ID HMHA1_HUMAN Reviewed; 1136 AA. AC Q92619; B4DTS4; F6QP70; Q6P189; Q7LE26; Q86WS1; Q8HX84; Q9GJN9; Q9GJP0; AC Q9GJP1; Q9MY24; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 2. DT 27-MAR-2024, entry version 177. DE RecName: Full=Rho GTPase-activating protein 45 {ECO:0000312|HGNC:HGNC:17102}; DE Contains: DE RecName: Full=Minor histocompatibility antigen HA-1; DE Short=mHag HA-1; GN Name=ARHGAP45 {ECO:0000312|HGNC:HGNC:17102}; GN Synonyms=HMHA1 {ECO:0000312|HGNC:HGNC:17102}, KIAA0223 GN {ECO:0000312|HGNC:HGNC:17102}; 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 [GENOMIC DNA]. RX PubMed=11095984; DOI=10.1006/bbrc.2000.3880; RA Kaminski W.E., Piehler A., Schmitz G.; RT "Genomic organization of the human cholesterol-responsive ABC transporter RT ABCA7: tandem linkage with the minor histocompatibility antigen HA-1 RT gene."; RL Biochem. Biophys. Res. Commun. 278:782-789(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=9039502; DOI=10.1093/dnares/3.5.321; RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., RA Tanaka A., Kotani H., Miyajima N., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. VI. The RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of RT cDNA clones from cell line KG-1 and brain."; RL DNA Res. 3:321-329(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS HIS-139; RP ASP-259 AND GLY-439. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and Testis; 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 [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-140, AND VARIANT HIS-139. RX PubMed=10958358; DOI=10.1034/j.1399-0039.2000.560109.x; RA Arostegui J.I., Gallardo D., Rodriguez-Luaces M., Querol S., Madrigal J.A., RA Garcia-Lopez J., Granena A.; RT "Genomic typing of minor histocompatibility antigen HA-1 by reference RT strand mediated conformation analysis (RSCA)."; RL Tissue Antigens 56:69-76(2000). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-140, AND VARIANT HIS-139. RX PubMed=16202172; DOI=10.1186/1471-2350-6-36; RA Graziano C., Giorgi M., Malentacchi C., Mattiuz P.L., Porfirio B.; RT "Sequence diversity within the HA-1 gene as detected by melting temperature RT assay without oligonucleotide probes."; RL BMC Med. Genet. 6:36-36(2005). RN [9] RP PROTEIN SEQUENCE OF 137-145, IDENTIFICATION BY MASS SPECTROMETRY, AND RP VARIANT HIS-139. RX PubMed=9461441; DOI=10.1126/science.279.5353.1054; RA den Haan J.M., Meadows L.M., Wang W., Pool J., Blokland E., Bishop T.L., RA Reinhardus C., Shabanowitz J., Offringa R., Hunt D.F., Engelhard V.H., RA Goulmy E.; RT "The minor histocompatibility antigen HA-1: a diallelic gene with a single RT amino acid polymorphism."; RL Science 279:1054-1057(1998). RN [10] RP FUNCTION. RX PubMed=8260714; RA Marijt W.A.F., Veenhof W.F.J., Goulmy E., Willemze R., van Rood J.J., RA Falkenburg J.H.F.; RT "Minor histocompatibility antigens HA-1-, -2-, and -4-, and HY-specific RT cytotoxic T-cell clones inhibit human hematopoietic progenitor cell growth RT by a mechanism that is dependent on direct cell-cell contact."; RL Blood 82:3778-3785(1993). RN [11] RP FUNCTION. RX PubMed=8532022; DOI=10.1056/nejm199602013340501; RA Goulmy E., Schipper R., Pool J., Blokland E., Falkenburg J.H., Vossen J., RA Gratwohl A., Vogelsang G.B., van Houwelingen H.C., van Rood J.J.; RT "Mismatches of minor histocompatibility antigens between HLA-identical RT donors and recipients and the development of graft-versus-host disease RT after bone marrow transplantation."; RL N. Engl. J. Med. 334:281-285(1996). RN [12] RP TISSUE SPECIFICITY. RX PubMed=8843592; DOI=10.1016/s0966-3274(96)80009-8; RA van Lochem E., van der Keur M., Mommaas A.M., de Gast G.C., Goulmy E.; RT "Functional expression of minor histocompatibility antigens on human RT peripheral blood dendritic cells and epidermal Langerhans cells."; RL Transpl. Immunol. 4:151-157(1996). RN [13] RP FUNCTION. RX PubMed=9798702; DOI=10.1097/00007890-199810150-00016; RA Rufer N., Wolpert E., Helg C., Tiercy J.-M., Gratwohl A., Chapuis B., RA Jeannet M., Goulmy E., Roosnek E.; RT "HA-1 and the SMCY-derived peptide FIDSYICQV (H-Y) are immunodominant minor RT histocompatibility antigens after bone marrow transplantation."; RL Transplantation 66:910-916(1998). RN [14] RP TISSUE SPECIFICITY. RX PubMed=11965046; DOI=10.1097/00007890-200204150-00022; RA Fujii N., Hiraki A., Ikeda K., Ohmura Y., Nozaki I., Shinagawa K., RA Ishimaru F., Kiura K., Shimizu N., Tanimoto M., Harada M.; RT "Expression of minor histocompatibility antigen, HA-1, in solid tumor RT cells."; RL Transplantation 73:1137-1141(2002). RN [15] RP FUNCTION. RX PubMed=12601144; DOI=10.1073/pnas.0530192100; RA Marijt W.A.E., Heemskerk M.H.M., Kloosterboer F.M., Goulmy E., RA Kester M.G.D., van der Hoorn M.A.W.G., van Luxemburg-Heys S.A.P., RA Hoogeboom M., Mutis T., Drijfhout J.W., van Rood J.J., Willemze R., RA Falkenburg J.H.F.; RT "Hematopoiesis-restricted minor histocompatibility antigens HA-1- or HA-2- RT specific T cells can induce complete remissions of relapsed leukemia."; RL Proc. Natl. Acad. Sci. U.S.A. 100:2742-2747(2003). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND SER-25, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-569, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-73; SER-93; SER-99; RP SER-569 AND SER-619, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Leukemic T-cell; 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 [20] 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., Buerckstuemmer 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-73; SER-569 AND RP SER-592, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [22] RP FUNCTION, DOMAIN, AND SUBCELLULAR LOCATION. RX PubMed=24086303; DOI=10.1371/journal.pone.0073962; RA de Kreuk B.J., Schaefer A., Anthony E.C., Tol S., Fernandez-Borja M., RA Geerts D., Pool J., Hambach L., Goulmy E., Hordijk P.L.; RT "The human minor histocompatibility antigen 1 is a RhoGAP."; RL PLoS ONE 8:E73962-E73962(2013). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-569; SER-578; SER-619 RP AND SER-949, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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). RN [24] RP VARIANT HIS-139. RX PubMed=9820595; DOI=10.1111/j.1399-0039.1998.tb03052.x; RA Tseng L.-H., Lin M.-T., Martin P.J., Pei J., Smith A.G., Hansen J.A.; RT "Definition of the gene encoding the minor histocompatibility antigen HA-1 RT and typing for HA-1 from genomic DNA."; RL Tissue Antigens 52:305-311(1998). RN [25] RP VARIANT HIS-139. RX PubMed=16399573; DOI=10.1016/j.bbmt.2005.09.017; RA Di Terlizzi S., Zino E., Mazzi B., Magnani C., Tresoldi C., Perna S.K., RA Bregni M., Rossini S., Ciceri F., Bordignon C., Bonini C., Fleischhauer K.; RT "Therapeutic and diagnostic applications of minor histocompatibility RT antigen HA-1 and HA-2 disparities in allogeneic hematopoietic stem cell RT transplantation: a survey of different populations."; RL Biol. Blood Marrow Transplant. 12:95-101(2006). CC -!- FUNCTION: Contains a GTPase activator for the Rho-type GTPases (RhoGAP) CC domain that would be able to negatively regulate the actin cytoskeleton CC as well as cell spreading. However, also contains N-terminally a BAR- CC domin which is able to play an autoinhibitory effect on this RhoGAP CC activity. {ECO:0000269|PubMed:24086303}. CC -!- FUNCTION: Precursor of the histocompatibility antigen HA-1. More CC generally, minor histocompatibility antigens (mHags) refer to CC immunogenic peptide which, when complexed with MHC, can generate an CC immune response after recognition by specific T-cells. The peptides are CC derived from polymorphic intracellular proteins, which are cleaved by CC normal pathways of antigen processing. The binding of these peptides to CC MHC class I or class II molecules and its expression on the cell CC surface can stimulate T-cell responses and thereby trigger graft CC rejection or graft-versus-host disease (GVHD) after hematopoietic stem CC cell transplantation from HLA-identical sibling donor. GVHD is a CC frequent complication after bone marrow transplantation (BMT), due to CC mismatch of minor histocompatibility antigen in HLA-matched sibling CC marrow transplants. Specifically, mismatching for mHag HA-1 which is CC recognized as immunodominant, is shown to be associated with the CC development of severe GVHD after HLA-identical BMT. HA-1 is presented CC to the cell surface by MHC class I HLA-A*0201, but also by other HLA-A CC alleles. This complex specifically elicits donor-cytotoxic T-lymphocyte CC (CTL) reactivity against hematologic malignancies after treatment by CC HLA-identical allogenic BMT. It induces cell recognition and lysis by CC CTL. {ECO:0000269|PubMed:12601144, ECO:0000269|PubMed:8260714, CC ECO:0000269|PubMed:8532022, ECO:0000269|PubMed:9798702}. CC -!- SUBUNIT: HA-1 forms a complex with MHC class I HLA-A*0201. CC -!- INTERACTION: CC Q92619; Q8TD16-2: BICD2; NbExp=3; IntAct=EBI-2825900, EBI-11975051; CC Q92619; Q9P107: GMIP; NbExp=3; IntAct=EBI-2825900, EBI-11603420; CC Q92619; Q08379: GOLGA2; NbExp=3; IntAct=EBI-2825900, EBI-618309; CC Q92619; O75031: HSF2BP; NbExp=3; IntAct=EBI-2825900, EBI-7116203; CC Q92619; Q5VU43-2: PDE4DIP; NbExp=3; IntAct=EBI-2825900, EBI-9640281; CC Q92619; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-2825900, EBI-14066006; CC Q92619; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-2825900, EBI-1105153; CC Q92619; P63000: RAC1; NbExp=3; IntAct=EBI-2825900, EBI-413628; CC Q92619; Q6NUQ1: RINT1; NbExp=5; IntAct=EBI-2825900, EBI-726876; CC Q92619; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-2825900, EBI-11952721; CC Q92619; Q86XT4: TRIM50; NbExp=3; IntAct=EBI-2825900, EBI-9867283; CC Q92619; Q96AP4: ZUP1; NbExp=3; IntAct=EBI-2825900, EBI-744706; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24086303}. Cell CC projection, ruffle membrane {ECO:0000269|PubMed:24086303}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q92619-1; Sequence=Displayed; CC Name=2; CC IsoId=Q92619-2; Sequence=VSP_044707; CC -!- TISSUE SPECIFICITY: Expressed on cells of the hematopoietic lineage. CC Detected in dendritic cells and epidermal Langerhans cells. Expressed CC in peripheral blood mononuclear cells, in all leukemia/lymphoma cell CC lines. Detected also in some solid tumors and tissues such as cancerous CC and non-cancerous tissue. {ECO:0000269|PubMed:11965046, CC ECO:0000269|PubMed:8843592}. CC -!- DOMAIN: Rho-GAP domain is able to regulate RhoGTPase activity, actin CC cytoskeleton and cell spreading. However N-terminally BAR domain plays CC an autoinhibitory role. {ECO:0000269|PubMed:24086303}. CC -!- POLYMORPHISM: The HA-1H allele is presented on the cell surface and CC recognized by CTL, whereas the HA-1R allele is poorly represented by CC HLA-A and non-immunogenic, although HA-1R allelic frequency is the CC highest (PubMed:9820595, PubMed:16399573). CC {ECO:0000269|PubMed:16399573, ECO:0000269|PubMed:9820595}. CC -!- MISCELLANEOUS: Infusion of lymphocyte from mHag HA-1-negative donors CC results in a durable remission in mHag HA-1-positive patients with CC leukemia or multiple myeloma. CC -!- SEQUENCE CAUTION: CC Sequence=BAA13212.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF308066; AAN04658.1; -; Genomic_DNA. DR EMBL; AF308045; AAN04658.1; JOINED; Genomic_DNA. DR EMBL; AF308046; AAN04658.1; JOINED; Genomic_DNA. DR EMBL; AF308047; AAN04658.1; JOINED; Genomic_DNA. DR EMBL; AF308048; AAN04658.1; JOINED; Genomic_DNA. DR EMBL; AF308049; AAN04658.1; JOINED; Genomic_DNA. DR EMBL; AF308050; AAN04658.1; JOINED; Genomic_DNA. DR EMBL; AF308051; AAN04658.1; JOINED; Genomic_DNA. DR EMBL; AF308052; AAN04658.1; JOINED; Genomic_DNA. DR EMBL; AF308053; AAN04658.1; JOINED; Genomic_DNA. DR EMBL; AF308054; AAN04658.1; JOINED; Genomic_DNA. DR EMBL; AF308055; AAN04658.1; JOINED; Genomic_DNA. DR EMBL; AF308056; AAN04658.1; JOINED; Genomic_DNA. DR EMBL; AF308057; AAN04658.1; JOINED; Genomic_DNA. DR EMBL; AF308058; AAN04658.1; JOINED; Genomic_DNA. DR EMBL; AF308059; AAN04658.1; JOINED; Genomic_DNA. DR EMBL; AF308060; AAN04658.1; JOINED; Genomic_DNA. DR EMBL; AF308061; AAN04658.1; JOINED; Genomic_DNA. DR EMBL; AF308062; AAN04658.1; JOINED; Genomic_DNA. DR EMBL; AF308063; AAN04658.1; JOINED; Genomic_DNA. DR EMBL; AF308064; AAN04658.1; JOINED; Genomic_DNA. DR EMBL; AF308065; AAN04658.1; JOINED; Genomic_DNA. DR EMBL; AF311102; AAN04658.1; JOINED; Genomic_DNA. DR EMBL; D86976; BAA13212.1; ALT_INIT; mRNA. DR EMBL; AK300341; BAG62086.1; -; mRNA. DR EMBL; AC004151; AAC03237.1; -; Genomic_DNA. DR EMBL; AC011558; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC093066; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471139; EAW69551.1; -; Genomic_DNA. DR EMBL; BC048129; AAH48129.1; -; mRNA. DR EMBL; BC065223; AAH65223.1; -; mRNA. DR EMBL; AF207595; AAG02014.1; -; Genomic_DNA. DR EMBL; AF207596; AAG02015.1; -; Genomic_DNA. DR EMBL; AF207597; AAG02016.1; -; Genomic_DNA. DR EMBL; AF236756; AAF91292.1; -; Genomic_DNA. DR CCDS; CCDS32863.1; -. [Q92619-1] DR CCDS; CCDS58637.1; -. [Q92619-2] DR PIR; D59433; D59433. DR RefSeq; NP_001245257.1; NM_001258328.2. [Q92619-2] DR RefSeq; NP_001269263.1; NM_001282334.1. DR RefSeq; NP_001269264.1; NM_001282335.1. DR RefSeq; NP_036424.2; NM_012292.4. [Q92619-1] DR PDB; 3D25; X-ray; 1.30 A; C=140-145. DR PDB; 3FT3; X-ray; 1.95 A; P=137-145. DR PDBsum; 3D25; -. DR PDBsum; 3FT3; -. DR AlphaFoldDB; Q92619; -. DR SMR; Q92619; -. DR BioGRID; 117072; 23. DR IntAct; Q92619; 20. DR STRING; 9606.ENSP00000439601; -. DR GlyCosmos; Q92619; 2 sites, 2 glycans. DR GlyGen; Q92619; 2 sites, 2 O-linked glycans (2 sites). DR iPTMnet; Q92619; -. DR PhosphoSitePlus; Q92619; -. DR SwissPalm; Q92619; -. DR BioMuta; ARHGAP45; -. DR DMDM; 187471158; -. DR EPD; Q92619; -. DR jPOST; Q92619; -. DR MassIVE; Q92619; -. DR MaxQB; Q92619; -. DR PaxDb; 9606-ENSP00000439601; -. DR PeptideAtlas; Q92619; -. DR ProteomicsDB; 27852; -. DR ProteomicsDB; 75372; -. [Q92619-1] DR Pumba; Q92619; -. DR Antibodypedia; 10356; 218 antibodies from 29 providers. DR DNASU; 23526; -. DR Ensembl; ENST00000313093.7; ENSP00000316772.2; ENSG00000180448.11. [Q92619-1] DR Ensembl; ENST00000539243.6; ENSP00000439601.1; ENSG00000180448.11. [Q92619-2] DR GeneID; 23526; -. DR KEGG; hsa:23526; -. DR MANE-Select; ENST00000313093.7; ENSP00000316772.2; NM_012292.5; NP_036424.2. DR UCSC; uc002lqz.4; human. [Q92619-1] DR AGR; HGNC:17102; -. DR CTD; 23526; -. DR DisGeNET; 23526; -. DR GeneCards; ARHGAP45; -. DR HGNC; HGNC:17102; ARHGAP45. DR HPA; ENSG00000180448; Group enriched (bone marrow, intestine, lung, lymphoid tissue). DR MIM; 601155; gene. DR neXtProt; NX_Q92619; -. DR NIAGADS; ENSG00000180448; -. DR OpenTargets; ENSG00000180448; -. DR PharmGKB; PA128394633; -. DR VEuPathDB; HostDB:ENSG00000180448; -. DR eggNOG; KOG1453; Eukaryota. DR GeneTree; ENSGT00950000183110; -. DR HOGENOM; CLU_006236_0_1_1; -. DR InParanoid; Q92619; -. DR OMA; PLACLCR; -. DR OrthoDB; 5395569at2759; -. DR PhylomeDB; Q92619; -. DR TreeFam; TF351450; -. DR PathwayCommons; Q92619; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-8980692; RHOA GTPase cycle. DR Reactome; R-HSA-9013148; CDC42 GTPase cycle. DR Reactome; R-HSA-9013149; RAC1 GTPase cycle. DR SignaLink; Q92619; -. DR BioGRID-ORCS; 23526; 44 hits in 1160 CRISPR screens. DR ChiTaRS; ARHGAP45; human. DR EvolutionaryTrace; Q92619; -. DR GeneWiki; HMHA1; -. DR GenomeRNAi; 23526; -. DR Pharos; Q92619; Tbio. DR PRO; PR:Q92619; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q92619; Protein. DR Bgee; ENSG00000180448; Expressed in granulocyte and 158 other cell types or tissues. DR ExpressionAtlas; Q92619; baseline and differential. DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome. DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome. 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; IPR001060; FCH_dom. 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; SM00055; FCH; 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. DR Genevisible; Q92619; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Cell projection; KW Coiled coil; Cytoplasm; Direct protein sequencing; GTPase activation; KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Zinc; KW Zinc-finger. FT CHAIN 1..1136 FT /note="Rho GTPase-activating protein 45" FT /id="PRO_0000330312" FT PEPTIDE 137..145 FT /note="Minor histocompatibility antigen HA-1" FT /id="PRO_0000330313" FT DOMAIN 269..539 FT /note="F-BAR" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077" FT DOMAIN 761..974 FT /note="Rho-GAP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172" FT ZN_FING 702..747 FT /note="Phorbol-ester/DAG-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226" FT REGION 1..73 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 91..110 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 583..662 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1061..1136 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 376..412 FT /evidence="ECO:0000255" FT COILED 440..499 FT /evidence="ECO:0000255" FT COMPBIAS 1061..1076 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1095..1111 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 23 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 25 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243" FT MOD_RES 73 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 93 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 99 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19367720, FT ECO:0007744|PubMed:19690332" FT MOD_RES 569 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19367720, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 578 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 592 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 619 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:24275569" FT MOD_RES 949 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1027 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q3TBD2" FT MOD_RES 1030 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q3TBD2" FT MOD_RES 1032 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q3TBD2" FT VAR_SEQ 1..30 FT /note="MFSRKKRELMKTPSISKKNRAGSPSPQPSG -> MSRGQRVLKGLLGWVCTW FT TWAWRARLGARGCGLHVLCPRDLPLPPE (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044707" FT VARIANT 139 FT /note="R -> H (in allele HA-1H; induction of CTL FT recognition for epitope HA-1; dbSNP:rs1801284)" FT /evidence="ECO:0000269|PubMed:10958358, FT ECO:0000269|PubMed:16202172, ECO:0000269|PubMed:16399573, FT ECO:0000269|PubMed:9461441, ECO:0000269|PubMed:9820595, FT ECO:0000269|Ref.5" FT /id="VAR_042693" FT VARIANT 259 FT /note="E -> D (in dbSNP:rs2074442)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_042694" FT VARIANT 439 FT /note="S -> G (in dbSNP:rs7251797)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_042695" FT VARIANT 515 FT /note="M -> I (in dbSNP:rs36084354)" FT /id="VAR_042696" FT VARIANT 886 FT /note="A -> P (in dbSNP:rs34569196)" FT /id="VAR_042697" FT CONFLICT 648 FT /note="S -> F (in Ref. 3; BAG62086)" FT /evidence="ECO:0000305" SQ SEQUENCE 1136 AA; 124614 MW; 9536787B3B1EE16D CRC64; MFSRKKRELM KTPSISKKNR AGSPSPQPSG ELPRKDGADA VFPGPSLEPP AGSSGVKATG TLKRPTSLSR HASAAGFPLS GAASWTLGRS HRSPLTAASP GELPTEGAGP DVVEDISHLL ADVARFAEGL EKLKECVLRD DLLEARRPRA HECLGEALRV MHQIISKYPL LNTVETLTAA GTLIAKVKAF HYESNNDLEK QEFEKALETI AVAFSSTVSE FLMGEVDSST LLAVPPGDSS QSMESLYGPG SEGTPPSLED CDAGCLPAEE VDVLLQRCEG GVDAALLYAK NMAKYMKDLI SYLEKRTTLE MEFAKGLQKI AHNCRQSVMQ EPHMPLLSIY SLALEQDLEF GHSMVQAVGT LQTQTFMQPL TLRRLEHEKR RKEIKEAWHR AQRKLQEAES NLRKAKQGYV QRCEDHDKAR FLVAKAEEEQ AGSAPGAGST ATKTLDKRRR LEEEAKNKAE EAMATYRTCV ADAKTQKQEL EDTKVTALRQ IQEVIRQSDQ TIKSATISYY QMMHMQTAPL PVHFQMLCES SKLYDPGQQY ASHVRQLQRD QEPDVHYDFE PHVSANAWSP VMRARKSSFN VSDVARPEAA GSPPEEGGCT EGTPAKDHRA GRGHQVHKSW PLSISDSDSG LDPGPGAGDF KKFERTSSSG TMSSTEELVD PDGGAGASAF EQADLNGMTP ELPVAVPSGP FRHEGLSKAA RTHRLRKLRT PAKCRECNSY VYFQGAECEE CCLACHKKCL ETLAIQCGHK KLQGRLQLFG QDFSHAARSA PDGVPFIVKK CVCEIERRAL RTKGIYRVNG VKTRVEKLCQ AFENGKELVE LSQASPHDIS NVLKLYLRQL PEPLISFRLY HELVGLAKDS LKAEAEAKAA SRGRQDGSES EAVAVALAGR LRELLRDLPP ENRASLQYLL RHLRRIVEVE QDNKMTPGNL GIVFGPTLLR PRPTEATVSL SSLVDYPHQA RVIETLIVHY GLVFEEEPEE TPGGQDESSN QRAEVVVQVP YLEAGEAVVY PLQEAAADGC RESRVVSNDS DSDLEEASEL LSSSEASALG HLSFLEQQQS EASLEVASGS HSGSEEQLEA TAREDGDGDE DGPAQQLSGF NTNQSNNVLQ APLPPMRLRG GRMTLGSCRE RQPEFV //