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O60447 (EVI5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ecotropic viral integration site 5 protein homolog

Short name=EVI-5
Alternative name(s):
Neuroblastoma stage 4S gene protein
Gene names
Name:EVI5
Synonyms:NB4S
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length810 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as a regulator of cell cycle progression by stabilizing the FBXO5 protein and promoting cyclin-A accumulation during interphase. May play a role in cytokinesis. Ref.4

Subunit structure

Dimeric and monomeric. Interacts with alpha- and gamma-tubulin. Interacts with FBXO5. Interacts with the chromosome passenger complex (CPC) which is at least composed of AURKB/aurora-B, BIRC5/survivin, CDCA8/borealin and INCENP. Ref.3 Ref.4 Ref.5

Subcellular location

Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle. Note: Associates with the mitotic spindle through anaphase and remains within the midzone and midbody until completion of cytokinesis. Ref.3 Ref.4 Ref.5

Tissue specificity

Expressed in various cell lines (at protein level). Expressed in a wide range of tissues including brain and adrenal. Ref.1 Ref.3

Induction

Down-regulated during mitosis through proteasomal degradation. Ref.4

Post-translational modification

Probably phosphorylated by PLK1; may be required for degradation during mitosis. Ref.4

Ubiquitinated. Degradation during prophase is ubiquitin-dependent. Ref.4

Involvement in disease

A chromosomal aberration involving EVI5 is found is a patient with stage 4S neuroblastoma. Translocation t(1;10)(p22;q21) that forms a EVI5-TRNG10 fusion protein. TRNG10 is a probable structural transcript which is normally not translated. Ref.1

Miscellaneous

Depletion of EVI5 by RNAi causes cell cycle arrest and mitotic abnormalities.

Sequence similarities

Contains 1 Rab-GAP TBC domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FBXO5Q9UKT46EBI-852291,EBI-852298
PLK1P533502EBI-852291,EBI-476768

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 810810Ecotropic viral integration site 5 protein homolog
PRO_0000256241

Regions

Domain163 – 348186Rab-GAP TBC
Region1 – 483483Interaction with alpha-tubulin, gamma-tubulin, BIRC5 and FBXO5
Region128 – 693566Dimerization
Region377 – 810434Targeting to the centrosomes
Region487 – 810324Interaction with AURKB and INCENP
Coiled coil406 – 716311 Potential
Compositional bias28 – 128101Ser-rich

Sites

Site5941Breakpoint for translocation to form EVI5-TRNG10 fusion protein

Amino acid modifications

Modified residue7761Phosphoserine Ref.6
Modified residue7781Phosphoserine By similarity

Natural variations

Natural variant821D → V. Ref.1
Corresponds to variant rs1064580 [ dbSNP | Ensembl ].
VAR_047753
Natural variant3361I → V. Ref.1
Corresponds to variant rs2391199 [ dbSNP | Ensembl ].
VAR_028890
Natural variant6121Q → H.
Corresponds to variant rs11808092 [ dbSNP | Ensembl ].
VAR_028891

Experimental info

Sequence conflict941R → I in AAC16031. Ref.1
Sequence conflict4021K → Q in AAC16031. Ref.1
Sequence conflict7141R → K in AAC16031. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O60447 [UniParc].

Last modified November 30, 2010. Version 3.
Checksum: 4A2CC99A9192F632

FASTA81092,949
        10         20         30         40         50         60 
MVTNKMTAAF RNPSGKQVAT DKVAEKLSST LSWVKNTVSH TVSQMASQVA SPSTSLHTTS 

        70         80         90        100        110        120 
SSTTLSTPAL SPSSPSQLSP DDLELLAKLE EQNRLLETDS KSLRSVNGSR RNSGSSLVSS 

       130        140        150        160        170        180 
SSASSNLSHL EEDSWILWGR IVNEWEDVRK KKEKQVKELV HKGIPHHFRA IVWQLLCSAQ 

       190        200        210        220        230        240 
SMPIKDQYSE LLKMTSPCEK LIRRDIARTY PEHNFFKEKD SLGQEVLFNV MKAYSLVDRE 

       250        260        270        280        290        300 
VGYCQGSAFI VGLLLMQMPE EEAFCVFVKL MQDYRLRELF KPSMAELGLC MYQFECMIQE 

       310        320        330        340        350        360 
HLPELFVHFQ SQSFHTSMYA SSWFLTIFLT TFPLPIATRI FDIFMSEGLE IVFRVGLALL 

       370        380        390        400        410        420 
QMNQAELMQL DMEGMLQHFQ KVIPHQFDGV PDKLIQAAYQ VKYNSKKMKK LEKEYTTIKT 

       430        440        450        460        470        480 
KEMEEQVEIK RLRTENRLLK QRIETLEKHK CSSNYNEDFV LQLEKELVQA RLSEAESQCA 

       490        500        510        520        530        540 
LKEMQDKVLD IEKRNNSLPD ENNIARLQEE LIAVKLREAE AIMGLKELRQ QVKDLEEHWQ 

       550        560        570        580        590        600 
RHLARTTGRW KDPPKKNAMN ELQDELMTIR LREAETQAEI REIKQRMMEM ETQNQINSNH 

       610        620        630        640        650        660 
LRRAEQEVIS LQEKVQYLSA QNKGLLTQLS EAKRKQAEIE CKNKEEVMAV RLREADSIAA 

       670        680        690        700        710        720 
VAELRQHIAE LEIQKEEGKL QGQLNKSDSN QYIGELKDQI AELNHELRCL KGQRGFSGQP 

       730        740        750        760        770        780 
PFDGIHIVNH LIGDDESFHS SDEDFIDNSL QETGVGFPLH GKSGSMSLDP AVADGSESET 

       790        800        810 
EDSVLETRES NQVVQKERPP RRRESYSTTV 

« Hide

References

« Hide 'large scale' references
[1]"NB4S, a member of the TBC1 domain family of genes, is truncated as a result of a constitutional t(1;10)(p22;q21) chromosome translocation in a patient with stage 4S neuroblastoma."
Roberts T., Chernova O., Cowell J.K.
Hum. Mol. Genet. 7:1169-1178(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DISEASE, CHROMOSOMAL TRANSLOCATION WITH TRNG10, VARIANTS VAL-82 AND VAL-336.
Tissue: Brain.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"EVI5 is a novel centrosomal protein that binds to alpha- and gamma-tubulin."
Faitar S.L., Dabbeekeh J.T.S., Ranalli T.A., Cowell J.K.
Genomics 86:594-605(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, OLIGOMERIZATION, SUBCELLULAR LOCATION, INTERACTION WITH ALPHA-TUBULIN AND GAMMA-TUBULIN.
[4]"The evi5 oncogene regulates cyclin accumulation by stabilizing the anaphase-promoting complex inhibitor emi1."
Eldridge A.G., Loktev A.V., Hansen D.V., Verschuren E.W., Reimann J.D.R., Jackson P.K.
Cell 124:367-380(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FBXO5, INDUCTION, UBIQUITINATION, SUBCELLULAR LOCATION, PHOSPHORYLATION BY PLK1.
[5]"EVI5 protein associates with the INCENP-aurora B kinase-survivin chromosomal passenger complex and is involved in the completion of cytokinesis."
Faitar S.L., Sossey-Alaoui K., Ranalli T.A., Cowell J.K.
Exp. Cell Res. 312:2325-2335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AURKB; BIRC5 AND INCENP, SUBCELLULAR LOCATION.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-776, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF008915 mRNA. Translation: AAC16031.1.
AL133332 expand/collapse EMBL AC list , AC104332, AC104456, AL354890 Genomic DNA. Translation: CAC19437.2.
AL354890 expand/collapse EMBL AC list , AC104332, AC104456, AL133332 Genomic DNA. Translation: CAI21914.1.
CCDSCCDS30774.1.
RefSeqNP_005656.4. NM_005665.4.
UniGeneHs.594434.

3D structure databases

ProteinModelPortalO60447.
SMRO60447. Positions 129-419.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113584. 6 interactions.
DIPDIP-38024N.
IntActO60447. 4 interactions.
STRING9606.ENSP00000359356.

PTM databases

PhosphoSiteO60447.

Proteomic databases

MaxQBO60447.
PaxDbO60447.
PRIDEO60447.

Protocols and materials databases

DNASU7813.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370331; ENSP00000359356; ENSG00000067208.
ENST00000540033; ENSP00000440826; ENSG00000067208.
GeneID7813.
KEGGhsa:7813.
UCSCuc001dox.3. human.

Organism-specific databases

CTD7813.
GeneCardsGC01M092974.
HGNCHGNC:3501. EVI5.
HPAHPA027339.
HPA053724.
MIM602942. gene.
neXtProtNX_O60447.
PharmGKBPA27915.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5210.
HOVERGENHBG081486.
InParanoidO60447.
OrthoDBEOG7PS1DT.
PhylomeDBO60447.
TreeFamTF317184.

Gene expression databases

ArrayExpressO60447.
BgeeO60447.
CleanExHS_EVI5.
GenevestigatorO60447.

Family and domain databases

InterProIPR000195. Rab-GTPase-TBC_dom.
[Graphical view]
PfamPF00566. RabGAP-TBC. 1 hit.
[Graphical view]
SMARTSM00164. TBC. 1 hit.
[Graphical view]
SUPFAMSSF47923. SSF47923. 2 hits.
PROSITEPS50086. TBC_RABGAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEVI5. human.
GeneWikiEVI5.
GenomeRNAi7813.
NextBio30213.
PROO60447.
SOURCESearch...

Entry information

Entry nameEVI5_HUMAN
AccessionPrimary (citable) accession number: O60447
Secondary accession number(s): A6NKX8, Q9H1Y9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: November 30, 2010
Last modified: July 9, 2014
This is version 103 of the entry and version 3 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM