GenomeNet

Database: UniProt
Entry: E7EUN2_HUMAN
LinkDB: E7EUN2_HUMAN
Original site: E7EUN2_HUMAN 
ID   E7EUN2_HUMAN            Unreviewed;      1069 AA.
AC   E7EUN2;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   SubName: Full=ArfGAP with GTPase domain, ankyrin repeat and PH domain 1 {ECO:0000313|Ensembl:ENSP00000386897.1};
GN   Name=AGAP1 {ECO:0000313|Ensembl:ENSP00000386897.1};
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 {ECO:0000313|Ensembl:ENSP00000386897.1, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000386897.1, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [2] {ECO:0007829|PubMed:18220336}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.D., Yates J.R.;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [3] {ECO:0007829|PubMed:23186163}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=23186163;
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   [4] {ECO:0007829|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN   [5] {ECO:0000313|Ensembl:ENSP00000386897.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the centaurin gamma-like family.
CC       {ECO:0000256|ARBA:ARBA00005430}.
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DR   EMBL; AC012305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC019047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC064874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC073989; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC079400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; E7EUN2; -.
DR   SMR; E7EUN2; -.
DR   IntAct; E7EUN2; 14.
DR   MassIVE; E7EUN2; -.
DR   MaxQB; E7EUN2; -.
DR   ProteomicsDB; 18467; -.
DR   Antibodypedia; 34463; 159 antibodies from 25 providers.
DR   Ensembl; ENST00000409538.5; ENSP00000386897.1; ENSG00000157985.20.
DR   UCSC; uc061txv.1; human.
DR   HGNC; HGNC:16922; AGAP1.
DR   VEuPathDB; HostDB:ENSG00000157985; -.
DR   GeneTree; ENSGT00940000154793; -.
DR   HOGENOM; CLU_007326_5_0_1; -.
DR   PhylomeDB; E7EUN2; -.
DR   ChiTaRS; AGAP1; human.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; ENSG00000157985; Expressed in frontal pole and 199 other cell types or tissues.
DR   ExpressionAtlas; E7EUN2; baseline and differential.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd08853; ArfGap_AGAP2; 1.
DR   CDD; cd04103; Centaurin_gamma; 1.
DR   CDD; cd01250; PH_AGAP; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR037278; ARFGAP/RecO.
DR   InterPro; IPR001164; ArfGAP_dom.
DR   InterPro; IPR038508; ArfGAP_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR001806; Small_GTPase.
DR   PANTHER; PTHR45819:SF1; ARF-GAP WITH GTPASE, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR45819; CENTAURIN-GAMMA-1A; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00173; RAS; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS51419; RAB; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   1: Evidence at protein level;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Proteomics identification {ECO:0007829|EPD:E7EUN2,
KW   ECO:0007829|MaxQB:E7EUN2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00288}.
FT   DOMAIN          611..800
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          821..941
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50115"
FT   REPEAT          980..1012
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          1..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          532..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          669..759
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..561
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        583..602
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        683..724
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1069 AA;  116619 MW;  A3ECB976722085F7 CRC64;
     MYLLDGSGEP ASPPADAMPR GTPPRKTVYR ISVTMVRKEQ LAAPGSGGPD PRPVRRPRPA
     RSPDAPGRLE EEAEEAEGAE EPEGPRPRAW DFRTFRTRST GQLELGRLRP CARGLEPADL
     AGSAPAEEEG RGSPASGSPD VEGARAAPLR RSLSFRHWSG PEAPQGRTLG GGRRHSSSGS
     LAWAPCDEAA AGTTLEPATA TQPASEKRNT LDVGEVLSKN DALSDLERWE RSKSKNRTLD
     NSDLQRLERA RAAAGAGAAS EHRLLRFFSG IFARRDGGPG GGPSPRSGAS RPRGYFSLRR
     APAEAHSSSA ESIDGSPRRD AFVNSQEWTL SRSVPELKVG IVGNLASGKS ALVHRYLTGT
     YVQEESPEGG RFKKEIVVDG QSYLLLIRDE GGPPEAQFAM WVDAVIFVFS LEDEISFQTV
     YHYYSRMANY RNTSEIPLVL VGTQDAISSA NPRVIDDARA RKLSNDLKRC TYYETCATYG
     LNVERVFQDV AQKIVATRKK QQLSIGPCKS LPNSPSHSSV CSAQVSAVHI SQTSNGGGSL
     SDYSSSVPST PSTSQKELRI DVPPTANTPT PVRKQSKRRS NLFTSRKGSD PDKEKKGLES
     RADSIGSGRA IPIKQGMLLK RSGKSLNKEW KKKYVTLCDN GVLTYHPSLH DYMQNVHGKE
     IDLLRTTVKV PGKRPPRATS ACAPISSPKT NGLSKDMSSL HISPNSDTGL GDSVCSSPSI
     SSTTSPKLDP PPSPHANRKK HRRKKSTSNF KADGLSGTAE EQEENFEFII VSLTGQTWHF
     EATTYEERDA WVQAIESQIL ASLQSCESSK NKSRLTSQSE AMALQSIRNM RGNSHCVDCE
     TQNPNWASLN LGALMCIECS GIHRNLGTHL SRVRSLDLDD WPVELIKVMS SIGNELANSV
     WEESSQGRTK PSVDSTREEK ERWIRAKYEQ KLFLAPLPCT ELSLGQHLLR ATADEDLRTA
     ILLLAHGSRD EVNETCGEGD GRTALHLACR KGNVVLAQLL IWYGVDVTAR DAHGNTALAY
     ARQASSQECI DVLLQYGCPD ERFVLMATPN LSRRNNNRNN SSGRVPTII
//
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