Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Migration and invasion enhancer 1

Gene

MIEN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Increases cell migration by inducing filopodia formation at the leading edge of migrating cells. Plays a role in regulation of apoptosis, possibly through control of CASP3. May be involved in a redox-related process.2 Publications

GO - Molecular functioni

  1. selenium binding Source: InterPro

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cell redox homeostasis Source: InterPro
  3. negative regulation of apoptotic process Source: UniProtKB
  4. positive regulation of cell migration Source: UniProtKB
  5. positive regulation of filopodium assembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Names & Taxonomyi

Protein namesi
Recommended name:
Migration and invasion enhancer 1
Alternative name(s):
HBV X-transactivated gene 4 protein
HBV XAg-transactivated protein 4
Protein C35
Gene namesi
Name:MIEN1
Synonyms:C17orf37, RDX12, XTP4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:28230. MIEN1.

Subcellular locationi

  1. Cytoplasmcytosol
  2. Cell membrane; Lipid-anchor; Cytoplasmic side

  3. Note: Concentrates at the leading edge of migrating cells. Localizes outside membrane raft regions.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  4. intrinsic component of the cytoplasmic side of the plasma membrane Source: UniProtKB
  5. nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi112 – 1154Missing : No effect on subcellular location. Low protein abundance, suggesting that stability is affected. 1 Publication
Mutagenesisi112 – 1121C → S: Abolishes prenylation. Predominantly cysolic with little plasma membrane-associated expression. Reduces cell migration by affecting filopodia formation. 1 Publication

Organism-specific databases

PharmGKBiPA134947080.

Polymorphism and mutation databases

BioMutaiMIEN1.
DMDMi74732925.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 112111Migration and invasion enhancer 1PRO_0000265099Add
BLAST
Propeptidei113 – 1153Removed in mature formCuratedPRO_0000396008

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Disulfide bondi30 ↔ 33Redox-active1 Publication
Lipidationi112 – 1121S-geranylgeranyl cysteine2 Publications

Post-translational modificationi

Isoprenylation facilitates association with the plasma membrane and enhances the migratory phenotype of cells by inducing increased filopodia formation.3 Publications

Keywords - PTMi

Acetylation, Disulfide bond, Lipoprotein, Prenylation

Proteomic databases

MaxQBiQ9BRT3.
PaxDbiQ9BRT3.
PRIDEiQ9BRT3.

PTM databases

PhosphoSiteiQ9BRT3.

Expressioni

Tissue specificityi

Among normal tissues, present only in Leydig cells. Strongly up-regulated in breast cancers and in brain cancer distant metastasis (at protein level). Up-regulated in prostate cancer cells and in the higher grades of prostate adenocarcinoma (at protein level).2 Publications

Gene expression databases

BgeeiQ9BRT3.
CleanExiHS_C17orf37.
ExpressionAtlasiQ9BRT3. baseline and differential.
GenevestigatoriQ9BRT3.

Organism-specific databases

HPAiHPA056650.
HPA061344.

Interactioni

Subunit structurei

Interacts with GPX1.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
RELQ048643EBI-6137472,EBI-307352

Protein-protein interaction databases

BioGridi124025. 4 interactions.
IntActiQ9BRT3. 1 interaction.
STRINGi9606.ENSP00000377778.

Structurei

Secondary structure

1
115
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 294Combined sources
Turni31 – 344Combined sources
Helixi36 – 4611Combined sources
Turni47 – 493Combined sources
Beta strandi51 – 533Combined sources
Beta strandi56 – 594Combined sources
Beta strandi61 – 633Combined sources
Beta strandi65 – 684Combined sources
Helixi77 – 804Combined sources
Turni86 – 905Combined sources
Helixi91 – 966Combined sources
Turni97 – 993Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LJKNMR-A1-115[»]
ProteinModelPortaliQ9BRT3.
SMRiQ9BRT3. Positions 1-115.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SelWTH family.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiNOG85235.
GeneTreeiENSGT00390000010440.
HOGENOMiHOG000275576.
HOVERGENiHBG059755.
InParanoidiQ9BRT3.
KOiK07401.
OMAiRPPCIIL.
OrthoDBiEOG7SR4Q5.
PhylomeDBiQ9BRT3.
TreeFamiTF326627.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR011893. Selenoprotein_Rdx-typ.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF10262. Rdx. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR02174. CXXU_selWTH. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9BRT3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGEPGQTSV APPPEEVEPG SGVRIVVEYC EPCGFEATYL ELASAVKEQY
60 70 80 90 100
PGIEIESRLG GTGAFEIEIN GQLVFSKLEN GGFPYEKDLI EAIRRASNGE
110
TLEKITNSRP PCVIL
Length:115
Mass (Da):12,403
Last modified:June 1, 2001 - v1
Checksum:i5D8B911C0F23DDC1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY508814 mRNA. Translation: AAR92035.1.
AF490253 mRNA. Translation: AAO85461.1.
AC079199 Genomic DNA. No translation available.
BC006006 mRNA. Translation: AAH06006.1.
CCDSiCCDS11344.1.
RefSeqiNP_115715.3. NM_032339.3.
UniGeneiHs.333526.

Genome annotation databases

EnsembliENST00000394231; ENSP00000377778; ENSG00000141741.
GeneIDi84299.
KEGGihsa:84299.
UCSCiuc002hsq.3. human.

Polymorphism and mutation databases

BioMutaiMIEN1.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY508814 mRNA. Translation: AAR92035.1.
AF490253 mRNA. Translation: AAO85461.1.
AC079199 Genomic DNA. No translation available.
BC006006 mRNA. Translation: AAH06006.1.
CCDSiCCDS11344.1.
RefSeqiNP_115715.3. NM_032339.3.
UniGeneiHs.333526.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LJKNMR-A1-115[»]
ProteinModelPortaliQ9BRT3.
SMRiQ9BRT3. Positions 1-115.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124025. 4 interactions.
IntActiQ9BRT3. 1 interaction.
STRINGi9606.ENSP00000377778.

PTM databases

PhosphoSiteiQ9BRT3.

Polymorphism and mutation databases

BioMutaiMIEN1.
DMDMi74732925.

Proteomic databases

MaxQBiQ9BRT3.
PaxDbiQ9BRT3.
PRIDEiQ9BRT3.

Protocols and materials databases

DNASUi84299.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000394231; ENSP00000377778; ENSG00000141741.
GeneIDi84299.
KEGGihsa:84299.
UCSCiuc002hsq.3. human.

Organism-specific databases

CTDi84299.
GeneCardsiGC17M037886.
H-InvDBHIX0013783.
HGNCiHGNC:28230. MIEN1.
HPAiHPA056650.
HPA061344.
MIMi611802. gene.
neXtProtiNX_Q9BRT3.
PharmGKBiPA134947080.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG85235.
GeneTreeiENSGT00390000010440.
HOGENOMiHOG000275576.
HOVERGENiHBG059755.
InParanoidiQ9BRT3.
KOiK07401.
OMAiRPPCIIL.
OrthoDBiEOG7SR4Q5.
PhylomeDBiQ9BRT3.
TreeFamiTF326627.

Miscellaneous databases

ChiTaRSiMIEN1. human.
GenomeRNAii84299.
NextBioi73960.
PROiQ9BRT3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BRT3.
CleanExiHS_C17orf37.
ExpressionAtlasiQ9BRT3. baseline and differential.
GenevestigatoriQ9BRT3.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR011893. Selenoprotein_Rdx-typ.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF10262. Rdx. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR02174. CXXU_selWTH. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ISOPRENYLATION.
  2. "Cloning and identification of human gene 4 transactivated by hepatitis B virus X antigen."
    Liu Y., Cheng J., Lu Y., Wang G., Zhang L., Chen J., Li L.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Brain.
  5. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  6. "Novel gene C17orf37 in 17q12 amplicon promotes migration and invasion of prostate cancer cells."
    Dasgupta S., Wasson L.M., Rauniyar N., Prokai L., Borejdo J., Vishwanatha J.K.
    Oncogene 28:2860-2872(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-112.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Prenylated c17orf37 induces filopodia formation to promote cell migration and metastasis."
    Dasgupta S., Cushman I., Kpetemey M., Casey P.J., Vishwanatha J.K.
    J. Biol. Chem. 286:25935-25946(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-112, MUTAGENESIS OF CYS-112 AND 112-CYS--LEU-115.
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "Solution structure of the oncogenic MIEN1 protein reveals a thioredoxin-like fold with a redox-active motif."
    Hsu C.H., Shen T.L., Chang C.F., Chang Y.Y., Huang L.Y.
    PLoS ONE 7:E52292-E52292(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, DISULFIDE BOND.

Entry informationi

Entry nameiMIEN1_HUMAN
AccessioniPrimary (citable) accession number: Q9BRT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: June 1, 2001
Last modified: April 29, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.