ARFG1_HUMAN
ID ARFG1_HUMAN Reviewed; 406 AA.
AC Q8N6T3; B7Z3U0; B7Z8H8; B7ZBI3; E1P5I9; E7EV62; Q6PK71; Q96KC4; Q96T02;
AC Q9NSU3; Q9NVF6; Q9UIL0;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=ADP-ribosylation factor GTPase-activating protein 1;
DE Short=ARF GAP 1;
DE AltName: Full=ADP-ribosylation factor 1 GTPase-activating protein;
DE Short=ARF1 GAP;
DE AltName: Full=ARF1-directed GTPase-activating protein;
GN Name=ARFGAP1; Synonyms=ARF1GAP;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5).
RC TISSUE=Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain, and Fetal brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 240-406 (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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 299-406 (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Ueki N.;
RT "HRI NTT human fetal brain cDNA project.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-189, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135 AND SER-304, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-189, AND IDENTIFICATION BY
RP 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-231, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135 AND THR-189, 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135; THR-189; SER-246;
RP SER-343; THR-350 AND SER-361, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150 AND THR-189, 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 [15]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-128 IN COMPLEX WITH ZINC IONS.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the ARFGAP domain of human ARFGAP1.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: GTPase-activating protein (GAP) for the ADP ribosylation
CC factor 1 (ARF1). Involved in membrane trafficking and /or vesicle
CC transport. Promotes hydrolysis of the ARF1-bound GTP and thus, is
CC required for the dissociation of coat proteins from Golgi-derived
CC membranes and vesicles, a prerequisite for vesicle's fusion with target
CC compartment. Probably regulates ARF1-mediated transport via its
CC interaction with the KDELR proteins and TMED2. Overexpression induces
CC the redistribution of the entire Golgi complex to the endoplasmic
CC reticulum, as when ARF1 is deactivated. Its activity is stimulated by
CC phosphoinosides and inhibited by phosphatidylcholine (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ARF1. Interacts with the COPI coat proteins,
CC KDELR1 and TMED2. The interaction with TMED2 inhibits the GAP activity
CC (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8N6T3; Q6FG41: FOS; NbExp=3; IntAct=EBI-716933, EBI-10198738;
CC Q8N6T3; P60520: GABARAPL2; NbExp=3; IntAct=EBI-716933, EBI-720116;
CC Q8N6T3; P28799: GRN; NbExp=3; IntAct=EBI-716933, EBI-747754;
CC Q8N6T3; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-716933, EBI-10172052;
CC Q8N6T3; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-716933, EBI-751260;
CC Q8N6T3; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-716933, EBI-1044640;
CC Q8N6T3; P36406: TRIM23; NbExp=3; IntAct=EBI-716933, EBI-740098;
CC Q8N6T3-2; P60520: GABARAPL2; NbExp=3; IntAct=EBI-6288865, EBI-720116;
CC Q8N6T3-2; Q5S007: LRRK2; NbExp=6; IntAct=EBI-6288865, EBI-5323863;
CC Q8N6T3-3; Q92870-2: APBB2; NbExp=3; IntAct=EBI-10694449, EBI-21535880;
CC Q8N6T3-3; P54253: ATXN1; NbExp=6; IntAct=EBI-10694449, EBI-930964;
CC Q8N6T3-3; P14136: GFAP; NbExp=3; IntAct=EBI-10694449, EBI-744302;
CC Q8N6T3-3; P28799: GRN; NbExp=3; IntAct=EBI-10694449, EBI-747754;
CC Q8N6T3-3; P29474: NOS3; NbExp=3; IntAct=EBI-10694449, EBI-1391623;
CC Q8N6T3-3; D3DTS7: PMP22; NbExp=3; IntAct=EBI-10694449, EBI-25882629;
CC Q8N6T3-3; P37840: SNCA; NbExp=3; IntAct=EBI-10694449, EBI-985879;
CC Q8N6T3-3; P09936: UCHL1; NbExp=3; IntAct=EBI-10694449, EBI-714860;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus
CC {ECO:0000250}. Note=Associates with the Golgi complex. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8N6T3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N6T3-2; Sequence=VSP_000298, VSP_000299;
CC Name=3;
CC IsoId=Q8N6T3-3; Sequence=VSP_021818;
CC Name=4;
CC IsoId=Q8N6T3-4; Sequence=VSP_055379, VSP_055380;
CC Name=5;
CC IsoId=Q8N6T3-5; Sequence=VSP_055739, VSP_000298, VSP_000299;
CC -!- DOMAIN: The region downstream of Arf-GAP domain is essential to GAP
CC activity in vivo. This region may be required for its targeting to
CC Golgi membranes (By similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55009.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB55113.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB70901.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AK001629; BAA91796.1; -; mRNA.
DR EMBL; AK027268; BAB55009.1; ALT_INIT; mRNA.
DR EMBL; AK296351; BAH12326.1; -; mRNA.
DR EMBL; AK027441; BAB55113.1; ALT_INIT; mRNA.
DR EMBL; AK303454; BAH13964.1; -; mRNA.
DR EMBL; AL121827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75292.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75294.1; -; Genomic_DNA.
DR EMBL; BC000786; AAH00786.1; -; mRNA.
DR EMBL; BC006085; AAH06085.1; -; mRNA.
DR EMBL; BC011876; AAH11876.1; -; mRNA.
DR EMBL; BC028233; AAH28233.1; -; mRNA.
DR EMBL; AL137744; CAB70901.1; ALT_SEQ; mRNA.
DR EMBL; AB015340; BAA88117.1; -; mRNA.
DR CCDS; CCDS13515.1; -. [Q8N6T3-1]
DR CCDS; CCDS13516.1; -. [Q8N6T3-2]
DR CCDS; CCDS63326.1; -. [Q8N6T3-3]
DR CCDS; CCDS63327.1; -. [Q8N6T3-5]
DR CCDS; CCDS63328.1; -. [Q8N6T3-4]
DR PIR; T46298; T46298.
DR RefSeq; NP_001268411.1; NM_001281482.1. [Q8N6T3-3]
DR RefSeq; NP_001268412.1; NM_001281483.1. [Q8N6T3-5]
DR RefSeq; NP_001268413.1; NM_001281484.1. [Q8N6T3-4]
DR RefSeq; NP_060679.1; NM_018209.3. [Q8N6T3-1]
DR RefSeq; NP_783202.1; NM_175609.2. [Q8N6T3-2]
DR PDB; 3DWD; X-ray; 2.40 A; A/B=1-128.
DR PDB; 3O47; X-ray; 2.80 A; A/B=1-140.
DR PDBsum; 3DWD; -.
DR PDBsum; 3O47; -.
DR AlphaFoldDB; Q8N6T3; -.
DR SMR; Q8N6T3; -.
DR BioGRID; 120856; 98.
DR IntAct; Q8N6T3; 69.
DR MINT; Q8N6T3; -.
DR STRING; 9606.ENSP00000314615; -.
DR GlyGen; Q8N6T3; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q8N6T3; -.
DR PhosphoSitePlus; Q8N6T3; -.
DR SwissPalm; Q8N6T3; -.
DR BioMuta; ARFGAP1; -.
DR DMDM; 27923731; -.
DR EPD; Q8N6T3; -.
DR jPOST; Q8N6T3; -.
DR MassIVE; Q8N6T3; -.
DR MaxQB; Q8N6T3; -.
DR PaxDb; Q8N6T3; -.
DR PeptideAtlas; Q8N6T3; -.
DR PRIDE; Q8N6T3; -.
DR ProteomicsDB; 18575; -.
DR ProteomicsDB; 6951; -.
DR ProteomicsDB; 72229; -. [Q8N6T3-1]
DR ProteomicsDB; 72230; -. [Q8N6T3-2]
DR ProteomicsDB; 72231; -. [Q8N6T3-3]
DR Antibodypedia; 29683; 416 antibodies from 33 providers.
DR DNASU; 55738; -.
DR Ensembl; ENST00000353546.7; ENSP00000314615.3; ENSG00000101199.13. [Q8N6T3-2]
DR Ensembl; ENST00000370275.8; ENSP00000359298.4; ENSG00000101199.13. [Q8N6T3-3]
DR Ensembl; ENST00000370283.9; ENSP00000359306.4; ENSG00000101199.13. [Q8N6T3-1]
DR Ensembl; ENST00000519273.6; ENSP00000443716.1; ENSG00000101199.13. [Q8N6T3-4]
DR Ensembl; ENST00000519604.5; ENSP00000430500.1; ENSG00000101199.13. [Q8N6T3-5]
DR GeneID; 55738; -.
DR KEGG; hsa:55738; -.
DR MANE-Select; ENST00000370283.9; ENSP00000359306.4; NM_018209.4; NP_060679.1.
DR UCSC; uc002yel.5; human. [Q8N6T3-1]
DR CTD; 55738; -.
DR DisGeNET; 55738; -.
DR GeneCards; ARFGAP1; -.
DR HGNC; HGNC:15852; ARFGAP1.
DR HPA; ENSG00000101199; Low tissue specificity.
DR MIM; 608377; gene.
DR neXtProt; NX_Q8N6T3; -.
DR OpenTargets; ENSG00000101199; -.
DR PharmGKB; PA164741246; -.
DR VEuPathDB; HostDB:ENSG00000101199; -.
DR eggNOG; KOG0704; Eukaryota.
DR GeneTree; ENSGT00890000139515; -.
DR HOGENOM; CLU_044516_0_0_1; -.
DR InParanoid; Q8N6T3; -.
DR OMA; NVCCDCN; -.
DR OrthoDB; 1155557at2759; -.
DR PhylomeDB; Q8N6T3; -.
DR TreeFam; TF105931; -.
DR PathwayCommons; Q8N6T3; -.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
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-8856828; Clathrin-mediated endocytosis.
DR SignaLink; Q8N6T3; -.
DR SIGNOR; Q8N6T3; -.
DR BioGRID-ORCS; 55738; 6 hits in 1087 CRISPR screens.
DR ChiTaRS; ARFGAP1; human.
DR EvolutionaryTrace; Q8N6T3; -.
DR GeneWiki; ARFGAP1; -.
DR GenomeRNAi; 55738; -.
DR Pharos; Q8N6T3; Tbio.
DR PRO; PR:Q8N6T3; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q8N6T3; protein.
DR Bgee; ENSG00000101199; Expressed in adenohypophysis and 186 other tissues.
DR ExpressionAtlas; Q8N6T3; baseline and differential.
DR Genevisible; Q8N6T3; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IBA:GO_Central.
DR GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
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; Acetylation; Alternative splicing; Cytoplasm;
KW ER-Golgi transport; Golgi apparatus; GTPase activation; Metal-binding;
KW Phosphoprotein; Protein transport; Reference proteome; Transport; Zinc;
KW Zinc-finger.
FT CHAIN 1..406
FT /note="ADP-ribosylation factor GTPase-activating protein 1"
FT /id="PRO_0000074190"
FT DOMAIN 7..124
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT ZN_FING 22..45
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 297..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 135
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 189
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 231
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPJ9"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPJ9"
FT MOD_RES 350
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPJ9"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62848"
FT VAR_SEQ 1..57
FT /note="MASPRTRKVLKEVRVQDENNVCFECGAFNPQWVSVTYGIWICLECSGRHRGL
FT GVHLS -> MRTT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055739"
FT VAR_SEQ 1..34
FT /note="MASPRTRKVLKEVRVQDENNVCFECGAFNPQWVS -> MLSSESSWSLRRIT
FT ILAGPCRRSTTAEPRPSLGI (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055379"
FT VAR_SEQ 35..147
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055380"
FT VAR_SEQ 239
FT /note="K -> KFWGHKQQPEP (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_000298"
FT VAR_SEQ 279..406
FT /note="VQGVGSKGWRDVTTFFSGKAEGPLDSPSEGHSYQNSGLDHFQNSNIDQSFWE
FT TFGSAEPTKTRKSPSSDSWTCADTSTERRSSDSWEVWGSASTNRNSNSDGGEGGEGTKK
FT AVPPAVPTDDGWDNQNW -> CQRRLCCHQSHCSAGHLGRAFCPVSWHEALCGQTGREE
FT QASLLPPKHVVGALEVCARGCPRCHVPHTPGTAAEWPGRLCLSRESVVRDGGTSPPFFR
FT GKQRAPWTAPRRATVIRTAVWTTSKTAT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021818"
FT VAR_SEQ 279..280
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_000299"
FT VARIANT 184
FT /note="V -> M (in dbSNP:rs2273499)"
FT /id="VAR_015187"
FT CONFLICT 274
FT /note="Q -> R (in Ref. 1; BAB55009)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="R -> G (in Ref. 1; BAH12326)"
FT /evidence="ECO:0000305"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:3DWD"
FT TURN 17..20
FT /evidence="ECO:0007829|PDB:3DWD"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:3DWD"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:3DWD"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:3DWD"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:3DWD"
FT HELIX 43..52
FT /evidence="ECO:0007829|PDB:3DWD"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:3DWD"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:3DWD"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:3DWD"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:3DWD"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:3DWD"
FT HELIX 106..119
FT /evidence="ECO:0007829|PDB:3DWD"
SQ SEQUENCE 406 AA; 44668 MW; CAE41828DE660621 CRC64;
MASPRTRKVL KEVRVQDENN VCFECGAFNP QWVSVTYGIW ICLECSGRHR GLGVHLSFVR
SVTMDKWKDI ELEKMKAGGN AKFREFLESQ EDYDPCWSLQ EKYNSRAAAL FRDKVVALAE
GREWSLESSP AQNWTPPQPR TLPSMVHRVS GQPQSVTASS DKAFEDWLND DLGSYQGAQG
NRYVGFGNTP PPQKKEDDFL NNAMSSLYSG WSSFTTGASR FASAAKEGAT KFGSQASQKA
SELGHSLNEN VLKPAQEKVK EGKIFDDVSS GVSQLASKVQ GVGSKGWRDV TTFFSGKAEG
PLDSPSEGHS YQNSGLDHFQ NSNIDQSFWE TFGSAEPTKT RKSPSSDSWT CADTSTERRS
SDSWEVWGSA STNRNSNSDG GEGGEGTKKA VPPAVPTDDG WDNQNW
