G45IP_MOUSE
ID G45IP_MOUSE Reviewed; 222 AA.
AC Q9CR59; Q8BT05;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
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;
GN Name=Gadd45gip1; Synonyms=Mrpl59;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, Testis, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 {ECO:0000250|UniProtKB:Q8TAE8}.
CC -!- SUBUNIT: Component of the mitochondrial ribosome large subunit (39S)
CC which comprises a 16S rRNA and about 50 distinct proteins. Interacts
CC with GADD45A, GADD45B and GADD45G. Interacts with NR4A1 via the NR4A1
CC AB domain. Interacts with ATAD3A and ATAD3B.
CC {ECO:0000250|UniProtKB:Q8TAE8}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8TAE8}.
CC Nucleus {ECO:0000250|UniProtKB:Q8TAE8}. Note=Using N-terminally tagged
CC constructs, has been found in the nucleus. C-terminally tagged
CC constructs are targeted exclusively to mitochondria. This discrepancy
CC may be explained by masking of a potential N-terminal mitochondrial
CC targeting signal by the tag. {ECO:0000250|UniProtKB:Q8TAE8}.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mL64 family. {ECO:0000305}.
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DR EMBL; AK002738; BAB22318.1; -; mRNA.
DR EMBL; AK003314; BAB22710.1; -; mRNA.
DR EMBL; AK028227; BAC25826.1; -; mRNA.
DR EMBL; AK009723; BAB26464.1; -; mRNA.
DR EMBL; AK019570; BAB31797.1; -; mRNA.
DR EMBL; BC061069; AAH61069.1; -; mRNA.
DR CCDS; CCDS22478.1; -.
DR RefSeq; NP_899202.3; NM_183358.4.
DR AlphaFoldDB; Q9CR59; -.
DR SMR; Q9CR59; -.
DR BioGRID; 221787; 4.
DR ComplexPortal; CPX-5302; 39S mitochondrial large ribosomal subunit.
DR DIP; DIP-61653N; -.
DR STRING; 10090.ENSMUSP00000037783; -.
DR iPTMnet; Q9CR59; -.
DR PhosphoSitePlus; Q9CR59; -.
DR EPD; Q9CR59; -.
DR jPOST; Q9CR59; -.
DR MaxQB; Q9CR59; -.
DR PaxDb; Q9CR59; -.
DR PeptideAtlas; Q9CR59; -.
DR PRIDE; Q9CR59; -.
DR ProteomicsDB; 267550; -.
DR Antibodypedia; 26334; 167 antibodies from 31 providers.
DR DNASU; 102060; -.
DR Ensembl; ENSMUST00000036734; ENSMUSP00000037783; ENSMUSG00000033751.
DR GeneID; 102060; -.
DR KEGG; mmu:102060; -.
DR UCSC; uc009mnj.1; mouse.
DR CTD; 90480; -.
DR MGI; MGI:1914947; Gadd45gip1.
DR VEuPathDB; HostDB:ENSMUSG00000033751; -.
DR eggNOG; KOG4848; Eukaryota.
DR GeneTree; ENSGT00390000013719; -.
DR HOGENOM; CLU_102022_0_0_1; -.
DR InParanoid; Q9CR59; -.
DR OMA; EQHIAEC; -.
DR OrthoDB; 1431395at2759; -.
DR PhylomeDB; Q9CR59; -.
DR TreeFam; TF323794; -.
DR Reactome; R-MMU-5389840; Mitochondrial translation elongation.
DR Reactome; R-MMU-5419276; Mitochondrial translation termination.
DR BioGRID-ORCS; 102060; 19 hits in 74 CRISPR screens.
DR ChiTaRS; Gadd45gip1; mouse.
DR PRO; PR:Q9CR59; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9CR59; protein.
DR Bgee; ENSMUSG00000033751; Expressed in left lobe of liver and 237 other tissues.
DR Genevisible; Q9CR59; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; IC:ComplexPortal.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IC:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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 Cell cycle; Coiled coil; Mitochondrion; Nucleus; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..222
FT /note="Growth arrest and DNA damage-inducible proteins-
FT interacting protein 1"
FT /id="PRO_0000228621"
FT REGION 21..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 98..207
FT /evidence="ECO:0000255"
FT MOTIF 184..200
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 186..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 184
FT /note="K -> Q (in Ref. 1; BAC25826)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 222 AA; 25820 MW; 1CB0F5AF4ACFF504 CRC64;
MAALAMRSGY LLRLSVALGP RSRSYRAPPP PRRRPGPHSP DPENLLTPRW QLTPRYVAKQ
FGRHGAISGV PPASLWPTPE QLRELEAEEQ EWYPSLATMQ ESLRLQQQAL EARRQAREQR
IAECMAKMPQ MIENWRKQKR ERWEKIQADK ERRARLQAEA QERLGYHVDP RSARFQELLQ
DLDKQQRKRL KEERQRQKKE ARIAAMASAE AQDSAVSGEP SS
