Q9Y316 (MEMO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	297 AA.
Sequence status	Complete.
Protein existence	Evidence 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 diversity	Alternative splicing
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	regulation of microtubule-based process Inferred from mutant phenotype Ref.10. Source: UniProtKB
Cellular_component	cytosol Inferred from direct assay PubMed 16780588. Source: UniProtKB nucleus Inferred from direct assay PubMed 16780588. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 297

297

Protein MEMO1

PRO_0000134394

Amino acid modifications

Modified residue

210

1

Phosphotyrosine By similarity

Natural variations

Alternative sequence

49 – 71

23

Missing in isoform 2.

VSP_041092

Experimental info

Mutagenesis

16

1

W → A: Abolishes interaction with ERBB2. Ref.12

Mutagenesis

49

1

H → A: Abolishes interaction with ERBB2. Ref.12

Mutagenesis

54

1

Y → A: Diminishes interaction with ERBB2. Ref.12

Mutagenesis

81

1

H → A: Abolishes interaction with ERBB2. Ref.12

Mutagenesis

192

1

H → A: Abolishes interaction with ERBB2. Ref.12

Mutagenesis

244

1

C → A: Abolishes interaction with ERBB2. Ref.12

Sequence conflict

23

1

Q → H in AAH70046. Ref.8

Sequence conflict

172

1

L → P in BAG59632. Ref.5

Secondary structure

1

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297

Helix Strand Turn

Details...

Turn

11 – 15

5

Helix

21 – 32

12

Beta strand

43 – 47

5

Helix

52 – 63

12

Turn

68 – 70

3

Beta strand

73 – 79

7

Beta strand

81 – 83

3

Beta strand

86 – 90

5

Beta strand

94 – 96

3

Beta strand

103 – 105

3

Helix

107 – 115

9

Beta strand

119 – 121

3

Helix

124 – 129

6

Helix

134 – 136

3

Helix

137 – 143

7

Helix

145 – 147

3

Beta strand

152 – 158

7

Helix

163 – 177

15

Beta strand

182 – 187

6

Beta strand

192 – 194

3

Helix

195 – 197

3

Helix

204 – 206

3

Helix

209 – 225

17

Helix

229 – 239

11

Helix

246 – 261

16

Beta strand

266 – 277

12

Beta strand

286 – 296

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: E315FD5587776211	FASTA	297	33,733
	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
	Isoform 2 [UniParc]. Checksum: 1BE5B4A07A5D44D8	FASTA	274	31,307
	10 20 30 40 50 60 MSNRVVCREA SHAGSWYTAS GPQLNAQLEG WLSQVQSTKR PARAIIAPRR IFILGPSHHV 70 80 90 100 110 120 PLSRCALSSV DIYRTPLYDL RIDQKIYGEL WKTGMFERMS LQTDEDEHSI EMHLPYTAKA 130 140 150 160 170 180 MESHKDEFTI IPVLVGALSE SKEQEFGKLF SKYLADPSNL FVVSSDFCHW GQRFRYSYYD 190 200 210 220 230 240 ESQGEIYRSI EHLDKMGMSI IEQLDPVSFS NYLKKYHNTI CGRHPIGVLL NAITELQKNG 250 260 270 MNMSFSFLNY AQSSQCRNWQ DSSVSYAAGA LTVH

References

	« Hide 'large scale' referencesShow '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] (ISOFORM 1). 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. , 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. , 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. , 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.
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.

IPI

IPI00032426.
IPI01015226.

RefSeq

NP_001131074.1. NM_001137602.1.
NP_057039.1. NM_015955.2.

UniGene

Hs.444969.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BCZ	X-ray	2.10	A/B/C/D	5-297	[»]
3BD0	X-ray	3.01	A/B/C/D	5-297	[»]

ProteinModelPortal

Q9Y316.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y316. 2 interactions.

MINT

MINT-3085289.

STRING

9606.ENSP00000295065.

PTM databases

PhosphoSite

Q9Y316.

Polymorphism databases

DMDM

7388490.

Proteomic databases

PaxDb

Q9Y316.

PRIDE

Q9Y316.

Protocols and materials databases

DNASU

51072.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000295065; ENSP00000295065; ENSG00000162959.
ENST00000404530; ENSP00000385557; ENSG00000162959.
ENST00000426310; ENSP00000400795; ENSG00000162959.

GeneID

51072.

KEGG

hsa:51072.

UCSC

uc002rnx.3. human.
uc010ymu.2. human.

Organism-specific databases

GeneCards

GC02M032092.

HGNC

HGNC:14014. MEMO1.

HPA

HPA042603.

MIM

611786. gene.

neXtProt

NX_Q9Y316.

PharmGKB

PA162395745.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1355.

HOGENOM

HOG000225260.

HOVERGEN

HBG050811.

KO

K06990.

OrthoDB

EOG4PC9SH.

PhylomeDB

Q9Y316.

Gene expression databases

ArrayExpress

Q9Y316.

Bgee

Q9Y316.

CleanEx

HS_MEMO1.

Genevestigator

Q9Y316.

GermOnline

ENSG00000162959. Homo sapiens.

Family and domain databases

InterPro

IPR002737. UPF0103/Memo-related.
[Graphical view]

PANTHER

PTHR11060. PTHR11060. 1 hit.

Pfam

PF01875. Memo. 1 hit.
[Graphical view]

TIGRFAMs

TIGR04336. AmmeMemoSam_B. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

MEMO1. human.

EvolutionaryTrace

Q9Y316.

GenomeRNAi

51072.

NextBio

53687.

SOURCE

Search...

Entry information

Entry name

MEMO1_HUMAN

Accession

Primary (citable) accession number: Q9Y316
Secondary accession number(s): B4DLS0 , D6W575, Q5R2V9, Q6NSL5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	May 29, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.