G45IP_HUMAN
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 03-AUG-2022, entry version 156.
DE RecName: Full=Growth arrest and DNA damage-inducible proteins-interacting protein 1;
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=Mitochondrial large ribosomal subunit protein mL64 {ECO:0000303|PubMed:27023846};
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="http://atlasgeneticsoncology.org/Genes/GADD45GIP1ID40668ch19p13.html";
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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; 7QH6; EM; 3.08 A; q=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; 7QH6; -.
DR AlphaFoldDB; Q8TAE8; -.
DR SMR; Q8TAE8; -.
DR BioGRID; 124721; 279.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR IntAct; Q8TAE8; 141.
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 BioMuta; GADD45GIP1; -.
DR DMDM; 74730346; -.
DR EPD; Q8TAE8; -.
DR jPOST; Q8TAE8; -.
DR MassIVE; Q8TAE8; -.
DR MaxQB; Q8TAE8; -.
DR PaxDb; Q8TAE8; -.
DR PeptideAtlas; Q8TAE8; -.
DR PRIDE; Q8TAE8; -.
DR ProteomicsDB; 73869; -.
DR Antibodypedia; 26334; 167 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 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; EQHIAEC; -.
DR OrthoDB; 1431395at2759; -.
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; 205 hits in 1080 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 169 other tissues.
DR Genevisible; Q8TAE8; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IC: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; IC:ComplexPortal.
DR Gene3D; 6.10.280.120; -; 1.
DR InterPro; IPR043035; Damage-induce-interact_sf.
DR InterPro; IPR018472; Damage-induce-interacting_prot.
DR PANTHER; PTHR31761; PTHR31761; 1.
DR Pfam; PF10147; CR6_interact; 1.
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="Growth arrest and DNA damage-inducible proteins-
FT interacting protein 1"
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 45..47
FT /evidence="ECO:0007829|PDB:5OOM"
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
