Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ecotropic viral integration site 5 protein

Gene

Evi5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Names & Taxonomyi

Protein namesi
Recommended name:
Ecotropic viral integration site 5 protein
Short name:
EVI-5
Gene namesi
Name:Evi5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:104736. Evi5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 809809Ecotropic viral integration site 5 proteinPRO_0000256242Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei113 – 1131PhosphoserineCombined sources
Modified residuei497 – 4971PhosphoserineBy similarity
Modified residuei776 – 7761PhosphoserineCombined sources
Modified residuei778 – 7781PhosphoserineCombined sources

Post-translational modificationi

Probably phosphorylated by PLK1; may be required for degradation during mitosis.By similarity
Ubiquitinated. Degradation during prophase is ubiquitin-dependent (By similarity).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP97366.
MaxQBiP97366.
PaxDbiP97366.
PRIDEiP97366.

PTM databases

iPTMnetiP97366.
PhosphoSiteiP97366.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Developmental stagei

Detected in the embryo from E7 to E17.1 Publication

Gene expression databases

CleanExiMM_EVI5.

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 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiP97366. 1 interaction.
MINTiMINT-1751311.
STRINGi10090.ENSMUSP00000108261.

Structurei

3D structure databases

ProteinModelPortaliP97366.
SMRiP97366. Positions 156-419.
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 FBXO5By similarityAdd
BLAST
Regioni128 – 693566DimerizationBy similarityAdd
BLAST
Regioni377 – 809433Targeting to the centrosomesBy similarityAdd
BLAST
Regioni487 – 809323Interaction with AURKB and INCENPBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili406 – 717312Sequence 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

eggNOGiKOG4436. Eukaryota.
ENOG410YWJY. LUCA.
HOGENOMiHOG000044859.
HOVERGENiHBG081486.
InParanoidiP97366.
PhylomeDBiP97366.

Family and domain databases

InterProiIPR031214. Evi5.
IPR000195. Rab-GTPase-TBC_dom.
[Graphical view]
PANTHERiPTHR22957:SF197. PTHR22957:SF197. 1 hit.
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.

P97366-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTTKMTAAF RNPNRRQVAT DKVAEKLSST LSWVKNTVSH TVSQMASQVA
60 70 80 90 100
SPSASLHTTS SSTTLSTPTQ SPSSPSKLSP DDLELLAKLE EQNRLIETDS
110 120 130 140 150
KSLRSVNGSR RNSGSSLVSS SSASSNLSHL EEDSWILWGR IVNEWDDVRK
160 170 180 190 200
KKEKQVKELV RKGIPHHFRA IVWQLLCNAQ SMTIKDQYSE LLKMTSPCEK
210 220 230 240 250
LIRRDIARTY PEHNFFKEKD SLGQEVLFNV MKAYSLVDRE LVTVRAVLSS
260 270 280 290 300
LDCCCMQMPE EEAFCVFVKL MQDYRLRELF KPSMAELGLC MYQFECMIQE
310 320 330 340 350
YLPELFVHFQ SQSFHTSMYA SSWFLTIFLT TFPLPIATRI FDIFMSEGLE
360 370 380 390 400
IVFRVGLALL QMNQAELMQL DMEGMLQHFQ KVIPHQFDGG PEKLIQSAYQ
410 420 430 440 450
VKYNSKKMKK LEKEYTTIKT KEMEEQGEIK RLRTENRLLK QRIETLEKHK
460 470 480 490 500
CSSTYNEDFV LQLEKELVQA RLSEAESQCA LKEMQDKVLD IEKKNNSFPD
510 520 530 540 550
ENNIARLQEE LIAVKLREAE AIMGLKELRQ QVRTLEEHWQ RHLARTSGRW
560 570 580 590 600
KDPPKKNAVN ELQDELMSIR LREAETQAEI REMKQRMMEM ETQNQINSNQ
610 620 630 640 650
LRRAEQEVNS LQEKVCSLSV KNKGLLAQLS EAKRRQAEIE CKNKEEVMAV
660 670 680 690 700
RLREADSIAA VAELQQHIAE LEIQKEEGKL QGQLNRSDSN QYIRELKDQI
710 720 730 740 750
AELTHELRCL KGQRDFSSRP PFDGIHIVSH LIGDDELFHS SDEDFIDSSL
760 770 780 790 800
QESAIGFPLH RKSGPMSLNP ALADGSESEA EDGMLGPQES DPEAPQKQPP

QRESYSTTV
Length:809
Mass (Da):92,943
Last modified:October 31, 2006 - v2
Checksum:i7AB17F9A403B1189
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti672 – 6721E → K in AAB40607 (PubMed:9070650).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53586 mRNA. Translation: AAB40607.1.
AK164208 mRNA. Translation: BAE37684.1.
CCDSiCCDS39198.1.
UniGeneiMm.35796.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53586 mRNA. Translation: AAB40607.1.
AK164208 mRNA. Translation: BAE37684.1.
CCDSiCCDS39198.1.
UniGeneiMm.35796.

3D structure databases

ProteinModelPortaliP97366.
SMRiP97366. Positions 156-419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP97366. 1 interaction.
MINTiMINT-1751311.
STRINGi10090.ENSMUSP00000108261.

PTM databases

iPTMnetiP97366.
PhosphoSiteiP97366.

Proteomic databases

EPDiP97366.
MaxQBiP97366.
PaxDbiP97366.
PRIDEiP97366.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:104736. Evi5.

Phylogenomic databases

eggNOGiKOG4436. Eukaryota.
ENOG410YWJY. LUCA.
HOGENOMiHOG000044859.
HOVERGENiHBG081486.
InParanoidiP97366.
PhylomeDBiP97366.

Miscellaneous databases

PROiP97366.
SOURCEiSearch...

Gene expression databases

CleanExiMM_EVI5.

Family and domain databases

InterProiIPR031214. Evi5.
IPR000195. Rab-GTPase-TBC_dom.
[Graphical view]
PANTHERiPTHR22957:SF197. PTHR22957:SF197. 1 hit.
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. "Proviral integrations at the Evi5 locus disrupt a novel 90 kDa protein with homology to the Tre2 oncogene and cell-cycle regulatory proteins."
    Liao X., Du Y., Morse H.C. III, Jenkins N.A., Copeland N.G.
    Oncogene 14:1023-1029(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: C57BL/6 X CBA.
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 609-809.
    Strain: C57BL/6J.
    Tissue: Embryo.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-776 AND SER-778, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-776 AND SER-778, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiEVI5_MOUSE
AccessioniPrimary (citable) accession number: P97366
Secondary accession number(s): Q3TPQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: March 16, 2016
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This gene is a common site of retroviral integration in T-cell lymphomas of AKXD mice.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.