ID K7ES92_HUMAN Unreviewed; 771 AA.
AC K7ES92;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Rho GTPase activating protein 45 {ECO:0000313|Ensembl:ENSP00000468607.1};
GN Name=ARHGAP45 {ECO:0000313|Ensembl:ENSP00000468607.1};
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:ENSP00000468607.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000468607.1, ECO:0000313|Proteomes:UP000005640}
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 [2] {ECO:0007829|PubMed:19367720}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [3] {ECO:0007829|PubMed:19690332}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [4] {ECO:0007829|PubMed:21269460}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [5] {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 [6] {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 [7] {ECO:0000313|Ensembl:ENSP00000468607.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AC004151; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011558; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001269263.1; NM_001282334.1.
DR AlphaFoldDB; K7ES92; -.
DR SMR; K7ES92; -.
DR MassIVE; K7ES92; -.
DR MaxQB; K7ES92; -.
DR PeptideAtlas; K7ES92; -.
DR Antibodypedia; 10356; 218 antibodies from 29 providers.
DR DNASU; 23526; -.
DR Ensembl; ENST00000590577.2; ENSP00000468607.1; ENSG00000180448.11.
DR GeneID; 23526; -.
DR UCSC; uc002lrc.4; human.
DR CTD; 23526; -.
DR HGNC; HGNC:17102; ARHGAP45.
DR NIAGADS; ENSG00000180448; -.
DR VEuPathDB; HostDB:ENSG00000180448; -.
DR GeneTree; ENSGT00950000183110; -.
DR HOGENOM; CLU_006236_0_0_1; -.
DR OrthoDB; 5395569at2759; -.
DR BioGRID-ORCS; 23526; 44 hits in 1160 CRISPR screens.
DR ChiTaRS; ARHGAP45; human.
DR GenomeRNAi; 23526; -.
DR Proteomes; UP000005640; Chromosome 19.
DR Bgee; ENSG00000180448; Expressed in granulocyte and 158 other cell types or tissues.
DR ExpressionAtlas; K7ES92; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd20816; C1_GMIP-like; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR15228:SF18; RHO GTPASE-ACTIVATING PROTEIN 45; 1.
DR PANTHER; PTHR15228; SPERMATHECAL PHYSIOLOGY VARIANT; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01077}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Proteomics identification {ECO:0007829|EPD:K7ES92,
KW ECO:0007829|MaxQB:K7ES92};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 1..174
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 337..382
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 396..609
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 771 AA; 84623 MW; 105A3A4253CE2347 CRC64;
MGVGRKGGAG ETESHPRIGL ELASWLPHPQ QEAESNLRKA KQGYVQRCED HDKARFLVAK
AEEEQAGSAP GAGSTATKTL DKRRRLEEEA KNKAEEAMAT YRTCVADAKT QKQELEDTKV
TALRQIQEVI RQSDQTIKSA TISYYQMMHM QTAPLPVHFQ MLCESSKLYD PGQQYASHVR
QLQRDQEPDV HYDFEPHVSA NAWSPVMRAR KSSFNVSDVA RPEAAGSPPE EGGCTEGTPA
KDHRAGRGHQ VHKSWPLSIS DSDSGLDPGP GAGDFKKFER TSSSGTMSST EELVDPDGGA
GASAFEQADL NGMTPELPVA VPSGPFRHEG LSKAARTHRL RKLRTPAKCR ECNSYVYFQG
AECEECCLAC HKKCLETLAI QCGHKKLQGR LQLFGQDFSH AARSAPDGVP FIVKKCVCEI
ERRALRTKGI YRVNGVKTRV EKLCQAFENG KELVELSQAS PHDISNVLKL YLRQLPEPLI
SFRLYHELVG LAKDSLKAEA EAKAASRGRQ DGSESEAVAV ALAGRLRELL RDLPPENRAS
LQYLLRHLRR IVEVEQDNKM TPGNLGIVFG PTLLRPRPTE ATVSLSSLVD YPHQARVIET
LIVHYGLVFE EEPEETPGGQ DESSNQRAEV VVQVPYLEAG EAVVYPLQEA AADGCRESRV
VSNDSDSDLE EASELLSSSE ASALGHLSFL EQQQSEASLE VASGSHSGSE EQLEATARED
GDGDEDGPAQ QLSGFNTNQS NNVLQAPLPP MRLRGGRMTL GSCRERQPEF V
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