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   27-MAR-2024, entry version 163.
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.
DR   AlphaFoldDB; Q96CN4; -.
DR   SMR; Q96CN4; -.
DR   BioGRID; 125449; 65.
DR   IntAct; Q96CN4; 37.
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; 9606-ENSP00000445905; -.
DR   PeptideAtlas; Q96CN4; -.
DR   ProteomicsDB; 76196; -. [Q96CN4-1]
DR   ProteomicsDB; 76197; -. [Q96CN4-2]
DR   Pumba; Q96CN4; -.
DR   Antibodypedia; 24676; 96 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   AGR; HGNC:30464; -.
DR   CTD; 115704; -.
DR   DisGeNET; 115704; -.
DR   GeneCards; EVI5L; -.
DR   HGNC; HGNC:30464; EVI5L.
DR   HPA; ENSG00000142459; Tissue enhanced (brain).
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; SECWTEV; -.
DR   OrthoDB; 2908929at2759; -.
DR   PhylomeDB; Q96CN4; -.
DR   TreeFam; TF317184; -.
DR   PathwayCommons; Q96CN4; -.
DR   SignaLink; Q96CN4; -.
DR   BioGRID-ORCS; 115704; 9 hits in 1153 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 164 other cell types or tissues.
DR   ExpressionAtlas; Q96CN4; baseline and differential.
DR   GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
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   Gene3D; 1.10.8.270; putative rabgap domain of human tbc1 domain family member 14 like domains; 1.
DR   Gene3D; 1.10.10.750; Ypt/Rab-GAP domain of gyp1p, domain 1; 1.
DR   Gene3D; 1.10.472.80; Ypt/Rab-GAP domain of gyp1p, domain 3; 1.
DR   InterPro; IPR000195; Rab-GAP-TBC_dom.
DR   InterPro; IPR035969; Rab-GAP_TBC_sf.
DR   PANTHER; PTHR47219:SF17; EVI5-LIKE PROTEIN ISOFORM X1; 1.
DR   PANTHER; PTHR47219; RAB GTPASE-ACTIVATING PROTEIN 1-LIKE; 1.
DR   Pfam; PF00566; RabGAP-TBC; 1.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; Ypt/Rab-GAP domain of gyp1p; 2.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
DR   Genevisible; Q96CN4; HS.
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
//