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MGP004038

UniProt Annotations

Entry Information

Gene Name	TBC1 domain family, member 4
Protein Entry	TBCD4_HUMAN
UniProt ID	O60343
Species	Human

Comments

Comment type	Description
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.; 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.;
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}.
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:16964243, ECO:0000269\|PubMed:17081983, ECO:0000269\|PubMed:18669648, ECO:0000269\|PubMed:18771725, ECO:0000269\|PubMed:19690332, ECO:0000269\|PubMed:20068231, ECO:0000269\|PubMed:21406692}.
Sequence Caution	Sequence=BAA25529.2; Type=Erroneous initiation; Evidence={ECO:0000305};
Similarity	Contains 1 Rab-GAP TBC domain. {ECO:0000255\|PROSITE- ProRule:PRU00163}.
Similarity	Contains 2 PID domains. {ECO:0000255\|PROSITE- ProRule:PRU00148}.
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.
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}.