EVI5L_HUMAN
ID EVI5L_HUMAN Reviewed; 794 AA.
AC Q96CN4; B9A6I9;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=EVI5-like protein;
DE AltName: Full=Ecotropic viral integration site 5-like protein;
GN Name=EVI5L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=19077034; DOI=10.1111/j.1365-2443.2008.01251.x;
RA Ishibashi K., Kanno E., Itoh T., Fukuda M.;
RT "Identification and characterization of a novel Tre-2/Bub2/Cdc16 (TBC)
RT protein that possesses Rab3A-GAP activity.";
RL Genes Cells 14:41-52(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND INTERACTION WITH RAB10.
RX PubMed=16923123; DOI=10.1111/j.1365-2443.2006.00997.x;
RA Itoh T., Satoh M., Kanno E., Fukuda M.;
RT "Screening for target Rabs of TBC (Tre-2/Bub2/Cdc16) domain-containing
RT proteins based on their Rab-binding activity.";
RL Genes Cells 11:1023-1037(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-685, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Functions as a GTPase-activating protein (GAP) with a broad
CC specificity. {ECO:0000269|PubMed:16923123}.
CC -!- SUBUNIT: May interact with RAB10.
CC -!- INTERACTION:
CC Q96CN4; A1A5B0: ANKRD36; NbExp=3; IntAct=EBI-749523, EBI-14100900;
CC Q96CN4; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-749523, EBI-541426;
CC Q96CN4; Q8N715: CCDC185; NbExp=3; IntAct=EBI-749523, EBI-740814;
CC Q96CN4; O95995: GAS8; NbExp=3; IntAct=EBI-749523, EBI-1052570;
CC Q96CN4; Q5XKE5: KRT79; NbExp=3; IntAct=EBI-749523, EBI-2514135;
CC Q96CN4; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-749523, EBI-739832;
CC Q96CN4; Q6ZVK8: NUDT18; NbExp=3; IntAct=EBI-749523, EBI-740486;
CC Q96CN4; Q99633: PRPF18; NbExp=3; IntAct=EBI-749523, EBI-2798416;
CC Q96CN4; Q9Y580: RBM7; NbExp=3; IntAct=EBI-749523, EBI-746903;
CC Q96CN4; Q8IYX1: TBC1D21; NbExp=3; IntAct=EBI-749523, EBI-12018146;
CC Q96CN4; Q5T619: ZNF648; NbExp=3; IntAct=EBI-749523, EBI-11985915;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96CN4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96CN4-2; Sequence=VSP_043456;
CC -!- DOMAIN: The arginine and glutamine fingers are critical for the GTPase-
CC activating mechanism, they pull out Rab's 'switch 2' glutamine and
CC insert in Rab's active site. {ECO:0000250}.
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DR EMBL; AB449874; BAH16617.1; -; mRNA.
DR EMBL; AC008812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014111; AAH14111.1; -; mRNA.
DR CCDS; CCDS12188.1; -. [Q96CN4-1]
DR CCDS; CCDS54209.1; -. [Q96CN4-2]
DR RefSeq; NP_001153416.1; NM_001159944.2. [Q96CN4-2]
DR RefSeq; NP_660288.1; NM_145245.4. [Q96CN4-1]
DR RefSeq; XP_005272515.1; XM_005272458.4.
DR RefSeq; XP_016881728.1; XM_017026239.1. [Q96CN4-2]
DR AlphaFoldDB; Q96CN4; -.
DR SMR; Q96CN4; -.
DR BioGRID; 125449; 63.
DR IntAct; Q96CN4; 35.
DR STRING; 9606.ENSP00000445905; -.
DR iPTMnet; Q96CN4; -.
DR PhosphoSitePlus; Q96CN4; -.
DR BioMuta; EVI5L; -.
DR DMDM; 74731362; -.
DR EPD; Q96CN4; -.
DR jPOST; Q96CN4; -.
DR MassIVE; Q96CN4; -.
DR MaxQB; Q96CN4; -.
DR PaxDb; Q96CN4; -.
DR PeptideAtlas; Q96CN4; -.
DR PRIDE; Q96CN4; -.
DR ProteomicsDB; 76196; -. [Q96CN4-1]
DR ProteomicsDB; 76197; -. [Q96CN4-2]
DR Antibodypedia; 24676; 84 antibodies from 14 providers.
DR DNASU; 115704; -.
DR Ensembl; ENST00000270530.8; ENSP00000270530.3; ENSG00000142459.9. [Q96CN4-1]
DR Ensembl; ENST00000538904.7; ENSP00000445905.1; ENSG00000142459.9. [Q96CN4-2]
DR GeneID; 115704; -.
DR KEGG; hsa:115704; -.
DR MANE-Select; ENST00000538904.7; ENSP00000445905.1; NM_001159944.3; NP_001153416.1. [Q96CN4-2]
DR UCSC; uc002min.4; human. [Q96CN4-1]
DR CTD; 115704; -.
DR DisGeNET; 115704; -.
DR GeneCards; EVI5L; -.
DR HGNC; HGNC:30464; EVI5L.
DR HPA; ENSG00000142459; Low tissue specificity.
DR neXtProt; NX_Q96CN4; -.
DR OpenTargets; ENSG00000142459; -.
DR PharmGKB; PA134905968; -.
DR VEuPathDB; HostDB:ENSG00000142459; -.
DR eggNOG; KOG4436; Eukaryota.
DR GeneTree; ENSGT00940000153846; -.
DR HOGENOM; CLU_005350_6_0_1; -.
DR InParanoid; Q96CN4; -.
DR OMA; GHIVADW; -.
DR OrthoDB; 191811at2759; -.
DR PhylomeDB; Q96CN4; -.
DR TreeFam; TF317184; -.
DR PathwayCommons; Q96CN4; -.
DR SignaLink; Q96CN4; -.
DR BioGRID-ORCS; 115704; 9 hits in 1077 CRISPR screens.
DR ChiTaRS; EVI5L; human.
DR GenomeRNAi; 115704; -.
DR Pharos; Q96CN4; Tbio.
DR PRO; PR:Q96CN4; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96CN4; protein.
DR Bgee; ENSG00000142459; Expressed in prefrontal cortex and 163 other tissues.
DR ExpressionAtlas; Q96CN4; baseline and differential.
DR Genevisible; Q96CN4; HS.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:1902018; P:negative regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
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 Alternative splicing; Coiled coil; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..794
FT /note="EVI5-like protein"
FT /id="PRO_0000263097"
FT DOMAIN 115..300
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 358..449
FT /evidence="ECO:0000255"
FT COILED 569..709
FT /evidence="ECO:0000255"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 156
FT /note="Arginine finger"
FT /evidence="ECO:0000250"
FT SITE 197
FT /note="Glutamine finger"
FT /evidence="ECO:0000250"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 400
FT /note="K -> KESAALADRLIQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19077034"
FT /id="VSP_043456"
SQ SEQUENCE 794 AA; 91376 MW; 598B06DD2F098664 CRC64;
MASPTLSPDS SSQEALSAPT CSPTSDSENL SPDELELLAK LEEQNRLLEA DSKSMRSMNG
SRRNSGSSLV SSSSASSNLS HLEEDTWILW GRIANEWEEW RRRKEKLLKE LIRKGIPHHF
RAIVWQLLCS ATDMPVKNQY SELLKMSSPC EKLIRRDIAR TYPEHEFFKG QDSLGQEVLF
NVMKAYSLVD REVGYCQGSA FIVGLLLMQM PEEEAFCVFV RLMQEYRLRE LFKPSMAELG
LCIYQFEYML QEQLPDLNTH FRSQSFHTSM YASSWFLTLF LTTFPLPVAT RVFDIFMYEG
LEIVFRVGLA LLQVNQAELM QLDMEGMSQY FQRVIPHQFD SCPDKLVLKA YQVKYNPKKM
KRLEKEYAAM KSKEMEEQIE IKRLRTENRL LKQRIETLEK GQVTRAQEAE ENYVIKRELA
VVRQQCSSAA EDLQKAQSTI RQLQEQQENP RLTEDFVSHL ETELEQSRLR ETETLGALRE
MQDKVLDMEK RNSSLPDENN VAQLQEELKA LKVREGQAVA STRELKLQLQ ELSDTWQAHL
ARGGRWKESP RKLVVGELQD ELMSVRLREA QALAEGRELR QRVVELETQD HIHRNLLNRV
EAERAALQEK LQYLAAQNKG LQTQLSESRR KQAEAECKSK EEVMAVRLRE ADSMAAVAEM
RQRIAELEIQ REEGRIQGQL NHSDSSQYIR ELKDQIEELK AEVRLLKGPP PFEDPLAFDG
LSLARHLDED SLPSSDEELL GVGVGAALQD ALYPLSPRDA RFFRRLERPA KDSEGSSDSD
ADELAAPYSQ GLDN
