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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 - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • negative regulation of apoptotic process Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of filopodium assembly Source: UniProtKB

Keywordsi

Biological processApoptosis

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
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000141741.11.
HGNCiHGNC:28230. MIEN1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi112 – 115Missing : No effect on subcellular location. Low protein abundance, suggesting that stability is affected. 1 Publication4
Mutagenesisi112C → S: Abolishes prenylation. Predominantly cysolic with little plasma membrane-associated expression. Reduces cell migration by affecting filopodia formation. 1 Publication1

Organism-specific databases

DisGeNETi84299.
OpenTargetsiENSG00000141741.
PharmGKBiPA134947080.

Polymorphism and mutation databases

BioMutaiMIEN1.
DMDMi74732925.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002650992 – 112Migration and invasion enhancer 1Add BLAST111
PropeptideiPRO_0000396008113 – 115Removed in mature formCurated3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Disulfide bondi30 ↔ 33Redox-active1 Publication
Lipidationi112S-geranylgeranyl cysteine2 Publications1

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

EPDiQ9BRT3.
MaxQBiQ9BRT3.
PaxDbiQ9BRT3.
PeptideAtlasiQ9BRT3.
PRIDEiQ9BRT3.

PTM databases

iPTMnetiQ9BRT3.
PhosphoSitePlusiQ9BRT3.

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

BgeeiENSG00000141741.
CleanExiHS_C17orf37.
ExpressionAtlasiQ9BRT3. baseline and differential.
GenevisibleiQ9BRT3. HS.

Organism-specific databases

HPAiHPA061344.

Interactioni

Subunit structurei

Interacts with GPX1.By similarity

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi124025. 5 interactors.
IntActiQ9BRT3. 12 interactors.
STRINGi9606.ENSP00000377778.

Structurei

Secondary structure

1115
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi26 – 29Combined sources4
Turni31 – 34Combined sources4
Helixi36 – 46Combined sources11
Turni47 – 49Combined sources3
Beta strandi51 – 53Combined sources3
Beta strandi56 – 59Combined sources4
Beta strandi61 – 63Combined sources3
Beta strandi65 – 68Combined sources4
Helixi77 – 80Combined sources4
Turni86 – 90Combined sources5
Helixi91 – 96Combined sources6
Turni97 – 99Combined sources3

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the SelWTH family.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG410J06V. Eukaryota.
ENOG41127T6. LUCA.
GeneTreeiENSGT00390000010440.
HOGENOMiHOG000275576.
HOVERGENiHBG059755.
InParanoidiQ9BRT3.
KOiK07401.
OMAiCLAFPQH.
PhylomeDBiQ9BRT3.
TreeFamiTF326627.

Family and domain databases

InterProiView protein in InterPro
IPR011893. Selenoprotein_Rdx-typ.
IPR036249. Thioredoxin-like_sf.
PfamiView protein in Pfam
PF10262. Rdx. 1 hit.
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_001317135.1. NM_001330206.1.
NP_115715.3. NM_032339.4.
UniGeneiHs.333526.

Genome annotation databases

EnsembliENST00000394231; ENSP00000377778; ENSG00000141741.
GeneIDi84299.
KEGGihsa:84299.
UCSCiuc002hsq.4. human.

Similar proteinsi

Entry informationi

Entry nameiMIEN1_HUMAN
AccessioniPrimary (citable) accession number: Q9BRT3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: June 1, 2001
Last modified: October 25, 2017
This is version 122 of the entry and version 1 of the sequence. See 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