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Mesoderm induction early response protein 1 (Early response 1) (Er1) (Mi-er1) (hMi-er1)

 MIER1_HUMAN             Reviewed;         512 AA.
Q8N108; C9JFD4; Q08AE0; Q32NC4; Q5T104; Q5TAD1; Q5TAD2; Q5TAD4;
Q5TAD5; Q6AHY8; Q86TB4; Q8N156; Q8N161; Q8NC37; Q8NES4; Q8NES5;
Q8NES6; Q8WWG2; Q9HCG2;
22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
21-MAR-2012, sequence version 2.
08-MAY-2019, entry version 155.
RecName: Full=Mesoderm induction early response protein 1;
Short=Early response 1;
Short=Er1;
Short=Mi-er1;
Short=hMi-er1;
Name=MIER1; Synonyms=KIAA1610;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), TISSUE
SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=12242014; DOI=10.1016/S0378-1119(02)00823-5;
Paterno G.D., Ding Z., Yew Y.-Y., Nash G.W., Mercer F.C.,
Gillespie L.L.;
"Genomic organization of the human mi-er1 gene and characterization of
alternatively spliced isoforms: regulated use of a facultative intron
determines subcellular localization.";
Gene 295:79-88(2002).
[2]
SEQUENCE REVISION.
Paterno G.D., Ding Z., Lew Y.Y., Nash G.W., Mercer F.C.,
Gillespie L.L.;
Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-204 (ISOFORMS 1/6).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 7).
TISSUE=Retina, and Skeletal muscle;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 8; 9 AND 10), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-199 (ISOFORMS 1/6).
TISSUE=Lung, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-512 (ISOFORMS 1/2/3/7).
PubMed=10997877; DOI=10.1093/dnares/7.4.271;
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes.
XVIII. The complete sequences of 100 new cDNA clones from brain which
code for large proteins in vitro.";
DNA Res. 7:273-281(2000).
[9]
FUNCTION, INTERACTION WITH HDAC1, AND MUTAGENESIS OF TRP-214 AND
227-PHE--LEU-228.
PubMed=12482978; DOI=10.1128/MCB.23.1.250-258.2003;
Ding Z., Gillespie L.L., Paterno G.D.;
"Human MI-ER1 alpha and beta function as transcriptional repressors by
recruitment of histone deacetylase 1 to their conserved ELM2 domain.";
Mol. Cell. Biol. 23:250-258(2003).
[10]
TISSUE SPECIFICITY.
PubMed=9813250; DOI=10.1016/S0378-1119(98)00473-9;
Paterno G.D., Mercer F.C., Chayter J.J., Yang X., Robb J.D.,
Gillespie L.L.;
"Molecular cloning of human er1 cDNA and its differential expression
in breast tumours and tumour-derived cell lines.";
Gene 222:77-82(1998).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[12]
IDENTIFICATION IN A COMPLEX WITH CDYL; MIER2; HDAC1 AND HDAC2.
PubMed=19061646; DOI=10.1016/j.molcel.2008.10.025;
Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B.,
Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J.,
Shi Y.;
"CDYL bridges REST and histone methyltransferases for gene repression
and suppression of cellular transformation.";
Mol. Cell 32:718-726(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-155; SER-160; SER-166;
SER-483 AND SER-488, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND SER-166, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166 AND SER-483, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-166; SER-483
AND SER-488, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141; SER-367; SER-369;
SER-377; THR-448; SER-483; SER-488 AND SER-491, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-377, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-420, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-239 AND LYS-420, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Transcriptional repressor regulating the expression of a
number of genes including SP1 target genes. Probably functions
through recruitment of HDAC1 a histone deacetylase involved in
chromatin silencing. {ECO:0000269|PubMed:12482978}.
-!- SUBUNIT: Interacts with HDAC1. Part of a complex containing at
least CDYL, MIER1, MIER2, HDAC1 and HDAC2.
{ECO:0000269|PubMed:12482978, ECO:0000269|PubMed:19061646}.
-!- INTERACTION:
Q13547:HDAC1; NbExp=7; IntAct=EBI-3504940, EBI-301834;
Q8WVE6:TMEM171; NbExp=3; IntAct=EBI-10264833, EBI-10264837;
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus.
-!- SUBCELLULAR LOCATION: Isoform 3: Nucleus.
-!- SUBCELLULAR LOCATION: Isoform 4: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform 5: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform 6: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=10;
Name=1; Synonyms=N3-beta;
IsoId=Q8N108-11; Sequence=Displayed;
Name=2; Synonyms=N2-beta;
IsoId=Q8N108-12; Sequence=VSP_042450;
Note=Ref.1 (AAM76041/AAM97503/AAM97506) sequences are in
conflict in position: 1:M->L. It is uncertain whether Met-1 or
Met-55 is the initiator. {ECO:0000305};
Name=3; Synonyms=N1-beta;
IsoId=Q8N108-13; Sequence=VSP_042451;
Name=4; Synonyms=N1-alpha;
IsoId=Q8N108-14; Sequence=VSP_042451, VSP_042452, VSP_042453;
Name=5; Synonyms=N2-alpha;
IsoId=Q8N108-15; Sequence=VSP_042450, VSP_042452, VSP_042453;
Note=Ref.1 (AAM97500) sequence is in conflict in position:
1:M->L. It is uncertain whether Met-1 or Met-55 is the
initiator. {ECO:0000305};
Name=6; Synonyms=N3-alpha;
IsoId=Q8N108-16; Sequence=VSP_042452, VSP_042453;
Name=7;
IsoId=Q8N108-17; Sequence=VSP_042449;
Note=No experimental confirmation available.;
Name=8;
IsoId=Q8N108-18; Sequence=VSP_042451, VSP_043218;
Name=9;
IsoId=Q8N108-19; Sequence=VSP_044343, VSP_044344;
Name=10;
IsoId=Q8N108-20; Sequence=VSP_042451, VSP_055710, VSP_055711;
-!- TISSUE SPECIFICITY: Ubiquitously expressed, but at very low
levels. However, consistent level of expression are observed in
heart, testis, thyroid, ovary and adrenal gland. Transcripts are
up-regulated in breast carcinoma cell lines and tumor.
{ECO:0000269|PubMed:12242014, ECO:0000269|PubMed:9813250}.
-!- SEQUENCE CAUTION:
Sequence=AAH17423.1; Type=Miscellaneous discrepancy; Note=Wrong choice of CDS. Probable cloning artifact due to reverse transcription from RNA internal poly-A tracts.; Evidence={ECO:0000305};
Sequence=AAM76041.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAM97500.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAM97503.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAM97506.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC11339.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. C-terminal is identical to the product of the WLS gene.; Evidence={ECO:0000305};
Sequence=CAD89921.1; Type=Miscellaneous discrepancy; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MIER1ID50389ch1p31.html";
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EMBL; AF515446; AAM76040.1; -; mRNA.
EMBL; AF515447; AAM76041.1; ALT_INIT; mRNA.
EMBL; AF515448; AAM76042.2; -; mRNA.
EMBL; AY124186; AAM97499.2; -; mRNA.
EMBL; AY124187; AAM97500.1; ALT_INIT; mRNA.
EMBL; AY124188; AAM97501.1; -; mRNA.
EMBL; AY124189; AAM97502.2; -; mRNA.
EMBL; AY124190; AAM97503.1; ALT_INIT; mRNA.
EMBL; AY124191; AAM97504.1; -; mRNA.
EMBL; AY124192; AAM97505.2; -; mRNA.
EMBL; AY124193; AAM97506.1; ALT_INIT; mRNA.
EMBL; AY124194; AAM97507.1; -; mRNA.
EMBL; AK074990; BAC11339.1; ALT_SEQ; mRNA.
EMBL; AK302061; BAG63451.1; -; mRNA.
EMBL; AL831987; CAD89921.1; ALT_SEQ; mRNA.
EMBL; CR627441; CAH10526.1; -; mRNA.
EMBL; AL139216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL500525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX06505.1; -; Genomic_DNA.
EMBL; CH471059; EAX06508.1; -; Genomic_DNA.
EMBL; BC017423; AAH17423.1; ALT_SEQ; mRNA.
EMBL; BC066898; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC108726; AAI08727.1; -; mRNA.
EMBL; BC125217; AAI25218.1; -; mRNA.
EMBL; BC125218; AAI25219.1; -; mRNA.
EMBL; AB046830; BAB13436.1; -; mRNA.
CCDS; CCDS41347.1; -. [Q8N108-16]
CCDS; CCDS41348.1; -. [Q8N108-11]
CCDS; CCDS53325.1; -. [Q8N108-15]
CCDS; CCDS53326.1; -. [Q8N108-12]
CCDS; CCDS53327.1; -. [Q8N108-14]
CCDS; CCDS53328.1; -. [Q8N108-18]
CCDS; CCDS53329.1; -. [Q8N108-13]
CCDS; CCDS53330.1; -. [Q8N108-19]
CCDS; CCDS60163.1; -. [Q8N108-20]
RefSeq; NP_001071168.2; NM_001077700.2. [Q8N108-12]
RefSeq; NP_001071169.1; NM_001077701.2. [Q8N108-11]
RefSeq; NP_001071170.2; NM_001077702.2. [Q8N108-14]
RefSeq; NP_001071171.2; NM_001077703.2. [Q8N108-15]
RefSeq; NP_001071172.1; NM_001077704.2. [Q8N108-16]
RefSeq; NP_001139582.1; NM_001146110.1. [Q8N108-13]
RefSeq; NP_001139583.1; NM_001146111.1. [Q8N108-18]
RefSeq; NP_001139584.1; NM_001146112.1. [Q8N108-17]
RefSeq; NP_001139585.1; NM_001146113.1. [Q8N108-19]
RefSeq; NP_001265144.1; NM_001278215.1. [Q8N108-20]
RefSeq; NP_065999.2; NM_020948.3. [Q8N108-13]
RefSeq; XP_005271133.1; XM_005271076.3. [Q8N108-13]
RefSeq; XP_016857413.1; XM_017001924.1. [Q8N108-13]
RefSeq; XP_016857414.1; XM_017001925.1. [Q8N108-13]
RefSeq; XP_016857415.1; XM_017001926.1. [Q8N108-13]
RefSeq; XP_016857416.1; XM_017001927.1.
RefSeq; XP_016857417.1; XM_017001928.1.
RefSeq; XP_016857420.1; XM_017001931.1. [Q8N108-17]
SMR; Q8N108; -.
BioGrid; 121732; 36.
IntAct; Q8N108; 20.
MINT; Q8N108; -.
STRING; 9606.ENSP00000383820; -.
iPTMnet; Q8N108; -.
PhosphoSitePlus; Q8N108; -.
BioMuta; MIER1; -.
DMDM; 380865399; -.
EPD; Q8N108; -.
jPOST; Q8N108; -.
PaxDb; Q8N108; -.
PeptideAtlas; Q8N108; -.
PRIDE; Q8N108; -.
ProteomicsDB; 71504; -.
ProteomicsDB; 71505; -. [Q8N108-12]
ProteomicsDB; 71506; -. [Q8N108-13]
ProteomicsDB; 71507; -. [Q8N108-14]
ProteomicsDB; 71508; -. [Q8N108-15]
ProteomicsDB; 71509; -. [Q8N108-16]
ProteomicsDB; 71510; -. [Q8N108-17]
ProteomicsDB; 71511; -. [Q8N108-18]
Ensembl; ENST00000355356; ENSP00000347514; ENSG00000198160. [Q8N108-11]
Ensembl; ENST00000355977; ENSP00000348253; ENSG00000198160. [Q8N108-19]
Ensembl; ENST00000357692; ENSP00000350321; ENSG00000198160. [Q8N108-13]
Ensembl; ENST00000371012; ENSP00000360051; ENSG00000198160. [Q8N108-20]
Ensembl; ENST00000371014; ENSP00000360053; ENSG00000198160. [Q8N108-15]
Ensembl; ENST00000371016; ENSP00000360055; ENSG00000198160. [Q8N108-14]
Ensembl; ENST00000371018; ENSP00000360057; ENSG00000198160. [Q8N108-18]
Ensembl; ENST00000401041; ENSP00000383820; ENSG00000198160. [Q8N108-12]
Ensembl; ENST00000401042; ENSP00000383821; ENSG00000198160. [Q8N108-16]
GeneID; 57708; -.
KEGG; hsa:57708; -.
UCSC; uc001dda.6; human. [Q8N108-11]
CTD; 57708; -.
DisGeNET; 57708; -.
GeneCards; MIER1; -.
HGNC; HGNC:29657; MIER1.
HPA; HPA019589; -.
HPA; HPA050306; -.
neXtProt; NX_Q8N108; -.
OpenTargets; ENSG00000198160; -.
PharmGKB; PA142671456; -.
eggNOG; KOG4329; Eukaryota.
eggNOG; ENOG410Y9DJ; LUCA.
GeneTree; ENSGT00950000182752; -.
HOGENOM; HOG000015798; -.
InParanoid; Q8N108; -.
OMA; DCELFER; -.
OrthoDB; 1062529at2759; -.
TreeFam; TF106453; -.
ChiTaRS; MIER1; human.
GeneWiki; MIER1; -.
GenomeRNAi; 57708; -.
PRO; PR:Q8N108; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000198160; Expressed in 210 organ(s), highest expression level in intestine.
Genevisible; Q8N108; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0017053; C:transcriptional repressor complex; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IBA:GO_Central.
GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
GO; GO:0016575; P:histone deacetylation; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0031937; P:positive regulation of chromatin silencing; IDA:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
InterPro; IPR000949; ELM2_dom.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR040138; MIER/MTA.
InterPro; IPR031169; MIER1.
InterPro; IPR001005; SANT/Myb.
InterPro; IPR017884; SANT_dom.
PANTHER; PTHR10865; PTHR10865; 1.
PANTHER; PTHR10865:SF24; PTHR10865:SF24; 1.
Pfam; PF01448; ELM2; 1.
Pfam; PF00249; Myb_DNA-binding; 1.
SMART; SM01189; ELM2; 1.
SMART; SM00717; SANT; 1.
SUPFAM; SSF46689; SSF46689; 1.
PROSITE; PS51156; ELM2; 1.
PROSITE; PS51293; SANT; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Isopeptide bond;
Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 512 Mesoderm induction early response protein
1.
/FTId=PRO_0000197141.
DOMAIN 180 278 ELM2. {ECO:0000255|PROSITE-
ProRule:PRU00512}.
DOMAIN 283 335 SANT. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
REGION 180 284 Interaction with HDAC1.
{ECO:0000269|PubMed:12482978}.
COMPBIAS 36 181 Glu-rich.
MOD_RES 10 10 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 141 141 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 155 155 Phosphotyrosine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 160 160 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692}.
MOD_RES 166 166 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 367 367 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 369 369 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 377 377 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 448 448 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 483 483 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 488 488 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 491 491 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 239 239 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 420 420 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 63 Missing (in isoform 9).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044343.
VAR_SEQ 1 27 Missing (in isoform 7).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_042449.
VAR_SEQ 1 3 MAE -> MDGASSGGGGSSEGGGGSSGSGYGVVARFSQCLA
EFRTWLRTNWLRFNADKTDVML (in isoform 2 and
isoform 5). {ECO:0000303|PubMed:12242014,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_042450.
VAR_SEQ 1 3 MAE -> MFMFNWFTDCLWTLFLSNYQ (in isoform
3, isoform 4, isoform 8 and isoform 10).
{ECO:0000303|PubMed:12242014,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_042451.
VAR_SEQ 61 64 EGDM -> VNNM (in isoform 10).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_055710.
VAR_SEQ 65 512 Missing (in isoform 10).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_055711.
VAR_SEQ 412 512 EILNKEEVKVEGLHINGPTGGNKKPLHADMDTNGYETDNLT
TDPKLAHMTARNENDFDEKSERPAKRRRVNSNGKESPGSSE
FFQEAVSHGKFEELENTDD -> ILQMLLPVHFSAISSRAN
AFLK (in isoform 9).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044344.
VAR_SEQ 412 433 EILNKEEVKVEGLHINGPTGGN -> ILQMLLPVHFSAISS
RANAFLK (in isoform 4, isoform 5 and
isoform 6).
{ECO:0000303|PubMed:12242014}.
/FTId=VSP_042452.
VAR_SEQ 432 512 GNKKPLHADMDTNGYETDNLTTDPKLAHMTARNENDFDEKS
ERPAKRRRVNSNGKESPGSSEFFQEAVSHGKFEELENTDD
-> ILQMLLPVHFSAISSRANAFLK (in isoform 8).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043218.
VAR_SEQ 434 512 Missing (in isoform 4, isoform 5 and
isoform 6).
{ECO:0000303|PubMed:12242014}.
/FTId=VSP_042453.
MUTAGEN 214 214 W->A: Loss of transcriptional repression
and HDAC1 recruitment activity.
{ECO:0000269|PubMed:12482978}.
MUTAGEN 227 228 FL->AA: Loss of transcriptional
repression and HDAC1 recruitment
activity. {ECO:0000269|PubMed:12482978}.
CONFLICT 14 14 S -> P (in Ref. 7; BC066898).
{ECO:0000305}.
CONFLICT 142 142 Q -> H (in Ref. 4; CAH10526).
{ECO:0000305}.
CONFLICT 156 156 F -> S (in Ref. 3; BAC11339).
{ECO:0000305}.
CONFLICT 237 237 D -> G (in Ref. 4; CAH10526).
{ECO:0000305}.
SEQUENCE 512 AA; 57983 MW; 182C92C7FC5063AD CRC64;
MAEPSVESSS PGGSATSDDH EFDPSADMLV HDFDDERTLE EEEMMEGETN FSSEIEDLAR
EGDMPIHELL SLYGYGSTVR LPEEDEEEEE EEEEGEDDED ADNDDNSGCS GENKEENIKD
SSGQEDETQS SNDDPSQSVA SQDAQEIIRP RRCKYFDTNS EVEEESEEDE DYIPSEDWKK
EIMVGSMFQA EIPVGICRYK ENEKVYENDD QLLWDPEYLP EDKVIIFLKD ASRRTGDEKG
VEAIPEGSHI KDNEQALYEL VKCNFDTEEA LRRLRFNVKA AREELSVWTE EECRNFEQGL
KAYGKDFHLI QANKVRTRSV GECVAFYYMW KKSERYDFFA QQTRFGKKKY NLHPGVTDYM
DRLLDESESA ASSRAPSPPP TASNSSNSQS EKEDGTVSTA NQNGVSSNGP GEILNKEEVK
VEGLHINGPT GGNKKPLHAD MDTNGYETDN LTTDPKLAHM TARNENDFDE KSERPAKRRR
VNSNGKESPG SSEFFQEAVS HGKFEELENT DD


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Related Genes :
[MIER1 KIAA1610] Mesoderm induction early response protein 1 (Early response 1) (Er1) (Mi-er1) (hMi-er1)
[TY1B-ER1 YERCTy1-1 POL YER138C] Transposon Ty1-ER1 Gag-Pol polyprotein (Gag-Pol-p199) (TY1A-TY1B) (Transposon Ty1 TYA-TYB polyprotein) (p190) [Cleaved into: Capsid protein (CA) (Gag-p45) (p54); Ty1 protease (PR) (EC 3.4.23.-) (Pol-p20) (p23); Integrase (IN) (Pol-p71) (p84) (p90); Reverse transcriptase/ribonuclease H (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4) (Pol-p63) (p60)]
[MAT1; MAT3] Mating pheromone Er-1/Er-3 (Euplomone R1/R3)
[nnrD nnrE HW45_10915] Multifunctional fusion protein [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6) (NAD(P)HX epimerase)]
[pyrG HW45_19815] CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase)
[pfkA Cus16_2294] ATP-dependent 6-phosphofructokinase (ATP-PFK) (Phosphofructokinase) (EC 2.7.1.11) (Phosphohexokinase)
[pyrG Cus16_3086] CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase)
[dusA HW45_18850] tRNA-dihydrouridine(20/20a) synthase (EC 1.3.1.-) (EC 1.3.1.91) (U20-specific dihydrouridine synthase) (U20-specific Dus) (tRNA-dihydrouridine synthase A)
[katG HW45_13705] Catalase-peroxidase (CP) (EC 1.11.1.21) (Peroxidase/catalase)
[cca HW45_20250] Multifunctional CCA protein [Includes: CCA-adding enzyme (EC 2.7.7.72) (CCA tRNA nucleotidyltransferase) (tRNA CCA-pyrophosphorylase) (tRNA adenylyl-/cytidylyl-transferase) (tRNA nucleotidyltransferase) (tRNA-NT); 2'-nucleotidase (EC 3.1.3.-); 2',3'-cyclic phosphodiesterase (EC 3.1.4.-); Phosphatase]
[leuB Cus16_1870] 3-isopropylmalate dehydrogenase (EC 1.1.1.85) (3-IPM-DH) (Beta-IPM dehydrogenase) (IMDH)
[mutM fpg Cus16_0045] Formamidopyrimidine-DNA glycosylase (Fapy-DNA glycosylase) (EC 3.2.2.23) (DNA-(apurinic or apyrimidinic site) lyase MutM) (AP lyase MutM) (EC 4.2.99.18)
[dapB HW45_00805] 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8)
[katG HW45_12210] Catalase-peroxidase (CP) (EC 1.11.1.21) (Peroxidase/catalase)
[kdpB Cus16_2813] Potassium-transporting ATPase ATP-binding subunit (EC 7.2.2.6) (ATP phosphohydrolase [potassium-transporting] B chain) (Potassium-binding and translocating subunit B) (Potassium-translocating ATPase B chain)
[leuB HW45_20560] 3-isopropylmalate dehydrogenase (EC 1.1.1.85) (3-IPM-DH) (Beta-IPM dehydrogenase) (IMDH)
[mutM fpg HW45_00250] Formamidopyrimidine-DNA glycosylase (Fapy-DNA glycosylase) (EC 3.2.2.23) (DNA-(apurinic or apyrimidinic site) lyase MutM) (AP lyase MutM) (EC 4.2.99.18)
[rbsK HW45_09770] Ribokinase (RK) (EC 2.7.1.15)
[pdxA HW45_20520] 4-hydroxythreonine-4-phosphate dehydrogenase (EC 1.1.1.262) (4-(phosphohydroxy)-L-threonine dehydrogenase)
[HW45_15235] Bifunctional protein PutA [Includes: Proline dehydrogenase (EC 1.5.5.2) (Proline oxidase); Delta-1-pyrroline-5-carboxylate dehydrogenase (P5C dehydrogenase) (EC 1.2.1.88) (L-glutamate gamma-semialdehyde dehydrogenase)]
[iscS HW45_16040] Cysteine desulfurase IscS (EC 2.8.1.7)
[sucC Cus16_2450] Succinate--CoA ligase [ADP-forming] subunit beta (EC 6.2.1.5) (Succinyl-CoA synthetase subunit beta) (SCS-beta)
[mltF HW45_15755] Membrane-bound lytic murein transglycosylase F (EC 4.2.2.n1) (Murein lyase F)
[aroB Cus16_0217] 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4)
[cheB HW45_21350] Protein-glutamate methylesterase/protein-glutamine glutaminase (EC 3.1.1.61) (EC 3.5.1.44)
[IER3 DIF2 IEX1 PRG1] Radiation-inducible immediate-early gene IEX-1 (Differentiation-dependent gene 2 protein) (Protein DIF-2) (Immediate early protein GLY96) (Immediate early response 3 protein) (PACAP-responsive gene 1 protein) (Protein PRG1)
[murQ HW45_00650] N-acetylmuramic acid 6-phosphate etherase (MurNAc-6-P etherase) (EC 4.2.1.126) (N-acetylmuramic acid 6-phosphate hydrolase) (N-acetylmuramic acid 6-phosphate lyase)
[murQ HW45_03985] N-acetylmuramic acid 6-phosphate etherase (MurNAc-6-P etherase) (EC 4.2.1.126) (N-acetylmuramic acid 6-phosphate hydrolase) (N-acetylmuramic acid 6-phosphate lyase)
[recB HW45_20685] RecBCD enzyme subunit RecB (EC 3.1.11.5) (Exonuclease V subunit RecB) (ExoV subunit RecB) (Helicase/nuclease RecBCD subunit RecB)
[mobA HW45_25505] Molybdenum cofactor guanylyltransferase (MoCo guanylyltransferase) (EC 2.7.7.77) (GTP:molybdopterin guanylyltransferase) (Mo-MPT guanylyltransferase) (Molybdopterin guanylyltransferase) (Molybdopterin-guanine dinucleotide synthase) (MGD synthase)

Bibliography :
[12242014] Genomic organization of the human mi-er1 gene and characterization of alternatively spliced isoforms: regulated use of a facultative intron determines subcellular localization.