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Q9Y316 (MEMO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein MEMO1
Alternative name(s):
C21orf19-like protein
Hepatitis C virus NS5A-transactivated protein 7
Short name=HCV NS5A-transactivated protein 7
Mediator of ErbB2-driven cell motility 1
Short name=Mediator of cell motility 1
Short name=Memo-1
Gene names
Name:MEMO1
Synonyms:C2orf4, MEMO, NS5ATP7
ORF Names:CGI-27
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May control cell migration by relaying extracellular chemotactic signals to the microtubule cytoskeleton. Mediator of ERBB2 signaling. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Is required for breast carcinoma cell migration. Ref.9 Ref.10

Subunit structure

Interacts with ERBB2 phosphorylated on 'Tyr-1248'. Ref.9 Ref.12

Sequence similarities

Belongs to the MEMO1 family.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processregulation of microtubule-based process

Inferred from mutant phenotype Ref.10. Source: UniProtKB

   Cellular_componentcytosol

Inferred from direct assay PubMed 16780588. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 16780588. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ERBB2P046266EBI-1104564,EBI-641062

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y316-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9Y316-2)

The sequence of this isoform differs from the canonical sequence as follows:
     49-71: Missing.
Isoform 3 (identifier: Q9Y316-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MSNRVVCREASHAGSWYTAS → MPLWRADKCQDVQSASWRPRRAD

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 297297Protein MEMO1 HAMAP-Rule MF_00055
PRO_0000134394

Amino acid modifications

Modified residue2101Phosphotyrosine By similarity

Natural variations

Alternative sequence1 – 2020MSNRV…WYTAS → MPLWRADKCQDVQSASWRPR RAD in isoform 3.
VSP_047693
Alternative sequence49 – 7123Missing in isoform 2.
VSP_041092

Experimental info

Mutagenesis161W → A: Abolishes interaction with ERBB2. Ref.12
Mutagenesis491H → A: Abolishes interaction with ERBB2. Ref.12
Mutagenesis541Y → A: Diminishes interaction with ERBB2. Ref.12
Mutagenesis811H → A: Abolishes interaction with ERBB2. Ref.12
Mutagenesis1921H → A: Abolishes interaction with ERBB2. Ref.12
Mutagenesis2441C → A: Abolishes interaction with ERBB2. Ref.12
Sequence conflict231Q → H in AAH70046. Ref.8
Sequence conflict1721L → P in BAG59632. Ref.5

Secondary structure

..................................................... 297
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: E315FD5587776211

FASTA29733,733
        10         20         30         40         50         60 
MSNRVVCREA SHAGSWYTAS GPQLNAQLEG WLSQVQSTKR PARAIIAPHA GYTYCGSCAA 

        70         80         90        100        110        120 
HAYKQVDPSI TRRIFILGPS HHVPLSRCAL SSVDIYRTPL YDLRIDQKIY GELWKTGMFE 

       130        140        150        160        170        180 
RMSLQTDEDE HSIEMHLPYT AKAMESHKDE FTIIPVLVGA LSESKEQEFG KLFSKYLADP 

       190        200        210        220        230        240 
SNLFVVSSDF CHWGQRFRYS YYDESQGEIY RSIEHLDKMG MSIIEQLDPV SFSNYLKKYH 

       250        260        270        280        290 
NTICGRHPIG VLLNAITELQ KNGMNMSFSF LNYAQSSQCR NWQDSSVSYA AGALTVH 

« Hide

Isoform 2 [UniParc].

Checksum: 1BE5B4A07A5D44D8
Show »

FASTA27431,307
Isoform 3 [UniParc].

Checksum: 0778186B7CCA0ADA
Show »

FASTA30034,294

References

« Hide 'large scale' references
[1]"From PREDs and open reading frames to cDNA isolation: revisiting the human chromosome 21 transcription map."
Reymond A., Friedli M., Neergaard Henrichsen C., Chapot F., Deutsch S., Ucla C., Rossier C., Lyle R., Guipponi M., Antonarakis S.E.
Genomics 78:46-54(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Cloning of two isoforms of C2orf4 gene."
Shibuya K., Kudoh J., Shimizu N.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
Tissue: Heart and Skeletal muscle.
[3]"Cloning and identification of human gene 7 transactivated by hepatitis C virus NS5A protein."
Liu Y., Cheng J., Wang G., Wang J., Zhang L., Chen J., Li L.
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: B-cell, PNS and Testis.
[9]"Memo mediates ErbB2-driven cell motility."
Marone R., Hess D., Dankort D., Muller W.J., Hynes N.E., Badache A.
Nat. Cell Biol. 6:515-522(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ERBB2.
[10]"ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells."
Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.
Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Memo is homologous to nonheme iron dioxygenases and binds an ErbB2-derived phosphopeptide in its vestigial active site."
Qiu C., Lienhard S., Hynes N.E., Badache A., Leahy D.J.
J. Biol. Chem. 283:2734-2740(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 5-297, INTERACTION WITH ERBB2, MUTAGENESIS OF TRP-16; HIS-49; TYR-54; HIS-81; HIS-192 AND CYS-244.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF363446 mRNA. Translation: AAL34462.1.
AB041018 mRNA. Translation: BAD74066.1.
AB041019 mRNA. Translation: BAD74067.1.
AF529368 mRNA. Translation: AAQ09602.1.
AF132961 mRNA. Translation: AAD27736.1.
AK297128 mRNA. Translation: BAG59632.1.
AL121652 Genomic DNA. No translation available.
AL121655 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAX00467.1.
CH471053 Genomic DNA. Translation: EAX00469.1.
CH471053 Genomic DNA. Translation: EAX00470.1.
CH471053 Genomic DNA. Translation: EAX00472.1.
BC018733 mRNA. Translation: AAH18733.1.
BC070046 mRNA. Translation: AAH70046.1.
BC094681 mRNA. Translation: AAH94681.1.
RefSeqNP_001131074.1. NM_001137602.1.
NP_057039.1. NM_015955.2.
XP_005264408.1. XM_005264351.1.
UniGeneHs.444969.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BCZX-ray2.10A/B/C/D5-297[»]
3BD0X-ray3.01A/B/C/D5-297[»]
ProteinModelPortalQ9Y316.
SMRQ9Y316. Positions 5-297.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119263. 5 interactions.
IntActQ9Y316. 4 interactions.
MINTMINT-3085289.
STRING9606.ENSP00000295065.

PTM databases

PhosphoSiteQ9Y316.

Polymorphism databases

DMDM7388490.

Proteomic databases

PaxDbQ9Y316.
PRIDEQ9Y316.

Protocols and materials databases

DNASU51072.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295065; ENSP00000295065; ENSG00000162959. [Q9Y316-1]
ENST00000379383; ENSP00000368691; ENSG00000162959. [Q9Y316-3]
ENST00000404530; ENSP00000385557; ENSG00000162959. [Q9Y316-1]
ENST00000426310; ENSP00000400795; ENSG00000162959. [Q9Y316-2]
GeneID51072.
KEGGhsa:51072.
UCSCuc002rnx.3. human. [Q9Y316-1]
uc010ymu.2. human. [Q9Y316-2]

Organism-specific databases

GeneCardsGC02M032092.
HGNCHGNC:14014. MEMO1.
HPAHPA042603.
MIM611786. gene.
neXtProtNX_Q9Y316.
PharmGKBPA162395745.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1355.
HOGENOMHOG000225260.
HOVERGENHBG050811.
KOK06990.
OMAEHSLEMH.
OrthoDBEOG7FFMS1.
PhylomeDBQ9Y316.
TreeFamTF300014.

Gene expression databases

BgeeQ9Y316.
CleanExHS_MEMO1.
GenevestigatorQ9Y316.

Family and domain databases

HAMAPMF_00055. MEMO1.
InterProIPR002737. MEMO1_fam.
[Graphical view]
PANTHERPTHR11060. PTHR11060. 1 hit.
PfamPF01875. Memo. 1 hit.
[Graphical view]
TIGRFAMsTIGR04336. AmmeMemoSam_B. 1 hit.
ProtoNetSearch...

Other

ChiTaRSMEMO1. human.
EvolutionaryTraceQ9Y316.
GenomeRNAi51072.
NextBio53687.
PROQ9Y316.
SOURCESearch...

Entry information

Entry nameMEMO1_HUMAN
AccessionPrimary (citable) accession number: Q9Y316
Secondary accession number(s): B4DLS0 expand/collapse secondary AC list , D6W575, Q5R2V8, Q5R2V9, Q6NSL5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Uncharacterized protein families (UPF)

List of uncharacterized protein family (UPF) entries

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM