EVI5_MOUSE
ID EVI5_MOUSE Reviewed; 809 AA.
AC P97366; Q3TPQ1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Ecotropic viral integration site 5 protein;
DE Short=EVI-5;
GN Name=Evi5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX PubMed=9070650; DOI=10.1038/sj.onc.1200929;
RA Liao X., Du Y., Morse H.C. III, Jenkins N.A., Copeland N.G.;
RT "Proviral integrations at the Evi5 locus disrupt a novel 90 kDa protein
RT with homology to the Tre2 oncogene and cell-cycle regulatory proteins.";
RL Oncogene 14:1023-1029(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 609-809.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-776 AND SER-778, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-776 AND SER-778, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Functions as a regulator of cell cycle progression by
CC stabilizing the FBXO5 protein and promoting cyclin-A accumulation
CC during interphase. May play a role in cytokinesis (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Dimeric and monomeric. Interacts with alpha- and gamma-
CC tubulin. Interacts with FBXO5. Interacts with the chromosome passenger
CC complex (CPC) which is at least composed of AURKB/aurora-B,
CC BIRC5/survivin, CDCA8/borealin and INCENP (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250}. Note=Associates with the mitotic
CC spindle through anaphase and remains within the midzone and midbody
CC until completion of cytokinesis. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9070650}.
CC -!- DEVELOPMENTAL STAGE: Detected in the embryo from 7 dpc to 17 dpc.
CC {ECO:0000269|PubMed:9070650}.
CC -!- PTM: Probably phosphorylated by PLK1; may be required for degradation
CC during mitosis. {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Degradation during prophase is ubiquitin-dependent
CC (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: This gene is a common site of retroviral integration in
CC T-cell lymphomas of AKXD mice.
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DR EMBL; U53586; AAB40607.1; -; mRNA.
DR EMBL; AK164208; BAE37684.1; -; mRNA.
DR CCDS; CCDS39198.1; -.
DR AlphaFoldDB; P97366; -.
DR SMR; P97366; -.
DR IntAct; P97366; 1.
DR STRING; 10090.ENSMUSP00000108261; -.
DR iPTMnet; P97366; -.
DR PhosphoSitePlus; P97366; -.
DR MaxQB; P97366; -.
DR PaxDb; P97366; -.
DR PRIDE; P97366; -.
DR ProteomicsDB; 271506; -.
DR MGI; MGI:104736; Evi5.
DR eggNOG; KOG4436; Eukaryota.
DR InParanoid; P97366; -.
DR PhylomeDB; P97366; -.
DR ChiTaRS; Evi5; mouse.
DR PRO; PR:P97366; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P97366; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
DR InterPro; IPR031214; Evi5.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR PANTHER; PTHR22957:SF254; PTHR22957:SF254; 2.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..809
FT /note="Ecotropic viral integration site 5 protein"
FT /id="PRO_0000256242"
FT DOMAIN 163..348
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..483
FT /note="Interaction with alpha-tubulin, gamma-tubulin, BIRC5
FT and FBXO5"
FT /evidence="ECO:0000250"
FT REGION 49..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..693
FT /note="Dimerization"
FT /evidence="ECO:0000250"
FT REGION 377..809
FT /note="Targeting to the centrosomes"
FT /evidence="ECO:0000250"
FT REGION 487..809
FT /note="Interaction with AURKB and INCENP"
FT /evidence="ECO:0000250"
FT REGION 758..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 406..717
FT /evidence="ECO:0000255"
FT COMPBIAS 49..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60447"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60447"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60447"
FT MOD_RES 776
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 672
FT /note="E -> K (in Ref. 1; AAB40607)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 809 AA; 92943 MW; 7AB17F9A403B1189 CRC64;
MVTTKMTAAF RNPNRRQVAT DKVAEKLSST LSWVKNTVSH TVSQMASQVA SPSASLHTTS
SSTTLSTPTQ SPSSPSKLSP DDLELLAKLE EQNRLIETDS KSLRSVNGSR RNSGSSLVSS
SSASSNLSHL EEDSWILWGR IVNEWDDVRK KKEKQVKELV RKGIPHHFRA IVWQLLCNAQ
SMTIKDQYSE LLKMTSPCEK LIRRDIARTY PEHNFFKEKD SLGQEVLFNV MKAYSLVDRE
LVTVRAVLSS LDCCCMQMPE EEAFCVFVKL MQDYRLRELF KPSMAELGLC MYQFECMIQE
YLPELFVHFQ SQSFHTSMYA SSWFLTIFLT TFPLPIATRI FDIFMSEGLE IVFRVGLALL
QMNQAELMQL DMEGMLQHFQ KVIPHQFDGG PEKLIQSAYQ VKYNSKKMKK LEKEYTTIKT
KEMEEQGEIK RLRTENRLLK QRIETLEKHK CSSTYNEDFV LQLEKELVQA RLSEAESQCA
LKEMQDKVLD IEKKNNSFPD ENNIARLQEE LIAVKLREAE AIMGLKELRQ QVRTLEEHWQ
RHLARTSGRW KDPPKKNAVN ELQDELMSIR LREAETQAEI REMKQRMMEM ETQNQINSNQ
LRRAEQEVNS LQEKVCSLSV KNKGLLAQLS EAKRRQAEIE CKNKEEVMAV RLREADSIAA
VAELQQHIAE LEIQKEEGKL QGQLNRSDSN QYIRELKDQI AELTHELRCL KGQRDFSSRP
PFDGIHIVSH LIGDDELFHS SDEDFIDSSL QESAIGFPLH RKSGPMSLNP ALADGSESEA
EDGMLGPQES DPEAPQKQPP QRESYSTTV
