPL SKVRLVDAGF VWTEPHSKRL KVKLTIQKEV
MNGAILQQVF VVDYVVQSQM CGDCHRVEAK DFWKAVIQVR QKTLHKKTFY YLEQLILKYG
MHQNTLRIKE IHDGLDFYYS SKQHAQKMVE FLQCTVPCRY KASQRLISQD IHSNTYNYKS
TFSVEIVPIC KDNVVCLSPK LAQSLGNMNQ ICVCIRVTSA IHLIDPNTLQ VADIDGSTFW
SHPFNSLCHP KQLEEFIVME CSIVQDIKRA AGAGMISKKH TLGEVWVQKT SEMNTDKQYF
CRTHLGHLLN PGDLVLGFDL ANCNLNDEHV NKMNSDRVPD VVLIKKSYDR TKRQRRRNWK
LKELAREREN MDTDDERQYQ DFLEDLEEDE AIRKNVNIYR DSAIPVESDT DDEGAPRISL
AEMLEDLHIS QDATGEEGAS MLT
