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TBC1 domain family member 4 (Akt substrate of 160 kDa) (AS160)

 TBCD4_HUMAN             Reviewed;        1298 AA.
O60343; A7E2X8; B4DU25; B4E235; B6ETN8; B6ETN9; Q5W0B9; Q68D14;
10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 2.
22-NOV-2017, entry version 159.
RecName: Full=TBC1 domain family member 4;
AltName: Full=Akt substrate of 160 kDa;
Short=AS160;
Name=TBC1D4; Synonyms=AS160, KIAA0603;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND PHOSPHORYLATION AT THR-642.
TISSUE=Testis;
PubMed=18771725; DOI=10.1016/j.cellsig.2008.08.010;
Baus D., Heermeier K., De Hoop M., Metz-Weidmann C., Gassenhuber J.,
Dittrich W., Welte S., Tennagels N.;
"Identification of a novel AS160 splice variant that regulates GLUT4
translocation and glucose-uptake in rat muscle cells.";
Cell. Signal. 20:2237-2246(2008).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ILE-819 AND
ALA-1275.
TISSUE=Brain;
PubMed=19077034; DOI=10.1111/j.1365-2443.2008.01251.x;
Ishibashi K., Kanno E., Itoh T., Fukuda M.;
"Identification and characterization of a novel Tre-2/Bub2/Cdc16 (TBC)
protein that possesses Rab3A-GAP activity.";
Genes Cells 14:41-52(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ILE-819 AND ALA-1275.
TISSUE=Brain;
PubMed=9628581; DOI=10.1093/dnares/5.1.31;
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
Ohara O.;
"Prediction of the coding sequences of unidentified human genes. IX.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:31-39(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
TISSUE=Placenta, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ILE-819 AND ALA-1275.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 600-1298 (ISOFORM 3), AND
VARIANT ILE-819.
TISSUE=Fetal liver;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
PHOSPHORYLATION AT SER-588 AND THR-642.
PubMed=11994271; DOI=10.1074/jbc.C200198200;
Kane S., Sano H., Liu S.C.H., Asara J.M., Lane W.S., Garner C.C.,
Lienhard G.E.;
"A method to identify serine kinase substrates. Akt phosphorylates a
novel adipocyte protein with a Rab GTPase-activating protein (GAP)
domain.";
J. Biol. Chem. 277:22115-22118(2002).
[9]
MUTAGENESIS OF SER-318; SER-588; THR-642; SER-751 AND ARG-972, AND
EFFECT ON GLUT4 TRANSLOCATION.
PubMed=12637568; DOI=10.1074/jbc.C300063200;
Sano H., Kane S., Sano E., Miinea C.P., Asara J.M., Lane W.S.,
Garner C.W., Lienhard G.E.;
"Insulin-stimulated phosphorylation of a Rab GTPase-activating protein
regulates GLUT4 translocation.";
J. Biol. Chem. 278:14599-14602(2003).
[10]
FUNCTION, AND MUTAGENESIS OF ARG-972.
PubMed=15971998; DOI=10.1042/BJ20050887;
Miinea C.P., Sano H., Kane S., Sano E., Fukuda M., Peraenen J.,
Lane W.S., Lienhard G.E.;
"AS160, the Akt substrate regulating GLUT4 translocation, has a
functional Rab GTPase-activating protein domain.";
Biochem. J. 391:87-93(2005).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND SER-591, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[13]
TISSUE SPECIFICITY.
PubMed=18276765; DOI=10.2337/db07-1469;
Bouzakri K., Ribaux P., Tomas A., Parnaud G., Rickenbach K.,
Halban P.A.;
"Rab GTPase-activating protein AS160 is a major downstream effector of
protein kinase B/Akt signaling in pancreatic beta-cells.";
Diabetes 57:1195-1204(2008).
[14]
TISSUE SPECIFICITY.
PubMed=15304337; DOI=10.1016/j.febslet.2004.07.023;
Matsumoto Y., Imai Y., Lu Yoshida N., Sugita Y., Tanaka T.,
Tsujimoto G., Saito H., Oshida T.;
"Upregulation of the transcript level of GTPase activating protein
KIAA0603 in T cells from patients with atopic dermatitis.";
FEBS Lett. 572:135-140(2004).
[15]
PHOSPHORYLATION.
PubMed=15919790; DOI=10.2337/diabetes.54.6.1692;
Karlsson H.K.R., Zierath J.R., Kane S., Krook A., Lienhard G.E.,
Wallberg-Henriksson H.;
"Insulin-stimulated phosphorylation of the Akt substrate AS160 is
impaired in skeletal muscle of type 2 diabetic subjects.";
Diabetes 54:1692-1697(2005).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341; SER-566 AND
SER-570, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; SER-672
AND SER-678 (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566; THR-568; SER-570
AND SER-588, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-477, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341; SER-566 AND
SER-588, VARIANT [LARGE SCALE ANALYSIS] ILE-819, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341; SER-344; SER-588
AND SER-591, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[24]
FUNCTION.
PubMed=22908308; DOI=10.1083/jcb.201111091;
Chen Y., Wang Y., Zhang J., Deng Y., Jiang L., Song E., Wu X.S.,
Hammer J.A., Xu T., Lippincott-Schwartz J.;
"Rab10 and myosin-Va mediate insulin-stimulated GLUT4 storage vesicle
translocation in adipocytes.";
J. Cell Biol. 198:545-560(2012).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314; SER-341; SER-566;
THR-568; SER-570; SER-588; SER-591; SER-666 AND SER-754, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262; SER-588 AND
SER-591, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[27]
INVOLVEMENT IN NIDDM5.
PubMed=25043022; DOI=10.1038/nature13425;
Moltke I., Grarup N., Jorgensen M.E., Bjerregaard P., Treebak J.T.,
Fumagalli M., Korneliussen T.S., Andersen M.A., Nielsen T.S.,
Krarup N.T., Gjesing A.P., Zierath J.R., Linneberg A., Wu X., Sun G.,
Jin X., Al-Aama J., Wang J., Borch-Johnsen K., Pedersen O.,
Nielsen R., Albrechtsen A., Hansen T.;
"A common Greenlandic TBC1D4 variant confers muscle insulin resistance
and type 2 diabetes.";
Nature 512:190-193(2014).
[28]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 874-1170.
PubMed=21454505; DOI=10.1074/jbc.M110.217323;
Park S.Y., Jin W., Woo J.R., Shoelson S.E.;
"Crystal structures of human TBC1D1 and TBC1D4 (AS160) RabGTPase-
activating protein (RabGAP) domains reveal critical elements for GLUT4
translocation.";
J. Biol. Chem. 286:18130-18138(2011).
-!- FUNCTION: May act as a GTPase-activating protein for RAB2A, RAB8A,
RAB10 and RAB14. Isoform 2 promotes insulin-induced glucose
transporter SLC2A4/GLUT4 translocation at the plasma membrane,
thus increasing glucose uptake. {ECO:0000269|PubMed:15971998,
ECO:0000269|PubMed:18771725, ECO:0000269|PubMed:22908308}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18771725}.
Note=Isoform 2 shows a cytoplasmic perinuclear localization in a
myoblastic cell line in resting and insulin-stimulated cells.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=O60343-1; Sequence=Displayed;
Name=2; Synonyms=AS160_tv2;
IsoId=O60343-2; Sequence=VSP_036869;
Note=Contains a phosphoserine at position 666. Contains a
phosphoserine at position 672. Contains a phosphoserine at
position 678. {ECO:0000244|PubMed:18669648};
Name=3; Synonyms=AS160_tv3;
IsoId=O60343-3; Sequence=VSP_036870;
Name=4;
IsoId=O60343-4; Sequence=VSP_036868, VSP_036871;
Note=No experimental confirmation available.;
Name=5;
IsoId=O60343-5; Sequence=VSP_036868;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Isoform 2 is the highest
overexpressed in most tissues. Isoform 1 is highly expressed in
skeletal muscle and heart, but was not detectable in the liver nor
in adipose tissue. Isoform 2 is strongly expressed in adrenal and
thyroid gland, and also in lung, kidney, colon, brain and adipose
tissue. Isoform 2 is moderately expressed in skeletal muscle.
Expressed in pancreatic Langerhans islets, including beta cells
(at protein level). Expression is decreased by twofold in
pancreatic islets in type 2 diabetes patients compared to control
subjects. Up-regulated in T-cells from patients with atopic
dermatitis. {ECO:0000269|PubMed:15304337,
ECO:0000269|PubMed:18276765, ECO:0000269|PubMed:18771725}.
-!- PTM: Phosphorylated by AKT1; insulin-induced. Also phosphorylated
by AMPK in response to insulin. Insulin-stimulated phosphorylation
is required for SLC2A4/GLUT4 translocation. Has no effect on
SLC2A4/GLUT4 internalization. Physiological hyperinsulinemia
increases phosphorylation in skeletal muscle. Insulin-stimulated
phosphorylation is reduced by 39% in type 2 diabetic patients.
{ECO:0000269|PubMed:11994271, ECO:0000269|PubMed:15919790,
ECO:0000269|PubMed:18771725}.
-!- DISEASE: Diabetes mellitus, non-insulin-dependent, 5 (NIDDM5)
[MIM:616087]: A multifactorial disorder of glucose homeostasis
caused by a lack of sensitivity to the body's own insulin.
Affected individuals usually have an obese body habitus and
manifestations of a metabolic syndrome characterized by diabetes,
insulin resistance, hypertension and hypertriglyceridemia. The
disease results in long-term complications that affect the eyes,
kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:25043022}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=BAA25529.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; FM207106; CAR62509.1; -; mRNA.
EMBL; FM207107; CAR62510.1; -; mRNA.
EMBL; AB449885; BAH16628.1; -; mRNA.
EMBL; AB011175; BAA25529.2; ALT_INIT; mRNA.
EMBL; AK300468; BAG62187.1; -; mRNA.
EMBL; AK304091; BAG64997.1; -; mRNA.
EMBL; AL139230; CAH70991.1; -; Genomic_DNA.
EMBL; AL162571; CAH70991.1; JOINED; Genomic_DNA.
EMBL; AL162571; CAI39591.1; -; Genomic_DNA.
EMBL; AL139230; CAI39591.1; JOINED; Genomic_DNA.
EMBL; BC151239; AAI51240.1; -; mRNA.
EMBL; CR749622; CAH18416.1; -; mRNA.
CCDS; CCDS41901.1; -. [O60343-1]
CCDS; CCDS66563.1; -. [O60343-2]
CCDS; CCDS66564.1; -. [O60343-3]
PIR; T00261; T00261.
RefSeq; NP_001273587.1; NM_001286658.2. [O60343-3]
RefSeq; NP_001273588.1; NM_001286659.2. [O60343-2]
RefSeq; NP_055647.2; NM_014832.4. [O60343-1]
UniGene; Hs.210891; -.
PDB; 3QYB; X-ray; 3.50 A; A=874-1170.
PDBsum; 3QYB; -.
ProteinModelPortal; O60343; -.
SMR; O60343; -.
BioGrid; 115213; 61.
IntAct; O60343; 28.
MINT; MINT-5005871; -.
STRING; 9606.ENSP00000366863; -.
TCDB; 8.A.87.1.1; the tbc1 domain (tbc1) family.
iPTMnet; O60343; -.
PhosphoSitePlus; O60343; -.
BioMuta; TBC1D4; -.
EPD; O60343; -.
MaxQB; O60343; -.
PaxDb; O60343; -.
PeptideAtlas; O60343; -.
PRIDE; O60343; -.
DNASU; 9882; -.
Ensembl; ENST00000377625; ENSP00000366852; ENSG00000136111. [O60343-2]
Ensembl; ENST00000377636; ENSP00000366863; ENSG00000136111. [O60343-1]
Ensembl; ENST00000431480; ENSP00000395986; ENSG00000136111. [O60343-3]
GeneID; 9882; -.
KEGG; hsa:9882; -.
UCSC; uc001vjl.3; human. [O60343-1]
CTD; 9882; -.
DisGeNET; 9882; -.
EuPathDB; HostDB:ENSG00000136111.12; -.
GeneCards; TBC1D4; -.
H-InvDB; HIX0017963; -.
HGNC; HGNC:19165; TBC1D4.
HPA; HPA040145; -.
HPA; HPA059885; -.
MalaCards; TBC1D4; -.
MIM; 612465; gene.
MIM; 616087; phenotype.
neXtProt; NX_O60343; -.
OpenTargets; ENSG00000136111; -.
PharmGKB; PA38807; -.
eggNOG; KOG4436; Eukaryota.
eggNOG; ENOG410YWJY; LUCA.
GeneTree; ENSGT00750000117238; -.
HOVERGEN; HBG059376; -.
InParanoid; O60343; -.
KO; K17902; -.
OMA; LWYHKLC; -.
OrthoDB; EOG091G01QW; -.
PhylomeDB; O60343; -.
TreeFam; TF317184; -.
Reactome; R-HSA-1445148; Translocation of GLUT4 to the plasma membrane.
SIGNOR; O60343; -.
ChiTaRS; TBC1D4; human.
EvolutionaryTrace; O60343; -.
GeneWiki; TBC1D4; -.
GenomeRNAi; 9882; -.
PMAP-CutDB; O60343; -.
PRO; PR:O60343; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000136111; -.
CleanEx; HS_TBC1D4; -.
ExpressionAtlas; O60343; baseline and differential.
Genevisible; O60343; HS.
GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005622; C:intracellular; IBA:GO_Central.
GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
GO; GO:0017137; F:Rab GTPase binding; IBA:GO_Central.
GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
GO; GO:0032869; P:cellular response to insulin stimulus; IMP:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0031339; P:negative regulation of vesicle fusion; IEA:Ensembl.
GO; GO:0031338; P:regulation of vesicle fusion; IBA:GO_Central.
GO; GO:0016192; P:vesicle-mediated transport; IMP:UniProtKB.
Gene3D; 2.30.29.30; -; 2.
InterPro; IPR021785; DUF3350.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR006020; PTB/PI_dom.
InterPro; IPR000195; Rab-GTPase-TBC_dom.
InterPro; IPR035969; Rab-GTPase_TBC_sf.
InterPro; IPR033564; TBC1D4.
PANTHER; PTHR22957:SF195; PTHR22957:SF195; 1.
Pfam; PF11830; DUF3350; 1.
Pfam; PF00640; PID; 2.
Pfam; PF00566; RabGAP-TBC; 1.
SMART; SM00462; PTB; 2.
SMART; SM00164; TBC; 1.
SUPFAM; SSF47923; SSF47923; 2.
SUPFAM; SSF50729; SSF50729; 3.
PROSITE; PS01179; PID; 1.
PROSITE; PS50086; TBC_RABGAP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Diabetes mellitus; GTPase activation; Methylation;
Phosphoprotein; Polymorphism; Reference proteome; Repeat.
CHAIN 1 1298 TBC1 domain family member 4.
/FTId=PRO_0000208026.
DOMAIN 53 209 PID 1. {ECO:0000255|PROSITE-
ProRule:PRU00148}.
DOMAIN 312 468 PID 2. {ECO:0000255|PROSITE-
ProRule:PRU00148}.
DOMAIN 918 1112 Rab-GAP TBC. {ECO:0000255|PROSITE-
ProRule:PRU00163}.
COMPBIAS 672 759 Ser-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 262 262 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 314 314 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 318 318 Phosphoserine; by PKB/AKT1.
{ECO:0000250|UniProtKB:Q8BYJ6}.
MOD_RES 341 341 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 344 344 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:21406692}.
MOD_RES 477 477 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 566 566 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 568 568 Phosphothreonine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 570 570 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 577 577 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q8BYJ6}.
MOD_RES 588 588 Phosphoserine; by PKB/AKT1.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:11994271}.
MOD_RES 591 591 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 609 609 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BYJ6}.
MOD_RES 613 613 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8BYJ6}.
MOD_RES 617 617 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BYJ6}.
MOD_RES 642 642 Phosphothreonine; by PKB/AKT1.
{ECO:0000269|PubMed:11994271,
ECO:0000269|PubMed:18771725}.
MOD_RES 666 666 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 751 751 Phosphoserine; by PKB/AKT1.
{ECO:0000250|UniProtKB:Q8BYJ6}.
MOD_RES 754 754 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 757 757 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BYJ6}.
MOD_RES 763 763 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8BYJ6}.
VAR_SEQ 1 783 Missing (in isoform 4 and isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036868.
VAR_SEQ 678 740 Missing (in isoform 2).
{ECO:0000303|PubMed:18771725}.
/FTId=VSP_036869.
VAR_SEQ 733 740 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005,
ECO:0000303|PubMed:18771725}.
/FTId=VSP_036870.
VAR_SEQ 865 917 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036871.
VARIANT 619 619 P -> L (in dbSNP:rs56223054).
/FTId=VAR_061891.
VARIANT 819 819 V -> I (in dbSNP:rs1062087).
{ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005,
ECO:0000269|PubMed:19077034,
ECO:0000269|PubMed:9628581}.
/FTId=VAR_059855.
VARIANT 1119 1119 V -> A (in dbSNP:rs58232698).
/FTId=VAR_061892.
VARIANT 1147 1147 T -> M (in dbSNP:rs9600455).
/FTId=VAR_052534.
VARIANT 1275 1275 V -> A (in dbSNP:rs557337).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:19077034,
ECO:0000269|PubMed:9628581}.
/FTId=VAR_052535.
VARIANT 1284 1284 L -> I (in dbSNP:rs11616741).
/FTId=VAR_054862.
MUTAGEN 318 318 S->A: 80% reduction of insulin-stimulated
GLUT4 translocation; when associated with
A-588; A-642 and A-751.
{ECO:0000269|PubMed:12637568}.
MUTAGEN 588 588 S->A: 80% reduction of insulin-stimulated
GLUT4 translocation; when associated with
A-318; A-642 and A-751.
{ECO:0000269|PubMed:12637568}.
MUTAGEN 642 642 T->A: 80% reduction of insulin-stimulated
GLUT4 translocation; when associated with
A-318; A-588 and A-751.
{ECO:0000269|PubMed:12637568}.
MUTAGEN 751 751 S->A: 80% reduction of insulin-stimulated
GLUT4 translocation; when associated with
A-318; A-588 and A-642.
{ECO:0000269|PubMed:12637568}.
MUTAGEN 972 972 R->K: Loss of Rab GTPase activation. Only
20% reduction of GLUT4 translocation;
even when associated with A-318; A-588;
A-642 and A-751.
{ECO:0000269|PubMed:12637568,
ECO:0000269|PubMed:15971998}.
CONFLICT 644 644 S -> G (in Ref. 7; CAH18416).
{ECO:0000305}.
CONFLICT 845 845 K -> E (in Ref. 7; CAH18416).
{ECO:0000305}.
CONFLICT 864 864 E -> EG (in Ref. 2; BAH16628, 3; BAA25529
and 6; AAI51240). {ECO:0000305}.
CONFLICT 867 867 R -> G (in Ref. 7; CAH18416).
{ECO:0000305}.
CONFLICT 1137 1137 F -> L (in Ref. 7; CAH18416).
{ECO:0000305}.
CONFLICT 1178 1178 E -> G (in Ref. 4; BAG62187).
{ECO:0000305}.
TURN 874 877 {ECO:0000244|PDB:3QYB}.
HELIX 887 896 {ECO:0000244|PDB:3QYB}.
HELIX 908 917 {ECO:0000244|PDB:3QYB}.
TURN 921 923 {ECO:0000244|PDB:3QYB}.
HELIX 924 937 {ECO:0000244|PDB:3QYB}.
STRAND 943 946 {ECO:0000244|PDB:3QYB}.
HELIX 952 956 {ECO:0000244|PDB:3QYB}.
HELIX 963 970 {ECO:0000244|PDB:3QYB}.
HELIX 978 981 {ECO:0000244|PDB:3QYB}.
HELIX 986 1001 {ECO:0000244|PDB:3QYB}.
TURN 1002 1005 {ECO:0000244|PDB:3QYB}.
HELIX 1011 1019 {ECO:0000244|PDB:3QYB}.
HELIX 1024 1035 {ECO:0000244|PDB:3QYB}.
TURN 1036 1039 {ECO:0000244|PDB:3QYB}.
TURN 1041 1044 {ECO:0000244|PDB:3QYB}.
HELIX 1049 1063 {ECO:0000244|PDB:3QYB}.
HELIX 1067 1075 {ECO:0000244|PDB:3QYB}.
HELIX 1080 1083 {ECO:0000244|PDB:3QYB}.
HELIX 1085 1090 {ECO:0000244|PDB:3QYB}.
TURN 1091 1095 {ECO:0000244|PDB:3QYB}.
HELIX 1098 1108 {ECO:0000244|PDB:3QYB}.
TURN 1109 1111 {ECO:0000244|PDB:3QYB}.
HELIX 1115 1124 {ECO:0000244|PDB:3QYB}.
TURN 1128 1133 {ECO:0000244|PDB:3QYB}.
HELIX 1137 1144 {ECO:0000244|PDB:3QYB}.
TURN 1145 1149 {ECO:0000244|PDB:3QYB}.
HELIX 1153 1164 {ECO:0000244|PDB:3QYB}.
SEQUENCE 1298 AA; 146563 MW; 8DC70CE887C0B311 CRC64;
MEPPSCIQDE PFPHPLEPEP GVSAQPGPGK PSDKRFRLWY VGGSCLDHRT TLPMLPWLMA
EIRRRSQKPE AGGCGAPAAR EVILVLSAPF LRCVPAPGAG ASGGTSPSAT QPNPAVFIFE
HKAQHISRFI HNSHDLTYFA YLIKAQPDDP ESQMACHVFR ATDPSQVPDV ISSIRQLSKA
AMKEDAKPSK DNEDAFYNSQ KFEVLYCGKV TVTHKKAPSS LIDDCMEKFS LHEQQRLKIQ
GEQRGPDPGE DLADLEVVVP GSPGDCLPEE ADGTDTHLGL PAGASQPALT SSRVCFPERI
LEDSGFDEQQ EFRSRCSSVT GVQRRVHEGS QKSQPRRRHA SAPSHVQPSD SEKNRTMLFQ
VGRFEINLIS PDTKSVVLEK NFKDISSCSQ GIKHVDHFGF ICRESPEPGL SQYICYVFQC
ASESLVDEVM LTLKQAFSTA AALQSAKTQI KLCEACPMHS LHKLCERIEG LYPPRAKLVI
QRHLSSLTDN EQADIFERVQ KMKPVSDQEE NELVILHLRQ LCEAKQKTHV HIGEGPSTIS
NSTIPENATS SGRFKLDILK NKAKRSLTSS LENIFSRGAN RMRGRLGSVD SFERSNSLAS
EKDYSPGDSP PGTPPASPPS SAWQTFPEED SDSPQFRRRA HTFSHPPSST KRKLNLQDGR
AQGVRSPLLR QSSSEQCSNL SSVRRMYKES NSSSSLPSLH TSFSAPSFTA PSFLKSFYQN
SGRLSPQYEN EIRQDTASES SDGEGRKRTS STCSNESLSV GGTSVTPRRI SWRQRIFLRV
ASPMNKSPSA MQQQDGLDRN ELLPLSPLSP TMEEEPLVVF LSGEDDPEKI EERKKSKELR
SLWRKAIHQQ ILLLRMEKEN QKLEASRDEL QSRKVKLDYE EVGACQKEVL ITWDKKLLNC
RAKIRCDMED IHTLLKEGVP KSRRGEIWQF LALQYRLRHR LPNKQQPPDI SYKELLKQLT
AQQHAILVDL GRTFPTHPYF SVQLGPGQLS LFNLLKAYSL LDKEVGYCQG ISFVAGVLLL
HMSEEQAFEM LKFLMYDLGF RKQYRPDMMS LQIQMYQLSR LLHDYHRDLY NHLEENEISP
SLYAAPWFLT LFASQFSLGF VARVFDIIFL QGTEVIFKVA LSLLSSQETL IMECESFENI
VEFLKNTLPD MNTSEMEKII TQVFEMDISK QLHAYEVEYH VLQDELQESS YSCEDSETLE
KLERANSQLK RQNMDLLEKL QVAHTKIQAL ESNLENLLTR ETKMKSLIRT LEQEKMAYQK
TVEQLRKLLP ADALVNCDLL LRDLNCNPNN KAKIGNKP


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