Full text data of ASPSCR1
ASPSCR1
(ASPL, RCC17, TUG, UBXD9, UBXN9)
[Confidence: low (only semi-automatic identification from reviews)]
Tether containing UBX domain for GLUT4 (Alveolar soft part sarcoma chromosomal region candidate gene 1 protein; Alveolar soft part sarcoma locus; Renal papillary cell carcinoma protein 17; UBX domain-containing protein 9)
Tether containing UBX domain for GLUT4 (Alveolar soft part sarcoma chromosomal region candidate gene 1 protein; Alveolar soft part sarcoma locus; Renal papillary cell carcinoma protein 17; UBX domain-containing protein 9)
UniProt
Q9BZE9
ID ASPC1_HUMAN Reviewed; 553 AA.
AC Q9BZE9; A8K3K9; Q7Z6N7; Q8WV59; Q96LS5; Q96M40;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 91.
DE RecName: Full=Tether containing UBX domain for GLUT4;
DE AltName: Full=Alveolar soft part sarcoma chromosomal region candidate gene 1 protein;
DE AltName: Full=Alveolar soft part sarcoma locus;
DE AltName: Full=Renal papillary cell carcinoma protein 17;
DE AltName: Full=UBX domain-containing protein 9;
GN Name=ASPSCR1; Synonyms=ASPL, RCC17, TUG, UBXD9, UBXN9;
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] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION WITH
RP TFE3, TISSUE SPECIFICITY, AND INVOLVEMENT IN ASPS.
RX PubMed=11244503; DOI=10.1038/sj.onc.1204074;
RA Ladanyi M., Lui M.Y., Antonescu C.R., Krause-Boehm A., Meindl A.,
RA Argani P., Healey J.H., Ueda T., Yoshikawa H., Meloni-Ehrig A.,
RA Sorensen P.H.B., Mertens F., Mandahl N., van den Berghe H., Sciot R.,
RA Dal Cin P., Bridge J.;
RT "The der(17)t(X;17)(p11;q25) of human alveolar soft part sarcoma fuses
RT the TFE3 transcription factor gene to ASPL, a novel gene at 17q25.";
RL Oncogene 20:48-57(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND
RP VARIANT GLN-252.
RC TISSUE=Brain, Heart, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
RP GLN-252.
RC TISSUE=Eye, and Skin;
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 [4]
RP CHROMOSOMAL TRANSLOCATION WITH TFE3, AND TISSUE SPECIFICITY.
RX PubMed=11358836;
RA Heimann P., El Housni H., Ogur G., Weterman M.A.J., Petty E.M.,
RA Vassart G.;
RT "Fusion of a novel gene, RCC17, to the TFE3 gene in
RT t(X;17)(p11.2;q25.3)-bearing papillary renal cell carcinomas.";
RL Cancer Res. 61:4130-4135(2001).
RN [5]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP FUNCTION IN VCP METHYLATION, INTERACTION WITH VCPKMT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
RA Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
RT "A newly uncovered group of distantly related lysine
RT methyltransferases preferentially interact with molecular chaperones
RT to regulate their activity.";
RL PLoS Genet. 9:E1003210-E1003210(2013).
CC -!- FUNCTION: Tethering protein that sequesters GLUT4-containing
CC vesicles in the cytoplasm in the absence of insulin. Modulates the
CC amount of GLUT4 that is available at the cell surface (By
CC similarity). Enhances VCP methylation catalyzed by VCPKMT.
CC -!- SUBUNIT: Interacts with GLUT4 (By similarity). Interacts with
CC VCPKMT.
CC -!- INTERACTION:
CC P55072:VCP; NbExp=3; IntAct=EBI-1993677, EBI-355164;
CC -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane
CC protein (By similarity). Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9BZE9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BZE9-2; Sequence=VSP_020578;
CC Name=3;
CC IsoId=Q9BZE9-3; Sequence=VSP_020574, VSP_020577;
CC Name=4;
CC IsoId=Q9BZE9-4; Sequence=VSP_020574, VSP_020575, VSP_020576;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in testis, heart,
CC skeletal muscle and pancreas.
CC -!- DISEASE: Note=A chromosomal aberration involving ASPSCR1 is found
CC in patients with alveolar soft part sarcoma. Translocation
CC t(X;17)(p11;q25) with TFE3 forms a ASPSCR1-TFE3 fusion protein.
CC -!- DISEASE: Note=A chromosomal aberration involving ASPSCR1 has been
CC found in two patients with of papillary renal cell carcinoma.
CC Translocation t(X;17)(p11.2;q25).
CC -!- SIMILARITY: Contains 1 UBX domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ASPSCR1ID358.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF324219; AAK08959.2; -; mRNA.
DR EMBL; AK057403; BAB71472.1; -; mRNA.
DR EMBL; AK057851; BAB71595.1; -; mRNA.
DR EMBL; AK290624; BAF83313.1; -; mRNA.
DR EMBL; BC006152; AAH06152.1; -; mRNA.
DR EMBL; BC018722; AAH18722.1; -; mRNA.
DR RefSeq; NP_001238817.1; NM_001251888.1.
DR RefSeq; NP_076988.1; NM_024083.3.
DR UniGene; Hs.298351; -.
DR ProteinModelPortal; Q9BZE9; -.
DR SMR; Q9BZE9; 10-85.
DR IntAct; Q9BZE9; 4.
DR MINT; MINT-4650542; -.
DR STRING; 9606.ENSP00000302176; -.
DR PhosphoSite; Q9BZE9; -.
DR DMDM; 74717746; -.
DR PaxDb; Q9BZE9; -.
DR PRIDE; Q9BZE9; -.
DR DNASU; 79058; -.
DR Ensembl; ENST00000306729; ENSP00000306625; ENSG00000169696.
DR Ensembl; ENST00000306739; ENSP00000302176; ENSG00000169696.
DR Ensembl; ENST00000580534; ENSP00000462329; ENSG00000169696.
DR GeneID; 79058; -.
DR KEGG; hsa:79058; -.
DR UCSC; uc002kcx.3; human.
DR CTD; 79058; -.
DR GeneCards; GC17P079935; -.
DR H-InvDB; HIX0022398; -.
DR HGNC; HGNC:13825; ASPSCR1.
DR HPA; HPA026749; -.
DR MIM; 606236; gene.
DR neXtProt; NX_Q9BZE9; -.
DR Orphanet; 163699; Alveolar soft-part sarcoma.
DR Orphanet; 319308; Translocation renal cell carcinoma.
DR PharmGKB; PA25058; -.
DR eggNOG; NOG317887; -.
DR HOGENOM; HOG000231241; -.
DR HOVERGEN; HBG066860; -.
DR KO; K15627; -.
DR OMA; FQRTVLD; -.
DR OrthoDB; EOG7S7SF9; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR ChiTaRS; ASPSCR1; human.
DR GeneWiki; ASPSCR1; -.
DR GenomeRNAi; 79058; -.
DR NextBio; 67822; -.
DR PRO; PR:Q9BZE9; -.
DR ArrayExpress; Q9BZE9; -.
DR Bgee; Q9BZE9; -.
DR CleanEx; HS_ASPSCR1; -.
DR Genevestigator; Q9BZE9; -.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic to membrane; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0012506; C:vesicle membrane; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IEA:Ensembl.
DR GO; GO:0046324; P:regulation of glucose import; IEA:Ensembl.
DR InterPro; IPR021569; TUG/UBX4.
DR InterPro; IPR001012; UBX.
DR Pfam; PF11470; TUG-UBL1; 1.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00166; UBX; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromosomal rearrangement;
KW Complete proteome; Cytoplasm; Membrane; Nucleus; Phosphoprotein;
KW Polymorphism; Proto-oncogene; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 553 Tether containing UBX domain for GLUT4.
FT /FTId=PRO_0000249885.
FT DOMAIN 386 462 UBX.
FT REGION 317 380 Interaction with GLUT4 (By similarity).
FT SITE 311 312 Breakpoint for translocation to form
FT ASPSCR1-TFE3.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 500 500 Phosphoserine.
FT VAR_SEQ 1 77 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_020574.
FT VAR_SEQ 390 425 KVALRVLFPDRYVLQGFFRPSETVGDLRDFVRSHLG -> R
FT RSLSLSPRLESVVPSQLTASSASRVQVVLLPQPPK (in
FT isoform 4).
FT /FTId=VSP_020575.
FT VAR_SEQ 426 553 Missing (in isoform 4).
FT /FTId=VSP_020576.
FT VAR_SEQ 434 434 F -> CLSSFGRMDGRGPRCFLTRRCLLSSV (in
FT isoform 3).
FT /FTId=VSP_020577.
FT VAR_SEQ 451 451 Q -> QPQLGDRVAPFTLGPSLKRCLGPEQRTRLPVVGDGG
FT DVDSGRLLFWGPSRGRASPSTGQPPCHPVCRPSSPPSPRPS
FT SGDPSRVKAGHKHVGTGR (in isoform 2).
FT /FTId=VSP_020578.
FT VARIANT 252 252 L -> Q (in dbSNP:rs8074498).
FT /FTId=VAR_027503.
FT VARIANT 318 318 V -> M (in dbSNP:rs34085048).
FT /FTId=VAR_034745.
FT VARIANT 487 487 D -> E (in dbSNP:rs13087).
FT /FTId=VAR_027504.
FT CONFLICT 257 257 G -> E (in Ref. 2; BAB71595).
FT CONFLICT 444 444 D -> G (in Ref. 2; BAB71595).
SQ SEQUENCE 553 AA; 60183 MW; B013FDF9A48D2E5E CRC64;
MAAPAGGGGS AVSVLAPNGR RHTVKVTPST VLLQVLEDTC RRQDFNPCEY DLKFQRSVLD
LSLQWRFANL PNNAKLEMVP ASRSREGPEN MVRIALQLDD GSRLQDSFCS GQTLWELLSH
FPQIRECLQH PGGATPVCVY TRDEVTGEAA LRGTTLQSLG LTGGSATIRF VMKCYDPVGK
TPGSLGSSAS AGQAAASAPL PLESGELSRG DLSRPEDADT SGPCCEHTQE KQSTRAPAAA
PFVPFSGGGQ RLGGPPGPTR PLTSSSAKLP KSLSSPGGPS KPKKSKSGQD PQQEQEQERE
RDPQQEQERE RPVDREPVDR EPVVCHPDLE ERLQAWPAEL PDEFFELTVD DVRRRLAQLK
SERKRLEEAP LVTKAFREAQ IKEKLERYPK VALRVLFPDR YVLQGFFRPS ETVGDLRDFV
RSHLGNPELS FYLFITPPKT VLDDHTQTLF QANLFPAALV HLGAEEPAGV YLEPGLLEHA
ISPSAADVLV ARYMSRAAGS PSPLPAPDPA PKSEPAAEEG ALVPPEPIPG TAQPVKRSLG
KVPKWLKLPA SKR
//
ID ASPC1_HUMAN Reviewed; 553 AA.
AC Q9BZE9; A8K3K9; Q7Z6N7; Q8WV59; Q96LS5; Q96M40;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 91.
DE RecName: Full=Tether containing UBX domain for GLUT4;
DE AltName: Full=Alveolar soft part sarcoma chromosomal region candidate gene 1 protein;
DE AltName: Full=Alveolar soft part sarcoma locus;
DE AltName: Full=Renal papillary cell carcinoma protein 17;
DE AltName: Full=UBX domain-containing protein 9;
GN Name=ASPSCR1; Synonyms=ASPL, RCC17, TUG, UBXD9, UBXN9;
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] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION WITH
RP TFE3, TISSUE SPECIFICITY, AND INVOLVEMENT IN ASPS.
RX PubMed=11244503; DOI=10.1038/sj.onc.1204074;
RA Ladanyi M., Lui M.Y., Antonescu C.R., Krause-Boehm A., Meindl A.,
RA Argani P., Healey J.H., Ueda T., Yoshikawa H., Meloni-Ehrig A.,
RA Sorensen P.H.B., Mertens F., Mandahl N., van den Berghe H., Sciot R.,
RA Dal Cin P., Bridge J.;
RT "The der(17)t(X;17)(p11;q25) of human alveolar soft part sarcoma fuses
RT the TFE3 transcription factor gene to ASPL, a novel gene at 17q25.";
RL Oncogene 20:48-57(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND
RP VARIANT GLN-252.
RC TISSUE=Brain, Heart, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
RP GLN-252.
RC TISSUE=Eye, and Skin;
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 [4]
RP CHROMOSOMAL TRANSLOCATION WITH TFE3, AND TISSUE SPECIFICITY.
RX PubMed=11358836;
RA Heimann P., El Housni H., Ogur G., Weterman M.A.J., Petty E.M.,
RA Vassart G.;
RT "Fusion of a novel gene, RCC17, to the TFE3 gene in
RT t(X;17)(p11.2;q25.3)-bearing papillary renal cell carcinomas.";
RL Cancer Res. 61:4130-4135(2001).
RN [5]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP FUNCTION IN VCP METHYLATION, INTERACTION WITH VCPKMT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
RA Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
RT "A newly uncovered group of distantly related lysine
RT methyltransferases preferentially interact with molecular chaperones
RT to regulate their activity.";
RL PLoS Genet. 9:E1003210-E1003210(2013).
CC -!- FUNCTION: Tethering protein that sequesters GLUT4-containing
CC vesicles in the cytoplasm in the absence of insulin. Modulates the
CC amount of GLUT4 that is available at the cell surface (By
CC similarity). Enhances VCP methylation catalyzed by VCPKMT.
CC -!- SUBUNIT: Interacts with GLUT4 (By similarity). Interacts with
CC VCPKMT.
CC -!- INTERACTION:
CC P55072:VCP; NbExp=3; IntAct=EBI-1993677, EBI-355164;
CC -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane
CC protein (By similarity). Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9BZE9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BZE9-2; Sequence=VSP_020578;
CC Name=3;
CC IsoId=Q9BZE9-3; Sequence=VSP_020574, VSP_020577;
CC Name=4;
CC IsoId=Q9BZE9-4; Sequence=VSP_020574, VSP_020575, VSP_020576;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in testis, heart,
CC skeletal muscle and pancreas.
CC -!- DISEASE: Note=A chromosomal aberration involving ASPSCR1 is found
CC in patients with alveolar soft part sarcoma. Translocation
CC t(X;17)(p11;q25) with TFE3 forms a ASPSCR1-TFE3 fusion protein.
CC -!- DISEASE: Note=A chromosomal aberration involving ASPSCR1 has been
CC found in two patients with of papillary renal cell carcinoma.
CC Translocation t(X;17)(p11.2;q25).
CC -!- SIMILARITY: Contains 1 UBX domain.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ASPSCR1ID358.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF324219; AAK08959.2; -; mRNA.
DR EMBL; AK057403; BAB71472.1; -; mRNA.
DR EMBL; AK057851; BAB71595.1; -; mRNA.
DR EMBL; AK290624; BAF83313.1; -; mRNA.
DR EMBL; BC006152; AAH06152.1; -; mRNA.
DR EMBL; BC018722; AAH18722.1; -; mRNA.
DR RefSeq; NP_001238817.1; NM_001251888.1.
DR RefSeq; NP_076988.1; NM_024083.3.
DR UniGene; Hs.298351; -.
DR ProteinModelPortal; Q9BZE9; -.
DR SMR; Q9BZE9; 10-85.
DR IntAct; Q9BZE9; 4.
DR MINT; MINT-4650542; -.
DR STRING; 9606.ENSP00000302176; -.
DR PhosphoSite; Q9BZE9; -.
DR DMDM; 74717746; -.
DR PaxDb; Q9BZE9; -.
DR PRIDE; Q9BZE9; -.
DR DNASU; 79058; -.
DR Ensembl; ENST00000306729; ENSP00000306625; ENSG00000169696.
DR Ensembl; ENST00000306739; ENSP00000302176; ENSG00000169696.
DR Ensembl; ENST00000580534; ENSP00000462329; ENSG00000169696.
DR GeneID; 79058; -.
DR KEGG; hsa:79058; -.
DR UCSC; uc002kcx.3; human.
DR CTD; 79058; -.
DR GeneCards; GC17P079935; -.
DR H-InvDB; HIX0022398; -.
DR HGNC; HGNC:13825; ASPSCR1.
DR HPA; HPA026749; -.
DR MIM; 606236; gene.
DR neXtProt; NX_Q9BZE9; -.
DR Orphanet; 163699; Alveolar soft-part sarcoma.
DR Orphanet; 319308; Translocation renal cell carcinoma.
DR PharmGKB; PA25058; -.
DR eggNOG; NOG317887; -.
DR HOGENOM; HOG000231241; -.
DR HOVERGEN; HBG066860; -.
DR KO; K15627; -.
DR OMA; FQRTVLD; -.
DR OrthoDB; EOG7S7SF9; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR ChiTaRS; ASPSCR1; human.
DR GeneWiki; ASPSCR1; -.
DR GenomeRNAi; 79058; -.
DR NextBio; 67822; -.
DR PRO; PR:Q9BZE9; -.
DR ArrayExpress; Q9BZE9; -.
DR Bgee; Q9BZE9; -.
DR CleanEx; HS_ASPSCR1; -.
DR Genevestigator; Q9BZE9; -.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic to membrane; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0012506; C:vesicle membrane; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IEA:Ensembl.
DR GO; GO:0046324; P:regulation of glucose import; IEA:Ensembl.
DR InterPro; IPR021569; TUG/UBX4.
DR InterPro; IPR001012; UBX.
DR Pfam; PF11470; TUG-UBL1; 1.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00166; UBX; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromosomal rearrangement;
KW Complete proteome; Cytoplasm; Membrane; Nucleus; Phosphoprotein;
KW Polymorphism; Proto-oncogene; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 553 Tether containing UBX domain for GLUT4.
FT /FTId=PRO_0000249885.
FT DOMAIN 386 462 UBX.
FT REGION 317 380 Interaction with GLUT4 (By similarity).
FT SITE 311 312 Breakpoint for translocation to form
FT ASPSCR1-TFE3.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 500 500 Phosphoserine.
FT VAR_SEQ 1 77 Missing (in isoform 3 and isoform 4).
FT /FTId=VSP_020574.
FT VAR_SEQ 390 425 KVALRVLFPDRYVLQGFFRPSETVGDLRDFVRSHLG -> R
FT RSLSLSPRLESVVPSQLTASSASRVQVVLLPQPPK (in
FT isoform 4).
FT /FTId=VSP_020575.
FT VAR_SEQ 426 553 Missing (in isoform 4).
FT /FTId=VSP_020576.
FT VAR_SEQ 434 434 F -> CLSSFGRMDGRGPRCFLTRRCLLSSV (in
FT isoform 3).
FT /FTId=VSP_020577.
FT VAR_SEQ 451 451 Q -> QPQLGDRVAPFTLGPSLKRCLGPEQRTRLPVVGDGG
FT DVDSGRLLFWGPSRGRASPSTGQPPCHPVCRPSSPPSPRPS
FT SGDPSRVKAGHKHVGTGR (in isoform 2).
FT /FTId=VSP_020578.
FT VARIANT 252 252 L -> Q (in dbSNP:rs8074498).
FT /FTId=VAR_027503.
FT VARIANT 318 318 V -> M (in dbSNP:rs34085048).
FT /FTId=VAR_034745.
FT VARIANT 487 487 D -> E (in dbSNP:rs13087).
FT /FTId=VAR_027504.
FT CONFLICT 257 257 G -> E (in Ref. 2; BAB71595).
FT CONFLICT 444 444 D -> G (in Ref. 2; BAB71595).
SQ SEQUENCE 553 AA; 60183 MW; B013FDF9A48D2E5E CRC64;
MAAPAGGGGS AVSVLAPNGR RHTVKVTPST VLLQVLEDTC RRQDFNPCEY DLKFQRSVLD
LSLQWRFANL PNNAKLEMVP ASRSREGPEN MVRIALQLDD GSRLQDSFCS GQTLWELLSH
FPQIRECLQH PGGATPVCVY TRDEVTGEAA LRGTTLQSLG LTGGSATIRF VMKCYDPVGK
TPGSLGSSAS AGQAAASAPL PLESGELSRG DLSRPEDADT SGPCCEHTQE KQSTRAPAAA
PFVPFSGGGQ RLGGPPGPTR PLTSSSAKLP KSLSSPGGPS KPKKSKSGQD PQQEQEQERE
RDPQQEQERE RPVDREPVDR EPVVCHPDLE ERLQAWPAEL PDEFFELTVD DVRRRLAQLK
SERKRLEEAP LVTKAFREAQ IKEKLERYPK VALRVLFPDR YVLQGFFRPS ETVGDLRDFV
RSHLGNPELS FYLFITPPKT VLDDHTQTLF QANLFPAALV HLGAEEPAGV YLEPGLLEHA
ISPSAADVLV ARYMSRAAGS PSPLPAPDPA PKSEPAAEEG ALVPPEPIPG TAQPVKRSLG
KVPKWLKLPA SKR
//
MIM
606236
*RECORD*
*FIELD* NO
606236
*FIELD* TI
*606236 ALVEOLAR SOFT PART SARCOMA CHROMOSOME REGION, CANDIDATE 1; ASPSCR1
;;ASPL;;
read moreTETHER, CONTAINING UBX DOMAIN FOR GLUT4; TUG
ASPSCR1/TFE3 FUSION GENE, INCLUDED
*FIELD* TX
CLONING
Cytogenetic studies identified a recurrent der(17) due to a
nonreciprocal t(X;17)(p11.2;q25) in cases of alveolar soft-part sarcoma
(ASPS; 606243) (Joyama et al., 1999). By Southern blot analysis using a
TFE3 (314310) probe, Ladanyi et al. (2001) identified nongermline bands
in several ASPS cases, consistent with rearrangement and possible fusion
of TFE3 with a gene on 17q25. By amplification of the 5-prime portion of
cDNAs containing the 3-prime portion of TFE3 in 2 ASPS cases, they
identified a novel sequence, ASPSCR1 (designated ASPL by the authors),
fused in-frame to TFE3 exon 4 or exon 3. RT-PCR analysis detected an
ASPSCR1/TFE3 fusion transcript in all 12 ASPS cases studied. The
ASPSCR1/TFE3 fusion replaces the N-terminal portion of TFE3 by the fused
ASPSCR1 sequences, while retaining the TFE3 DNA-binding domain,
implicating transcriptional deregulation in the pathogenesis of ASPS.
Ladanyi et al. (2001) identified major and minor splice forms of the
ASPSCR1 transcript which differ by the absence or presence of a
47-nucleotide segment from exon 2, which encodes part of the 5-prime
untranslated portion of ASPSCR1. They determined that the ASPSCR1 cDNA
encodes a deduced 476-amino acid protein containing a UBX-like domain in
its C terminus. Northern blot analysis detected a predominant 1.9-kb
transcript in all tissues tested, with highest expression in heart,
skeletal muscle, pancreas, and testis. Expression in fetal tissues
appeared notably lower than in adult tissues. ASPSCR1 expression was
also found in all cancer cell lines tested.
Independently, Heimann et al. (2001) identified the ASPSCR1 gene, which
they called RCC17, partnered with TFE3 in two 5-year-old Belgian girls
of African origin in whom papillary renal cell carcinomas (300854)
carried the translocation t(X;17)(p11.2;q25). In both patients, the
t(X;17) fused the N terminal region of RCC17 to the C terminal region of
TFE3 including the bHLH DNA-binding domain and the leucine zipper
dimerization domain. The reciprocal fusion transcript TFE3/RCC17 was
also expressed.
Cloutier et al. (2013) stated that the deduced 553-amino acid ASPSCR1
protein contains 2 N-terminal ubiquitin-like domains, followed by an SHP
box, a coiled-coil region, and a ubiquitin regulatory X domain.
GENE FUNCTION
Insulin (176730) stimulates glucose uptake in fat and muscle by
mobilizing the GLUT4 glucose transporter (138190). GLUT4 is sequestered
intracellularly in the absence of insulin, and is redistributed to the
plasma membrane within minutes of insulin stimulation. Bogan et al.
(2003) described a functional screen to identify proteins that modulate
GLUT4 distribution, and identified TUG as a putative tether, containing
a UBX domain, for GLUT4. They identified the ASPL protein as the
probable human homolog of murine TUG. In truncated form, TUG acts in a
dominant-negative manner to inhibit insulin-stimulated GLUT4
redistribution in Chinese hamster ovary cells and 3T3-L1 adipocytes.
Full-length TUG forms a complex specifically with GLUT4; in 3T3-L1
adipocytes, this complex is present in unstimulated cells and is largely
disassembled by insulin. Endogenous TUG is localized with the
insulin-mobilizable pool of GLUT4 in unstimulated 3T3-L1 adipocytes, and
is not mobilized to the plasma membrane by insulin. Distinct regions of
TUG are required to bind GLUT4 and to retain GLUT4 intracellularly in
transfected, nonadipose cells. Bogan et al. (2003) concluded that TUG
traps endocytosed GLUT4 and tethers it intracellularly, and that insulin
mobilizes this pool of retained GLUT4 by releasing this tether. Bogan et
al. (2003) found that TUG exists in 2 isoforms, the longer of which
contains a sequence at the amino terminus with similarity to ubiquitin
that is predicted to be 550 residues long. The probable start codon in
the short form is equivalent to methionine-78 of the long form.
By affinity purification, SDS-PAGE, and mass spectrometry, Cloutier et
al. (2013) found that VCP (601023), ASPSCR1, UBXN6 (611946), and
METTL21D (615260) interacted in METTL21D-transfected HEK293 cells.
Recombinant METTL21D did not methylate ASPSRC1 or UBXN6 in an in vitro
methylation reaction, but the presence of ASPSRC1, but not UBXN6,
enhanced METTL21D-dependent VCP methylation.
*FIELD* RF
1. Bogan, J. S.; Hendon, N.; McKee, A. E.; Tsao, T.-S.; Lodish, H.
F.: Functional cloning of TUG as a regulator of GLUT4 glucose transporter
trafficking. Nature 425: 727-733, 2003.
2. Cloutier, P.; Lavallee-Adam, M.; Faubert, D.; Blanchette, M.; Coulombe,
B.: A newly uncovered group of distantly related lysine methyltransferases
preferentially interact with molecular chaperones to regulate their
activity. PLoS Genet. 9: e1003210, 2013. Note: Electronic Article.
3. Heimann, P.; El Housni, H.; Ogur, G.; Weterman, M. A. J.; Petty,
E. M.; Vassart, G.: Fusion of a novel gene, RCC17, to the TFE3 gene
in t(X;17)(p11.2;q25.3)-bearing papillary renal cell carcinomas. Cancer
Res. 61: 4130-4135, 2001.
4. Joyama, S.; Ueda, T.; Shimizu, K.; Kudawara, I.; Mano, M.; Funai,
H.; Takemura, K.; Yoshikawa, H.: Chromosome rearrangement at 17q25
and Xp11.2 in alveolar soft-part sarcoma: a case report and review
of the literature. Cancer 86: 1246-1250, 1999.
5. Ladanyi, M.; Lui, M. Y.; Antonescu, C. R.; Krause-Boehm, A.; Meindl,
A.; Argani, P.; Healey, J. H.; Ueda, T.; Yoshikawa, H.; Meloni-Ehrig,
A.; Sorensen, P. H. B.; Mertens, F.; Mandahl, N.; van den Berghe,
H.; Sciot, R.; Dal Cin, P.; Bridge, J.: The der(17)t(X;17)(p11;q25)
of human alveolar soft part sarcoma fuses the TFE3 transcription factor
gene to ASPL, a novel gene at 17q25. Oncogene 20: 48-57, 2001.
*FIELD* CN
Patricia A. Hartz - updated: 05/31/2013
Ada Hamosh - updated: 10/29/2003
Victor A. McKusick - updated: 8/30/2001
*FIELD* CD
Carol A. Bocchini: 8/30/2001
*FIELD* ED
mgross: 05/31/2013
carol: 9/15/2011
ckniffin: 9/13/2011
terry: 9/9/2010
alopez: 4/5/2010
carol: 7/10/2006
alopez: 10/29/2003
terry: 10/29/2003
carol: 8/31/2001
carol: 8/30/2001
mcapotos: 8/30/2001
carol: 8/30/2001
*RECORD*
*FIELD* NO
606236
*FIELD* TI
*606236 ALVEOLAR SOFT PART SARCOMA CHROMOSOME REGION, CANDIDATE 1; ASPSCR1
;;ASPL;;
read moreTETHER, CONTAINING UBX DOMAIN FOR GLUT4; TUG
ASPSCR1/TFE3 FUSION GENE, INCLUDED
*FIELD* TX
CLONING
Cytogenetic studies identified a recurrent der(17) due to a
nonreciprocal t(X;17)(p11.2;q25) in cases of alveolar soft-part sarcoma
(ASPS; 606243) (Joyama et al., 1999). By Southern blot analysis using a
TFE3 (314310) probe, Ladanyi et al. (2001) identified nongermline bands
in several ASPS cases, consistent with rearrangement and possible fusion
of TFE3 with a gene on 17q25. By amplification of the 5-prime portion of
cDNAs containing the 3-prime portion of TFE3 in 2 ASPS cases, they
identified a novel sequence, ASPSCR1 (designated ASPL by the authors),
fused in-frame to TFE3 exon 4 or exon 3. RT-PCR analysis detected an
ASPSCR1/TFE3 fusion transcript in all 12 ASPS cases studied. The
ASPSCR1/TFE3 fusion replaces the N-terminal portion of TFE3 by the fused
ASPSCR1 sequences, while retaining the TFE3 DNA-binding domain,
implicating transcriptional deregulation in the pathogenesis of ASPS.
Ladanyi et al. (2001) identified major and minor splice forms of the
ASPSCR1 transcript which differ by the absence or presence of a
47-nucleotide segment from exon 2, which encodes part of the 5-prime
untranslated portion of ASPSCR1. They determined that the ASPSCR1 cDNA
encodes a deduced 476-amino acid protein containing a UBX-like domain in
its C terminus. Northern blot analysis detected a predominant 1.9-kb
transcript in all tissues tested, with highest expression in heart,
skeletal muscle, pancreas, and testis. Expression in fetal tissues
appeared notably lower than in adult tissues. ASPSCR1 expression was
also found in all cancer cell lines tested.
Independently, Heimann et al. (2001) identified the ASPSCR1 gene, which
they called RCC17, partnered with TFE3 in two 5-year-old Belgian girls
of African origin in whom papillary renal cell carcinomas (300854)
carried the translocation t(X;17)(p11.2;q25). In both patients, the
t(X;17) fused the N terminal region of RCC17 to the C terminal region of
TFE3 including the bHLH DNA-binding domain and the leucine zipper
dimerization domain. The reciprocal fusion transcript TFE3/RCC17 was
also expressed.
Cloutier et al. (2013) stated that the deduced 553-amino acid ASPSCR1
protein contains 2 N-terminal ubiquitin-like domains, followed by an SHP
box, a coiled-coil region, and a ubiquitin regulatory X domain.
GENE FUNCTION
Insulin (176730) stimulates glucose uptake in fat and muscle by
mobilizing the GLUT4 glucose transporter (138190). GLUT4 is sequestered
intracellularly in the absence of insulin, and is redistributed to the
plasma membrane within minutes of insulin stimulation. Bogan et al.
(2003) described a functional screen to identify proteins that modulate
GLUT4 distribution, and identified TUG as a putative tether, containing
a UBX domain, for GLUT4. They identified the ASPL protein as the
probable human homolog of murine TUG. In truncated form, TUG acts in a
dominant-negative manner to inhibit insulin-stimulated GLUT4
redistribution in Chinese hamster ovary cells and 3T3-L1 adipocytes.
Full-length TUG forms a complex specifically with GLUT4; in 3T3-L1
adipocytes, this complex is present in unstimulated cells and is largely
disassembled by insulin. Endogenous TUG is localized with the
insulin-mobilizable pool of GLUT4 in unstimulated 3T3-L1 adipocytes, and
is not mobilized to the plasma membrane by insulin. Distinct regions of
TUG are required to bind GLUT4 and to retain GLUT4 intracellularly in
transfected, nonadipose cells. Bogan et al. (2003) concluded that TUG
traps endocytosed GLUT4 and tethers it intracellularly, and that insulin
mobilizes this pool of retained GLUT4 by releasing this tether. Bogan et
al. (2003) found that TUG exists in 2 isoforms, the longer of which
contains a sequence at the amino terminus with similarity to ubiquitin
that is predicted to be 550 residues long. The probable start codon in
the short form is equivalent to methionine-78 of the long form.
By affinity purification, SDS-PAGE, and mass spectrometry, Cloutier et
al. (2013) found that VCP (601023), ASPSCR1, UBXN6 (611946), and
METTL21D (615260) interacted in METTL21D-transfected HEK293 cells.
Recombinant METTL21D did not methylate ASPSRC1 or UBXN6 in an in vitro
methylation reaction, but the presence of ASPSRC1, but not UBXN6,
enhanced METTL21D-dependent VCP methylation.
*FIELD* RF
1. Bogan, J. S.; Hendon, N.; McKee, A. E.; Tsao, T.-S.; Lodish, H.
F.: Functional cloning of TUG as a regulator of GLUT4 glucose transporter
trafficking. Nature 425: 727-733, 2003.
2. Cloutier, P.; Lavallee-Adam, M.; Faubert, D.; Blanchette, M.; Coulombe,
B.: A newly uncovered group of distantly related lysine methyltransferases
preferentially interact with molecular chaperones to regulate their
activity. PLoS Genet. 9: e1003210, 2013. Note: Electronic Article.
3. Heimann, P.; El Housni, H.; Ogur, G.; Weterman, M. A. J.; Petty,
E. M.; Vassart, G.: Fusion of a novel gene, RCC17, to the TFE3 gene
in t(X;17)(p11.2;q25.3)-bearing papillary renal cell carcinomas. Cancer
Res. 61: 4130-4135, 2001.
4. Joyama, S.; Ueda, T.; Shimizu, K.; Kudawara, I.; Mano, M.; Funai,
H.; Takemura, K.; Yoshikawa, H.: Chromosome rearrangement at 17q25
and Xp11.2 in alveolar soft-part sarcoma: a case report and review
of the literature. Cancer 86: 1246-1250, 1999.
5. Ladanyi, M.; Lui, M. Y.; Antonescu, C. R.; Krause-Boehm, A.; Meindl,
A.; Argani, P.; Healey, J. H.; Ueda, T.; Yoshikawa, H.; Meloni-Ehrig,
A.; Sorensen, P. H. B.; Mertens, F.; Mandahl, N.; van den Berghe,
H.; Sciot, R.; Dal Cin, P.; Bridge, J.: The der(17)t(X;17)(p11;q25)
of human alveolar soft part sarcoma fuses the TFE3 transcription factor
gene to ASPL, a novel gene at 17q25. Oncogene 20: 48-57, 2001.
*FIELD* CN
Patricia A. Hartz - updated: 05/31/2013
Ada Hamosh - updated: 10/29/2003
Victor A. McKusick - updated: 8/30/2001
*FIELD* CD
Carol A. Bocchini: 8/30/2001
*FIELD* ED
mgross: 05/31/2013
carol: 9/15/2011
ckniffin: 9/13/2011
terry: 9/9/2010
alopez: 4/5/2010
carol: 7/10/2006
alopez: 10/29/2003
terry: 10/29/2003
carol: 8/31/2001
carol: 8/30/2001
mcapotos: 8/30/2001
carol: 8/30/2001