RBG1L_HUMAN
ID RBG1L_HUMAN Reviewed; 815 AA.
AC Q5R372; O75059; Q3ZTR8; Q5R369; Q8IVV0; Q8N921; Q8WV78; Q9NSP8; Q9UQ19;
AC Q9UQP5; Q9Y6Y5; Q9Y6Y6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Rab GTPase-activating protein 1-like;
GN Name=RABGAP1L {ECO:0000312|EMBL:CAI18937.1};
GN Synonyms=HHL {ECO:0000312|EMBL:AAQ76819.1},
GN KIAA0471 {ECO:0000312|EMBL:BAA32316.2};
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] {ECO:0000305, ECO:0000312|EMBL:BAA77332.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5; 6 AND 7).
RC TISSUE=Testis {ECO:0000312|EMBL:BAA77332.1};
RA Aihara T., Yasuo M., Kumiko K., Sasaki Y., Imaoka S., Monden M.,
RA Nakamura Y.;
RT "Genes preferentially expressed in precancerous lesion of HCC.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAA32316.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
RC TISSUE=Brain {ECO:0000312|EMBL:BAA32316.2};
RX PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA Nomura N., Ohara O.;
RT "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT human brain.";
RL DNA Res. 4:345-349(1997).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAA77332.1}
RP SEQUENCE REVISION.
RA Ohara O.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:BAA77332.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-570 (ISOFORM 3).
RA Rhodes S., Huckle E.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:BAC04635.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Chondrocyte {ECO:0000312|EMBL:BAC04635.1};
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 [6] {ECO:0000312|EMBL:CAH70225.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7] {ECO:0000305, ECO:0000312|EMBL:BAA77332.1}
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 [8] {ECO:0000305, ECO:0000312|EMBL:AAH41888.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 9), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 676-815 (ISOFORMS 1/3/4).
RC TISSUE=B-cell {ECO:0000312|EMBL:AAH18630.2},
RC Colon {ECO:0000312|EMBL:AAH12094.1}, and
RC Testis {ECO:0000312|EMBL:AAH41888.1};
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 [9] {ECO:0000305, ECO:0000312|EMBL:AAQ76819.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 333-815 (ISOFORM 4).
RX PubMed=16533400; DOI=10.1186/1471-2164-7-48;
RA Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P.,
RA Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.;
RT "NovelFam3000 -- uncharacterized human protein domains conserved across
RT model organisms.";
RL BMC Genomics 7:48-48(2006).
RN [10] {ECO:0000305}
RP INDUCTION.
RX PubMed=12706106; DOI=10.1016/s0888-7543(03)00023-5;
RA Sharma R., Samantaray S., Shukla N.K., Ralhan R.;
RT "Transcriptional gene expression profile of human esophageal squamous cell
RT carcinoma.";
RL Genomics 81:481-488(2003).
RN [11] {ECO:0000305}
RP INDUCTION.
RX PubMed=15367492; DOI=10.1093/hmg/ddh293;
RA de Yebra L., Adroer R., de Gregorio-Rocasolano N., Blesa R., Trullas R.,
RA Mahy N.;
RT "Reduced KIAA0471 mRNA expression in Alzheimer's patients: a new candidate
RT gene product linked to the disease?";
RL Hum. Mol. Genet. 13:2607-2612(2004).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHYLOGENETIC ANALYSIS.
RX PubMed=16923123; DOI=10.1111/j.1365-2443.2006.00997.x;
RA Itoh T., Satoh M., Kanno E., Fukuda M.;
RT "Screening for target Rabs of TBC (Tre-2/Bub2/Cdc16) domain-containing
RT proteins based on their Rab-binding activity.";
RL Genes Cells 11:1023-1037(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-471; SER-480 AND SER-490, 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 INVOLVEMENT IN AML, AND CHROMOSOMAL REARRANGEMENT.
RX PubMed=19184099; DOI=10.1007/s00428-009-0732-z;
RA Roberti M.C., La Starza R., Surace C., Sirleto P., Pinto R.M., Pierini V.,
RA Crescenzi B., Mecucci C., Angioni A.;
RT "RABGAP1L gene rearrangement resulting from a der(Y)t(Y;1)(q12;q25) in
RT acute myeloid leukemia arising in a child with Klinefelter syndrome.";
RL Virchows Arch. 454:311-316(2009).
RN [15]
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 [16]
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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [18]
RP INTERACTION WITH ANK2.
RX PubMed=27718357; DOI=10.7554/elife.20417;
RA Qu F., Lorenzo D.N., King S.J., Brooks R., Bear J.E., Bennett V.;
RT "Ankyrin-B is a PI3P effector that promotes polarized alpha5beta1-integrin
RT recycling via recruiting RabGAP1L to early endosomes.";
RL Elife 5:0-0(2016).
RN [19] {ECO:0000305, ECO:0000312|EMBL:BAA77332.1}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 507-815.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the RabGAP domain of the RABGAP1L protein.";
RL Submitted (JUL-2009) to the PDB data bank.
CC -!- FUNCTION: GTP-hydrolysis activating protein (GAP) for small GTPase
CC RAB22A, converting active RAB22A-GTP to the inactive form RAB22A-GDP
CC (PubMed:16923123). Plays a role in endocytosis and intracellular
CC protein transport. Recruited by ANK2 to phosphatidylinositol 3-
CC phosphate (PI3P)-positive early endosomes, where it inactivates RAB22A,
CC and promotes polarized trafficking to the leading edge of the migrating
CC cells. Part of the ANK2/RABGAP1L complex which is required for the
CC polarized recycling of fibronectin receptor ITGA5 ITGB1 to the plasma
CC membrane that enables continuous directional cell migration (By
CC similarity). {ECO:0000250|UniProtKB:A6H6A9,
CC ECO:0000269|PubMed:16923123}.
CC -!- SUBUNIT: Interacts (via Rab-GAP TBC domain) with ANK2 (via death
CC domain). {ECO:0000269|PubMed:27718357}.
CC -!- INTERACTION:
CC Q5R372-2; Q8TAL5: C9orf43; NbExp=3; IntAct=EBI-10692254, EBI-10694291;
CC Q5R372-2; Q03112: MECOM; NbExp=3; IntAct=EBI-10692254, EBI-1384862;
CC Q5R372-9; P55212: CASP6; NbExp=3; IntAct=EBI-10699389, EBI-718729;
CC Q5R372-9; P13473-2: LAMP2; NbExp=3; IntAct=EBI-10699389, EBI-21591415;
CC Q5R372-9; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-10699389, EBI-5280197;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:A6H6A9}. Early endosome
CC {ECO:0000269|PubMed:16923123}. Golgi apparatus
CC {ECO:0000269|PubMed:16923123}. Note=Colocalizes on endosomes partially
CC with EEA1 (PubMed:16923123). Colocalizes and cotransports on motile
CC vesicles with ANK2 (By similarity). {ECO:0000250|UniProtKB:A6H6A9,
CC ECO:0000269|PubMed:16923123}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=1 {ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:16710414};
CC IsoId=Q5R372-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16710414};
CC IsoId=Q5R372-2; Sequence=VSP_052916, VSP_052919, VSP_052920;
CC Name=3 {ECO:0000269|PubMed:16710414};
CC IsoId=Q5R372-3; Sequence=VSP_052917;
CC Name=4 {ECO:0000269|PubMed:16533400};
CC IsoId=Q5R372-4; Sequence=VSP_052918;
CC Name=5 {ECO:0000269|PubMed:16710414, ECO:0000269|Ref.1};
CC IsoId=Q5R372-5; Sequence=VSP_052915, VSP_035087, VSP_052924;
CC Name=6 {ECO:0000269|PubMed:16710414, ECO:0000269|Ref.1};
CC IsoId=Q5R372-6; Sequence=VSP_052915, VSP_052921, VSP_052924;
CC Name=7 {ECO:0000269|PubMed:16710414, ECO:0000269|Ref.1};
CC IsoId=Q5R372-7; Sequence=VSP_052913, VSP_052924;
CC Name=8 {ECO:0000269|PubMed:16710414, ECO:0000269|PubMed:9455484};
CC IsoId=Q5R372-8; Sequence=VSP_052914, VSP_052922, VSP_052924;
CC Name=9 {ECO:0000269|PubMed:15489334};
CC IsoId=Q5R372-9; Sequence=VSP_052912, VSP_052923;
CC Name=10; Synonyms=D;
CC IsoId=B7ZAP0-1; Sequence=External;
CC -!- INDUCTION: Up-regulated in esophageal squamous cell carcinomas.
CC Expression is strongly inhibited in the medial septum and hippocampus
CC brain regions of some Alzheimer disease patients.
CC {ECO:0000269|PubMed:12706106, ECO:0000269|PubMed:15367492}.
CC -!- DOMAIN: The arginine and glutamine fingers are critical for the GTPase-
CC activating mechanism, they pull out Rab's 'switch 2' glutamine and
CC insert in Rab's active site. {ECO:0000250}.
CC -!- DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of
CC acute leukemia, a cancer of the white blood cells. AML is a malignant
CC disease of bone marrow characterized by maturational arrest of
CC hematopoietic precursors at an early stage of development. Clonal
CC expansion of myeloid blasts occurs in bone marrow, blood, and other
CC tissue. Myelogenous leukemias develop from changes in cells that
CC normally produce neutrophils, basophils, eosinophils and monocytes.
CC {ECO:0000269|PubMed:19184099}. Note=The gene represented in this entry
CC may be involved in disease pathogenesis.
CC -!- DISEASE: Note=A chromosomal aberration involving RABGAP1L has been
CC found in bone marrow cells from a child with leukemia, acute
CC myelogenous. Translocation der(Y)t(Y;1)(q12;q25). The breakpoint at
CC 1q25 disrupts RABGAP1L. {ECO:0000269|PubMed:19184099}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA32316.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB019489; BAA77330.1; -; mRNA.
DR EMBL; AB019491; BAA77332.1; -; mRNA.
DR EMBL; AB019492; BAA77333.2; -; mRNA.
DR EMBL; AB019493; BAA77334.1; -; mRNA.
DR EMBL; AB007940; BAA32316.2; ALT_INIT; mRNA.
DR EMBL; AL049702; CAB41266.1; -; mRNA.
DR EMBL; AL157958; CAB76100.1; -; mRNA.
DR EMBL; AK095838; BAC04635.1; -; mRNA.
DR EMBL; AL021069; CAI23486.1; -; Genomic_DNA.
DR EMBL; AL022171; CAI23486.1; JOINED; Genomic_DNA.
DR EMBL; AL022400; CAI23486.1; JOINED; Genomic_DNA.
DR EMBL; AL031286; CAI23486.1; JOINED; Genomic_DNA.
DR EMBL; AL022171; CAI20382.1; -; Genomic_DNA.
DR EMBL; AL022400; CAI20382.1; JOINED; Genomic_DNA.
DR EMBL; AL031286; CAI20382.1; JOINED; Genomic_DNA.
DR EMBL; AL022171; CAI20383.1; -; Genomic_DNA.
DR EMBL; AL021069; CAI20383.1; JOINED; Genomic_DNA.
DR EMBL; AL022400; CAI20383.1; JOINED; Genomic_DNA.
DR EMBL; AL031286; CAI20383.1; JOINED; Genomic_DNA.
DR EMBL; AL022171; CAI20384.1; -; Genomic_DNA.
DR EMBL; AL022400; CAI20384.1; JOINED; Genomic_DNA.
DR EMBL; AL031286; CAI20384.1; JOINED; Genomic_DNA.
DR EMBL; AL136377; CAI20384.1; JOINED; Genomic_DNA.
DR EMBL; AL161671; CAI20384.1; JOINED; Genomic_DNA.
DR EMBL; AL591108; CAI20384.1; JOINED; Genomic_DNA.
DR EMBL; Z99127; CAI20384.1; JOINED; Genomic_DNA.
DR EMBL; AL022400; CAI22876.1; -; Genomic_DNA.
DR EMBL; AL022171; CAI22876.1; JOINED; Genomic_DNA.
DR EMBL; AL031286; CAI22876.1; JOINED; Genomic_DNA.
DR EMBL; AL022400; CAI22877.1; -; Genomic_DNA.
DR EMBL; AL021069; CAI22877.1; JOINED; Genomic_DNA.
DR EMBL; AL022171; CAI22877.1; JOINED; Genomic_DNA.
DR EMBL; AL031286; CAI22877.1; JOINED; Genomic_DNA.
DR EMBL; AL022400; CAI22878.1; -; Genomic_DNA.
DR EMBL; AL022171; CAI22878.1; JOINED; Genomic_DNA.
DR EMBL; AL031286; CAI22878.1; JOINED; Genomic_DNA.
DR EMBL; AL136377; CAI22878.1; JOINED; Genomic_DNA.
DR EMBL; AL161671; CAI22878.1; JOINED; Genomic_DNA.
DR EMBL; AL591108; CAI22878.1; JOINED; Genomic_DNA.
DR EMBL; Z99127; CAI22878.1; JOINED; Genomic_DNA.
DR EMBL; AL031286; CAI22380.1; -; Genomic_DNA.
DR EMBL; AL022171; CAI22380.1; JOINED; Genomic_DNA.
DR EMBL; AL022400; CAI22380.1; JOINED; Genomic_DNA.
DR EMBL; AL031286; CAI22381.1; -; Genomic_DNA.
DR EMBL; AL021069; CAI22381.1; JOINED; Genomic_DNA.
DR EMBL; AL022171; CAI22381.1; JOINED; Genomic_DNA.
DR EMBL; AL022400; CAI22381.1; JOINED; Genomic_DNA.
DR EMBL; AL031286; CAI22382.1; -; Genomic_DNA.
DR EMBL; AL022171; CAI22382.1; JOINED; Genomic_DNA.
DR EMBL; AL022400; CAI22382.1; JOINED; Genomic_DNA.
DR EMBL; AL136377; CAI22382.1; JOINED; Genomic_DNA.
DR EMBL; AL161671; CAI22382.1; JOINED; Genomic_DNA.
DR EMBL; AL591108; CAI22382.1; JOINED; Genomic_DNA.
DR EMBL; Z99127; CAI22382.1; JOINED; Genomic_DNA.
DR EMBL; AL136377; CAI22932.1; -; Genomic_DNA.
DR EMBL; AL161671; CAI22932.1; JOINED; Genomic_DNA.
DR EMBL; Z99127; CAI22932.1; JOINED; Genomic_DNA.
DR EMBL; AL136377; CAI22933.1; -; Genomic_DNA.
DR EMBL; AL161671; CAI22933.1; JOINED; Genomic_DNA.
DR EMBL; Z99127; CAI22933.1; JOINED; Genomic_DNA.
DR EMBL; AL136377; CAI22934.1; -; Genomic_DNA.
DR EMBL; AL161671; CAI22934.1; JOINED; Genomic_DNA.
DR EMBL; Z99127; CAI22934.1; JOINED; Genomic_DNA.
DR EMBL; AL136377; CAI22935.1; -; Genomic_DNA.
DR EMBL; AL022171; CAI22935.1; JOINED; Genomic_DNA.
DR EMBL; AL022400; CAI22935.1; JOINED; Genomic_DNA.
DR EMBL; AL031286; CAI22935.1; JOINED; Genomic_DNA.
DR EMBL; AL161671; CAI22935.1; JOINED; Genomic_DNA.
DR EMBL; AL591108; CAI22935.1; JOINED; Genomic_DNA.
DR EMBL; Z99127; CAI22935.1; JOINED; Genomic_DNA.
DR EMBL; AL161671; CAI16277.1; -; Genomic_DNA.
DR EMBL; Z99127; CAI16277.1; JOINED; Genomic_DNA.
DR EMBL; AL161671; CAI16278.1; -; Genomic_DNA.
DR EMBL; AL136377; CAI16278.1; JOINED; Genomic_DNA.
DR EMBL; Z99127; CAI16278.1; JOINED; Genomic_DNA.
DR EMBL; AL161671; CAI16279.1; -; Genomic_DNA.
DR EMBL; AL136377; CAI16279.1; JOINED; Genomic_DNA.
DR EMBL; Z99127; CAI16279.1; JOINED; Genomic_DNA.
DR EMBL; AL161671; CAI16280.1; -; Genomic_DNA.
DR EMBL; AL136377; CAI16280.1; JOINED; Genomic_DNA.
DR EMBL; Z99127; CAI16280.1; JOINED; Genomic_DNA.
DR EMBL; AL161671; CAI16281.1; -; Genomic_DNA.
DR EMBL; AL022171; CAI16281.1; JOINED; Genomic_DNA.
DR EMBL; AL022400; CAI16281.1; JOINED; Genomic_DNA.
DR EMBL; AL031286; CAI16281.1; JOINED; Genomic_DNA.
DR EMBL; AL136377; CAI16281.1; JOINED; Genomic_DNA.
DR EMBL; AL591108; CAI16281.1; JOINED; Genomic_DNA.
DR EMBL; Z99127; CAI16281.1; JOINED; Genomic_DNA.
DR EMBL; AL591108; CAH70225.1; -; Genomic_DNA.
DR EMBL; AL022171; CAH70225.1; JOINED; Genomic_DNA.
DR EMBL; AL022400; CAH70225.1; JOINED; Genomic_DNA.
DR EMBL; AL031286; CAH70225.1; JOINED; Genomic_DNA.
DR EMBL; AL136377; CAH70225.1; JOINED; Genomic_DNA.
DR EMBL; AL161671; CAH70225.1; JOINED; Genomic_DNA.
DR EMBL; Z99127; CAH70225.1; JOINED; Genomic_DNA.
DR EMBL; Z99127; CAI18933.1; -; Genomic_DNA.
DR EMBL; AL161671; CAI18933.1; JOINED; Genomic_DNA.
DR EMBL; Z99127; CAI18934.1; -; Genomic_DNA.
DR EMBL; AL136377; CAI18934.1; JOINED; Genomic_DNA.
DR EMBL; AL161671; CAI18934.1; JOINED; Genomic_DNA.
DR EMBL; Z99127; CAI18935.1; -; Genomic_DNA.
DR EMBL; AL136377; CAI18935.1; JOINED; Genomic_DNA.
DR EMBL; AL161671; CAI18935.1; JOINED; Genomic_DNA.
DR EMBL; Z99127; CAI18936.1; -; Genomic_DNA.
DR EMBL; AL136377; CAI18936.1; JOINED; Genomic_DNA.
DR EMBL; AL161671; CAI18936.1; JOINED; Genomic_DNA.
DR EMBL; Z99127; CAI18937.1; -; Genomic_DNA.
DR EMBL; AL022171; CAI18937.1; JOINED; Genomic_DNA.
DR EMBL; AL022400; CAI18937.1; JOINED; Genomic_DNA.
DR EMBL; AL031286; CAI18937.1; JOINED; Genomic_DNA.
DR EMBL; AL136377; CAI18937.1; JOINED; Genomic_DNA.
DR EMBL; AL161671; CAI18937.1; JOINED; Genomic_DNA.
DR EMBL; AL591108; CAI18937.1; JOINED; Genomic_DNA.
DR EMBL; CH471067; EAW90977.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW90979.1; -; Genomic_DNA.
DR EMBL; BC012094; AAH12094.1; -; mRNA.
DR EMBL; BC018630; AAH18630.2; -; mRNA.
DR EMBL; BC041888; AAH41888.1; -; mRNA.
DR EMBL; AY364260; AAQ76819.1; -; mRNA.
DR CCDS; CCDS1314.1; -. [Q5R372-1]
DR CCDS; CCDS41437.1; -. [Q5R372-9]
DR CCDS; CCDS58046.1; -. [Q5R372-8]
DR RefSeq; NP_001030307.1; NM_001035230.2. [Q5R372-9]
DR RefSeq; NP_001230692.1; NM_001243763.1. [Q5R372-9]
DR RefSeq; NP_001230694.1; NM_001243765.1. [Q5R372-8]
DR RefSeq; NP_055672.3; NM_014857.4. [Q5R372-1]
DR PDB; 3HZJ; X-ray; 2.30 A; A/B/C=507-815.
DR PDBsum; 3HZJ; -.
DR AlphaFoldDB; Q5R372; -.
DR SMR; Q5R372; -.
DR BioGRID; 115239; 116.
DR IntAct; Q5R372; 43.
DR STRING; 9606.ENSP00000251507; -.
DR iPTMnet; Q5R372; -.
DR MetOSite; Q5R372; -.
DR PhosphoSitePlus; Q5R372; -.
DR BioMuta; RABGAP1L; -.
DR DMDM; 205829393; -.
DR EPD; Q5R372; -.
DR jPOST; Q5R372; -.
DR MassIVE; Q5R372; -.
DR MaxQB; Q5R372; -.
DR PaxDb; Q5R372; -.
DR PeptideAtlas; Q5R372; -.
DR PRIDE; Q5R372; -.
DR ProteomicsDB; 63709; -. [Q5R372-1]
DR ProteomicsDB; 63710; -. [Q5R372-2]
DR ProteomicsDB; 63711; -. [Q5R372-3]
DR ProteomicsDB; 63712; -. [Q5R372-4]
DR ProteomicsDB; 63713; -. [Q5R372-5]
DR ProteomicsDB; 63714; -. [Q5R372-6]
DR ProteomicsDB; 63715; -. [Q5R372-7]
DR ProteomicsDB; 63716; -. [Q5R372-8]
DR ProteomicsDB; 63717; -. [Q5R372-9]
DR Antibodypedia; 34402; 80 antibodies from 21 providers.
DR DNASU; 9910; -.
DR Ensembl; ENST00000251507.8; ENSP00000251507.4; ENSG00000152061.24. [Q5R372-1]
DR Ensembl; ENST00000325589.9; ENSP00000318603.5; ENSG00000152061.24. [Q5R372-7]
DR Ensembl; ENST00000347255.6; ENSP00000281844.5; ENSG00000152061.24. [Q5R372-5]
DR Ensembl; ENST00000357444.10; ENSP00000350027.6; ENSG00000152061.24. [Q5R372-2]
DR Ensembl; ENST00000367687.5; ENSP00000356660.1; ENSG00000152061.24. [Q5R372-6]
DR Ensembl; ENST00000478442.5; ENSP00000434600.1; ENSG00000152061.24. [Q5R372-9]
DR Ensembl; ENST00000486220.5; ENSP00000432490.1; ENSG00000152061.24. [Q5R372-9]
DR Ensembl; ENST00000489615.5; ENSP00000420660.1; ENSG00000152061.24. [Q5R372-8]
DR GeneID; 9910; -.
DR UCSC; uc001gjw.4; human. [Q5R372-1]
DR CTD; 9910; -.
DR DisGeNET; 9910; -.
DR GeneCards; RABGAP1L; -.
DR HGNC; HGNC:24663; RABGAP1L.
DR HPA; ENSG00000152061; Tissue enhanced (heart).
DR MIM; 601626; phenotype.
DR MIM; 609238; gene.
DR neXtProt; NX_Q5R372; -.
DR OpenTargets; ENSG00000152061; -.
DR PharmGKB; PA134940645; -.
DR VEuPathDB; HostDB:ENSG00000152061; -.
DR eggNOG; KOG1102; Eukaryota.
DR GeneTree; ENSGT00940000154611; -.
DR HOGENOM; CLU_007394_1_1_1; -.
DR InParanoid; Q5R372; -.
DR OMA; XDSAQES; -.
DR OrthoDB; 191811at2759; -.
DR PhylomeDB; Q5R372; -.
DR TreeFam; TF317184; -.
DR PathwayCommons; Q5R372; -.
DR SignaLink; Q5R372; -.
DR BioGRID-ORCS; 9910; 20 hits in 1083 CRISPR screens.
DR ChiTaRS; RABGAP1L; human.
DR EvolutionaryTrace; Q5R372; -.
DR GenomeRNAi; 9910; -.
DR Pharos; Q5R372; Tbio.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5R372; protein.
DR Bgee; ENSG00000152061; Expressed in calcaneal tendon and 203 other tissues.
DR ExpressionAtlas; Q5R372; baseline and differential.
DR Genevisible; Q5R372; HS.
DR GO; GO:0005769; C:early endosome; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0031267; F:small GTPase binding; IDA:BHF-UCL.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032880; P:regulation of protein localization; IDA:MGI.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR InterPro; IPR042809; RABGAP1L.
DR PANTHER; PTHR22957:SF205; PTHR22957:SF205; 1.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosomal rearrangement;
KW Cytoplasmic vesicle; Endocytosis; Endosome; Golgi apparatus;
KW GTPase activation; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..815
FT /note="Rab GTPase-activating protein 1-like"
FT /id="PRO_0000348054"
FT DOMAIN 126..282
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 538..724
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 580
FT /note="Arginine finger"
FT /evidence="ECO:0000250"
FT SITE 621
FT /note="Glutamine finger"
FT /evidence="ECO:0000250"
FT MOD_RES 471
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..743
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_052912"
FT VAR_SEQ 1..693
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:16710414, ECO:0000303|Ref.1"
FT /id="VSP_052913"
FT VAR_SEQ 1..681
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:16710414,
FT ECO:0000303|PubMed:9455484"
FT /id="VSP_052914"
FT VAR_SEQ 1..673
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:16710414, ECO:0000303|Ref.1"
FT /id="VSP_052915"
FT VAR_SEQ 10..46
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16710414"
FT /id="VSP_052916"
FT VAR_SEQ 291
FT /note="F -> FRLLVIPIPFEYF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16710414, ECO:0000303|Ref.4"
FT /id="VSP_052917"
FT VAR_SEQ 478..492
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16533400"
FT /id="VSP_052918"
FT VAR_SEQ 571..642
FT /note="DSAQESVITRDIHRTFPAHDYFKDTGGDGQESLYKICKAYSVYDEDIGYCQG
FT QSFLAAVLLLHMPEEQAFCV -> QQMKFSLTPRQTIHLVKYEGSMKVSMTPCNQLQFD
FT IRLDVLITYTFCFSSFPEPELYKYVLKHQLIKRLNAC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16710414"
FT /id="VSP_052919"
FT VAR_SEQ 643..815
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16710414"
FT /id="VSP_052920"
FT VAR_SEQ 674..675
FT /note="MQ -> M (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16710414, ECO:0000303|Ref.1"
FT /id="VSP_052921"
FT VAR_SEQ 675
FT /note="Q -> K (in isoform 5)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_035087"
FT VAR_SEQ 682..737
FT /note="HSHFSDLNLEAHMYASQWFLTLFTAKFPLCMVFHIIDLLLCEGLNIIFHVAL
FT ALLK -> MEEGVPCPAPAAKLTPPVKKSQDMHDERSKLVNEYACRVLELLGMGHRLFV
FT PRLLA (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:16710414,
FT ECO:0000303|PubMed:9455484"
FT /id="VSP_052922"
FT VAR_SEQ 744..780
FT /note="LQADFEGALKFFRVQLPKRYRAEENARRLMEQACNIK -> MMEEISIMVAY
FT DAHVFSQLHDEDFLTSLVAISKPRSM (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_052923"
FT VAR_SEQ 812..815
FT /note="FVYL -> RENRRLQEASMRLEQENDDLAHELVTSKIALRNDLDQAEDKADV
FT LNKELLLTKQRLVETEEEKRKQEEETAQLKEVFRKQLEKAEYEIKKTTAIIAEYKQICS
FT QLSTRLEKQQAASKEELEVVKGKMMACKHCSDIFSKEGALKLAATGREDQGIETDDEKD
FT SLKKQLREMELELAQTKLQLVEAKCKIQELEHQRGALMNEIQAAKNSWFSKTLNSIKTA
FT TGTQPLQPAPVTQPPKEST (in isoform 5, isoform 6, isoform 7 and
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:16710414,
FT ECO:0000303|PubMed:9455484, ECO:0000303|Ref.1"
FT /id="VSP_052924"
FT VARIANT 277
FT /note="S -> G (in dbSNP:rs7339904)"
FT /id="VAR_052533"
FT CONFLICT 311
FT /note="K -> R (in Ref. 5; BAC04635)"
FT /evidence="ECO:0000305"
FT HELIX 513..521
FT /evidence="ECO:0007829|PDB:3HZJ"
FT HELIX 531..537
FT /evidence="ECO:0007829|PDB:3HZJ"
FT HELIX 541..543
FT /evidence="ECO:0007829|PDB:3HZJ"
FT HELIX 544..551
FT /evidence="ECO:0007829|PDB:3HZJ"
FT HELIX 558..567
FT /evidence="ECO:0007829|PDB:3HZJ"
FT HELIX 575..582
FT /evidence="ECO:0007829|PDB:3HZJ"
FT TURN 590..592
FT /evidence="ECO:0007829|PDB:3HZJ"
FT HELIX 598..613
FT /evidence="ECO:0007829|PDB:3HZJ"
FT TURN 615..617
FT /evidence="ECO:0007829|PDB:3HZJ"
FT HELIX 623..633
FT /evidence="ECO:0007829|PDB:3HZJ"
FT HELIX 636..648
FT /evidence="ECO:0007829|PDB:3HZJ"
FT HELIX 652..655
FT /evidence="ECO:0007829|PDB:3HZJ"
FT HELIX 657..677
FT /evidence="ECO:0007829|PDB:3HZJ"
FT HELIX 679..688
FT /evidence="ECO:0007829|PDB:3HZJ"
FT HELIX 692..694
FT /evidence="ECO:0007829|PDB:3HZJ"
FT HELIX 697..702
FT /evidence="ECO:0007829|PDB:3HZJ"
FT TURN 703..707
FT /evidence="ECO:0007829|PDB:3HZJ"
FT HELIX 710..723
FT /evidence="ECO:0007829|PDB:3HZJ"
FT HELIX 727..738
FT /evidence="ECO:0007829|PDB:3HZJ"
FT HELIX 740..744
FT /evidence="ECO:0007829|PDB:3HZJ"
FT HELIX 748..756
FT /evidence="ECO:0007829|PDB:3HZJ"
FT HELIX 758..761
FT /evidence="ECO:0007829|PDB:3HZJ"
FT HELIX 766..778
FT /evidence="ECO:0007829|PDB:3HZJ"
FT HELIX 783..796
FT /evidence="ECO:0007829|PDB:3HZJ"
SQ SEQUENCE 815 AA; 92513 MW; 6928AEB23DDD0D3E CRC64;
MEVRASLQKV SGSSDSVATM NSEEFVLVPQ YADDNSTKHE EKPQLKIVSN GDEQLEKAME
EILRDSEKRP SSLLVDCQSS SEISDHSFGD IPASQTNKPS LQLILDPSNT EISTPRPSSP
GGLPEEDSVL FNKLTYLGCM KVSSPRNEVE ALRAMATMKS SSQYPFPVTL YVPNVPEGSV
RIIDQSSNVE IASFPIYKVL FCARGHDGTT ESNCFAFTES SHGSEEFQIH VFSCEIKEAV
SRILYSFCTA FKRSSRQVSD VKDSVIPTPD SDVFTFSVSL EVKEDDGKGN FSPVPKDRDK
FYFKLKQGIE KKVVITVQQL SNKELAIERC FGMLLSPGRN VKNSDMHLLD MESMGKSYDG
RAYVITGMWN PNAPVFLALN EETPKDKQVY MTVAVDMVVT EVVEPVRFLL ETVVRVYPAN
ERFWYFSRKT FTETFFMRLK QSEGKGHTNA GDAIYEVVSL QRESDKEEPV TPTSGGGPMS
PQDDEAEEES DNELSSGTGD VSKDCPEKIL YSWGELLGKW HSNLGARPKG LSTLVKSGVP
EALRAEVWQL LAGCHDNQAM LDRYRILITK DSAQESVITR DIHRTFPAHD YFKDTGGDGQ
ESLYKICKAY SVYDEDIGYC QGQSFLAAVL LLHMPEEQAF CVLVKIMYDY GLRDLYRNNF
EDLHCKFYQL ERLMQEQLPD LHSHFSDLNL EAHMYASQWF LTLFTAKFPL CMVFHIIDLL
LCEGLNIIFH VALALLKTSK EDLLQADFEG ALKFFRVQLP KRYRAEENAR RLMEQACNIK
VPTKKLKKYE KEYQTMRESQ LQQEDPMDRY KFVYL
