ASPC1_MOUSE
ID ASPC1_MOUSE Reviewed; 550 AA.
AC Q8VBT9; A2ABZ7; A2AC06; Q3UKD1; Q6V7K5; Q9CT64;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Tether containing UBX domain for GLUT4;
DE AltName: Full=Alveolar soft part sarcoma chromosomal region candidate gene 1 protein homolog;
GN Name=Aspscr1; Synonyms=Tug;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH
RP GLUT4, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver, and Muscle;
RX PubMed=14562105; DOI=10.1038/nature01989;
RA Bogan J.S., Hendon N., McKee A.E., Tsao T.-S., Lodish H.F.;
RT "Functional cloning of TUG as a regulator of GLUT4 glucose transporter
RT trafficking.";
RL Nature 425:727-733(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP STRUCTURE BY NMR OF 1-90.
RX PubMed=16501224; DOI=10.1110/ps.051901806;
RA Tettamanzi M.C., Yu C., Bogan J.S., Hodsdon M.E.;
RT "Solution structure and backbone dynamics of an N-terminal ubiquitin-like
RT domain in the GLUT4-regulating protein, TUG.";
RL Protein Sci. 15:498-508(2006).
CC -!- FUNCTION: Enhances VCP methylation catalyzed by VCPKMT (By similarity).
CC Tethering protein that sequesters GLUT4-containing vesicles in the
CC cytoplasm in the absence of insulin. Modulates the amount of GLUT4 that
CC is available at the cell surface. {ECO:0000250,
CC ECO:0000269|PubMed:14562105}.
CC -!- SUBUNIT: Interacts with VCP. Interacts with VCPKMT (By similarity).
CC Interacts with GLUT4. {ECO:0000250, ECO:0000250|UniProtKB:Q9BZE9,
CC ECO:0000269|PubMed:14562105}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000269|PubMed:14562105}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14562105}. Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000250|UniProtKB:Q9BZE9}; Peripheral
CC membrane protein. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long;
CC IsoId=Q8VBT9-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q8VBT9-2; Sequence=VSP_020579;
CC Name=3;
CC IsoId=Q8VBT9-3; Sequence=VSP_020579, VSP_020580;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:14562105}.
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DR EMBL; AY349132; AAR01613.1; -; mRNA.
DR EMBL; AY349133; AAR01614.1; -; mRNA.
DR EMBL; AK004509; BAB23341.1; -; mRNA.
DR EMBL; AK146061; BAE26870.1; -; mRNA.
DR EMBL; AL663030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019177; AAH19177.1; -; mRNA.
DR EMBL; BC022115; AAH22115.1; -; mRNA.
DR EMBL; BC031153; AAH31153.1; -; mRNA.
DR CCDS; CCDS25751.1; -. [Q8VBT9-1]
DR CCDS; CCDS25752.1; -. [Q8VBT9-2]
DR CCDS; CCDS49008.1; -. [Q8VBT9-3]
DR RefSeq; NP_001157696.1; NM_001164224.1. [Q8VBT9-3]
DR RefSeq; NP_081153.1; NM_026877.2. [Q8VBT9-1]
DR RefSeq; NP_937866.1; NM_198223.2. [Q8VBT9-2]
DR RefSeq; XP_006534149.1; XM_006534086.3. [Q8VBT9-2]
DR RefSeq; XP_006534150.1; XM_006534087.3. [Q8VBT9-2]
DR PDB; 2AL3; NMR; -; A=1-90.
DR PDBsum; 2AL3; -.
DR AlphaFoldDB; Q8VBT9; -.
DR BMRB; Q8VBT9; -.
DR SMR; Q8VBT9; -.
DR BioGRID; 213125; 22.
DR STRING; 10090.ENSMUSP00000026135; -.
DR iPTMnet; Q8VBT9; -.
DR PhosphoSitePlus; Q8VBT9; -.
DR SwissPalm; Q8VBT9; -.
DR REPRODUCTION-2DPAGE; Q8VBT9; -.
DR EPD; Q8VBT9; -.
DR jPOST; Q8VBT9; -.
DR MaxQB; Q8VBT9; -.
DR PaxDb; Q8VBT9; -.
DR PeptideAtlas; Q8VBT9; -.
DR PRIDE; Q8VBT9; -.
DR ProteomicsDB; 281848; -. [Q8VBT9-1]
DR ProteomicsDB; 281849; -. [Q8VBT9-2]
DR ProteomicsDB; 281850; -. [Q8VBT9-3]
DR Antibodypedia; 19857; 300 antibodies from 30 providers.
DR DNASU; 68938; -.
DR Ensembl; ENSMUST00000026135; ENSMUSP00000026135; ENSMUSG00000025142. [Q8VBT9-1]
DR Ensembl; ENSMUST00000103016; ENSMUSP00000099305; ENSMUSG00000025142. [Q8VBT9-2]
DR Ensembl; ENSMUST00000106158; ENSMUSP00000101764; ENSMUSG00000025142. [Q8VBT9-3]
DR Ensembl; ENSMUST00000106159; ENSMUSP00000101765; ENSMUSG00000025142. [Q8VBT9-2]
DR Ensembl; ENSMUST00000106160; ENSMUSP00000101766; ENSMUSG00000025142. [Q8VBT9-3]
DR GeneID; 68938; -.
DR KEGG; mmu:68938; -.
DR UCSC; uc007mua.2; mouse. [Q8VBT9-1]
DR UCSC; uc007mub.1; mouse. [Q8VBT9-3]
DR CTD; 79058; -.
DR MGI; MGI:1916188; Aspscr1.
DR VEuPathDB; HostDB:ENSMUSG00000025142; -.
DR eggNOG; KOG2699; Eukaryota.
DR GeneTree; ENSGT00940000156853; -.
DR HOGENOM; CLU_025227_0_0_1; -.
DR InParanoid; Q8VBT9; -.
DR OMA; EEGAHYA; -.
DR OrthoDB; 1104599at2759; -.
DR PhylomeDB; Q8VBT9; -.
DR TreeFam; TF320363; -.
DR BioGRID-ORCS; 68938; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Aspscr1; mouse.
DR EvolutionaryTrace; Q8VBT9; -.
DR PRO; PR:Q8VBT9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8VBT9; protein.
DR Bgee; ENSMUSG00000025142; Expressed in spermatid and 227 other tissues.
DR ExpressionAtlas; Q8VBT9; baseline and differential.
DR Genevisible; Q8VBT9; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0012506; C:vesicle membrane; IDA:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IDA:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IDA:MGI.
DR GO; GO:0031401; P:positive regulation of protein modification process; ISO:MGI.
DR GO; GO:0046324; P:regulation of glucose import; IDA:MGI.
DR InterPro; IPR021569; TUG-UBL1.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR Pfam; PF11470; TUG-UBL1; 1.
DR Pfam; PF00789; UBX; 1.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BZE9"
FT CHAIN 2..550
FT /note="Tether containing UBX domain for GLUT4"
FT /id="PRO_0000249886"
FT DOMAIN 382..458
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 185..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..376
FT /note="Interaction with GLUT4"
FT /evidence="ECO:0000269|PubMed:14562105"
FT REGION 496..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZE9"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZE9"
FT VAR_SEQ 1..77
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14562105,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_020579"
FT VAR_SEQ 410..430
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020580"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:2AL3"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:2AL3"
FT HELIX 32..42
FT /evidence="ECO:0007829|PDB:2AL3"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:2AL3"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:2AL3"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:2AL3"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:2AL3"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:2AL3"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:2AL3"
SQ SEQUENCE 550 AA; 59796 MW; CC2EB6F7BD43E113 CRC64;
MAAPAGGGGS AVSVLAPNGR RHTVKVTPST VLLQVLEDTC RRQDFNPSEY DLKFQRTVLD
LSLQWRFANL PNNAKLEMVP VSRSREGPEN IVRIAFQLDD GSRLQDAFCS RQTLWELLSH
FAQTRERLQQ LGEKTPVCVY MRNEVTGRAA LQNTTLQSLG LTGGSATIRF VIKQCDTAGK
QESIAVRSKA PGSPVSSLSA DQASSSTLLP LNSGEFSRGD LNHEGDANTS GTGLEGGPKP
TDAQTKQSTS EPASAPFVPF SGGGQRLGGP SASLRPLTSP SANSSKSFSG PGGPSKPKKP
KPGEEPQQEP EPPVDRDPVV YHPDLEDLLQ PWPAEVPDEF FEVTVDDVRR RLAQLKSERK
RLEEAPLVTK AFREAQMKEK LERYPKVALR VLFPDRYILQ GFFRPSETVG DLRDFVRSHL
GNPELSFYLF IAPPKMVLDD HTLTLFQANL FPAALVHFGA EEPTGLYLEP GLLEHTVSPS
TADVLVARCM SRASGSPPLL PAPDPVSLES EPIAEDGALG PPEPIQGTAQ PVKRSLGKVP
KWLKLPASKR
