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Protein

Ecotropic viral integration site 5 protein homolog

Gene

EVI5

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

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei594 – 5941Breakpoint for translocation to form EVI5-TRNG10 fusion protein

GO - Molecular functioni

  1. Rab GTPase activator activity Source: UniProtKB
  2. Rab GTPase binding Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. cell proliferation Source: ProtInc
  4. multicellular organismal development Source: ProtInc
  5. positive regulation of GTP catabolic process Source: UniProtKB
  6. positive regulation of Rab GTPase activity Source: GOC
  7. retrograde transport, endosome to Golgi Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Names & Taxonomyi

Protein namesi
Recommended name:
Ecotropic viral integration site 5 protein homolog
Short name:
EVI-5
Alternative name(s):
Neuroblastoma stage 4S gene protein
Gene namesi
Name:EVI5
Synonyms:NB4S
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3501. EVI5.

Subcellular locationi

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

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. Golgi apparatus Source: HPA
  3. intracellular membrane-bounded organelle Source: HPA
  4. microtubule organizing center Source: UniProtKB-SubCell
  5. nucleus Source: UniProtKB-SubCell
  6. spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Organism-specific databases

PharmGKBiPA27915.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 810810Ecotropic viral integration site 5 protein homologPRO_0000256241Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei776 – 7761Phosphoserine1 Publication
Modified residuei778 – 7781PhosphoserineBy similarity

Post-translational modificationi

Probably phosphorylated by PLK1; may be required for degradation during mitosis.2 Publications
Ubiquitinated. Degradation during prophase is ubiquitin-dependent.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO60447.
PaxDbiO60447.
PRIDEiO60447.

PTM databases

PhosphoSiteiO60447.

Expressioni

Tissue specificityi

Expressed in various cell lines (at protein level). Expressed in a wide range of tissues including brain and adrenal.2 Publications

Inductioni

Down-regulated during mitosis through proteasomal degradation.1 Publication

Gene expression databases

BgeeiO60447.
CleanExiHS_EVI5.
ExpressionAtlasiO60447. baseline and differential.
GenevestigatoriO60447.

Organism-specific databases

HPAiHPA027339.
HPA053724.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FBXO5Q9UKT46EBI-852291,EBI-852298
PLK1P533502EBI-852291,EBI-476768

Protein-protein interaction databases

BioGridi113584. 5 interactions.
DIPiDIP-38024N.
IntActiO60447. 4 interactions.
STRINGi9606.ENSP00000359356.

Structurei

3D structure databases

ProteinModelPortaliO60447.
SMRiO60447. Positions 129-419.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini163 – 348186Rab-GAP TBCPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 483483Interaction with alpha-tubulin, gamma-tubulin, BIRC5 and FBXO5Add
BLAST
Regioni128 – 693566DimerizationAdd
BLAST
Regioni377 – 810434Targeting to the centrosomesAdd
BLAST
Regioni487 – 810324Interaction with AURKB and INCENPAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili406 – 716311Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi28 – 128101Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 Rab-GAP TBC domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5210.
GeneTreeiENSGT00750000117238.
HOVERGENiHBG081486.
InParanoidiO60447.
OrthoDBiEOG7PS1DT.
PhylomeDBiO60447.
TreeFamiTF317184.

Family and domain databases

InterProiIPR000195. Rab-GTPase-TBC_dom.
[Graphical view]
PfamiPF00566. RabGAP-TBC. 1 hit.
[Graphical view]
SMARTiSM00164. TBC. 1 hit.
[Graphical view]
SUPFAMiSSF47923. SSF47923. 2 hits.
PROSITEiPS50086. TBC_RABGAP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O60447-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MVTNKMTAAF RNPSGKQVAT DKVAEKLSST LSWVKNTVSH TVSQMASQVA
60 70 80 90 100
SPSTSLHTTS SSTTLSTPAL SPSSPSQLSP DDLELLAKLE EQNRLLETDS
110 120 130 140 150
KSLRSVNGSR RNSGSSLVSS SSASSNLSHL EEDSWILWGR IVNEWEDVRK
160 170 180 190 200
KKEKQVKELV HKGIPHHFRA IVWQLLCSAQ SMPIKDQYSE LLKMTSPCEK
210 220 230 240 250
LIRRDIARTY PEHNFFKEKD SLGQEVLFNV MKAYSLVDRE VGYCQGSAFI
260 270 280 290 300
VGLLLMQMPE EEAFCVFVKL MQDYRLRELF KPSMAELGLC MYQFECMIQE
310 320 330 340 350
HLPELFVHFQ SQSFHTSMYA SSWFLTIFLT TFPLPIATRI FDIFMSEGLE
360 370 380 390 400
IVFRVGLALL QMNQAELMQL DMEGMLQHFQ KVIPHQFDGV PDKLIQAAYQ
410 420 430 440 450
VKYNSKKMKK LEKEYTTIKT KEMEEQVEIK RLRTENRLLK QRIETLEKHK
460 470 480 490 500
CSSNYNEDFV LQLEKELVQA RLSEAESQCA LKEMQDKVLD IEKRNNSLPD
510 520 530 540 550
ENNIARLQEE LIAVKLREAE AIMGLKELRQ QVKDLEEHWQ RHLARTTGRW
560 570 580 590 600
KDPPKKNAMN ELQDELMTIR LREAETQAEI REIKQRMMEM ETQNQINSNH
610 620 630 640 650
LRRAEQEVIS LQEKVQYLSA QNKGLLTQLS EAKRKQAEIE CKNKEEVMAV
660 670 680 690 700
RLREADSIAA VAELRQHIAE LEIQKEEGKL QGQLNKSDSN QYIGELKDQI
710 720 730 740 750
AELNHELRCL KGQRGFSGQP PFDGIHIVNH LIGDDESFHS SDEDFIDNSL
760 770 780 790 800
QETGVGFPLH GKSGSMSLDP AVADGSESET EDSVLETRES NQVVQKERPP
810
RRRESYSTTV
Length:810
Mass (Da):92,949
Last modified:November 30, 2010 - v3
Checksum:i4A2CC99A9192F632
GO
Isoform 2 (identifier: O60447-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     448-448: K → KESASLADRLIQ

Show »
Length:821
Mass (Da):94,133
Checksum:iFD0845FB2A2A74AB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941R → I in AAC16031. (PubMed:9618176)Curated
Sequence conflicti94 – 941R → I in BAH16618. (PubMed:19077034)Curated
Sequence conflicti402 – 4021K → Q in AAC16031. (PubMed:9618176)Curated
Sequence conflicti714 – 7141R → K in AAC16031. (PubMed:9618176)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti82 – 821D → V.2 Publications
Corresponds to variant rs1064580 [ dbSNP | Ensembl ].
VAR_047753
Natural varianti336 – 3361I → V.2 Publications
Corresponds to variant rs2391199 [ dbSNP | Ensembl ].
VAR_028890
Natural varianti612 – 6121Q → H.
Corresponds to variant rs11808092 [ dbSNP | Ensembl ].
VAR_028891

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei448 – 4481K → KESASLADRLIQ in isoform 2. 1 PublicationVSP_056828

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008915 mRNA. Translation: AAC16031.1.
AB449875 mRNA. Translation: BAH16618.1.
AL133332
, AC104332, AC104456, AL354890 Genomic DNA. Translation: CAC19437.2.
AL354890
, AC104332, AC104456, AL133332 Genomic DNA. Translation: CAI21914.1.
CCDSiCCDS30774.1. [O60447-1]
RefSeqiNP_005656.4. NM_005665.4. [O60447-1]
UniGeneiHs.594434.

Genome annotation databases

EnsembliENST00000370331; ENSP00000359356; ENSG00000067208. [O60447-1]
ENST00000540033; ENSP00000440826; ENSG00000067208. [O60447-2]
GeneIDi7813.
KEGGihsa:7813.
UCSCiuc001dox.3. human. [O60447-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008915 mRNA. Translation: AAC16031.1.
AB449875 mRNA. Translation: BAH16618.1.
AL133332
, AC104332, AC104456, AL354890 Genomic DNA. Translation: CAC19437.2.
AL354890
, AC104332, AC104456, AL133332 Genomic DNA. Translation: CAI21914.1.
CCDSiCCDS30774.1. [O60447-1]
RefSeqiNP_005656.4. NM_005665.4. [O60447-1]
UniGeneiHs.594434.

3D structure databases

ProteinModelPortaliO60447.
SMRiO60447. Positions 129-419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113584. 5 interactions.
DIPiDIP-38024N.
IntActiO60447. 4 interactions.
STRINGi9606.ENSP00000359356.

PTM databases

PhosphoSiteiO60447.

Proteomic databases

MaxQBiO60447.
PaxDbiO60447.
PRIDEiO60447.

Protocols and materials databases

DNASUi7813.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370331; ENSP00000359356; ENSG00000067208. [O60447-1]
ENST00000540033; ENSP00000440826; ENSG00000067208. [O60447-2]
GeneIDi7813.
KEGGihsa:7813.
UCSCiuc001dox.3. human. [O60447-1]

Organism-specific databases

CTDi7813.
GeneCardsiGC01M092974.
HGNCiHGNC:3501. EVI5.
HPAiHPA027339.
HPA053724.
MIMi602942. gene.
neXtProtiNX_O60447.
PharmGKBiPA27915.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5210.
GeneTreeiENSGT00750000117238.
HOVERGENiHBG081486.
InParanoidiO60447.
OrthoDBiEOG7PS1DT.
PhylomeDBiO60447.
TreeFamiTF317184.

Miscellaneous databases

ChiTaRSiEVI5. human.
GeneWikiiEVI5.
GenomeRNAii7813.
NextBioi30213.
PROiO60447.
SOURCEiSearch...

Gene expression databases

BgeeiO60447.
CleanExiHS_EVI5.
ExpressionAtlasiO60447. baseline and differential.
GenevestigatoriO60447.

Family and domain databases

InterProiIPR000195. Rab-GTPase-TBC_dom.
[Graphical view]
PfamiPF00566. RabGAP-TBC. 1 hit.
[Graphical view]
SMARTiSM00164. TBC. 1 hit.
[Graphical view]
SUPFAMiSSF47923. SSF47923. 2 hits.
PROSITEiPS50086. TBC_RABGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1), TISSUE SPECIFICITY, DISEASE, CHROMOSOMAL TRANSLOCATION WITH TRNG10, VARIANTS VAL-82 AND VAL-336.
    Tissue: Brain.
  2. "Identification and characterization of a novel Tre-2/Bub2/Cdc16 (TBC) protein that possesses Rab3A-GAP activity."
    Ishibashi K., Kanno E., Itoh T., Fukuda M.
    Genes Cells 14:41-52(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS VAL-82 AND VAL-336.
  3. "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.
    , 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].
  4. "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.
  5. "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.
  6. "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.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-776, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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].

Entry informationi

Entry nameiEVI5_HUMAN
AccessioniPrimary (citable) accession number: O60447
Secondary accession number(s): A6NKX8, B9A6J0, Q9H1Y9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: November 30, 2010
Last modified: February 4, 2015
This is version 108 of the entry and version 3 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

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.