5MP1_HUMAN
ID 5MP1_HUMAN Reviewed; 419 AA.
AC Q9Y6E2; A4D123; Q3B779; Q96JW5; Q9H3F7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=eIF5-mimic protein 1 {ECO:0000303|PubMed:21745818};
DE AltName: Full=Basic leucine zipper and W2 domain-containing protein 2;
GN Name=BZW2; Synonyms=5MP1 {ECO:0000303|PubMed:21745818};
GN ORFNames=HSPC028, MSTP017;
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] (ISOFORM 1).
RC TISSUE=Heart;
RA Zhao B., Xu Y.Y., Liu Y.Q., Wang X.Y., Liu B., Ye J., Song L., Zhao Y.,
RA Cao H.Q., Zhao X.W., Gao Y., Zhang C.L., Zhang J., Liu L.S., Ding J.F.,
RA Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow, Kidney, and 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 AND SER-414, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 AND SER-414, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
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 [10]
RP IDENTIFICATION BY MASS 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, AND IDENTIFICATION BY
RP 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 AND SER-414, 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 AND SER-414, AND
RP IDENTIFICATION BY 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 [16]
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 [17]
RP FUNCTION, NOMENCLATURE, SUBCELLULAR LOCATION, INTERACTION WITH EIF3E AND
RP EIF2S2, AND MUTAGENESIS OF 401-PHE--GLU-411.
RX PubMed=21745818; DOI=10.1093/nar/gkr339;
RA Singh C.R., Watanabe R., Zhou D., Jennings M.D., Fukao A., Lee B.,
RA Ikeda Y., Chiorini J.A., Campbell S.G., Ashe M.P., Fujiwara T., Wek R.C.,
RA Pavitt G.D., Asano K.;
RT "Mechanisms of translational regulation by a human eIF5-mimic protein.";
RL Nucleic Acids Res. 39:8314-8328(2011).
RN [18]
RP INTERACTION WITH EIF2S2.
RX PubMed=25147208; DOI=10.1093/nar/gku670;
RA Hiraishi H., Oatman J., Haller S.L., Blunk L., McGivern B., Morris J.,
RA Papadopoulos E., Gutierrez W., Gordon M., Bokhari W., Ikeda Y., Miles D.,
RA Fellers J., Asano M., Wagner G., Tazi L., Rothenburg S., Brown S.J.,
RA Asano K.;
RT "Essential role of eIF5-mimic protein in animal development is linked to
RT control of ATF4 expression.";
RL Nucleic Acids Res. 42:10321-10330(2014).
RN [19]
RP FUNCTION.
RX PubMed=28981728; DOI=10.1093/nar/gkx808;
RA Tang L., Morris J., Wan J., Moore C., Fujita Y., Gillaspie S., Aube E.,
RA Nanda J., Marques M., Jangal M., Anderson A., Cox C., Hiraishi H., Dong L.,
RA Saito H., Singh C.R., Witcher M., Topisirovic I., Qian S.B., Asano K.;
RT "Competition between translation initiation factor eIF5 and its mimic
RT protein 5MP determines non-AUG initiation rate genome-wide.";
RL Nucleic Acids Res. 45:11941-11953(2017).
RN [20]
RP FUNCTION.
RX PubMed=29470543; DOI=10.1371/journal.pone.0192648;
RA Loughran G., Firth A.E., Atkins J.F., Ivanov I.P.;
RT "Translational autoregulation of BZW1 and BZW2 expression by modulating the
RT stringency of start codon selection.";
RL PLoS ONE 13:e0192648-e0192648(2018).
RN [21]
RP FUNCTION, INTERACTION WITH EIF2S2 AND EIF3C, AND MUTAGENESIS OF
RP 380-LYS--LYS-391 AND 401-PHE--GLU-411.
RX PubMed=34260931; DOI=10.1016/j.celrep.2021.109376;
RA Singh C.R., Glineburg M.R., Moore C., Tani N., Jaiswal R., Zou Y., Aube E.,
RA Gillaspie S., Thornton M., Cecil A., Hilgers M., Takasu A., Asano I.,
RA Asano M., Escalante C.R., Nakamura A., Todd P.K., Asano K.;
RT "Human oncoprotein 5MP suppresses general and repeat-associated non-AUG
RT translation via eIF3 by a common mechanism.";
RL Cell Rep. 36:109376-109376(2021).
CC -!- FUNCTION: Translation initiation regulator which represses non-AUG
CC initiated translation and repeat-associated non-AUG (RAN) initiated
CC translation by acting as a competitive inhibitor of eukaryotic
CC translation initiation factor 5 (EIF5) function (PubMed:21745818,
CC PubMed:28981728, PubMed:34260931, PubMed:29470543). Increases the
CC accuracy of translation initiation by impeding EIF5-dependent
CC translation from non-AUG codons by competing with it for interaction
CC with EIF2S2 within the 43S pre-initiation complex (PIC) in an EIF3C-
CC binding dependent manner (PubMed:21745818, PubMed:28981728,
CC PubMed:34260931). {ECO:0000269|PubMed:21745818,
CC ECO:0000269|PubMed:28981728, ECO:0000269|PubMed:29470543,
CC ECO:0000269|PubMed:34260931}.
CC -!- SUBUNIT: Interacts with EIF3E (PubMed:21745818). Interacts with EIF2S2
CC (PubMed:21745818, PubMed:25147208, PubMed:34260931). Interacts with
CC EIF3C (PubMed:34260931). {ECO:0000269|PubMed:21745818,
CC ECO:0000269|PubMed:25147208, ECO:0000269|PubMed:34260931}.
CC -!- INTERACTION:
CC Q9Y6E2; P20042: EIF2S2; NbExp=2; IntAct=EBI-1051021, EBI-711977;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21745818}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y6E2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y6E2-2; Sequence=VSP_055568, VSP_055569;
CC -!- SIMILARITY: Belongs to the BZW family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI07758.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AF110323; AAG39278.1; -; mRNA.
DR EMBL; AF083246; AAD39844.1; -; mRNA.
DR EMBL; AK001218; BAA91562.1; -; mRNA.
DR EMBL; AK027837; BAB55401.1; -; mRNA.
DR EMBL; CH236948; EAL24285.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93675.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93678.1; -; Genomic_DNA.
DR EMBL; BC003056; AAH03056.1; -; mRNA.
DR EMBL; BC008453; AAH08453.1; -; mRNA.
DR EMBL; BC009597; AAH09597.1; -; mRNA.
DR EMBL; BC107757; AAI07758.1; ALT_SEQ; mRNA.
DR CCDS; CCDS5362.1; -. [Q9Y6E2-1]
DR RefSeq; NP_001153239.1; NM_001159767.1. [Q9Y6E2-1]
DR RefSeq; NP_054757.1; NM_014038.2. [Q9Y6E2-1]
DR RefSeq; XP_006715769.1; XM_006715706.1.
DR RefSeq; XP_006715770.1; XM_006715707.1. [Q9Y6E2-1]
DR RefSeq; XP_006715771.1; XM_006715708.1. [Q9Y6E2-1]
DR AlphaFoldDB; Q9Y6E2; -.
DR BioGRID; 118793; 99.
DR IntAct; Q9Y6E2; 43.
DR MINT; Q9Y6E2; -.
DR STRING; 9606.ENSP00000397249; -.
DR GlyGen; Q9Y6E2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y6E2; -.
DR MetOSite; Q9Y6E2; -.
DR PhosphoSitePlus; Q9Y6E2; -.
DR SwissPalm; Q9Y6E2; -.
DR BioMuta; BZW2; -.
DR DMDM; 74762077; -.
DR EPD; Q9Y6E2; -.
DR jPOST; Q9Y6E2; -.
DR MassIVE; Q9Y6E2; -.
DR MaxQB; Q9Y6E2; -.
DR PaxDb; Q9Y6E2; -.
DR PeptideAtlas; Q9Y6E2; -.
DR PRIDE; Q9Y6E2; -.
DR ProteomicsDB; 86659; -. [Q9Y6E2-1]
DR Antibodypedia; 11817; 105 antibodies from 25 providers.
DR DNASU; 28969; -.
DR Ensembl; ENST00000258761.8; ENSP00000258761.3; ENSG00000136261.16. [Q9Y6E2-1]
DR Ensembl; ENST00000433922.6; ENSP00000397249.2; ENSG00000136261.16. [Q9Y6E2-1]
DR GeneID; 28969; -.
DR KEGG; hsa:28969; -.
DR MANE-Select; ENST00000258761.8; ENSP00000258761.3; NM_014038.3; NP_054757.1.
DR UCSC; uc003stj.3; human. [Q9Y6E2-1]
DR CTD; 28969; -.
DR DisGeNET; 28969; -.
DR GeneCards; BZW2; -.
DR HGNC; HGNC:18808; BZW2.
DR HPA; ENSG00000136261; Tissue enhanced (heart muscle, skeletal muscle, tongue).
DR MIM; 619275; gene.
DR neXtProt; NX_Q9Y6E2; -.
DR OpenTargets; ENSG00000136261; -.
DR PharmGKB; PA38690; -.
DR VEuPathDB; HostDB:ENSG00000136261; -.
DR eggNOG; KOG2297; Eukaryota.
DR GeneTree; ENSGT00390000012561; -.
DR HOGENOM; CLU_032849_0_1_1; -.
DR InParanoid; Q9Y6E2; -.
DR OMA; QXSESEG; -.
DR PhylomeDB; Q9Y6E2; -.
DR TreeFam; TF324313; -.
DR PathwayCommons; Q9Y6E2; -.
DR SignaLink; Q9Y6E2; -.
DR SIGNOR; Q9Y6E2; -.
DR BioGRID-ORCS; 28969; 13 hits in 1081 CRISPR screens.
DR ChiTaRS; BZW2; human.
DR GeneWiki; BZW2; -.
DR GenomeRNAi; 28969; -.
DR Pharos; Q9Y6E2; Tbio.
DR PRO; PR:Q9Y6E2; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9Y6E2; protein.
DR Bgee; ENSG00000136261; Expressed in skeletal muscle tissue of biceps brachii and 206 other tissues.
DR ExpressionAtlas; Q9Y6E2; baseline and differential.
DR Genevisible; Q9Y6E2; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0006446; P:regulation of translational initiation; IDA: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; Alternative splicing; Cytoplasm; Phosphoprotein;
KW Reference proteome; Translation regulation.
FT CHAIN 1..419
FT /note="eIF5-mimic protein 1"
FT /id="PRO_0000254618"
FT DOMAIN 248..415
FT /note="W2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 117
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT VAR_SEQ 182..201
FT /note="IAASFAVKLFKAWMAEKDAN -> NEAPVFSPVRQQKKNKVTDS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055568"
FT VAR_SEQ 202..419
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055569"
FT VARIANT 44
FT /note="D -> A (in dbSNP:rs35233079)"
FT /id="VAR_033642"
FT MUTAGEN 380..391
FT /note="KWYKEAHVAKGK->QWYQEAQVAQGQ: Reduced interaction with
FT EIF3C."
FT /evidence="ECO:0000269|PubMed:34260931"
FT MUTAGEN 401..411
FT /note="FVEWLQNAEEE->AAEAAQNAAAA: Reduced interaction with
FT EIF2S2."
FT /evidence="ECO:0000269|PubMed:21745818,
FT ECO:0000269|PubMed:34260931"
FT CONFLICT 203
FT /note="V -> G (in Ref. 1; AAG39278)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 48162 MW; 7ABFE7A51501E721 CRC64;
MNKHQKPVLT GQRFKTRKRD EKEKFEPTVF RDTLVQGLNE AGDDLEAVAK FLDSTGSRLD
YRRYADTLFD ILVAGSMLAP GGTRIDDGDK TKMTNHCVFS ANEDHETIRN YAQVFNKLIR
RYKYLEKAFE DEMKKLLLFL KAFSETEQTK LAMLSGILLG NGTLPATILT SLFTDSLVKE
GIAASFAVKL FKAWMAEKDA NSVTSSLRKA NLDKRLLELF PVNRQSVDHF AKYFTDAGLK
ELSDFLRVQQ SLGTRKELQK ELQERLSQEC PIKEVVLYVK EEMKRNDLPE TAVIGLLWTC
IMNAVEWNKK EELVAEQALK HLKQYAPLLA VFSSQGQSEL ILLQKVQEYC YDNIHFMKAF
QKIVVLFYKA DVLSEEAILK WYKEAHVAKG KSVFLDQMKK FVEWLQNAEE ESESEGEEN
