Full text data of MEMO1
MEMO1
(C2orf4, MEMO, NS5ATP7)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Protein MEMO1 (C21orf19-like protein; Hepatitis C virus NS5A-transactivated protein 7; HCV NS5A-transactivated protein 7; Mediator of ErbB2-driven cell motility 1; Mediator of cell motility 1; Memo-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Protein MEMO1 (C21orf19-like protein; Hepatitis C virus NS5A-transactivated protein 7; HCV NS5A-transactivated protein 7; Mediator of ErbB2-driven cell motility 1; Mediator of cell motility 1; Memo-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00032426
IPI00032426 Protein C2orf4 B-cell soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
IPI00032426 Protein C2orf4 B-cell soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
UniProt
Q9Y316
ID MEMO1_HUMAN Reviewed; 297 AA.
AC Q9Y316; B4DLS0; D6W575; Q5R2V8; Q5R2V9; Q6NSL5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Protein MEMO1;
DE AltName: Full=C21orf19-like protein;
DE AltName: Full=Hepatitis C virus NS5A-transactivated protein 7;
DE Short=HCV NS5A-transactivated protein 7;
DE AltName: Full=Mediator of ErbB2-driven cell motility 1;
DE Short=Mediator of cell motility 1;
DE Short=Memo-1;
GN Name=MEMO1; Synonyms=C2orf4, MEMO, NS5ATP7; ORFNames=CGI-27;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11707072; DOI=10.1006/geno.2001.6640;
RA Reymond A., Friedli M., Neergaard Henrichsen C., Chapot F.,
RA Deutsch S., Ucla C., Rossier C., Lyle R., Guipponi M.,
RA Antonarakis S.E.;
RT "From PREDs and open reading frames to cDNA isolation: revisiting the
RT human chromosome 21 transcription map.";
RL Genomics 78:46-54(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Heart, and Skeletal muscle;
RA Shibuya K., Kudoh J., Shimizu N.;
RT "Cloning of two isoforms of C2orf4 gene.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Liu Y., Cheng J., Wang G., Wang J., Zhang L., Chen J., Li L.;
RT "Cloning and identification of human gene 7 transactivated by
RT hepatitis C virus NS5A protein.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [6]
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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell, PNS, and 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION, AND INTERACTION WITH ERBB2.
RX PubMed=15156151; DOI=10.1038/ncb1134;
RA Marone R., Hess D., Dankort D., Muller W.J., Hynes N.E., Badache A.;
RT "Memo mediates ErbB2-driven cell motility.";
RL Nat. Cell Biol. 6:515-522(2004).
RN [10]
RP FUNCTION.
RX PubMed=20937854; DOI=10.1073/pnas.1000975107;
RA Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.;
RT "ErbB2 receptor controls microtubule capture by recruiting ACF7 to the
RT plasma membrane of migrating cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010).
RN [11]
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.,
RA Buerckstuemmer T., 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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 5-297, INTERACTION WITH
RP ERBB2, AND MUTAGENESIS OF TRP-16; HIS-49; TYR-54; HIS-81; HIS-192 AND
RP CYS-244.
RX PubMed=18045866; DOI=10.1074/jbc.M703523200;
RA Qiu C., Lienhard S., Hynes N.E., Badache A., Leahy D.J.;
RT "Memo is homologous to nonheme iron dioxygenases and binds an ErbB2-
RT derived phosphopeptide in its vestigial active site.";
RL J. Biol. Chem. 283:2734-2740(2008).
CC -!- FUNCTION: May control cell migration by relaying extracellular
CC chemotactic signals to the microtubule cytoskeleton. Mediator of
CC ERBB2 signaling. The MEMO1-RHOA-DIAPH1 signaling pathway plays an
CC important role in ERBB2-dependent stabilization of microtubules at
CC the cell cortex. It controls the localization of APC and CLASP2 to
CC the cell membrane, via the regulation of GSK3B activity. In turn,
CC membrane-bound APC allows the localization of the MACF1 to the
CC cell membrane, which is required for microtubule capture and
CC stabilization. Is required for breast carcinoma cell migration.
CC -!- SUBUNIT: Interacts with ERBB2 phosphorylated on 'Tyr-1248'.
CC -!- INTERACTION:
CC P04626:ERBB2; NbExp=6; IntAct=EBI-1104564, EBI-641062;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y316-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y316-2; Sequence=VSP_041092;
CC Name=3;
CC IsoId=Q9Y316-3; Sequence=VSP_047693;
CC -!- SIMILARITY: Belongs to the MEMO1 family.
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DR EMBL; AF363446; AAL34462.1; -; mRNA.
DR EMBL; AB041018; BAD74066.1; -; mRNA.
DR EMBL; AB041019; BAD74067.1; -; mRNA.
DR EMBL; AF529368; AAQ09602.1; -; mRNA.
DR EMBL; AF132961; AAD27736.1; -; mRNA.
DR EMBL; AK297128; BAG59632.1; -; mRNA.
DR EMBL; AL121652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAX00467.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00469.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00470.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00472.1; -; Genomic_DNA.
DR EMBL; BC018733; AAH18733.1; -; mRNA.
DR EMBL; BC070046; AAH70046.1; -; mRNA.
DR EMBL; BC094681; AAH94681.1; -; mRNA.
DR RefSeq; NP_001131074.1; NM_001137602.1.
DR RefSeq; NP_057039.1; NM_015955.2.
DR RefSeq; XP_005264408.1; XM_005264351.1.
DR UniGene; Hs.444969; -.
DR PDB; 3BCZ; X-ray; 2.10 A; A/B/C/D=5-297.
DR PDB; 3BD0; X-ray; 3.01 A; A/B/C/D=5-297.
DR PDBsum; 3BCZ; -.
DR PDBsum; 3BD0; -.
DR ProteinModelPortal; Q9Y316; -.
DR SMR; Q9Y316; 5-297.
DR IntAct; Q9Y316; 4.
DR MINT; MINT-3085289; -.
DR STRING; 9606.ENSP00000295065; -.
DR PhosphoSite; Q9Y316; -.
DR DMDM; 7388490; -.
DR PaxDb; Q9Y316; -.
DR PRIDE; Q9Y316; -.
DR DNASU; 51072; -.
DR Ensembl; ENST00000295065; ENSP00000295065; ENSG00000162959.
DR Ensembl; ENST00000379383; ENSP00000368691; ENSG00000162959.
DR Ensembl; ENST00000404530; ENSP00000385557; ENSG00000162959.
DR Ensembl; ENST00000426310; ENSP00000400795; ENSG00000162959.
DR GeneID; 51072; -.
DR KEGG; hsa:51072; -.
DR UCSC; uc002rnx.3; human.
DR GeneCards; GC02M032092; -.
DR HGNC; HGNC:14014; MEMO1.
DR HPA; HPA042603; -.
DR MIM; 611786; gene.
DR neXtProt; NX_Q9Y316; -.
DR PharmGKB; PA162395745; -.
DR eggNOG; COG1355; -.
DR HOGENOM; HOG000225260; -.
DR HOVERGEN; HBG050811; -.
DR KO; K06990; -.
DR OMA; EHSLEMH; -.
DR OrthoDB; EOG7FFMS1; -.
DR PhylomeDB; Q9Y316; -.
DR ChiTaRS; MEMO1; human.
DR EvolutionaryTrace; Q9Y316; -.
DR GenomeRNAi; 51072; -.
DR NextBio; 53687; -.
DR PRO; PR:Q9Y316; -.
DR ArrayExpress; Q9Y316; -.
DR Bgee; Q9Y316; -.
DR CleanEx; HS_MEMO1; -.
DR Genevestigator; Q9Y316; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032886; P:regulation of microtubule-based process; IMP:UniProtKB.
DR HAMAP; MF_00055; MEMO1; 1; -.
DR InterPro; IPR002737; MEMO1_fam.
DR PANTHER; PTHR11060; PTHR11060; 1.
DR Pfam; PF01875; Memo; 1.
DR TIGRFAMs; TIGR04336; AmmeMemoSam_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1 297 Protein MEMO1.
FT /FTId=PRO_0000134394.
FT MOD_RES 210 210 Phosphotyrosine (By similarity).
FT VAR_SEQ 1 20 MSNRVVCREASHAGSWYTAS -> MPLWRADKCQDVQSASW
FT RPRRAD (in isoform 3).
FT /FTId=VSP_047693.
FT VAR_SEQ 49 71 Missing (in isoform 2).
FT /FTId=VSP_041092.
FT MUTAGEN 16 16 W->A: Abolishes interaction with ERBB2.
FT MUTAGEN 49 49 H->A: Abolishes interaction with ERBB2.
FT MUTAGEN 54 54 Y->A: Diminishes interaction with ERBB2.
FT MUTAGEN 81 81 H->A: Abolishes interaction with ERBB2.
FT MUTAGEN 192 192 H->A: Abolishes interaction with ERBB2.
FT MUTAGEN 244 244 C->A: Abolishes interaction with ERBB2.
FT CONFLICT 23 23 Q -> H (in Ref. 8; AAH70046).
FT CONFLICT 172 172 L -> P (in Ref. 5; BAG59632).
FT TURN 11 15
FT HELIX 21 32
FT STRAND 43 47
FT HELIX 52 63
FT TURN 68 70
FT STRAND 73 79
FT STRAND 81 83
FT STRAND 86 90
FT STRAND 94 96
FT STRAND 103 105
FT HELIX 107 115
FT STRAND 119 121
FT HELIX 124 129
FT HELIX 134 136
FT HELIX 137 143
FT HELIX 145 147
FT STRAND 152 158
FT HELIX 163 177
FT STRAND 182 187
FT STRAND 192 194
FT HELIX 195 197
FT HELIX 204 206
FT HELIX 209 225
FT HELIX 229 239
FT HELIX 246 261
FT STRAND 266 277
FT STRAND 286 296
SQ SEQUENCE 297 AA; 33733 MW; E315FD5587776211 CRC64;
MSNRVVCREA SHAGSWYTAS GPQLNAQLEG WLSQVQSTKR PARAIIAPHA GYTYCGSCAA
HAYKQVDPSI TRRIFILGPS HHVPLSRCAL SSVDIYRTPL YDLRIDQKIY GELWKTGMFE
RMSLQTDEDE HSIEMHLPYT AKAMESHKDE FTIIPVLVGA LSESKEQEFG KLFSKYLADP
SNLFVVSSDF CHWGQRFRYS YYDESQGEIY RSIEHLDKMG MSIIEQLDPV SFSNYLKKYH
NTICGRHPIG VLLNAITELQ KNGMNMSFSF LNYAQSSQCR NWQDSSVSYA AGALTVH
//
ID MEMO1_HUMAN Reviewed; 297 AA.
AC Q9Y316; B4DLS0; D6W575; Q5R2V8; Q5R2V9; Q6NSL5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Protein MEMO1;
DE AltName: Full=C21orf19-like protein;
DE AltName: Full=Hepatitis C virus NS5A-transactivated protein 7;
DE Short=HCV NS5A-transactivated protein 7;
DE AltName: Full=Mediator of ErbB2-driven cell motility 1;
DE Short=Mediator of cell motility 1;
DE Short=Memo-1;
GN Name=MEMO1; Synonyms=C2orf4, MEMO, NS5ATP7; ORFNames=CGI-27;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11707072; DOI=10.1006/geno.2001.6640;
RA Reymond A., Friedli M., Neergaard Henrichsen C., Chapot F.,
RA Deutsch S., Ucla C., Rossier C., Lyle R., Guipponi M.,
RA Antonarakis S.E.;
RT "From PREDs and open reading frames to cDNA isolation: revisiting the
RT human chromosome 21 transcription map.";
RL Genomics 78:46-54(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Heart, and Skeletal muscle;
RA Shibuya K., Kudoh J., Shimizu N.;
RT "Cloning of two isoforms of C2orf4 gene.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Liu Y., Cheng J., Wang G., Wang J., Zhang L., Chen J., Li L.;
RT "Cloning and identification of human gene 7 transactivated by
RT hepatitis C virus NS5A protein.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [6]
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.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA 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.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA 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.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell, PNS, and 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION, AND INTERACTION WITH ERBB2.
RX PubMed=15156151; DOI=10.1038/ncb1134;
RA Marone R., Hess D., Dankort D., Muller W.J., Hynes N.E., Badache A.;
RT "Memo mediates ErbB2-driven cell motility.";
RL Nat. Cell Biol. 6:515-522(2004).
RN [10]
RP FUNCTION.
RX PubMed=20937854; DOI=10.1073/pnas.1000975107;
RA Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.;
RT "ErbB2 receptor controls microtubule capture by recruiting ACF7 to the
RT plasma membrane of migrating cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010).
RN [11]
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.,
RA Buerckstuemmer T., 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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 5-297, INTERACTION WITH
RP ERBB2, AND MUTAGENESIS OF TRP-16; HIS-49; TYR-54; HIS-81; HIS-192 AND
RP CYS-244.
RX PubMed=18045866; DOI=10.1074/jbc.M703523200;
RA Qiu C., Lienhard S., Hynes N.E., Badache A., Leahy D.J.;
RT "Memo is homologous to nonheme iron dioxygenases and binds an ErbB2-
RT derived phosphopeptide in its vestigial active site.";
RL J. Biol. Chem. 283:2734-2740(2008).
CC -!- FUNCTION: May control cell migration by relaying extracellular
CC chemotactic signals to the microtubule cytoskeleton. Mediator of
CC ERBB2 signaling. The MEMO1-RHOA-DIAPH1 signaling pathway plays an
CC important role in ERBB2-dependent stabilization of microtubules at
CC the cell cortex. It controls the localization of APC and CLASP2 to
CC the cell membrane, via the regulation of GSK3B activity. In turn,
CC membrane-bound APC allows the localization of the MACF1 to the
CC cell membrane, which is required for microtubule capture and
CC stabilization. Is required for breast carcinoma cell migration.
CC -!- SUBUNIT: Interacts with ERBB2 phosphorylated on 'Tyr-1248'.
CC -!- INTERACTION:
CC P04626:ERBB2; NbExp=6; IntAct=EBI-1104564, EBI-641062;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y316-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y316-2; Sequence=VSP_041092;
CC Name=3;
CC IsoId=Q9Y316-3; Sequence=VSP_047693;
CC -!- SIMILARITY: Belongs to the MEMO1 family.
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DR EMBL; AF363446; AAL34462.1; -; mRNA.
DR EMBL; AB041018; BAD74066.1; -; mRNA.
DR EMBL; AB041019; BAD74067.1; -; mRNA.
DR EMBL; AF529368; AAQ09602.1; -; mRNA.
DR EMBL; AF132961; AAD27736.1; -; mRNA.
DR EMBL; AK297128; BAG59632.1; -; mRNA.
DR EMBL; AL121652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAX00467.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00469.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00470.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00472.1; -; Genomic_DNA.
DR EMBL; BC018733; AAH18733.1; -; mRNA.
DR EMBL; BC070046; AAH70046.1; -; mRNA.
DR EMBL; BC094681; AAH94681.1; -; mRNA.
DR RefSeq; NP_001131074.1; NM_001137602.1.
DR RefSeq; NP_057039.1; NM_015955.2.
DR RefSeq; XP_005264408.1; XM_005264351.1.
DR UniGene; Hs.444969; -.
DR PDB; 3BCZ; X-ray; 2.10 A; A/B/C/D=5-297.
DR PDB; 3BD0; X-ray; 3.01 A; A/B/C/D=5-297.
DR PDBsum; 3BCZ; -.
DR PDBsum; 3BD0; -.
DR ProteinModelPortal; Q9Y316; -.
DR SMR; Q9Y316; 5-297.
DR IntAct; Q9Y316; 4.
DR MINT; MINT-3085289; -.
DR STRING; 9606.ENSP00000295065; -.
DR PhosphoSite; Q9Y316; -.
DR DMDM; 7388490; -.
DR PaxDb; Q9Y316; -.
DR PRIDE; Q9Y316; -.
DR DNASU; 51072; -.
DR Ensembl; ENST00000295065; ENSP00000295065; ENSG00000162959.
DR Ensembl; ENST00000379383; ENSP00000368691; ENSG00000162959.
DR Ensembl; ENST00000404530; ENSP00000385557; ENSG00000162959.
DR Ensembl; ENST00000426310; ENSP00000400795; ENSG00000162959.
DR GeneID; 51072; -.
DR KEGG; hsa:51072; -.
DR UCSC; uc002rnx.3; human.
DR GeneCards; GC02M032092; -.
DR HGNC; HGNC:14014; MEMO1.
DR HPA; HPA042603; -.
DR MIM; 611786; gene.
DR neXtProt; NX_Q9Y316; -.
DR PharmGKB; PA162395745; -.
DR eggNOG; COG1355; -.
DR HOGENOM; HOG000225260; -.
DR HOVERGEN; HBG050811; -.
DR KO; K06990; -.
DR OMA; EHSLEMH; -.
DR OrthoDB; EOG7FFMS1; -.
DR PhylomeDB; Q9Y316; -.
DR ChiTaRS; MEMO1; human.
DR EvolutionaryTrace; Q9Y316; -.
DR GenomeRNAi; 51072; -.
DR NextBio; 53687; -.
DR PRO; PR:Q9Y316; -.
DR ArrayExpress; Q9Y316; -.
DR Bgee; Q9Y316; -.
DR CleanEx; HS_MEMO1; -.
DR Genevestigator; Q9Y316; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032886; P:regulation of microtubule-based process; IMP:UniProtKB.
DR HAMAP; MF_00055; MEMO1; 1; -.
DR InterPro; IPR002737; MEMO1_fam.
DR PANTHER; PTHR11060; PTHR11060; 1.
DR Pfam; PF01875; Memo; 1.
DR TIGRFAMs; TIGR04336; AmmeMemoSam_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1 297 Protein MEMO1.
FT /FTId=PRO_0000134394.
FT MOD_RES 210 210 Phosphotyrosine (By similarity).
FT VAR_SEQ 1 20 MSNRVVCREASHAGSWYTAS -> MPLWRADKCQDVQSASW
FT RPRRAD (in isoform 3).
FT /FTId=VSP_047693.
FT VAR_SEQ 49 71 Missing (in isoform 2).
FT /FTId=VSP_041092.
FT MUTAGEN 16 16 W->A: Abolishes interaction with ERBB2.
FT MUTAGEN 49 49 H->A: Abolishes interaction with ERBB2.
FT MUTAGEN 54 54 Y->A: Diminishes interaction with ERBB2.
FT MUTAGEN 81 81 H->A: Abolishes interaction with ERBB2.
FT MUTAGEN 192 192 H->A: Abolishes interaction with ERBB2.
FT MUTAGEN 244 244 C->A: Abolishes interaction with ERBB2.
FT CONFLICT 23 23 Q -> H (in Ref. 8; AAH70046).
FT CONFLICT 172 172 L -> P (in Ref. 5; BAG59632).
FT TURN 11 15
FT HELIX 21 32
FT STRAND 43 47
FT HELIX 52 63
FT TURN 68 70
FT STRAND 73 79
FT STRAND 81 83
FT STRAND 86 90
FT STRAND 94 96
FT STRAND 103 105
FT HELIX 107 115
FT STRAND 119 121
FT HELIX 124 129
FT HELIX 134 136
FT HELIX 137 143
FT HELIX 145 147
FT STRAND 152 158
FT HELIX 163 177
FT STRAND 182 187
FT STRAND 192 194
FT HELIX 195 197
FT HELIX 204 206
FT HELIX 209 225
FT HELIX 229 239
FT HELIX 246 261
FT STRAND 266 277
FT STRAND 286 296
SQ SEQUENCE 297 AA; 33733 MW; E315FD5587776211 CRC64;
MSNRVVCREA SHAGSWYTAS GPQLNAQLEG WLSQVQSTKR PARAIIAPHA GYTYCGSCAA
HAYKQVDPSI TRRIFILGPS HHVPLSRCAL SSVDIYRTPL YDLRIDQKIY GELWKTGMFE
RMSLQTDEDE HSIEMHLPYT AKAMESHKDE FTIIPVLVGA LSESKEQEFG KLFSKYLADP
SNLFVVSSDF CHWGQRFRYS YYDESQGEIY RSIEHLDKMG MSIIEQLDPV SFSNYLKKYH
NTICGRHPIG VLLNAITELQ KNGMNMSFSF LNYAQSSQCR NWQDSSVSYA AGALTVH
//
MIM
611786
*RECORD*
*FIELD* NO
611786
*FIELD* TI
*611786 MEDIATOR OF CELL MOTILITY 1; MEMO1
;;MEMO;;
C2ORF4
*FIELD* TX
CLONING
In a search for proteins that are required for ERBB2 (164870)-dependent
read morecell motility, a marker for more aggressive metastatic cancers, Marone
et al. (2004) used a phosphorylated peptide of ErbB2 in
immunoprecipitation experiments. One of the precipitated proteins,
identified by mass spectrometry, was a 33-kD product of a novel gene,
which the authors named MEMO (mediator of ERBB2-driven cell motility).
The predicted protein contains 297 amino acids. Marone et al. (2004)
noted that MEMO does not contain a predicted SH2- or
PTB-phosphotyrosine-binding domain and suggested it may interact with
ERBB2 through SHC (600560). A MEMO-specific siRNA was shown to markedly
reduce cell motility.
Qiu et al. (2008) determined the crystal structure of MEMO and showed it
to be homologous to class III nonheme iron-dependent dioxygenases.
Unlike MEMO proteins in other species, however, there was no evidence
for metal binding in the human protein. Qiu et al. (2008) showed that
human MEMO directly binds to the ERBB2 phosphopeptide using a vestigial
(dioxygenase) enzymatic active site.
MAPPING
Scott (2008) mapped the MEMO1 gene to chromosome 2p22-p21 based on an
alignment of the MEMO1 sequence (GenBank GENBANK AB041018) with the
genomic sequence (build 36.2).
*FIELD* RF
1. Marone, R.; Hess, D.; Dankort, D.; Muller, W. J.; Hynes, N. E.;
Badache, A.: Memo mediates ErbB2-driven cell motility. Nature Cell
Biol. 6: 515-522, 2004.
2. Qiu, C.; Lienhard, S.; Hynes, N. E.; Badache, A.; Leahy, D. J.
: Memo is homologous to nonheme iron dioxygenases and binds an ErbB2-derived
phosphopeptide in its vestigial active site. J. Biol. Chem. 283:
2734-2740, 2008.
3. Scott, A. F.: Personal Communication. Baltimore, Md. 2/12/2008.
*FIELD* CD
Alan F. Scott: 2/12/2008
*FIELD* ED
carol: 02/12/2008
*RECORD*
*FIELD* NO
611786
*FIELD* TI
*611786 MEDIATOR OF CELL MOTILITY 1; MEMO1
;;MEMO;;
C2ORF4
*FIELD* TX
CLONING
In a search for proteins that are required for ERBB2 (164870)-dependent
read morecell motility, a marker for more aggressive metastatic cancers, Marone
et al. (2004) used a phosphorylated peptide of ErbB2 in
immunoprecipitation experiments. One of the precipitated proteins,
identified by mass spectrometry, was a 33-kD product of a novel gene,
which the authors named MEMO (mediator of ERBB2-driven cell motility).
The predicted protein contains 297 amino acids. Marone et al. (2004)
noted that MEMO does not contain a predicted SH2- or
PTB-phosphotyrosine-binding domain and suggested it may interact with
ERBB2 through SHC (600560). A MEMO-specific siRNA was shown to markedly
reduce cell motility.
Qiu et al. (2008) determined the crystal structure of MEMO and showed it
to be homologous to class III nonheme iron-dependent dioxygenases.
Unlike MEMO proteins in other species, however, there was no evidence
for metal binding in the human protein. Qiu et al. (2008) showed that
human MEMO directly binds to the ERBB2 phosphopeptide using a vestigial
(dioxygenase) enzymatic active site.
MAPPING
Scott (2008) mapped the MEMO1 gene to chromosome 2p22-p21 based on an
alignment of the MEMO1 sequence (GenBank GENBANK AB041018) with the
genomic sequence (build 36.2).
*FIELD* RF
1. Marone, R.; Hess, D.; Dankort, D.; Muller, W. J.; Hynes, N. E.;
Badache, A.: Memo mediates ErbB2-driven cell motility. Nature Cell
Biol. 6: 515-522, 2004.
2. Qiu, C.; Lienhard, S.; Hynes, N. E.; Badache, A.; Leahy, D. J.
: Memo is homologous to nonheme iron dioxygenases and binds an ErbB2-derived
phosphopeptide in its vestigial active site. J. Biol. Chem. 283:
2734-2740, 2008.
3. Scott, A. F.: Personal Communication. Baltimore, Md. 2/12/2008.
*FIELD* CD
Alan F. Scott: 2/12/2008
*FIELD* ED
carol: 02/12/2008