5MP2_MOUSE
ID 5MP2_MOUSE Reviewed; 419 AA.
AC Q9CQC6; Q3THS5; Q3UZ94;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=eIF5-mimic protein 2 {ECO:0000250|UniProtKB:Q7L1Q6};
DE AltName: Full=Basic leucine zipper and W2 domain-containing protein 1;
GN Name=Bzw1; Synonyms=5mp2 {ECO:0000250|UniProtKB:Q7L1Q6};
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=BALB/cJ, C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Embryo, Head, Lung, Mammary gland, Testis, and Thymus;
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 STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
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 TISSUE SPECIFICITY.
RX PubMed=16690031; DOI=10.1016/j.bbrc.2006.04.113;
RA Yu M., Sha H., Gao Y., Zeng H., Zhu M., Gao X.;
RT "Alternative 3' UTR polyadenylation of Bzw1 transcripts display
RT differential translation efficiency and tissue-specific expression.";
RL Biochem. Biophys. Res. Commun. 345:479-485(2006).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411 AND SER-413, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, 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: Translation initiation regulator which represses repeat-
CC associated non-AUG (RAN) initiated translation probably by acting as a
CC competitive inhibitor of eukaryotic translation initiation factor 5
CC (EIF5) function (By similarity). Enhances histone H4 gene transcription
CC but does not seem to bind DNA directly (By similarity).
CC {ECO:0000250|UniProtKB:Q7L1Q6}.
CC -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in testis.
CC {ECO:0000269|PubMed:16690031}.
CC -!- SIMILARITY: Belongs to the BZW family. {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; AK004784; BAB23562.1; -; mRNA.
DR EMBL; AK013980; BAB29098.1; -; mRNA.
DR EMBL; AK076086; BAC36172.1; -; mRNA.
DR EMBL; AK076560; BAC36393.1; -; mRNA.
DR EMBL; AK088322; BAC40280.1; -; mRNA.
DR EMBL; AK133973; BAE21963.1; -; mRNA.
DR EMBL; AK151919; BAE30797.1; -; mRNA.
DR EMBL; AK153538; BAE32075.1; -; mRNA.
DR EMBL; AK161192; BAE36231.1; -; mRNA.
DR EMBL; AK166247; BAE38658.1; -; mRNA.
DR EMBL; AK167074; BAE39234.1; -; mRNA.
DR EMBL; AK168158; BAE40121.1; -; mRNA.
DR EMBL; BC005466; AAH05466.1; -; mRNA.
DR EMBL; BC028865; AAH28865.1; -; mRNA.
DR CCDS; CCDS14971.1; -.
DR RefSeq; NP_080100.1; NM_025824.3.
DR AlphaFoldDB; Q9CQC6; -.
DR SMR; Q9CQC6; -.
DR BioGRID; 211786; 14.
DR IntAct; Q9CQC6; 2.
DR MINT; Q9CQC6; -.
DR STRING; 10090.ENSMUSP00000051935; -.
DR iPTMnet; Q9CQC6; -.
DR PhosphoSitePlus; Q9CQC6; -.
DR EPD; Q9CQC6; -.
DR jPOST; Q9CQC6; -.
DR MaxQB; Q9CQC6; -.
DR PaxDb; Q9CQC6; -.
DR PeptideAtlas; Q9CQC6; -.
DR PRIDE; Q9CQC6; -.
DR ProteomicsDB; 273850; -.
DR Antibodypedia; 47644; 87 antibodies from 19 providers.
DR DNASU; 66882; -.
DR Ensembl; ENSMUST00000050552; ENSMUSP00000051935; ENSMUSG00000051223.
DR GeneID; 66882; -.
DR KEGG; mmu:66882; -.
DR UCSC; uc007bbq.1; mouse.
DR CTD; 9689; -.
DR MGI; MGI:1914132; Bzw1.
DR VEuPathDB; HostDB:ENSMUSG00000051223; -.
DR eggNOG; KOG2297; Eukaryota.
DR GeneTree; ENSGT00390000012561; -.
DR HOGENOM; CLU_032849_0_1_1; -.
DR InParanoid; Q9CQC6; -.
DR PhylomeDB; Q9CQC6; -.
DR TreeFam; TF324313; -.
DR BioGRID-ORCS; 66882; 7 hits in 72 CRISPR screens.
DR ChiTaRS; Bzw1; mouse.
DR PRO; PR:Q9CQC6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9CQC6; protein.
DR Bgee; ENSMUSG00000051223; Expressed in ureter smooth muscle and 257 other tissues.
DR ExpressionAtlas; Q9CQC6; baseline and differential.
DR Genevisible; Q9CQC6; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB.
DR CDD; cd11560; W2_eIF5C_like; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR043510; W2_BZW1/2.
DR InterPro; IPR003307; W2_domain.
DR Pfam; PF02020; W2; 1.
DR SMART; SM00515; eIF5C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51363; W2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Translation regulation; Ubl conjugation.
FT CHAIN 1..419
FT /note="eIF5-mimic protein 2"
FT /id="PRO_0000254610"
FT DOMAIN 247..414
FT /note="W2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L1Q6"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 368
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7L1Q6"
FT CONFLICT 38
FT /note="Q -> K (in Ref. 1; BAE40121)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 48043 MW; 9E952D52F5796F60 CRC64;
MNNQKQQKPT LSGQRFKTRK RDEKERFDPT QFQDCIIQGL TETGTDLEAV AKFLDASGAK
LDYRRYAETL FDILVAGGML APGGTLADDM MRTDVCVFAA QEDLETMQAF AQVFNKLIRR
YKYLEKGFED EVKKLLLFLK GFSESERNKL AMLTGVLLAN GTLNASILNS LYNENLVKEG
VSAAFAVKLF KSWINEKDIN AVAASLRKVS MDNRLMELFP ANKQSVEHFT KYFTEAGLKE
LSEYVRNQQT IGARKELQKE LQEQMSRGDP FKDIILYVKE EMKKNNIPEP VVIGIVWSSV
MSTVEWNKKE ELVAEQAIKH LKQYSPLLAA FTTQGQSELT LLLKIQEYCY DNIHFMKAFQ
KIVVLFYKAE VLSEEPILKW YKDAHVAKGK SVFLEQMKKF VEWLKNAEEE SESEAEEGD
