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Q9BRT3 (MIEN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Migration and invasion enhancer 1
Alternative name(s):
HBV X-transactivated gene 4 protein
HBV XAg-transactivated protein 4
Protein C35
Gene names
Name:MIEN1
Synonyms:C17orf37, RDX12, XTP4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length115 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.8

Subunit structure

Interacts with GPX1 By similarity.

Subcellular location

Cytoplasmcytosol. Cell membrane; Lipid-anchor; Cytoplasmic side. Note: Concentrates at the leading edge of migrating cells. Localizes outside membrane raft regions. Ref.1 Ref.6 Ref.8

Tissue specificity

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). Ref.1 Ref.6

Post-translational modification

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

Sequence similarities

Belongs to the SelWTH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 112111Migration and invasion enhancer 1
PRO_0000265099
Propeptide113 – 1153Removed in mature form Probable
PRO_0000396008

Amino acid modifications

Modified residue21N-acetylserine Ref.5 Ref.9
Lipidation1121S-geranylgeranyl cysteine Ref.1 Ref.6 Ref.8
Disulfide bond30 ↔ 33Redox-active Ref.10

Experimental info

Mutagenesis112 – 1154Missing: No effect on subcellular location. Low protein abundance, suggesting that stability is affected. Ref.8
Mutagenesis1121C → S: Abolishes prenylation. Predominantly cysolic with little plasma membrane-associated expression. Reduces cell migration by affecting filopodia formation. Ref.8

Secondary structure

...................... 115
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9BRT3 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 5D8B911C0F23DDC1

FASTA11512,403
        10         20         30         40         50         60 
MSGEPGQTSV APPPEEVEPG SGVRIVVEYC EPCGFEATYL ELASAVKEQY PGIEIESRLG 

        70         80         90        100        110 
GTGAFEIEIN GQLVFSKLEN GGFPYEKDLI EAIRRASNGE TLEKITNSRP PCVIL 

« Hide

References

« Hide 'large scale' references
[1]"C35 (C17orf37) is a novel tumor biomarker abundantly expressed in breast cancer."
Evans E.E., Henn A.D., Jonason A., Paris M.J., Schiffhauer L.M., Borrello M.A., Smith E.S., Sahasrabudhe D.M., Zauderer M.
Mol. Cancer Ther. 5:2919-2930(2006) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"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].
[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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY508814 mRNA. Translation: AAR92035.1.
AF490253 mRNA. Translation: AAO85461.1.
AC079199 Genomic DNA. No translation available.
BC006006 mRNA. Translation: AAH06006.1.
CCDSCCDS11344.1.
RefSeqNP_115715.3. NM_032339.3.
UniGeneHs.333526.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LJKNMR-A1-115[»]
ProteinModelPortalQ9BRT3.
SMRQ9BRT3. Positions 1-115.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000377778.

PTM databases

PhosphoSiteQ9BRT3.

Polymorphism databases

DMDM74732925.

Proteomic databases

MaxQBQ9BRT3.
PaxDbQ9BRT3.
PRIDEQ9BRT3.

Protocols and materials databases

DNASU84299.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000394231; ENSP00000377778; ENSG00000141741.
GeneID84299.
KEGGhsa:84299.
UCSCuc002hsq.3. human.

Organism-specific databases

CTD84299.
GeneCardsGC17M037886.
H-InvDBHIX0013783.
HGNCHGNC:28230. MIEN1.
HPAHPA056650.
HPA061344.
MIM611802. gene.
neXtProtNX_Q9BRT3.
PharmGKBPA134947080.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG85235.
HOGENOMHOG000275576.
HOVERGENHBG059755.
InParanoidQ9BRT3.
KOK07401.
OMAMYTSSAS.
OrthoDBEOG7SR4Q5.
PhylomeDBQ9BRT3.
TreeFamTF326627.

Gene expression databases

ArrayExpressQ9BRT3.
BgeeQ9BRT3.
CleanExHS_C17orf37.
GenevestigatorQ9BRT3.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR011893. Selenoprotein_Rdx-typ.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF10262. Rdx. 1 hit.
[Graphical view]
SUPFAMSSF52833. SSF52833. 1 hit.
TIGRFAMsTIGR02174. CXXU_selWTH. 1 hit.
ProtoNetSearch...

Other

ChiTaRSMIEN1. human.
GenomeRNAi84299.
NextBio73960.
PROQ9BRT3.
SOURCESearch...

Entry information

Entry nameMIEN1_HUMAN
AccessionPrimary (citable) accession number: Q9BRT3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 94 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

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 17

Human chromosome 17: entries, gene names and cross-references to MIM