Details for: TBC1D4

Gene ID: 9882

Symbol: TBC1D4

Ensembl ID: ENSG00000136111

Description: TBC1 domain family member 4

Associated with

Other Information

Genular Protein ID: 3039517845

Symbol: TBCD4_HUMAN

Name: TBC1 domain family member 4

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 18771725

Title: Identification of a novel AS160 splice variant that regulates GLUT4 translocation and glucose-uptake in rat muscle cells.

PubMed ID: 18771725

DOI: 10.1016/j.cellsig.2008.08.010

PubMed ID: 19077034

Title: Identification and characterization of a novel Tre-2/Bub2/Cdc16 (TBC) protein that possesses Rab3A-GAP activity.

PubMed ID: 19077034

DOI: 10.1111/j.1365-2443.2008.01251.x

PubMed ID: 9628581

Title: 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.

PubMed ID: 9628581

DOI: 10.1093/dnares/5.1.31

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15057823

Title: The DNA sequence and analysis of human chromosome 13.

PubMed ID: 15057823

DOI: 10.1038/nature02379

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 17974005

Title: The full-ORF clone resource of the German cDNA consortium.

PubMed ID: 17974005

DOI: 10.1186/1471-2164-8-399

PubMed ID: 11994271

Title: A method to identify serine kinase substrates. Akt phosphorylates a novel adipocyte protein with a Rab GTPase-activating protein (GAP) domain.

PubMed ID: 11994271

DOI: 10.1074/jbc.c200198200

PubMed ID: 12637568

Title: Insulin-stimulated phosphorylation of a Rab GTPase-activating protein regulates GLUT4 translocation.

PubMed ID: 12637568

DOI: 10.1074/jbc.c300063200

PubMed ID: 15971998

Title: AS160, the Akt substrate regulating GLUT4 translocation, has a functional Rab GTPase-activating protein domain.

PubMed ID: 15971998

DOI: 10.1042/bj20050887

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 18276765

Title: Rab GTPase-activating protein AS160 is a major downstream effector of protein kinase B/Akt signaling in pancreatic beta-cells.

PubMed ID: 18276765

DOI: 10.2337/db07-1469

PubMed ID: 15304337

Title: Upregulation of the transcript level of GTPase activating protein KIAA0603 in T cells from patients with atopic dermatitis.

PubMed ID: 15304337

DOI: 10.1016/j.febslet.2004.07.023

PubMed ID: 15919790

Title: Insulin-stimulated phosphorylation of the Akt substrate AS160 is impaired in skeletal muscle of type 2 diabetic subjects.

PubMed ID: 15919790

DOI: 10.2337/diabetes.54.6.1692

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22908308

Title: Rab10 and myosin-Va mediate insulin-stimulated GLUT4 storage vesicle translocation in adipocytes.

PubMed ID: 22908308

DOI: 10.1083/jcb.201111091

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25043022

Title: A common Greenlandic TBC1D4 variant confers muscle insulin resistance and type 2 diabetes.

PubMed ID: 25043022

DOI: 10.1038/nature13425

PubMed ID: 21454505

Title: Crystal structures of human TBC1D1 and TBC1D4 (AS160) RabGTPase-activating protein (RabGAP) domains reveal critical elements for GLUT4 translocation.

PubMed ID: 21454505

DOI: 10.1074/jbc.m110.217323

Sequence Information:

  • Length: 1298
  • Mass: 146563
  • Checksum: 8DC70CE887C0B311
  • Sequence:
  • 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

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.