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O60447

- EVI5_HUMAN

UniProt

O60447 - EVI5_HUMAN

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Protein

Ecotropic viral integration site 5 protein homolog

Gene
EVI5, NB4S
Organism
Homo sapiens (Human)
Status
Reviewed - 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. protein binding Source: IntAct
  2. Rab GTPase activator activity Source: InterPro

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
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.3 Publications

GO - Cellular componenti

  1. Golgi apparatus Source: HPA
  2. intracellular membrane-bounded organelle Source: HPA
  3. microtubule organizing center Source: UniProtKB-SubCell
  4. nucleus Source: UniProtKB-SubCell
  5. 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.1 Publication

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 – 7781Phosphoserine By similarity

Post-translational modificationi

Probably phosphorylated by PLK1; may be required for degradation during mitosis.1 Publication
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

ArrayExpressiO60447.
BgeeiO60447.
CleanExiHS_EVI5.
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. 6 interactions.
DIPiDIP-38024N.
IntActiO60447. 4 interactions.
STRINGi9606.ENSP00000359356.

Structurei

3D structure databases

ProteinModelPortaliO60447.
SMRiO60447. Positions 129-419.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini163 – 348186Rab-GAP TBCAdd
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 – 716311 Reviewed predictionAdd
BLAST

Compositional bias

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

Sequence similaritiesi

Contains 1 Rab-GAP TBC domain.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5210.
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]

Sequencei

Sequence statusi: Complete.

O60447-1 [UniParc]FASTAAdd to Basket

« Hide

MVTNKMTAAF RNPSGKQVAT DKVAEKLSST LSWVKNTVSH TVSQMASQVA    50
SPSTSLHTTS SSTTLSTPAL SPSSPSQLSP DDLELLAKLE EQNRLLETDS 100
KSLRSVNGSR RNSGSSLVSS SSASSNLSHL EEDSWILWGR IVNEWEDVRK 150
KKEKQVKELV HKGIPHHFRA IVWQLLCSAQ SMPIKDQYSE LLKMTSPCEK 200
LIRRDIARTY PEHNFFKEKD SLGQEVLFNV MKAYSLVDRE VGYCQGSAFI 250
VGLLLMQMPE EEAFCVFVKL MQDYRLRELF KPSMAELGLC MYQFECMIQE 300
HLPELFVHFQ SQSFHTSMYA SSWFLTIFLT TFPLPIATRI FDIFMSEGLE 350
IVFRVGLALL QMNQAELMQL DMEGMLQHFQ KVIPHQFDGV PDKLIQAAYQ 400
VKYNSKKMKK LEKEYTTIKT KEMEEQVEIK RLRTENRLLK QRIETLEKHK 450
CSSNYNEDFV LQLEKELVQA RLSEAESQCA LKEMQDKVLD IEKRNNSLPD 500
ENNIARLQEE LIAVKLREAE AIMGLKELRQ QVKDLEEHWQ RHLARTTGRW 550
KDPPKKNAMN ELQDELMTIR LREAETQAEI REIKQRMMEM ETQNQINSNH 600
LRRAEQEVIS LQEKVQYLSA QNKGLLTQLS EAKRKQAEIE CKNKEEVMAV 650
RLREADSIAA VAELRQHIAE LEIQKEEGKL QGQLNKSDSN QYIGELKDQI 700
AELNHELRCL KGQRGFSGQP PFDGIHIVNH LIGDDESFHS SDEDFIDNSL 750
QETGVGFPLH GKSGSMSLDP AVADGSESET EDSVLETRES NQVVQKERPP 800
RRRESYSTTV 810
Length:810
Mass (Da):92,949
Last modified:November 30, 2010 - v3
Checksum:i4A2CC99A9192F632
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti82 – 821D → V.1 Publication
Corresponds to variant rs1064580 [ dbSNP | Ensembl ].
VAR_047753
Natural varianti336 – 3361I → V.1 Publication
Corresponds to variant rs2391199 [ dbSNP | Ensembl ].
VAR_028890
Natural varianti612 – 6121Q → H.
Corresponds to variant rs11808092 [ dbSNP | Ensembl ].
VAR_028891

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941R → I in AAC16031. 1 Publication
Sequence conflicti402 – 4021K → Q in AAC16031. 1 Publication
Sequence conflicti714 – 7141R → K in AAC16031. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF008915 mRNA. Translation: AAC16031.1.
AL133332
, AC104332, AC104456, AL354890 Genomic DNA. Translation: CAC19437.2.
AL354890
, AC104332, AC104456, AL133332 Genomic DNA. Translation: CAI21914.1.
CCDSiCCDS30774.1.
RefSeqiNP_005656.4. NM_005665.4.
UniGeneiHs.594434.

Genome annotation databases

EnsembliENST00000370331; ENSP00000359356; ENSG00000067208.
ENST00000540033; ENSP00000440826; ENSG00000067208.
GeneIDi7813.
KEGGihsa:7813.
UCSCiuc001dox.3. human.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF008915 mRNA. Translation: AAC16031.1 .
AL133332
, AC104332 , AC104456 , AL354890 Genomic DNA. Translation: CAC19437.2 .
AL354890
, AC104332 , AC104456 , AL133332 Genomic DNA. Translation: CAI21914.1 .
CCDSi CCDS30774.1.
RefSeqi NP_005656.4. NM_005665.4.
UniGenei Hs.594434.

3D structure databases

ProteinModelPortali O60447.
SMRi O60447. Positions 129-419.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113584. 6 interactions.
DIPi DIP-38024N.
IntActi O60447. 4 interactions.
STRINGi 9606.ENSP00000359356.

PTM databases

PhosphoSitei O60447.

Proteomic databases

MaxQBi O60447.
PaxDbi O60447.
PRIDEi O60447.

Protocols and materials databases

DNASUi 7813.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000370331 ; ENSP00000359356 ; ENSG00000067208 .
ENST00000540033 ; ENSP00000440826 ; ENSG00000067208 .
GeneIDi 7813.
KEGGi hsa:7813.
UCSCi uc001dox.3. human.

Organism-specific databases

CTDi 7813.
GeneCardsi GC01M092974.
HGNCi HGNC:3501. EVI5.
HPAi HPA027339.
HPA053724.
MIMi 602942. gene.
neXtProti NX_O60447.
PharmGKBi PA27915.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5210.
HOVERGENi HBG081486.
InParanoidi O60447.
OrthoDBi EOG7PS1DT.
PhylomeDBi O60447.
TreeFami TF317184.

Miscellaneous databases

ChiTaRSi EVI5. human.
GeneWikii EVI5.
GenomeRNAii 7813.
NextBioi 30213.
PROi O60447.
SOURCEi Search...

Gene expression databases

ArrayExpressi O60447.
Bgeei O60447.
CleanExi HS_EVI5.
Genevestigatori O60447.

Family and domain databases

InterProi IPR000195. Rab-GTPase-TBC_dom.
[Graphical view ]
Pfami PF00566. RabGAP-TBC. 1 hit.
[Graphical view ]
SMARTi SM00164. TBC. 1 hit.
[Graphical view ]
SUPFAMi SSF47923. SSF47923. 2 hits.
PROSITEi PS50086. TBC_RABGAP. 1 hit.
[Graphical view ]
ProtoNeti Search...

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], 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.
    , 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. 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].

Entry informationi

Entry nameiEVI5_HUMAN
AccessioniPrimary (citable) accession number: O60447
Secondary accession number(s): A6NKX8, Q9H1Y9
Entry historyi
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 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

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