ID G45IP_HUMAN Reviewed; 222 AA. AC Q8TAE8; Q8IVM3; Q8TE51; Q969P9; Q9BSM6; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 24-JAN-2024, entry version 164. DE RecName: Full=Large ribosomal subunit protein mL64 {ECO:0000303|PubMed:27023846}; DE AltName: Full=39S ribosomal protein L59, mitochondrial; DE Short=MRP-L59; DE AltName: Full=CKII beta-associating protein; DE AltName: Full=CR6-interacting factor 1; DE Short=CRIF1; DE AltName: Full=Growth arrest and DNA damage-inducible proteins-interacting protein 1; DE AltName: Full=Papillomavirus L2-interacting nuclear protein 1; DE Short=PLINP; DE Short=PLINP-1; DE AltName: Full=p53-responsive gene 6 protein; GN Name=GADD45GIP1; Synonyms=MRPL59, PLINP1, PRG6; 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 [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH RP HPV16 L2 (MICROBIAL INFECTION). RC TISSUE=Keratinocyte; RX PubMed=12482659; DOI=10.1006/viro.2002.1670; RA Goernemann J., Hofmann T.G., Will H., Mueller M.; RT "Interaction of human papillomavirus type 16 L2 with cellular proteins: RT identification of novel nuclear body-associated proteins."; RL Virology 303:69-78(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH GADD45A; RP GADD45B AND GADD45G, AND TISSUE SPECIFICITY. RC TISSUE=Colon carcinoma; RX PubMed=12716909; DOI=10.1074/jbc.m212835200; RA Chung H.K., Yi Y.-W., Jung N.-C., Kim D., Suh J.M., Kim H., Park K.C., RA Song J.H., Kim D.W., Hwang E.S., Yoon S.-H., Bae Y.-S., Kim J.M., Bae I., RA Shong M.; RT "CR6-interacting factor 1 interacts with Gadd45 family proteins and RT modulates the cell cycle."; RL J. Biol. Chem. 278:28079-28088(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung, Muscle, and 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-222. RA Frigimelica E., Lanfranchi G.; RT "Full length sequencing of some human and murine muscular transcripts RT (Telethon Italy project B41)."; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 90-122, AND INDUCTION. RX PubMed=10441517; DOI=10.1006/bbrc.1999.1123; RA Horikoshi N., Cong J., Kley N., Shenk T.; RT "Isolation of differentially expressed cDNAs from p53-dependent apoptotic RT cells: activation of the human homologue of the Drosophila peroxidasin RT gene."; RL Biochem. Biophys. Res. Commun. 261:864-869(1999). RN [6] RP INTERACTION WITH NR4A1/NUR77. 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., Hwang E.S., RA Jung H.S., Park S.-H., Bae I., Lee I.K., Choi H.-S., Shong M.; RT "CR6-interacting factor 1 interacts with orphan nuclear receptor Nur77 and RT inhibits its transactivation."; RL Mol. Endocrinol. 19:12-24(2005). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [8] 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 [9] 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 [10] RP INTERACTION WITH ATAD3A AND ATAD3B, AND SUBCELLULAR LOCATION. RX PubMed=22453275; DOI=10.1093/nar/gks266; RA He J., Cooper H.M., Reyes A., Di Re M., Sembongi H., Litwin T.R., Gao J., RA Neuman K.C., Fearnley I.M., Spinazzola A., Walker J.E., Holt I.J.; RT "Mitochondrial nucleoid interacting proteins support mitochondrial protein RT synthesis."; RL Nucleic Acids Res. 40:6109-6121(2012). RN [11] RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=23908630; DOI=10.3389/fphys.2013.00183; RA Koc E.C., Cimen H., Kumcuoglu B., Abu N., Akpinar G., Haque M.E., RA Spremulli L.L., Koc H.; RT "Identification and characterization of CHCHD1, AURKAIP1, and CRIF1 as new RT members of the mammalian mitochondrial ribosome."; RL Front. Physiol. 4:183-183(2013). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [13] RP NOMENCLATURE. RX PubMed=27023846; DOI=10.1146/annurev-biochem-060815-014343; RA Greber B.J., Ban N.; RT "Structure and function of the mitochondrial ribosome."; RL Annu. Rev. Biochem. 85:103-132(2016). RN [14] {ECO:0007744|PDB:3J7Y} RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), SUBCELLULAR LOCATION, RP AND SUBUNIT. RX PubMed=25278503; DOI=10.1126/science.1258026; RA Brown A., Amunts A., Bai X.C., Sugimoto Y., Edwards P.C., Murshudov G., RA Scheres S.H., Ramakrishnan V.; RT "Structure of the large ribosomal subunit from human mitochondria."; RL Science 346:718-722(2014). RN [15] {ECO:0007744|PDB:3J9M} RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), SUBCELLULAR LOCATION, RP AND SUBUNIT. RX PubMed=25838379; DOI=10.1126/science.aaa1193; RA Amunts A., Brown A., Toots J., Scheres S.H., Ramakrishnan V.; RT "Ribosome. The structure of the human mitochondrial ribosome."; RL Science 348:95-98(2015). RN [16] {ECO:0007744|PDB:5OOL, ECO:0007744|PDB:5OOM} RP STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS), SUBCELLULAR LOCATION, RP AND SUBUNIT. RX PubMed=28892042; DOI=10.1038/nsmb.3464; RA Brown A., Rathore S., Kimanius D., Aibara S., Bai X.C., Rorbach J., RA Amunts A., Ramakrishnan V.; RT "Structures of the human mitochondrial ribosome in native states of RT assembly."; RL Nat. Struct. Mol. Biol. 24:866-869(2017). CC -!- FUNCTION: Acts as a negative regulator of G1 to S cell cycle phase CC progression by inhibiting cyclin-dependent kinases. Inhibitory effects CC are additive with GADD45 proteins but occurs also in the absence of CC GADD45 proteins. Acts as a repressor of the orphan nuclear receptor CC NR4A1 by inhibiting AB domain-mediated transcriptional activity. May be CC involved in the hormone-mediated regulation of NR4A1 transcriptional CC activity. May play a role in mitochondrial protein synthesis. CC -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt- CC LSU) (PubMed:28892042, PubMed:25838379, PubMed:25278503). Mature CC mammalian 55S mitochondrial ribosomes consist of a small (28S) and a CC large (39S) subunit. The 28S small subunit contains a 12S ribosomal RNA CC (12S mt-rRNA) and 30 different proteins. The 39S large subunit contains CC a 16S rRNA (16S mt-rRNA), a copy of mitochondrial valine transfer RNA CC (mt-tRNA(Val)), which plays an integral structural role, and 52 CC different proteins (PubMed:23908630, PubMed:25278503, PubMed:25838379). CC Interacts with GADD45A, GADD45B and GADD45G (PubMed:12716909). CC Interacts with NR4A1 via the NR4A1 AB domain (PubMed:15459248). CC Interacts with ATAD3A and ATAD3B (PubMed:22453275). CC {ECO:0000269|PubMed:12716909, ECO:0000269|PubMed:15459248, CC ECO:0000269|PubMed:22453275, ECO:0000269|PubMed:23908630, CC ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, CC ECO:0000269|PubMed:28892042}. CC -!- SUBUNIT: (Microbial infection) Interacts with the human papilloma virus CC type 16 (HPV 16) minor capsid protein L2. CC {ECO:0000269|PubMed:12482659}. CC -!- INTERACTION: CC Q8TAE8; O15084: ANKRD28; NbExp=3; IntAct=EBI-372506, EBI-359567; CC Q8TAE8; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-372506, EBI-953896; CC Q8TAE8; A2RRN7: CADPS; NbExp=3; IntAct=EBI-372506, EBI-10179719; CC Q8TAE8; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-372506, EBI-3866279; CC Q8TAE8; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-372506, EBI-11524851; CC Q8TAE8; P24863: CCNC; NbExp=3; IntAct=EBI-372506, EBI-395261; CC Q8TAE8; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-372506, EBI-739624; CC Q8TAE8; Q92997: DVL3; NbExp=3; IntAct=EBI-372506, EBI-739789; CC Q8TAE8; Q96JC9: EAF1; NbExp=3; IntAct=EBI-372506, EBI-769261; CC Q8TAE8; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-372506, EBI-744099; CC Q8TAE8; P24522: GADD45A; NbExp=3; IntAct=EBI-372506, EBI-448167; CC Q8TAE8; O95257: GADD45G; NbExp=4; IntAct=EBI-372506, EBI-448202; CC Q8TAE8; O95995: GAS8; NbExp=3; IntAct=EBI-372506, EBI-1052570; CC Q8TAE8; P55040: GEM; NbExp=3; IntAct=EBI-372506, EBI-744104; CC Q8TAE8; Q08379: GOLGA2; NbExp=3; IntAct=EBI-372506, EBI-618309; CC Q8TAE8; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-372506, EBI-11163335; CC Q8TAE8; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-372506, EBI-5916454; CC Q8TAE8; Q96D09: GPRASP2; NbExp=3; IntAct=EBI-372506, EBI-473189; CC Q8TAE8; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-372506, EBI-14103818; CC Q8TAE8; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-372506, EBI-740641; CC Q8TAE8; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-372506, EBI-2556193; CC Q8TAE8; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-372506, EBI-14069005; CC Q8TAE8; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-372506, EBI-3044087; CC Q8TAE8; Q15323: KRT31; NbExp=3; IntAct=EBI-372506, EBI-948001; CC Q8TAE8; O76011: KRT34; NbExp=3; IntAct=EBI-372506, EBI-1047093; CC Q8TAE8; Q6A162: KRT40; NbExp=3; IntAct=EBI-372506, EBI-10171697; CC Q8TAE8; O95751: LDOC1; NbExp=3; IntAct=EBI-372506, EBI-740738; CC Q8TAE8; Q5JTD7: LRRC73; NbExp=3; IntAct=EBI-372506, EBI-12003882; CC Q8TAE8; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-372506, EBI-741037; CC Q8TAE8; P43364: MAGEA11; NbExp=3; IntAct=EBI-372506, EBI-739552; CC Q8TAE8; P43360: MAGEA6; NbExp=3; IntAct=EBI-372506, EBI-1045155; CC Q8TAE8; O95983-2: MBD3; NbExp=3; IntAct=EBI-372506, EBI-11978579; CC Q8TAE8; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-372506, EBI-2548751; CC Q8TAE8; Q13064: MKRN3; NbExp=3; IntAct=EBI-372506, EBI-2340269; CC Q8TAE8; Q96DV4: MRPL38; NbExp=4; IntAct=EBI-372506, EBI-720441; CC Q8TAE8; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-372506, EBI-11522433; CC Q8TAE8; Q9HB07: MYG1; NbExp=3; IntAct=EBI-372506, EBI-709754; CC Q8TAE8; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-372506, EBI-10271199; CC Q8TAE8; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-372506, EBI-741158; CC Q8TAE8; O43482: OIP5; NbExp=3; IntAct=EBI-372506, EBI-536879; CC Q8TAE8; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-372506, EBI-10302990; CC Q8TAE8; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-372506, EBI-79165; CC Q8TAE8; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-372506, EBI-302345; CC Q8TAE8; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-372506, EBI-11320284; CC Q8TAE8; P20618: PSMB1; NbExp=3; IntAct=EBI-372506, EBI-372273; CC Q8TAE8; P57052: RBM11; NbExp=3; IntAct=EBI-372506, EBI-741332; CC Q8TAE8; P02549: SPTA1; NbExp=3; IntAct=EBI-372506, EBI-375617; CC Q8TAE8; P40763: STAT3; NbExp=4; IntAct=EBI-372506, EBI-518675; CC Q8TAE8; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-372506, EBI-1105213; CC Q8TAE8; Q13077: TRAF1; NbExp=3; IntAct=EBI-372506, EBI-359224; CC Q8TAE8; P14373: TRIM27; NbExp=3; IntAct=EBI-372506, EBI-719493; CC Q8TAE8; O00308: WWP2; NbExp=3; IntAct=EBI-372506, EBI-743923; CC Q8TAE8; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-372506, EBI-527853; CC Q8TAE8; P22339: Gadd45b; Xeno; NbExp=3; IntAct=EBI-372506, EBI-2266938; CC Q8TAE8; P42227: Stat3; Xeno; NbExp=3; IntAct=EBI-372506, EBI-602878; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22453275, CC ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, CC ECO:0000269|PubMed:28892042}. Nucleus {ECO:0000269|PubMed:12482659}. CC Note=Using N-terminally tagged constructs, has been found in the CC nucleus (PubMed:12482659). C-terminally tagged constructs are targeted CC exclusively to mitochondria (PubMed:22453275). This discrepancy may be CC explained by masking of a potential N-terminal mitochondrial targeting CC signal by the tag (PubMed:22453275). {ECO:0000269|PubMed:12482659, CC ECO:0000269|PubMed:22453275}. CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in the thyroid CC gland, heart, lymph nodes, trachea and adrenal tissues. Expressed at CC lower level in liver skeletal muscle, kidney, pancreas, testis, ovary CC and stomach. Barely detectable in adrenal adenoma and papillary thyroid CC cancer. {ECO:0000269|PubMed:12716909}. CC -!- INDUCTION: Down-regulated by p53/TP53 in apoptotic cells. CC {ECO:0000269|PubMed:10441517}. CC -!- MISCELLANEOUS: Cells overexpressing GADD45GIP1 were more likely to be CC in G1 and less likely to be in S phase and grow more slowly than CC control cells. Inhibiting the expression of GADD45GIP1 promotes cell CC cycle progression. CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein CC mL64 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/40668/GADD45GIP1"; 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; AJ429498; CAD22344.1; -; mRNA. DR EMBL; AF479749; AAL85877.1; -; mRNA. DR EMBL; AF475095; AAM10639.1; -; mRNA. DR EMBL; BC004944; AAH04944.1; -; mRNA. DR EMBL; BC013039; AAH13039.2; -; mRNA. DR EMBL; BC013027; AAH13027.2; -; mRNA. DR EMBL; BC069200; AAH69200.1; -; mRNA. DR EMBL; AJ295986; CAC82499.1; -; mRNA. DR EMBL; AF147080; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS12290.1; -. DR RefSeq; NP_443082.2; NM_052850.3. DR PDB; 3J7Y; EM; 3.40 A; q=1-222. DR PDB; 3J9M; EM; 3.50 A; q=1-222. DR PDB; 5OOL; EM; 3.06 A; q=1-222. DR PDB; 5OOM; EM; 3.03 A; q=1-222. DR PDB; 6I9R; EM; 3.90 A; q=1-222. DR PDB; 6NU2; EM; 3.90 A; q=25-152. DR PDB; 6NU3; EM; 4.40 A; q=1-222. DR PDB; 6VLZ; EM; 2.97 A; q=1-222. DR PDB; 6VMI; EM; 2.96 A; q=1-222. DR PDB; 6ZM5; EM; 2.89 A; q=1-222. DR PDB; 6ZM6; EM; 2.59 A; q=1-222. DR PDB; 6ZS9; EM; 4.00 A; q=25-222. DR PDB; 6ZSA; EM; 4.00 A; q=25-222. DR PDB; 6ZSB; EM; 4.50 A; q=25-222. DR PDB; 6ZSC; EM; 3.50 A; q=25-222. DR PDB; 6ZSD; EM; 3.70 A; q=25-222. DR PDB; 6ZSE; EM; 5.00 A; q=25-222. DR PDB; 6ZSG; EM; 4.00 A; q=25-222. DR PDB; 7A5F; EM; 4.40 A; q3=1-222. DR PDB; 7A5G; EM; 4.33 A; q3=1-222. DR PDB; 7A5H; EM; 3.30 A; q=1-222. DR PDB; 7A5I; EM; 3.70 A; q3=1-222. DR PDB; 7A5J; EM; 3.10 A; q=1-222. DR PDB; 7A5K; EM; 3.70 A; q3=1-222. DR PDB; 7L08; EM; 3.49 A; q=1-222. DR PDB; 7L20; EM; 3.15 A; q=1-222. DR PDB; 7O9K; EM; 3.10 A; q=1-222. DR PDB; 7O9M; EM; 2.50 A; q=1-222. DR PDB; 7ODR; EM; 2.90 A; q=1-222. DR PDB; 7ODS; EM; 3.10 A; q=1-222. DR PDB; 7ODT; EM; 3.10 A; q=1-222. DR PDB; 7OF0; EM; 2.20 A; q=1-222. DR PDB; 7OF2; EM; 2.70 A; q=1-222. DR PDB; 7OF3; EM; 2.70 A; q=1-222. DR PDB; 7OF4; EM; 2.70 A; q=1-222. DR PDB; 7OF5; EM; 2.90 A; q=1-222. DR PDB; 7OF6; EM; 2.60 A; q=1-222. DR PDB; 7OF7; EM; 2.50 A; q=1-222. DR PDB; 7OG4; EM; 3.80 A; q=1-222. DR PDB; 7OI6; EM; 5.70 A; q=1-222. DR PDB; 7OI7; EM; 3.50 A; q=1-222. DR PDB; 7OI8; EM; 3.50 A; q=1-222. DR PDB; 7OI9; EM; 3.30 A; q=1-222. DR PDB; 7OIA; EM; 3.20 A; q=1-222. DR PDB; 7OIB; EM; 3.30 A; q=1-222. DR PDB; 7OIC; EM; 3.10 A; q=1-222. DR PDB; 7OID; EM; 3.70 A; q=1-222. DR PDB; 7OIE; EM; 3.50 A; q=1-222. DR PDB; 7PD3; EM; 3.40 A; q=1-222. DR PDB; 7PO4; EM; 2.56 A; q=1-222. DR PDB; 7QH6; EM; 3.08 A; q=1-222. DR PDB; 7QH7; EM; 2.89 A; q=25-125. DR PDB; 7QI4; EM; 2.21 A; q=1-222. DR PDB; 7QI5; EM; 2.63 A; q=1-222. DR PDB; 7QI6; EM; 2.98 A; q=1-222. DR PDB; 8ANY; EM; 2.85 A; q=1-222. DR PDB; 8OIR; EM; 3.10 A; Bg=1-222. DR PDB; 8OIT; EM; 2.90 A; Bg=1-222. DR PDBsum; 3J7Y; -. DR PDBsum; 3J9M; -. DR PDBsum; 5OOL; -. DR PDBsum; 5OOM; -. DR PDBsum; 6I9R; -. DR PDBsum; 6NU2; -. DR PDBsum; 6NU3; -. DR PDBsum; 6VLZ; -. DR PDBsum; 6VMI; -. DR PDBsum; 6ZM5; -. DR PDBsum; 6ZM6; -. DR PDBsum; 6ZS9; -. DR PDBsum; 6ZSA; -. DR PDBsum; 6ZSB; -. DR PDBsum; 6ZSC; -. DR PDBsum; 6ZSD; -. DR PDBsum; 6ZSE; -. DR PDBsum; 6ZSG; -. DR PDBsum; 7A5F; -. DR PDBsum; 7A5G; -. DR PDBsum; 7A5H; -. DR PDBsum; 7A5I; -. DR PDBsum; 7A5J; -. DR PDBsum; 7A5K; -. DR PDBsum; 7L08; -. DR PDBsum; 7L20; -. DR PDBsum; 7O9K; -. DR PDBsum; 7O9M; -. DR PDBsum; 7ODR; -. DR PDBsum; 7ODS; -. DR PDBsum; 7ODT; -. DR PDBsum; 7OF0; -. DR PDBsum; 7OF2; -. DR PDBsum; 7OF3; -. DR PDBsum; 7OF4; -. DR PDBsum; 7OF5; -. DR PDBsum; 7OF6; -. DR PDBsum; 7OF7; -. DR PDBsum; 7OG4; -. DR PDBsum; 7OI6; -. DR PDBsum; 7OI7; -. DR PDBsum; 7OI8; -. DR PDBsum; 7OI9; -. DR PDBsum; 7OIA; -. DR PDBsum; 7OIB; -. DR PDBsum; 7OIC; -. DR PDBsum; 7OID; -. DR PDBsum; 7OIE; -. DR PDBsum; 7PD3; -. DR PDBsum; 7PO4; -. DR PDBsum; 7QH6; -. DR PDBsum; 7QH7; -. DR PDBsum; 7QI4; -. DR PDBsum; 7QI5; -. DR PDBsum; 7QI6; -. DR PDBsum; 8ANY; -. DR PDBsum; 8OIR; -. DR PDBsum; 8OIT; -. DR AlphaFoldDB; Q8TAE8; -. DR EMDB; EMD-0514; -. DR EMDB; EMD-0515; -. DR EMDB; EMD-11278; -. DR EMDB; EMD-11279; -. DR EMDB; EMD-11390; -. DR EMDB; EMD-11391; -. DR EMDB; EMD-11392; -. DR EMDB; EMD-11393; -. DR EMDB; EMD-11394; -. DR EMDB; EMD-11395; -. DR EMDB; EMD-11397; -. DR EMDB; EMD-11641; -. DR EMDB; EMD-11642; -. DR EMDB; EMD-11643; -. DR EMDB; EMD-11644; -. DR EMDB; EMD-11645; -. DR EMDB; EMD-11646; -. DR EMDB; EMD-12763; -. DR EMDB; EMD-12764; -. DR EMDB; EMD-12845; -. DR EMDB; EMD-12846; -. DR EMDB; EMD-12847; -. DR EMDB; EMD-12865; -. DR EMDB; EMD-12867; -. DR EMDB; EMD-12868; -. DR EMDB; EMD-12869; -. DR EMDB; EMD-12870; -. DR EMDB; EMD-12871; -. DR EMDB; EMD-12872; -. DR EMDB; EMD-12877; -. DR EMDB; EMD-12919; -. DR EMDB; EMD-12920; -. DR EMDB; EMD-12921; -. DR EMDB; EMD-12922; -. DR EMDB; EMD-12923; -. DR EMDB; EMD-12924; -. DR EMDB; EMD-12925; -. DR EMDB; EMD-12926; -. DR EMDB; EMD-12927; -. DR EMDB; EMD-13329; -. DR EMDB; EMD-13562; -. DR EMDB; EMD-13965; -. DR EMDB; EMD-13967; -. DR EMDB; EMD-13980; -. DR EMDB; EMD-13981; -. DR EMDB; EMD-13982; -. DR EMDB; EMD-15544; -. DR EMDB; EMD-16897; -. DR EMDB; EMD-16899; -. DR EMDB; EMD-21233; -. DR EMDB; EMD-21242; -. DR EMDB; EMD-23096; -. DR EMDB; EMD-23121; -. DR EMDB; EMD-3842; -. DR EMDB; EMD-3843; -. DR EMDB; EMD-4434; -. DR SMR; Q8TAE8; -. DR BioGRID; 124721; 288. DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit. DR IntAct; Q8TAE8; 140. DR MINT; Q8TAE8; -. DR STRING; 9606.ENSP00000323065; -. DR GlyGen; Q8TAE8; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8TAE8; -. DR PhosphoSitePlus; Q8TAE8; -. DR SwissPalm; Q8TAE8; -. DR BioMuta; GADD45GIP1; -. DR DMDM; 74730346; -. DR EPD; Q8TAE8; -. DR jPOST; Q8TAE8; -. DR MassIVE; Q8TAE8; -. DR MaxQB; Q8TAE8; -. DR PaxDb; 9606-ENSP00000323065; -. DR PeptideAtlas; Q8TAE8; -. DR ProteomicsDB; 73869; -. DR Pumba; Q8TAE8; -. DR Antibodypedia; 26334; 196 antibodies from 31 providers. DR DNASU; 90480; -. DR Ensembl; ENST00000316939.3; ENSP00000323065.1; ENSG00000179271.3. DR GeneID; 90480; -. DR KEGG; hsa:90480; -. DR MANE-Select; ENST00000316939.3; ENSP00000323065.1; NM_052850.4; NP_443082.2. DR UCSC; uc002mwb.5; human. DR AGR; HGNC:29996; -. DR CTD; 90480; -. DR DisGeNET; 90480; -. DR GeneCards; GADD45GIP1; -. DR HGNC; HGNC:29996; GADD45GIP1. DR HPA; ENSG00000179271; Low tissue specificity. DR MIM; 605162; gene. DR neXtProt; NX_Q8TAE8; -. DR OpenTargets; ENSG00000179271; -. DR PharmGKB; PA134954784; -. DR VEuPathDB; HostDB:ENSG00000179271; -. DR eggNOG; KOG4848; Eukaryota. DR GeneTree; ENSGT00390000013719; -. DR HOGENOM; CLU_102022_0_0_1; -. DR InParanoid; Q8TAE8; -. DR OMA; AYEAKLY; -. DR OrthoDB; 2880304at2759; -. DR PhylomeDB; Q8TAE8; -. DR TreeFam; TF323794; -. DR PathwayCommons; Q8TAE8; -. DR Reactome; R-HSA-5368286; Mitochondrial translation initiation. DR Reactome; R-HSA-5389840; Mitochondrial translation elongation. DR Reactome; R-HSA-5419276; Mitochondrial translation termination. DR SignaLink; Q8TAE8; -. DR SIGNOR; Q8TAE8; -. DR BioGRID-ORCS; 90480; 220 hits in 1157 CRISPR screens. DR ChiTaRS; GADD45GIP1; human. DR GeneWiki; GADD45GIP1; -. DR GenomeRNAi; 90480; -. DR Pharos; Q8TAE8; Tbio. DR PRO; PR:Q8TAE8; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q8TAE8; Protein. DR Bgee; ENSG00000179271; Expressed in apex of heart and 171 other cell types or tissues. DR GO; GO:0005743; C:mitochondrial inner membrane; NAS:ComplexPortal. DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; NAS:ComplexPortal. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0032543; P:mitochondrial translation; NAS:ComplexPortal. DR Gene3D; 6.10.280.120; Growth arrest and DNA-damage-inducible proteins-interacting protein 1; 1. DR InterPro; IPR018472; Ribosomal_mL64. DR InterPro; IPR043035; Ribosomal_mL64_sf. DR PANTHER; PTHR31761:SF1; GROWTH ARREST AND DNA DAMAGE-INDUCIBLE PROTEINS-INTERACTING PROTEIN 1; 1. DR PANTHER; PTHR31761; GROWTH ARREST AND DNA DAMAGE-INDUCIBLE PROTEINS-INTERACTING PROTEIN 1 GADD45GIP1; 1. DR Pfam; PF10147; CR6_interact; 1. DR Genevisible; Q8TAE8; HS. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Coiled coil; Host-virus interaction; KW Mitochondrion; Nucleus; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1..222 FT /note="Large ribosomal subunit protein mL64" FT /id="PRO_0000228620" FT REGION 19..46 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 188..222 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 99..212 FT /evidence="ECO:0000255" FT MOTIF 184..200 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT CONFLICT 7..10 FT /note="QARS -> KALN (in Ref. 1; CAD22344)" FT /evidence="ECO:0000305" FT STRAND 42..47 FT /evidence="ECO:0007829|PDB:7QH7" FT HELIX 49..51 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 54..64 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 65..68 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 72..75 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 79..92 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 96..151 FT /evidence="ECO:0007829|PDB:7OF0" FT TURN 166..169 FT /evidence="ECO:0007829|PDB:7OIA" FT HELIX 170..187 FT /evidence="ECO:0007829|PDB:7OIA" SQ SEQUENCE 222 AA; 25384 MW; 304C397AEC958804 CRC64; MAASVRQARS LLGVAATLAP GSRGYRARPP PRRRPGPRWP DPEDLLTPRW QLGPRYAAKQ FARYGAASGV VPGSLWPSPE QLRELEAEER EWYPSLATMQ ESLRVKQLAE EQKRREREQH IAECMAKMPQ MIVNWQQQQR ENWEKAQADK ERRARLQAEA QELLGYQVDP RSARFQELLQ DLEKKERKRL KEEKQKRKKE ARAAALAAAV AQDPAASGAP SS //