5MP2_HUMAN
ID 5MP2_HUMAN Reviewed; 419 AA.
AC Q7L1Q6; B4DLZ8; B4DWF7; Q14281; Q15394; Q9BUY0;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=eIF5-mimic protein 2 {ECO:0000303|PubMed:21745818};
DE AltName: Full=Basic leucine zipper and W2 domain-containing protein 1;
DE AltName: Full=Protein Orf;
GN Name=BZW1; Synonyms=5MP2 {ECO:0000303|PubMed:21745818}, BZAP45, KIAA0005;
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=Bone marrow;
RX PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S.,
RA Nagase T., Seki N., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. I. The
RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of
RT randomly sampled cDNA clones from human immature myeloid cell line KG-1.";
RL DNA Res. 1:27-35(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Brain, and Synovium;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Eye;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-74.
RC TISSUE=Fetal brain;
RA Dmitrenko V.V., Garifulin O.M., Kavsan V.M.;
RT "Characterization of different mRNA types expressed in human brain.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 6-15, DEVELOPMENTAL STAGE, AND FUNCTION.
RX PubMed=11524015; DOI=10.1021/bi010529o;
RA Mitra P., Vaughan P.S., Stein J.L., Stein G.S., van Wijnen A.J.;
RT "Purification and functional analysis of a novel leucine-zipper/nucleotide-
RT fold protein, BZAP45, stimulating cell cycle regulated histone H4 gene
RT transcription.";
RL Biochemistry 40:10693-10699(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411 AND SER-413, 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-411, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411 AND SER-413, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, AND IDENTIFICATION BY
RP 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 NOMENCLATURE.
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, AND IDENTIFICATION BY
RP 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-368, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [21]
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 [22]
RP FUNCTION.
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 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 (PubMed:29470543, PubMed:34260931). Enhances histone H4
CC gene transcription but does not seem to bind DNA directly
CC (PubMed:11524015). {ECO:0000269|PubMed:11524015,
CC ECO:0000269|PubMed:29470543, ECO:0000269|PubMed:34260931}.
CC -!- INTERACTION:
CC Q7L1Q6-2; Q14204: DYNC1H1; NbExp=3; IntAct=EBI-21557060, EBI-356015;
CC Q7L1Q6-2; Q92876: KLK6; NbExp=3; IntAct=EBI-21557060, EBI-2432309;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q7L1Q6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7L1Q6-2; Sequence=VSP_021266;
CC Name=3;
CC IsoId=Q7L1Q6-3; Sequence=VSP_043568;
CC Name=4;
CC IsoId=Q7L1Q6-4; Sequence=VSP_043569;
CC -!- DEVELOPMENTAL STAGE: Expressed in day 3 embryo.
CC {ECO:0000269|PubMed:11524015}.
CC -!- SIMILARITY: Belongs to the BZW family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA02795.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D13630; BAA02795.2; ALT_INIT; mRNA.
DR EMBL; AK297227; BAG59710.1; -; mRNA.
DR EMBL; AK301511; BAG63019.1; -; mRNA.
DR EMBL; AC007163; AAX93286.1; -; Genomic_DNA.
DR EMBL; BC001804; AAH01804.1; -; mRNA.
DR EMBL; BC026303; AAH26303.1; -; mRNA.
DR EMBL; Z70221; CAA94180.1; -; mRNA.
DR CCDS; CCDS56154.1; -. [Q7L1Q6-4]
DR CCDS; CCDS56155.1; -. [Q7L1Q6-3]
DR CCDS; CCDS56156.1; -. [Q7L1Q6-1]
DR RefSeq; NP_001193996.1; NM_001207067.1. [Q7L1Q6-1]
DR RefSeq; NP_001193997.1; NM_001207068.2. [Q7L1Q6-3]
DR RefSeq; NP_001193998.1; NM_001207069.1. [Q7L1Q6-4]
DR RefSeq; NP_001308617.1; NM_001321688.1. [Q7L1Q6-1]
DR RefSeq; NP_001308619.1; NM_001321690.1. [Q7L1Q6-1]
DR RefSeq; NP_001308620.1; NM_001321691.1.
DR RefSeq; NP_001308622.1; NM_001321693.1.
DR RefSeq; NP_001308623.1; NM_001321694.1.
DR RefSeq; NP_055485.2; NM_014670.3. [Q7L1Q6-2]
DR AlphaFoldDB; Q7L1Q6; -.
DR SMR; Q7L1Q6; -.
DR BioGRID; 115042; 78.
DR CORUM; Q7L1Q6; -.
DR IntAct; Q7L1Q6; 34.
DR MINT; Q7L1Q6; -.
DR STRING; 9606.ENSP00000394316; -.
DR GlyGen; Q7L1Q6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7L1Q6; -.
DR MetOSite; Q7L1Q6; -.
DR PhosphoSitePlus; Q7L1Q6; -.
DR SwissPalm; Q7L1Q6; -.
DR BioMuta; BZW1; -.
DR DMDM; 74738534; -.
DR EPD; Q7L1Q6; -.
DR jPOST; Q7L1Q6; -.
DR MassIVE; Q7L1Q6; -.
DR MaxQB; Q7L1Q6; -.
DR PaxDb; Q7L1Q6; -.
DR PeptideAtlas; Q7L1Q6; -.
DR PRIDE; Q7L1Q6; -.
DR ProteomicsDB; 68744; -. [Q7L1Q6-1]
DR ProteomicsDB; 68745; -. [Q7L1Q6-2]
DR ProteomicsDB; 68746; -. [Q7L1Q6-3]
DR ProteomicsDB; 68747; -. [Q7L1Q6-4]
DR TopDownProteomics; Q7L1Q6-1; -. [Q7L1Q6-1]
DR TopDownProteomics; Q7L1Q6-2; -. [Q7L1Q6-2]
DR Antibodypedia; 47644; 87 antibodies from 19 providers.
DR DNASU; 9689; -.
DR Ensembl; ENST00000409226.5; ENSP00000386837.1; ENSG00000082153.18. [Q7L1Q6-4]
DR Ensembl; ENST00000409600.6; ENSP00000386474.1; ENSG00000082153.18. [Q7L1Q6-1]
DR Ensembl; ENST00000452790.6; ENSP00000394316.2; ENSG00000082153.18. [Q7L1Q6-3]
DR GeneID; 9689; -.
DR KEGG; hsa:9689; -.
DR MANE-Select; ENST00000409600.6; ENSP00000386474.1; NM_001207067.2; NP_001193996.1.
DR UCSC; uc002uwc.4; human. [Q7L1Q6-1]
DR CTD; 9689; -.
DR DisGeNET; 9689; -.
DR GeneCards; BZW1; -.
DR HGNC; HGNC:18380; BZW1.
DR HPA; ENSG00000082153; Low tissue specificity.
DR MIM; 619252; gene.
DR neXtProt; NX_Q7L1Q6; -.
DR OpenTargets; ENSG00000082153; -.
DR PharmGKB; PA38535; -.
DR VEuPathDB; HostDB:ENSG00000082153; -.
DR eggNOG; KOG2297; Eukaryota.
DR GeneTree; ENSGT00390000012561; -.
DR HOGENOM; CLU_032849_0_1_1; -.
DR InParanoid; Q7L1Q6; -.
DR PhylomeDB; Q7L1Q6; -.
DR TreeFam; TF324313; -.
DR PathwayCommons; Q7L1Q6; -.
DR SignaLink; Q7L1Q6; -.
DR BioGRID-ORCS; 9689; 28 hits in 1069 CRISPR screens.
DR ChiTaRS; BZW1; human.
DR GeneWiki; BZW1; -.
DR GenomeRNAi; 9689; -.
DR Pharos; Q7L1Q6; Tbio.
DR PRO; PR:Q7L1Q6; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q7L1Q6; protein.
DR Bgee; ENSG00000082153; Expressed in palpebral conjunctiva and 209 other tissues.
DR ExpressionAtlas; Q7L1Q6; baseline and differential.
DR Genevisible; Q7L1Q6; 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:0003723; F:RNA binding; HDA:UniProtKB.
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; Activator; Alternative splicing; Direct protein sequencing;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Translation regulation; Ubl conjugation.
FT CHAIN 1..419
FT /note="eIF5-mimic protein 2"
FT /id="PRO_0000254609"
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:22814378"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008"
FT CROSSLNK 368
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1
FT /note="M -> MYGAPGAPAQSASVTVVRSLRRPPPQATGVSFM (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043568"
FT VAR_SEQ 1
FT /note="M -> MVSFM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043569"
FT VAR_SEQ 286..351
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021266"
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
