ARFG3_HUMAN
ID ARFG3_HUMAN Reviewed; 516 AA.
AC Q9NP61; E9PB03; Q9BSC6; Q9H9J0; Q9NT10; Q9NUP5; Q9Y4V3; Q9Y4V4;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein 3;
DE Short=ARF GAP 3;
GN Name=ARFGAP3; Synonyms=ARFGAP1;
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 1), AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=10704287; DOI=10.1006/geno.1999.6095;
RA Zhang C., Yu Y., Zhang S., Liu M., Xing G., Wei H., Bi J., Liu X., Zhou G.,
RA Dong C., Hu Z., Zhang Y., Luo L., Wu C., Zhao S., He F.;
RT "Characterization, chromosomal assignment, and tissue expression of a novel
RT human gene belonging to the ARF GAP family.";
RL Genomics 63:400-408(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12529303; DOI=10.1101/gr.695703;
RA Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S.,
RA Bye J.M., Beare D.M., Dunham I.;
RT "Reevaluating human gene annotation: a second-generation analysis of
RT chromosome 22.";
RL Genome Res. 13:27-36(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-355.
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-355.
RC TISSUE=Lung;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 44-516 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 118-516 (ISOFORM 1), AND VARIANT
RP ARG-355.
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 [8]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=11172815; DOI=10.1016/s0014-5793(01)02134-2;
RA Liu X., Zhang C., Xing G., Chen Q., He F.;
RT "Functional characterization of novel human ARFGAP3.";
RL FEBS Lett. 490:79-83(2001).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=17760859; DOI=10.1111/j.1600-0854.2007.00631.x;
RA Frigerio G., Grimsey N., Dale M., Majoul I., Duden R.;
RT "Two human ARFGAPs associated with COP-I-coated vesicles.";
RL Traffic 8:1644-1655(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331 AND SER-453, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370 AND SER-453, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-331, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274; SER-428; SER-451;
RP SER-455; SER-457 AND SER-458, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-270 AND SER-451, AND
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).
RN [16]
RP STRUCTURE BY NMR OF 1-136.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ARFGAP domain of ADP-ribosylation factor GTPase-
RT activating protein 3 (ARFGAP 3).";
RL Submitted (NOV-2005) to the PDB data bank.
RN [17]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-355, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [18]
RP VARIANT [LARGE SCALE ANALYSIS] GLY-290.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 1
CC (ARF1). Hydrolysis of ARF1-bound GTP may lead to dissociation of
CC coatomer from Golgi-derived membranes to allow fusion with target
CC membranes. {ECO:0000269|PubMed:11172815}.
CC -!- ACTIVITY REGULATION: GAP activity stimulated by phosphatidylinositol
CC 4,5-bisphosphate (PIP2). {ECO:0000269|PubMed:11172815}.
CC -!- INTERACTION:
CC Q9NP61; P54252: ATXN3; NbExp=3; IntAct=EBI-2875816, EBI-946046;
CC Q9NP61; Q9Y5Z0: BACE2; NbExp=3; IntAct=EBI-2875816, EBI-11282723;
CC Q9NP61; P45973: CBX5; NbExp=3; IntAct=EBI-2875816, EBI-78219;
CC Q9NP61; P48643: CCT5; NbExp=3; IntAct=EBI-2875816, EBI-355710;
CC Q9NP61; A5D8W4: CDH1; NbExp=3; IntAct=EBI-2875816, EBI-7793316;
CC Q9NP61; P02489: CRYAA; NbExp=3; IntAct=EBI-2875816, EBI-6875961;
CC Q9NP61; P50570-2: DNM2; NbExp=3; IntAct=EBI-2875816, EBI-10968534;
CC Q9NP61; Q14204: DYNC1H1; NbExp=3; IntAct=EBI-2875816, EBI-356015;
CC Q9NP61; O14908-2: GIPC1; NbExp=3; IntAct=EBI-2875816, EBI-25913156;
CC Q9NP61; P17302: GJA1; NbExp=3; IntAct=EBI-2875816, EBI-1103439;
CC Q9NP61; P04792: HSPB1; NbExp=3; IntAct=EBI-2875816, EBI-352682;
CC Q9NP61; P42858: HTT; NbExp=22; IntAct=EBI-2875816, EBI-466029;
CC Q9NP61; Q92876: KLK6; NbExp=3; IntAct=EBI-2875816, EBI-2432309;
CC Q9NP61; Q9H400: LIME1; NbExp=3; IntAct=EBI-2875816, EBI-2830566;
CC Q9NP61; O43920: NDUFS5; NbExp=3; IntAct=EBI-2875816, EBI-1246091;
CC Q9NP61; P49821: NDUFV1; NbExp=3; IntAct=EBI-2875816, EBI-748312;
CC Q9NP61; P07196: NEFL; NbExp=3; IntAct=EBI-2875816, EBI-475646;
CC Q9NP61; O43933: PEX1; NbExp=3; IntAct=EBI-2875816, EBI-988601;
CC Q9NP61; D3DTS7: PMP22; NbExp=3; IntAct=EBI-2875816, EBI-25882629;
CC Q9NP61; P30041: PRDX6; NbExp=3; IntAct=EBI-2875816, EBI-2255129;
CC Q9NP61; P60891: PRPS1; NbExp=3; IntAct=EBI-2875816, EBI-749195;
CC Q9NP61; P23219: PTGS1; NbExp=3; IntAct=EBI-2875816, EBI-6655935;
CC Q9NP61; P20340-2: RAB6A; NbExp=3; IntAct=EBI-2875816, EBI-8840191;
CC Q9NP61; P54725: RAD23A; NbExp=3; IntAct=EBI-2875816, EBI-746453;
CC Q9NP61; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-2875816, EBI-396669;
CC Q9NP61; Q8WWV3: RTN4IP1; NbExp=3; IntAct=EBI-2875816, EBI-743502;
CC Q9NP61; P50454: SERPINH1; NbExp=3; IntAct=EBI-2875816, EBI-350723;
CC Q9NP61; Q8IVP1: SH3GL3; NbExp=3; IntAct=EBI-2875816, EBI-6503765;
CC Q9NP61; P37840: SNCA; NbExp=3; IntAct=EBI-2875816, EBI-985879;
CC Q9NP61; Q16563: SYPL1; NbExp=3; IntAct=EBI-2875816, EBI-2800683;
CC Q9NP61; P37173: TGFBR2; NbExp=3; IntAct=EBI-2875816, EBI-296151;
CC Q9NP61; P02766: TTR; NbExp=3; IntAct=EBI-2875816, EBI-711909;
CC Q9NP61; O76024: WFS1; NbExp=3; IntAct=EBI-2875816, EBI-720609;
CC Q9NP61; Q8IUH5: ZDHHC17; NbExp=2; IntAct=EBI-2875816, EBI-524753;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17760859}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:17760859}; Peripheral membrane
CC protein {ECO:0000269|PubMed:17760859}; Cytoplasmic side
CC {ECO:0000269|PubMed:17760859}. Note=Also found on peripheral punctate
CC structures likely to be endoplasmic reticulum-Golgi intermediate
CC compartment.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NP61-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NP61-2; Sequence=VSP_046888;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest expression in endocrine
CC glands (pancreas, pituitary gland, salivary gland, and prostate) and
CC testis with a much higher expression in the testis than in the ovary.
CC {ECO:0000269|PubMed:10704287}.
CC -!- DEVELOPMENTAL STAGE: Expressed at higher level in adult thymus, brain
CC and lung, than in corresponding fetal tissues. Expressed at lower level
CC in spleen, heart, kidney and liver during development.
CC -!- CAUTION: Was originally termed ARFGAP1. {ECO:0000305|PubMed:10704287}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92076.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14236.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF111847; AAF40310.1; -; mRNA.
DR EMBL; AL159143; CAB76901.1; -; mRNA.
DR EMBL; CR456382; CAG30268.1; -; mRNA.
DR EMBL; AL049757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL049758; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005122; AAH05122.1; -; mRNA.
DR EMBL; AL137598; CAB70834.1; -; mRNA.
DR EMBL; AK002083; BAA92076.1; ALT_INIT; mRNA.
DR EMBL; AK022768; BAB14236.1; ALT_INIT; mRNA.
DR CCDS; CCDS14042.1; -. [Q9NP61-1]
DR CCDS; CCDS46722.1; -. [Q9NP61-2]
DR PIR; T46305; T46305.
DR RefSeq; NP_001135765.1; NM_001142293.1. [Q9NP61-2]
DR RefSeq; NP_055385.3; NM_014570.4. [Q9NP61-1]
DR PDB; 2CRW; NMR; -; A=1-136.
DR PDBsum; 2CRW; -.
DR AlphaFoldDB; Q9NP61; -.
DR SMR; Q9NP61; -.
DR BioGRID; 117668; 88.
DR IntAct; Q9NP61; 51.
DR STRING; 9606.ENSP00000263245; -.
DR GlyGen; Q9NP61; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NP61; -.
DR MetOSite; Q9NP61; -.
DR PhosphoSitePlus; Q9NP61; -.
DR BioMuta; ARFGAP3; -.
DR DMDM; 21263420; -.
DR EPD; Q9NP61; -.
DR jPOST; Q9NP61; -.
DR MassIVE; Q9NP61; -.
DR MaxQB; Q9NP61; -.
DR PaxDb; Q9NP61; -.
DR PeptideAtlas; Q9NP61; -.
DR PRIDE; Q9NP61; -.
DR ProteomicsDB; 19114; -.
DR ProteomicsDB; 81892; -. [Q9NP61-1]
DR TopDownProteomics; Q9NP61-1; -. [Q9NP61-1]
DR Antibodypedia; 34963; 286 antibodies from 37 providers.
DR DNASU; 26286; -.
DR Ensembl; ENST00000263245.10; ENSP00000263245.5; ENSG00000242247.11. [Q9NP61-1]
DR Ensembl; ENST00000437119.6; ENSP00000388791.2; ENSG00000242247.11. [Q9NP61-2]
DR GeneID; 26286; -.
DR KEGG; hsa:26286; -.
DR MANE-Select; ENST00000263245.10; ENSP00000263245.5; NM_014570.5; NP_055385.3.
DR UCSC; uc003bdd.3; human. [Q9NP61-1]
DR CTD; 26286; -.
DR DisGeNET; 26286; -.
DR GeneCards; ARFGAP3; -.
DR HGNC; HGNC:661; ARFGAP3.
DR HPA; ENSG00000242247; Low tissue specificity.
DR MIM; 612439; gene.
DR neXtProt; NX_Q9NP61; -.
DR OpenTargets; ENSG00000242247; -.
DR PharmGKB; PA35024; -.
DR VEuPathDB; HostDB:ENSG00000242247; -.
DR eggNOG; KOG0706; Eukaryota.
DR GeneTree; ENSGT00940000158466; -.
DR HOGENOM; CLU_023062_6_2_1; -.
DR InParanoid; Q9NP61; -.
DR OMA; ENGPSKV; -.
DR PhylomeDB; Q9NP61; -.
DR TreeFam; TF313985; -.
DR PathwayCommons; Q9NP61; -.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR SignaLink; Q9NP61; -.
DR SIGNOR; Q9NP61; -.
DR BioGRID-ORCS; 26286; 10 hits in 1075 CRISPR screens.
DR ChiTaRS; ARFGAP3; human.
DR EvolutionaryTrace; Q9NP61; -.
DR GeneWiki; ARFGAP3; -.
DR GenomeRNAi; 26286; -.
DR Pharos; Q9NP61; Tbio.
DR PRO; PR:Q9NP61; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9NP61; protein.
DR Bgee; ENSG00000242247; Expressed in jejunal mucosa and 207 other tissues.
DR ExpressionAtlas; Q9NP61; baseline and differential.
DR Genevisible; Q9NP61; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
DR GO; GO:0009306; P:protein secretion; IEP:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; NAS:UniProtKB.
DR Gene3D; 1.10.220.150; -; 1.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR Pfam; PF01412; ArfGap; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm;
KW ER-Golgi transport; Golgi apparatus; GTPase activation; Membrane;
KW Metal-binding; Phosphoprotein; Protein transport; Reference proteome;
KW Transport; Zinc; Zinc-finger.
FT CHAIN 1..516
FT /note="ADP-ribosylation factor GTPase-activating protein 3"
FT /id="PRO_0000074193"
FT DOMAIN 10..126
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT ZN_FING 25..48
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 170..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 243..263
FT /evidence="ECO:0000255"
FT COMPBIAS 398..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 88..131
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046888"
FT VARIANT 231
FT /note="S -> G (in dbSNP:rs9607957)"
FT /id="VAR_055523"
FT VARIANT 290
FT /note="E -> G (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036177"
FT VARIANT 355
FT /note="S -> R (in dbSNP:rs1018448)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15461802, ECO:0000269|PubMed:15489334,
FT ECO:0007744|PubMed:15592455"
FT /id="VAR_013447"
FT VARIANT 370
FT /note="S -> G (in dbSNP:rs16986123)"
FT /id="VAR_055524"
FT VARIANT 468
FT /note="Q -> H (in dbSNP:rs35498349)"
FT /id="VAR_055525"
FT VARIANT 482
FT /note="A -> T (in dbSNP:rs36003980)"
FT /id="VAR_055526"
FT VARIANT 490
FT /note="Q -> R (in dbSNP:rs11551619)"
FT /id="VAR_055527"
FT CONFLICT 339
FT /note="K -> R (in Ref. 7; BAA92076)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="T -> A (in Ref. 7; BAA92076)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="S -> P (in Ref. 7; BAB14236)"
FT /evidence="ECO:0000305"
FT HELIX 6..18
FT /evidence="ECO:0007829|PDB:2CRW"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:2CRW"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:2CRW"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:2CRW"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:2CRW"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:2CRW"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:2CRW"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:2CRW"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:2CRW"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:2CRW"
FT HELIX 108..126
FT /evidence="ECO:0007829|PDB:2CRW"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2CRW"
SQ SEQUENCE 516 AA; 56928 MW; E355E56A5D867F8E CRC64;
MGDPSKQDIL TIFKRLRSVP TNKVCFDCGA KNPSWASITY GVFLCIDCSG SHRSLGVHLS
FIRSTELDSN WSWFQLRCMQ VGGNASASSF FHQHGCSTND TNAKYNSRAA QLYREKIKSL
ASQATRKHGT DLWLDSCVVP PLSPPPKEED FFASHVSPEV SDTAWASAIA EPSSLTSRPV
ETTLENNEGG QEQGPSVEGL NVPTKATLEV SSIIKKKPNQ AKKGLGAKKG SLGAQKLANT
CFNEIEKQAQ AADKMKEQED LAKVVSKEES IVSSLRLAYK DLEIQMKKDE KMNISGKKNV
DSDRLGMGFG NCRSVISHSV TSDMQTIEQE SPIMAKPRKK YNDDSDDSYF TSSSSYFDEP
VELRSSSFSS WDDSSDSYWK KETSKDTETV LKTTGYSDRP TARRKPDYEP VENTDEAQKK
FGNVKAISSD MYFGRQSQAD YETRARLERL SASSSISSAD LFEEPRKQPA GNYSLSSVLP
NAPDMAQFKQ GVRSVAGKLS VFANGVVTSI QDRYGS
