RBCC

RABGAP1L (HHL, KIAA0471) [Confidence: low (only semi-automatic identification from reviews)]
Rab GTPase-activating protein 1-like

UniProt Q5R372
ID RBG1L_HUMAN Reviewed; 815 AA.
AC Q5R372; O75059; Q3ZTR8; Q5R369; Q8IVV0; Q8N921; Q8WV78; Q9NSP8;
read moreAC Q9UQ19; Q9UQP5; Q9Y6Y5; Q9Y6Y6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 22-JAN-2014, entry version 66.
DE RecName: Full=Rab GTPase-activating protein 1-like;
GN Name=RABGAP1L; Synonyms=HHL, KIAA0471;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5; 6 AND 7).
RC TISSUE=Testis;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
RC TISSUE=Brain;
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
RT from human brain.";
RL DNA Res. 4:345-349(1997).
RN [3]
RP SEQUENCE REVISION.
RA Ohara O.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9), AND NUCLEOTIDE
RP SEQUENCE [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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Chondrocyte;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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]
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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 9), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 676-815 (ISOFORMS 1/3/4).
RC TISSUE=B-cell, Colon, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
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
RT across model organisms.";
RL BMC Genomics 7:48-48(2006).
RN [10]
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
RT cell carcinoma.";
RL Genomics 81:481-488(2003).
RN [11]
RP INDUCTION.
RX PubMed=15367492; DOI=10.1093/hmg/ddh293;
RA de Yebra L., Adroer R., de Gregorio-Rocasolano N., Blesa R.,
RA Trullas R., Mahy N.;
RT "Reduced KIAA0471 mRNA expression in Alzheimer's patients: a new
RT candidate gene product linked to the disease?";
RL Hum. Mol. Genet. 13:2607-2612(2004).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-471; SER-480 AND
RP SER-490, AND MASS SPECTROMETRY.
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 [13]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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.,
RA Buerckstuemmer T., 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 [15]
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=1;
CC IsoId=Q5R372-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5R372-2; Sequence=VSP_052916, VSP_052919, VSP_052920;
CC Name=3;
CC IsoId=Q5R372-3; Sequence=VSP_052917;
CC Name=4;
CC IsoId=Q5R372-4; Sequence=VSP_052918;
CC Name=5;
CC IsoId=Q5R372-5; Sequence=VSP_052915, VSP_035087, VSP_052924;
CC Name=6;
CC IsoId=Q5R372-6; Sequence=VSP_052915, VSP_052921, VSP_052924;
CC Name=7;
CC IsoId=Q5R372-7; Sequence=VSP_052913, VSP_052924;
CC Name=8;
CC IsoId=Q5R372-8; Sequence=VSP_052914, VSP_052922, VSP_052924;
CC Name=9;
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
CC hippocampus brain regions of some Alzheimer disease patients.
CC -!- SIMILARITY: Contains 1 PID domain.
CC -!- SIMILARITY: Contains 1 Rab-GAP TBC domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA32316.2; Type=Erroneous initiation;
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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 RefSeq; NP_001030307.1; NM_001035230.2.
DR RefSeq; NP_001230692.1; NM_001243763.1.
DR RefSeq; NP_001230694.1; NM_001243765.1.
DR RefSeq; NP_055672.3; NM_014857.4.
DR RefSeq; XP_005245740.1; XM_005245683.1.
DR UniGene; Hs.585378; -.
DR UniGene; Hs.744937; -.
DR PDB; 3HZJ; X-ray; 2.30 A; A/B/C=507-815.
DR PDBsum; 3HZJ; -.
DR ProteinModelPortal; Q5R372; -.
DR SMR; Q5R372; 510-797.
DR IntAct; Q5R372; 4.
DR PhosphoSite; Q5R372; -.
DR DMDM; 205829393; -.
DR PaxDb; Q5R372; -.
DR PRIDE; Q5R372; -.
DR Ensembl; ENST00000251507; ENSP00000251507; ENSG00000152061.
DR Ensembl; ENST00000325589; ENSP00000318603; ENSG00000152061.
DR Ensembl; ENST00000347255; ENSP00000281844; ENSG00000152061.
DR Ensembl; ENST00000357444; ENSP00000350027; ENSG00000152061.
DR Ensembl; ENST00000367687; ENSP00000356660; ENSG00000152061.
DR Ensembl; ENST00000457696; ENSP00000403136; ENSG00000152061.
DR Ensembl; ENST00000478442; ENSP00000434600; ENSG00000152061.
DR Ensembl; ENST00000486220; ENSP00000432490; ENSG00000152061.
DR Ensembl; ENST00000489615; ENSP00000420660; ENSG00000152061.
DR GeneID; 9910; -.
DR KEGG; hsa:9910; -.
DR UCSC; uc001gjx.3; human.
DR CTD; 9910; -.
DR GeneCards; GC01P174128; -.
DR H-InvDB; HIX0022205; -.
DR HGNC; HGNC:24663; RABGAP1L.
DR MIM; 609238; gene.
DR neXtProt; NX_Q5R372; -.
DR PharmGKB; PA134940645; -.
DR eggNOG; COG5210; -.
DR HOVERGEN; HBG063892; -.
DR OMA; EGDGQES; -.
DR PhylomeDB; Q5R372; -.
DR ChiTaRS; RABGAP1L; human.
DR EvolutionaryTrace; Q5R372; -.
DR GenomeRNAi; 9910; -.
DR NextBio; 37381; -.
DR PRO; PR:Q5R372; -.
DR ArrayExpress; Q5R372; -.
DR Bgee; Q5R372; -.
DR Genevestigator; Q5R372; -.
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:0005097; F:Rab GTPase activator activity; IDA:MGI.
DR GO; GO:0017137; F:Rab GTPase binding; IDA:BHF-UCL.
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.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF00640; PID; 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; Complete proteome;
KW GTPase activation; Phosphoprotein; Polymorphism; Reference proteome;
KW Ribosomal frameshifting.
FT CHAIN 1 815 Rab GTPase-activating protein 1-like.
FT /FTId=PRO_0000348054.
FT DOMAIN 126 282 PID.
FT DOMAIN 538 724 Rab-GAP TBC.
FT MOD_RES 471 471 Phosphothreonine.
FT MOD_RES 480 480 Phosphoserine.
FT MOD_RES 490 490 Phosphoserine.
FT VAR_SEQ 1 743 Missing (in isoform 9).
FT /FTId=VSP_052912.
FT VAR_SEQ 1 693 Missing (in isoform 7).
FT /FTId=VSP_052913.
FT VAR_SEQ 1 681 Missing (in isoform 8).
FT /FTId=VSP_052914.
FT VAR_SEQ 1 673 Missing (in isoform 5 and isoform 6).
FT /FTId=VSP_052915.
FT VAR_SEQ 10 46 Missing (in isoform 2).
FT /FTId=VSP_052916.
FT VAR_SEQ 291 291 F -> FRLLVIPIPFEYF (in isoform 3).
FT /FTId=VSP_052917.
FT VAR_SEQ 478 492 Missing (in isoform 4).
FT /FTId=VSP_052918.
FT VAR_SEQ 571 642 DSAQESVITRDIHRTFPAHDYFKDTGGDGQESLYKICKAYS
FT VYDEDIGYCQGQSFLAAVLLLHMPEEQAFCV -> QQMKFS
FT LTPRQTIHLVKYEGSMKVSMTPCNQLQFDIRLDVLITYTFC
FT FSSFPEPELYKYVLKHQLIKRLNAC (in isoform 2).
FT /FTId=VSP_052919.
FT VAR_SEQ 643 815 Missing (in isoform 2).
FT /FTId=VSP_052920.
FT VAR_SEQ 674 675 MQ -> M (in isoform 6).
FT /FTId=VSP_052921.
FT VAR_SEQ 675 675 Q -> K (in isoform 5).
FT /FTId=VSP_035087.
FT VAR_SEQ 682 737 HSHFSDLNLEAHMYASQWFLTLFTAKFPLCMVFHIIDLLLC
FT EGLNIIFHVALALLK -> MEEGVPCPAPAAKLTPPVKKSQ
FT DMHDERSKLVNEYACRVLELLGMGHRLFVPRLLA (in
FT isoform 8).
FT /FTId=VSP_052922.
FT VAR_SEQ 744 780 LQADFEGALKFFRVQLPKRYRAEENARRLMEQACNIK ->
FT MMEEISIMVAYDAHVFSQLHDEDFLTSLVAISKPRSM (in
FT isoform 9).
FT /FTId=VSP_052923.
FT VAR_SEQ 812 815 FVYL -> RENRRLQEASMRLEQENDDLAHELVTSKIALRN
FT DLDQAEDKADVLNKELLLTKQRLVETEEEKRKQEEETAQLK
FT EVFRKQLEKAEYEIKKTTAIIAEYKQICSQLSTRLEKQQAA
FT SKEELEVVKGKMMACKHCSDIFSKEGALKLAATGREDQGIE
FT TDDEKDSLKKQLREMELELAQTKLQLVEAKCKIQELEHQRG
FT ALMNEIQAAKNSWFSKTLNSIKTATGTQPLQPAPVTQPPKE
FT ST (in isoform 5, isoform 6, isoform 7
FT and isoform 8).
FT /FTId=VSP_052924.
FT VARIANT 277 277 S -> G (in dbSNP:rs7339904).
FT /FTId=VAR_052533.
FT CONFLICT 311 311 K -> R (in Ref. 5; BAC04635).
FT HELIX 513 521
FT HELIX 531 537
FT HELIX 541 543
FT HELIX 544 551
FT HELIX 558 567
FT HELIX 575 582
FT TURN 590 592
FT HELIX 598 613
FT TURN 615 617
FT HELIX 623 633
FT HELIX 636 648
FT HELIX 652 655
FT HELIX 657 677
FT HELIX 679 688
FT HELIX 692 694
FT HELIX 697 702
FT TURN 703 707
FT HELIX 710 723
FT HELIX 727 738
FT HELIX 740 744
FT HELIX 748 756
FT HELIX 758 761
FT HELIX 766 778
FT HELIX 783 796
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
//

MIM 609238
*RECORD*
*FIELD* NO
609238
*FIELD* TI
*609238 RAB GTPase-ACTIVATING PROTEIN 1-LIKE; RABGAP1L
;;TBC1 DOMAIN FAMILY, MEMBER 18; TBC1D18;;
read moreKIAA0471
*FIELD* TX

CLONING

By sequencing clones obtained from a size-fractionated brain cDNA
library, Seki et al. (1997) cloned RABGAP1L, which they designated
KIAA0471. The transcript contains an Alu element in the 3-prime UTR. The
deduced protein contains 370 amino acids. SDS-PAGE detected RABGAP1L at
an apparent molecular mass of about 50 kD.

Using RT-PCR, Ishikawa et al. (1997) found ubiquitous RABGAP1L
expression. Highest expression was in placenta, liver, kidney, and small
intestine, and lowest expression was in skeletal muscle and spleen.

Hidaka et al. (2000) cloned mouse Rabgap1l, which they designated Hhl.
The deduced 298-amino acid protein contains a PTB domain and shares
homology with the N terminus of human GAPCENA (RABGAP1). Northern blot
analysis detected several Rabgap1l transcripts expressed in a
tissue-specific manner. In situ hybridization of day-14.5 embryos
revealed expression in heart and liver.

GENE FUNCTION

By differential display, Sharma et al. (2003) found that RABGAP1L
expression was upregulated in esophageal squamous cell carcinomas
compared with matched normal esophageal epithelial tissue. In
particular, RABGAP1L expression was upregulated in esophageal tumors
showing nodal invasion.

MAPPING

By radiation hybrid analysis, Ishikawa et al. (1997) mapped the RABGAP1L
gene to chromosome 1.

MOLECULAR GENETICS

Most patients with Alzheimer disease (AD; 104300) are considered
sporadic late-onset cases with a complex etiology. By differential
display RT-PCR analysis, De Yebra et al. (2004) found inhibition of
RABGAP1L expression in medial septum and hippocampus in 3 of 6 AD
patients, including 1 with a PSEN1 (104311) mutation.

*FIELD* RF
1. de Yebra, L.; Adroer, R.; de Gregorio-Rocasolano, N.; Blesa, R.;
Trullas, R.; Mahy, N.: Reduced KIAA0471 mRNA expression in Alzheimer's
patients: a new candidate gene product linked to the disease? Hum.
Molec. Genet. 13: 2607-2612, 2004.

2. Hidaka, M.; Caruana, G.; Stanford, W. L.; Sam, M.; Correll, P.
H.; Bernstein, A.: Gene trapping of two novel genes, Hzf and Hhl,
expressed in hematopoietic cells. Mech. Dev. 90: 3-15, 2000.

3. Ishikawa, K.; Nagase, T.; Nakajima, D.; Seki, N.; Ohira, M.; Miyajima,
N.; Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of
the coding sequences of unidentified human genes. VIII. 78 new cDNA
clones from brain which code for large proteins in vitro. DNA Res. 4:
307-313, 1997.

4. Seki, N.; Ohira, M.; Nagase, T.; Ishikawa, K.; Miyajima, N.; Nakajima,
D.; Nomura, N.; Ohara, O.: Characterization of cDNA clones in size-fractionated
cDNA libraries from human brain. DNA Res. 4: 345-349, 1997.

5. Sharma, R.; Samantary, S.; Shukla, N. K.; Ralhan, R.: Transcriptional
gene expression profile of human esophageal squamous cell carcinoma. Genomics 81:
481-488, 2003.

*FIELD* CN
George E. Tiller - updated: 6/13/2007

*FIELD* CD
Patricia A. Hartz: 3/3/2005

*FIELD* ED
wwang: 06/15/2007
terry: 6/13/2007
alopez: 3/2/2007
mgross: 3/3/2005

RBCC Red Blood Cell Collection

Full text data of RABGAP1L