GAPD1_HUMAN
ID GAPD1_HUMAN Reviewed; 1478 AA.
AC Q14C86; A8MYK3; B0QZ62; B0QZ63; B0QZ64; Q14C76; Q2Q1W1; Q8ND92; Q8WU86;
AC Q96CZ4; Q9NXQ1; Q9P207; Q9Y4N0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=GTPase-activating protein and VPS9 domain-containing protein 1;
DE AltName: Full=GAPex-5;
DE AltName: Full=Rab5-activating protein 6;
GN Name=GAPVD1; Synonyms=GAPEX5, KIAA1521, RAP6;
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 4), IDENTIFICATION BY MASS
RP SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RAB5A.
RX PubMed=16410077; DOI=10.1016/j.bbrc.2005.12.099;
RA Hunker C.M., Galvis A., Kruk I., Giambini H., Veisaga M.L., Barbieri M.A.;
RT "Rab5-activating protein 6, a novel endosomal protein with a role in
RT endocytosis.";
RL Biochem. Biophys. Res. Commun. 340:967-975(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Placenta;
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 [LARGE SCALE MRNA] OF 139-996 (ISOFORM 5).
RC TISSUE=Colon;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 675-1478 (ISOFORM 6).
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-390 AND SER-1019, 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1096, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-390 AND SER-1019, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-390; THR-458; SER-466;
RP THR-470; SER-566; SER-902; SER-903; SER-1019 AND SER-1096, 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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; SER-766; SER-902 AND
RP SER-1096, AND 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-390; SER-902; SER-966 AND
RP SER-1019, AND 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 [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-902, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227; THR-390; SER-466;
RP SER-746; SER-876; SER-902; SER-903; SER-1019 AND SER-1096, AND
RP 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-757 AND THR-762, 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).
CC -!- FUNCTION: Acts both as a GTPase-activating protein (GAP) and a guanine
CC nucleotide exchange factor (GEF), and participates in various processes
CC such as endocytosis, insulin receptor internalization or LC2A4/GLUT4
CC trafficking. Acts as a GEF for the Ras-related protein RAB31 by
CC exchanging bound GDP for free GTP, leading to regulate LC2A4/GLUT4
CC trafficking. In the absence of insulin, it maintains RAB31 in an active
CC state and promotes a futile cycle between LC2A4/GLUT4 storage vesicles
CC and early endosomes, retaining LC2A4/GLUT4 inside the cells. Upon
CC insulin stimulation, it is translocated to the plasma membrane,
CC releasing LC2A4/GLUT4 from intracellular storage vesicles. Also
CC involved in EGFR trafficking and degradation, possibly by promoting
CC EGFR ubiquitination and subsequent degradation by the proteasome. Has
CC GEF activity for Rab5 and GAP activity for Ras.
CC {ECO:0000269|PubMed:16410077}.
CC -!- SUBUNIT: Interacts with TRIP10/CIP4 (By similarity). Interacts with
CC RAB5A. {ECO:0000250, ECO:0000269|PubMed:16410077}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16410077};
CC Peripheral membrane protein {ECO:0000269|PubMed:16410077}. Endosome
CC {ECO:0000269|PubMed:16410077}. Note=Recruited to the plasma membrane by
CC TRIP10/CIP4 in response to insulin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q14C86-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14C86-2; Sequence=VSP_032362;
CC Name=3;
CC IsoId=Q14C86-3; Sequence=VSP_032361, VSP_032362;
CC Name=4;
CC IsoId=Q14C86-4; Sequence=VSP_032358, VSP_032362;
CC Name=5;
CC IsoId=Q14C86-5; Sequence=VSP_032359;
CC Name=6;
CC IsoId=Q14C86-6; Sequence=VSP_032360, VSP_032362;
CC -!- SIMILARITY: Belongs to the GAPVD1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21119.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH21119.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA90959.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA90959.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA96045.3; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ233254; ABB71126.1; -; mRNA.
DR EMBL; AB040954; BAA96045.3; ALT_INIT; mRNA.
DR EMBL; AL354710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL627223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87622.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87623.1; -; Genomic_DNA.
DR EMBL; BC013635; AAH13635.1; -; mRNA.
DR EMBL; BC021119; AAH21119.1; ALT_SEQ; mRNA.
DR EMBL; BC114937; AAI14938.1; -; mRNA.
DR EMBL; BC114962; AAI14963.1; -; mRNA.
DR EMBL; AK000126; BAA90959.1; ALT_SEQ; mRNA.
DR EMBL; AL080196; CAB45770.1; -; mRNA.
DR EMBL; AL834325; CAD38993.1; -; mRNA.
DR CCDS; CCDS35138.1; -. [Q14C86-6]
DR CCDS; CCDS65130.1; -. [Q14C86-4]
DR CCDS; CCDS65131.1; -. [Q14C86-2]
DR CCDS; CCDS65132.1; -. [Q14C86-1]
DR CCDS; CCDS83414.1; -. [Q14C86-3]
DR PIR; T12506; T12506.
DR RefSeq; NP_001269608.1; NM_001282679.1. [Q14C86-1]
DR RefSeq; NP_001269609.1; NM_001282680.1. [Q14C86-2]
DR RefSeq; NP_001269610.1; NM_001282681.1. [Q14C86-4]
DR RefSeq; NP_001317707.1; NM_001330778.1. [Q14C86-3]
DR RefSeq; NP_056450.2; NM_015635.3. [Q14C86-6]
DR RefSeq; XP_005251958.1; XM_005251901.3.
DR RefSeq; XP_005251961.1; XM_005251904.3. [Q14C86-3]
DR RefSeq; XP_006717107.1; XM_006717044.3.
DR RefSeq; XP_016870090.1; XM_017014601.1.
DR RefSeq; XP_016870091.1; XM_017014602.1.
DR RefSeq; XP_016870092.1; XM_017014603.1.
DR RefSeq; XP_016870093.1; XM_017014604.1.
DR RefSeq; XP_016870095.1; XM_017014606.1. [Q14C86-4]
DR RefSeq; XP_016870096.1; XM_017014607.1.
DR RefSeq; XP_016870097.1; XM_017014608.1.
DR RefSeq; XP_016870098.1; XM_017014609.1. [Q14C86-3]
DR AlphaFoldDB; Q14C86; -.
DR SMR; Q14C86; -.
DR BioGRID; 117568; 111.
DR IntAct; Q14C86; 28.
DR MINT; Q14C86; -.
DR STRING; 9606.ENSP00000377664; -.
DR GlyGen; Q14C86; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14C86; -.
DR MetOSite; Q14C86; -.
DR PhosphoSitePlus; Q14C86; -.
DR BioMuta; GAPVD1; -.
DR DMDM; 172046859; -.
DR EPD; Q14C86; -.
DR jPOST; Q14C86; -.
DR MassIVE; Q14C86; -.
DR MaxQB; Q14C86; -.
DR PaxDb; Q14C86; -.
DR PeptideAtlas; Q14C86; -.
DR PRIDE; Q14C86; -.
DR ProteomicsDB; 60308; -. [Q14C86-1]
DR ProteomicsDB; 60309; -. [Q14C86-2]
DR ProteomicsDB; 60310; -. [Q14C86-3]
DR ProteomicsDB; 60311; -. [Q14C86-4]
DR ProteomicsDB; 60312; -. [Q14C86-5]
DR ProteomicsDB; 60313; -. [Q14C86-6]
DR Antibodypedia; 30544; 101 antibodies from 18 providers.
DR DNASU; 26130; -.
DR Ensembl; ENST00000297933.11; ENSP00000297933.6; ENSG00000165219.23. [Q14C86-2]
DR Ensembl; ENST00000312123.13; ENSP00000309582.9; ENSG00000165219.23. [Q14C86-4]
DR Ensembl; ENST00000394104.6; ENSP00000377664.2; ENSG00000165219.23. [Q14C86-1]
DR Ensembl; ENST00000394105.6; ENSP00000377665.2; ENSG00000165219.23. [Q14C86-6]
DR Ensembl; ENST00000470056.5; ENSP00000419767.1; ENSG00000165219.23. [Q14C86-3]
DR Ensembl; ENST00000495955.5; ENSP00000419063.1; ENSG00000165219.23. [Q14C86-1]
DR GeneID; 26130; -.
DR KEGG; hsa:26130; -.
DR MANE-Select; ENST00000297933.11; ENSP00000297933.6; NM_001282680.3; NP_001269609.1. [Q14C86-2]
DR UCSC; uc004bpq.5; human. [Q14C86-1]
DR CTD; 26130; -.
DR DisGeNET; 26130; -.
DR GeneCards; GAPVD1; -.
DR HGNC; HGNC:23375; GAPVD1.
DR HPA; ENSG00000165219; Low tissue specificity.
DR MalaCards; GAPVD1; -.
DR MIM; 611714; gene.
DR neXtProt; NX_Q14C86; -.
DR OpenTargets; ENSG00000165219; -.
DR Orphanet; 656; Genetic steroid-resistant nephrotic syndrome.
DR PharmGKB; PA142671748; -.
DR VEuPathDB; HostDB:ENSG00000165219; -.
DR eggNOG; KOG2319; Eukaryota.
DR GeneTree; ENSGT00940000156611; -.
DR HOGENOM; CLU_002165_1_0_1; -.
DR InParanoid; Q14C86; -.
DR OMA; SCFLGKK; -.
DR PhylomeDB; Q14C86; -.
DR TreeFam; TF105908; -.
DR PathwayCommons; Q14C86; -.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q14C86; -.
DR BioGRID-ORCS; 26130; 10 hits in 985 CRISPR screens.
DR ChiTaRS; GAPVD1; human.
DR GeneWiki; GAPVD1; -.
DR GenomeRNAi; 26130; -.
DR Pharos; Q14C86; Tbio.
DR PRO; PR:Q14C86; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q14C86; protein.
DR Bgee; ENSG00000165219; Expressed in bronchial epithelial cell and 211 other tissues.
DR ExpressionAtlas; Q14C86; baseline and differential.
DR Genevisible; Q14C86; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0032794; F:GTPase activating protein binding; IMP:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IMP:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0051223; P:regulation of protein transport; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.506.10; -; 1.
DR Gene3D; 1.20.1050.80; -; 1.
DR InterPro; IPR041545; DUF5601.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR003123; VPS9.
DR InterPro; IPR045046; Vps9-like.
DR InterPro; IPR037191; VPS9_dom_sf.
DR PANTHER; PTHR23101; PTHR23101; 1.
DR Pfam; PF18151; DUF5601; 1.
DR Pfam; PF00616; RasGAP; 1.
DR Pfam; PF02204; VPS9; 1.
DR SMART; SM00167; VPS9; 1.
DR SUPFAM; SSF109993; SSF109993; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR PROSITE; PS51205; VPS9; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endocytosis; Endosome; GTPase activation;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1478
FT /note="GTPase-activating protein and VPS9 domain-containing
FT protein 1"
FT /id="PRO_0000324771"
FT DOMAIN 131..353
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT DOMAIN 1338..1478
FT /note="VPS9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00550"
FT REGION 574..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..979
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 390
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 458
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 470
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PAR5"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PAR5"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 762
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 766
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 876
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 902
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 903
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PAR5"
FT MOD_RES 966
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1019
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1046
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PAR5"
FT MOD_RES 1096
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 557..577
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16410077"
FT /id="VSP_032358"
FT VAR_SEQ 810..835
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032359"
FT VAR_SEQ 810
FT /note="G -> DFLYILQPKQHFQHIEAEADMRIQLSSS (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_032360"
FT VAR_SEQ 989..1015
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032361"
FT VAR_SEQ 1057..1074
FT /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16410077, ECO:0000303|PubMed:17974005"
FT /id="VSP_032362"
FT CONFLICT 294
FT /note="V -> E (in Ref. 1; ABB71126)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="C -> R (in Ref. 1; ABB71126)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="A -> T (in Ref. 7; BAA90959)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="S -> C (in Ref. 1; ABB71126)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="N -> D (in Ref. 7; BAA90959)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="L -> F (in Ref. 1; ABB71126)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="P -> L (in Ref. 1; ABB71126)"
FT /evidence="ECO:0000305"
FT CONFLICT 530
FT /note="M -> I (in Ref. 6; AAH21119)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="E -> G (in Ref. 7; BAA90959)"
FT /evidence="ECO:0000305"
FT CONFLICT 741
FT /note="C -> F (in Ref. 6; AAH21119)"
FT /evidence="ECO:0000305"
FT CONFLICT 902
FT /note="S -> G (in Ref. 7; BAA90959)"
FT /evidence="ECO:0000305"
FT CONFLICT 931
FT /note="P -> S (in Ref. 6; AAH13635)"
FT /evidence="ECO:0000305"
FT CONFLICT 1037
FT /note="R -> W (in Ref. 1; ABB71126)"
FT /evidence="ECO:0000305"
FT CONFLICT 1162
FT /note="L -> S (in Ref. 1; ABB71126)"
FT /evidence="ECO:0000305"
FT CONFLICT 1425
FT /note="V -> L (in Ref. 1; ABB71126)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1478 AA; 164980 MW; DD429B0EB207276C CRC64;
MVKLDIHTLA HHLKQERLYV NSEKQLIQRL NADVLKTAEK LYRTAWIAKQ QRINLDRLII
TSAEASPAEC CQHAKILEDT QFVDGYKQLG FQETAYGEFL SRLRENPRLI ASSLVAGEKL
NQENTQSVIY TVFTSLYGNC IMQEDESYLL QVLRYLIEFE LKESDNPRRL LRRGTCAFSI
LFKLFSEGLF SAKLFLTATL HEPIMQLLVE DEDHLETDPN KLIERFSPSQ QEKLFGEKGS
DRFRQKVQEM VESNEAKLVA LVNKFIGYLK QNTYCFPHSL RWIVSQMYKT LSCVDRLEVG
EVRAMCTDLL LACFICPAVV NPEQYGIISD APINEVARFN LMQVGRLLQQ LAMTGSEEGD
PRTKSSLGKF DKSCVAAFLD VVIGGRAVET PPLSSVNLLE GLSRTVVYIT YSQLITLVNF
MKSVMSGDQL REDRMALDNL LANLPPAKPG KSSSLEMTPY NTPQLSPATT PANKKNRLPI
ATRSRSRTNM LMDLHMDHEG SSQETIQEVQ PEEVLVISLG TGPQLTPGMM SENEVLNMQL
SDGGQGDVPV DENKLHGKPD KTLRFSLCSD NLEGISEGPS NRSNSVSSLD LEGESVSELG
AGPSGSNGVE ALQLLEHEQA TTQDNLDDKL RKFEIRDMMG LTDDRDISET VSETWSTDVL
GSDFDPNIDE DRLQEIAGAA AENMLGSLLC LPGSGSVLLD PCTGSTISET TSEAWSVEVL
PSDSEAPDLK QEERLQELES CSGLGSTSDD TDVREVSSRP STPGLSVVSG ISATSEDIPN
KIEDLRSECS SDFGGKDSVT SPDMDEITHG AHQLTSPPSQ SESLLAMFDP LSSHEGASAV
VRPKVHYARP SHPPPDPPIL EGAVGGNEAR LPNFGSHVLT PAEMEAFKQR HSYPERLVRS
RSSDIVSSVR RPMSDPSWNR RPGNEERELP PAAAIGATSL VAAPHSSSSS PSKDSSRGET
EERKDSDDEK SDRNRPWWRK RFVSAMPKAP IPFRKKEKQE KDKDDLGPDR FSTLTDDPSP
RLSAQAQVAE DILDKYRNAI KRTSPSDGAM ANYESTGDNH DRDLSSKLLY HSDKEVMGDG
ESAHDSPRDE ALQNISADDL PDSASQAAHP QDSAFSYRDA KKKLRLALCS ADSVAFPVLT
HSTRNGLPDH TDPEDNEIVC FLKVQIAEAI NLQDKNLMAQ LQETMRCVCR FDNRTCRKLL
ASIAEDYRKR APYIAYLTRC RQGLQTTQAH LERLLQRVLR DKEVANRYFT TVCVRLLLES
KEKKIREFIQ DFQKLTAADD KTAQVEDFLQ FLYGAMAQDV IWQNASEEQL QDAQLAIERS
VMNRIFKLAF YPNQDGDILR DQVLHEHIQR LSKVVTANHR ALQIPEVYLR EAPWPSAQSE
IRTISAYKTP RDKVQCILRM CSTIMNLLSL ANEDSVPGAD DFVPVLVFVL IKANPPCLLS
TVQYISSFYA SCLSGEESYW WMQFTAAVEF IKTIDDRK
