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O60343

- TBCD4_HUMAN

UniProt

O60343 - TBCD4_HUMAN

Protein

TBC1 domain family member 4

Gene

TBC1D4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (07 Jun 2005)
      Previous versions | rss
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    Functioni

    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.3 Publications

    GO - Molecular functioni

    1. Rab GTPase activator activity Source: InterPro

    GO - Biological processi

    1. cellular response to insulin stimulus Source: UniProtKB
    2. membrane organization Source: Reactome
    3. negative regulation of vesicle fusion Source: Ensembl
    4. vesicle-mediated transport Source: UniProtKB

    Keywords - Molecular functioni

    GTPase activation

    Enzyme and pathway databases

    ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    TBC1 domain family member 4
    Alternative name(s):
    Akt substrate of 160 kDa
    Short name:
    AS160
    Gene namesi
    Name:TBC1D4
    Synonyms:AS160, KIAA0603
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:19165. TBC1D4.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Isoform 2 shows a cytoplasmic perinuclear localization in a myoblastic cell line in resting and insulin-stimulated cells.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytoplasmic vesicle membrane Source: Reactome
    3. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi318 – 3181S → A: 80% reduction of insulin-stimulated GLUT4 translocation; when associated with A-588; A-642 and A-751. 1 Publication
    Mutagenesisi588 – 5881S → A: 80% reduction of insulin-stimulated GLUT4 translocation; when associated with A-318; A-642 and A-751. 1 Publication
    Mutagenesisi642 – 6421T → A: 80% reduction of insulin-stimulated GLUT4 translocation; when associated with A-318; A-588 and A-751. 1 Publication
    Mutagenesisi751 – 7511S → A: 80% reduction of insulin-stimulated GLUT4 translocation; when associated with A-318; A-588 and A-642. 1 Publication
    Mutagenesisi972 – 9721R → 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. 2 Publications

    Organism-specific databases

    PharmGKBiPA38807.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12981298TBC1 domain family member 4PRO_0000208026Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei318 – 3181Phosphoserine; by PKB/AKT1By similarity
    Modified residuei341 – 3411Phosphoserine4 Publications
    Modified residuei344 – 3441Phosphoserine3 Publications
    Modified residuei477 – 4771N6-acetyllysine1 Publication
    Modified residuei566 – 5661Phosphoserine4 Publications
    Modified residuei568 – 5681Phosphothreonine2 Publications
    Modified residuei570 – 5701Phosphoserine3 Publications
    Modified residuei588 – 5881Phosphoserine; by PKB/AKT16 Publications
    Modified residuei591 – 5911Phosphoserine3 Publications
    Modified residuei642 – 6421Phosphothreonine; by PKB/AKT13 Publications
    Modified residuei751 – 7511Phosphoserine; by PKB/AKT1By similarity

    Post-translational modificationi

    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.9 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO60343.
    PaxDbiO60343.
    PRIDEiO60343.

    PTM databases

    PhosphoSiteiO60343.

    Miscellaneous databases

    PMAP-CutDBO60343.

    Expressioni

    Tissue specificityi

    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.3 Publications

    Gene expression databases

    ArrayExpressiO60343.
    BgeeiO60343.
    CleanExiHS_TBC1D4.
    GenevestigatoriO60343.

    Organism-specific databases

    HPAiCAB011623.
    HPA040145.

    Interactioni

    Protein-protein interaction databases

    BioGridi115213. 20 interactions.
    IntActiO60343. 20 interactions.
    MINTiMINT-5005871.
    STRINGi9606.ENSP00000366863.

    Structurei

    Secondary structure

    1
    1298
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni874 – 8774
    Helixi887 – 89610
    Helixi908 – 91710
    Turni921 – 9233
    Helixi924 – 93714
    Beta strandi943 – 9464
    Helixi952 – 9565
    Helixi963 – 9708
    Helixi978 – 9814
    Helixi986 – 100116
    Turni1002 – 10054
    Helixi1011 – 10199
    Helixi1024 – 103512
    Turni1036 – 10394
    Turni1041 – 10444
    Helixi1049 – 106315
    Helixi1067 – 10759
    Helixi1080 – 10834
    Helixi1085 – 10906
    Turni1091 – 10955
    Helixi1098 – 110811
    Turni1109 – 11113
    Helixi1115 – 112410
    Turni1128 – 11336
    Helixi1137 – 11448
    Turni1145 – 11495
    Helixi1153 – 116412

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3QYBX-ray3.50A874-1170[»]
    ProteinModelPortaliO60343.
    SMRiO60343. Positions 874-1168.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60343.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini53 – 209157PID 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini312 – 468157PID 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini918 – 1112195Rab-GAP TBCPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi672 – 75988Ser-richAdd
    BLAST

    Sequence similaritiesi

    Contains 2 PID domains.PROSITE-ProRule annotation
    Contains 1 Rab-GAP TBC domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5210.
    HOVERGENiHBG059376.
    InParanoidiO60343.
    KOiK17902.
    OMAiFPHPLEP.
    OrthoDBiEOG76T9QM.
    PhylomeDBiO60343.
    TreeFamiTF317184.

    Family and domain databases

    Gene3Di2.30.29.30. 3 hits.
    InterProiIPR021785. DUF3350.
    IPR011993. PH_like_dom.
    IPR006020. PTB/PI_dom.
    IPR000195. Rab-GTPase-TBC_dom.
    [Graphical view]
    PfamiPF11830. DUF3350. 1 hit.
    PF00640. PID. 2 hits.
    PF00566. RabGAP-TBC. 1 hit.
    [Graphical view]
    SMARTiSM00462. PTB. 2 hits.
    SM00164. TBC. 1 hit.
    [Graphical view]
    SUPFAMiSSF47923. SSF47923. 2 hits.
    PROSITEiPS01179. PID. 1 hit.
    PS50086. TBC_RABGAP. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O60343-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEPPSCIQDE PFPHPLEPEP GVSAQPGPGK PSDKRFRLWY VGGSCLDHRT     50
    TLPMLPWLMA EIRRRSQKPE AGGCGAPAAR EVILVLSAPF LRCVPAPGAG 100
    ASGGTSPSAT QPNPAVFIFE HKAQHISRFI HNSHDLTYFA YLIKAQPDDP 150
    ESQMACHVFR ATDPSQVPDV ISSIRQLSKA AMKEDAKPSK DNEDAFYNSQ 200
    KFEVLYCGKV TVTHKKAPSS LIDDCMEKFS LHEQQRLKIQ GEQRGPDPGE 250
    DLADLEVVVP GSPGDCLPEE ADGTDTHLGL PAGASQPALT SSRVCFPERI 300
    LEDSGFDEQQ EFRSRCSSVT GVQRRVHEGS QKSQPRRRHA SAPSHVQPSD 350
    SEKNRTMLFQ VGRFEINLIS PDTKSVVLEK NFKDISSCSQ GIKHVDHFGF 400
    ICRESPEPGL SQYICYVFQC ASESLVDEVM LTLKQAFSTA AALQSAKTQI 450
    KLCEACPMHS LHKLCERIEG LYPPRAKLVI QRHLSSLTDN EQADIFERVQ 500
    KMKPVSDQEE NELVILHLRQ LCEAKQKTHV HIGEGPSTIS NSTIPENATS 550
    SGRFKLDILK NKAKRSLTSS LENIFSRGAN RMRGRLGSVD SFERSNSLAS 600
    EKDYSPGDSP PGTPPASPPS SAWQTFPEED SDSPQFRRRA HTFSHPPSST 650
    KRKLNLQDGR AQGVRSPLLR QSSSEQCSNL SSVRRMYKES NSSSSLPSLH 700
    TSFSAPSFTA PSFLKSFYQN SGRLSPQYEN EIRQDTASES SDGEGRKRTS 750
    STCSNESLSV GGTSVTPRRI SWRQRIFLRV ASPMNKSPSA MQQQDGLDRN 800
    ELLPLSPLSP TMEEEPLVVF LSGEDDPEKI EERKKSKELR SLWRKAIHQQ 850
    ILLLRMEKEN QKLEASRDEL QSRKVKLDYE EVGACQKEVL ITWDKKLLNC 900
    RAKIRCDMED IHTLLKEGVP KSRRGEIWQF LALQYRLRHR LPNKQQPPDI 950
    SYKELLKQLT AQQHAILVDL GRTFPTHPYF SVQLGPGQLS LFNLLKAYSL 1000
    LDKEVGYCQG ISFVAGVLLL HMSEEQAFEM LKFLMYDLGF RKQYRPDMMS 1050
    LQIQMYQLSR LLHDYHRDLY NHLEENEISP SLYAAPWFLT LFASQFSLGF 1100
    VARVFDIIFL QGTEVIFKVA LSLLSSQETL IMECESFENI VEFLKNTLPD 1150
    MNTSEMEKII TQVFEMDISK QLHAYEVEYH VLQDELQESS YSCEDSETLE 1200
    KLERANSQLK RQNMDLLEKL QVAHTKIQAL ESNLENLLTR ETKMKSLIRT 1250
    LEQEKMAYQK TVEQLRKLLP ADALVNCDLL LRDLNCNPNN KAKIGNKP 1298
    Length:1,298
    Mass (Da):146,563
    Last modified:June 7, 2005 - v2
    Checksum:i8DC70CE887C0B311
    GO
    Isoform 2 (identifier: O60343-2) [UniParc]FASTAAdd to Basket

    Also known as: AS160_tv2

    The sequence of this isoform differs from the canonical sequence as follows:
         678-740: Missing.

    Note: Contains a phosphoserine at position 666. Contains a phosphoserine at position 672. Contains a phosphoserine at position 678.

    Show »
    Length:1,235
    Mass (Da):139,556
    Checksum:i2A688BE2C17FD422
    GO
    Isoform 3 (identifier: O60343-3) [UniParc]FASTAAdd to Basket

    Also known as: AS160_tv3

    The sequence of this isoform differs from the canonical sequence as follows:
         733-740: Missing.

    Show »
    Length:1,290
    Mass (Da):145,689
    Checksum:i38A0D7A205A0D252
    GO
    Isoform 4 (identifier: O60343-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-783: Missing.
         865-917: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:462
    Mass (Da):53,850
    Checksum:iB063DE6885C060DA
    GO
    Isoform 5 (identifier: O60343-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-783: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:515
    Mass (Da):60,095
    Checksum:i18CDA70728CE1CBB
    GO

    Sequence cautioni

    The sequence BAA25529.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti644 – 6441S → G in CAH18416. (PubMed:17974005)Curated
    Sequence conflicti845 – 8451K → E in CAH18416. (PubMed:17974005)Curated
    Sequence conflicti864 – 8641E → EG in BAH16628. (PubMed:19077034)Curated
    Sequence conflicti864 – 8641E → EG in BAA25529. (PubMed:9628581)Curated
    Sequence conflicti864 – 8641E → EG in AAI51240. (PubMed:15489334)Curated
    Sequence conflicti867 – 8671R → G in CAH18416. (PubMed:17974005)Curated
    Sequence conflicti1137 – 11371F → L in CAH18416. (PubMed:17974005)Curated
    Sequence conflicti1178 – 11781E → G in BAG62187. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti619 – 6191P → L.
    Corresponds to variant rs56223054 [ dbSNP | Ensembl ].
    VAR_061891
    Natural varianti819 – 8191V → I.5 Publications
    Corresponds to variant rs1062087 [ dbSNP | Ensembl ].
    VAR_059855
    Natural varianti1119 – 11191V → A.
    Corresponds to variant rs58232698 [ dbSNP | Ensembl ].
    VAR_061892
    Natural varianti1147 – 11471T → M.
    Corresponds to variant rs9600455 [ dbSNP | Ensembl ].
    VAR_052534
    Natural varianti1275 – 12751V → A.3 Publications
    Corresponds to variant rs557337 [ dbSNP | Ensembl ].
    VAR_052535
    Natural varianti1284 – 12841L → I.
    Corresponds to variant rs11616741 [ dbSNP | Ensembl ].
    VAR_054862

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 783783Missing in isoform 4 and isoform 5. 1 PublicationVSP_036868Add
    BLAST
    Alternative sequencei678 – 74063Missing in isoform 2. 1 PublicationVSP_036869Add
    BLAST
    Alternative sequencei733 – 7408Missing in isoform 3. 2 PublicationsVSP_036870
    Alternative sequencei865 – 91753Missing in isoform 4. 1 PublicationVSP_036871Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FM207106 mRNA. Translation: CAR62509.1.
    FM207107 mRNA. Translation: CAR62510.1.
    AB449885 mRNA. Translation: BAH16628.1.
    AB011175 mRNA. Translation: BAA25529.2. Different initiation.
    AK300468 mRNA. Translation: BAG62187.1.
    AK304091 mRNA. Translation: BAG64997.1.
    AL139230, AL162571 Genomic DNA. Translation: CAH70991.1.
    AL162571, AL139230 Genomic DNA. Translation: CAI39591.1.
    BC151239 mRNA. Translation: AAI51240.1.
    CR749622 mRNA. Translation: CAH18416.1.
    CCDSiCCDS41901.1. [O60343-1]
    CCDS66563.1. [O60343-2]
    CCDS66564.1. [O60343-3]
    PIRiT00261.
    RefSeqiNP_001273587.1. NM_001286658.1. [O60343-3]
    NP_001273588.1. NM_001286659.1. [O60343-2]
    NP_055647.2. NM_014832.3. [O60343-1]
    UniGeneiHs.210891.

    Genome annotation databases

    EnsembliENST00000377625; ENSP00000366852; ENSG00000136111. [O60343-2]
    ENST00000377636; ENSP00000366863; ENSG00000136111. [O60343-1]
    ENST00000431480; ENSP00000395986; ENSG00000136111. [O60343-3]
    GeneIDi9882.
    KEGGihsa:9882.
    UCSCiuc001vjl.1. human. [O60343-1]
    uc010aer.2. human. [O60343-3]
    uc010aes.2. human. [O60343-2]
    uc010tht.1. human. [O60343-5]
    uc010thu.1. human. [O60343-4]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FM207106 mRNA. Translation: CAR62509.1 .
    FM207107 mRNA. Translation: CAR62510.1 .
    AB449885 mRNA. Translation: BAH16628.1 .
    AB011175 mRNA. Translation: BAA25529.2 . Different initiation.
    AK300468 mRNA. Translation: BAG62187.1 .
    AK304091 mRNA. Translation: BAG64997.1 .
    AL139230 , AL162571 Genomic DNA. Translation: CAH70991.1 .
    AL162571 , AL139230 Genomic DNA. Translation: CAI39591.1 .
    BC151239 mRNA. Translation: AAI51240.1 .
    CR749622 mRNA. Translation: CAH18416.1 .
    CCDSi CCDS41901.1. [O60343-1 ]
    CCDS66563.1. [O60343-2 ]
    CCDS66564.1. [O60343-3 ]
    PIRi T00261.
    RefSeqi NP_001273587.1. NM_001286658.1. [O60343-3 ]
    NP_001273588.1. NM_001286659.1. [O60343-2 ]
    NP_055647.2. NM_014832.3. [O60343-1 ]
    UniGenei Hs.210891.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3QYB X-ray 3.50 A 874-1170 [» ]
    ProteinModelPortali O60343.
    SMRi O60343. Positions 874-1168.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115213. 20 interactions.
    IntActi O60343. 20 interactions.
    MINTi MINT-5005871.
    STRINGi 9606.ENSP00000366863.

    PTM databases

    PhosphoSitei O60343.

    Proteomic databases

    MaxQBi O60343.
    PaxDbi O60343.
    PRIDEi O60343.

    Protocols and materials databases

    DNASUi 9882.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000377625 ; ENSP00000366852 ; ENSG00000136111 . [O60343-2 ]
    ENST00000377636 ; ENSP00000366863 ; ENSG00000136111 . [O60343-1 ]
    ENST00000431480 ; ENSP00000395986 ; ENSG00000136111 . [O60343-3 ]
    GeneIDi 9882.
    KEGGi hsa:9882.
    UCSCi uc001vjl.1. human. [O60343-1 ]
    uc010aer.2. human. [O60343-3 ]
    uc010aes.2. human. [O60343-2 ]
    uc010tht.1. human. [O60343-5 ]
    uc010thu.1. human. [O60343-4 ]

    Organism-specific databases

    CTDi 9882.
    GeneCardsi GC13M075858.
    H-InvDB HIX0017963.
    HGNCi HGNC:19165. TBC1D4.
    HPAi CAB011623.
    HPA040145.
    MIMi 612465. gene.
    neXtProti NX_O60343.
    PharmGKBi PA38807.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5210.
    HOVERGENi HBG059376.
    InParanoidi O60343.
    KOi K17902.
    OMAi FPHPLEP.
    OrthoDBi EOG76T9QM.
    PhylomeDBi O60343.
    TreeFami TF317184.

    Enzyme and pathway databases

    Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.

    Miscellaneous databases

    ChiTaRSi TBC1D4. human.
    EvolutionaryTracei O60343.
    GeneWikii TBC1D4.
    GenomeRNAii 9882.
    NextBioi 37248.
    PMAP-CutDB O60343.
    PROi O60343.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60343.
    Bgeei O60343.
    CleanExi HS_TBC1D4.
    Genevestigatori O60343.

    Family and domain databases

    Gene3Di 2.30.29.30. 3 hits.
    InterProi IPR021785. DUF3350.
    IPR011993. PH_like_dom.
    IPR006020. PTB/PI_dom.
    IPR000195. Rab-GTPase-TBC_dom.
    [Graphical view ]
    Pfami PF11830. DUF3350. 1 hit.
    PF00640. PID. 2 hits.
    PF00566. RabGAP-TBC. 1 hit.
    [Graphical view ]
    SMARTi SM00462. PTB. 2 hits.
    SM00164. TBC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47923. SSF47923. 2 hits.
    PROSITEi PS01179. PID. 1 hit.
    PS50086. TBC_RABGAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a novel AS160 splice variant that regulates GLUT4 translocation and glucose-uptake in rat muscle cells."
      Baus D., Heermeier K., De Hoop M., Metz-Weidmann C., Gassenhuber J., Dittrich W., Welte S., Tennagels N.
      Cell. Signal. 20:2237-2246(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT THR-642.
      Tissue: Testis.
    2. "Identification and characterization of a novel Tre-2/Bub2/Cdc16 (TBC) protein that possesses Rab3A-GAP activity."
      Ishibashi K., Kanno E., Itoh T., Fukuda M.
      Genes Cells 14:41-52(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ILE-819 AND ALA-1275.
      Tissue: Brain.
    3. "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."
      Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS ILE-819 AND ALA-1275.
      Tissue: Brain.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
      Tissue: Placenta and Trachea.
    5. "The DNA sequence and analysis of human chromosome 13."
      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.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS ILE-819 AND ALA-1275.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 600-1298 (ISOFORM 3), VARIANT ILE-819.
      Tissue: Fetal liver.
    8. "A method to identify serine kinase substrates. Akt phosphorylates a novel adipocyte protein with a Rab GTPase-activating protein (GAP) domain."
      Kane S., Sano H., Liu S.C.H., Asara J.M., Lane W.S., Garner C.C., Lienhard G.E.
      J. Biol. Chem. 277:22115-22118(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-588 AND THR-642.
    9. "Insulin-stimulated phosphorylation of a Rab GTPase-activating protein regulates GLUT4 translocation."
      Sano H., Kane S., Sano E., Miinea C.P., Asara J.M., Lane W.S., Garner C.W., Lienhard G.E.
      J. Biol. Chem. 278:14599-14602(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SER-318; SER-588; THR-642; SER-751 AND ARG-972, EFFECT ON GLUT4 TRANSLOCATION.
    10. "AS160, the Akt substrate regulating GLUT4 translocation, has a functional Rab GTPase-activating protein domain."
      Miinea C.P., Sano H., Kane S., Sano E., Fukuda M., Peraenen J., Lane W.S., Lienhard G.E.
      Biochem. J. 391:87-93(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ARG-972.
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND SER-591, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Rab GTPase-activating protein AS160 is a major downstream effector of protein kinase B/Akt signaling in pancreatic beta-cells."
      Bouzakri K., Ribaux P., Tomas A., Parnaud G., Rickenbach K., Halban P.A.
      Diabetes 57:1195-1204(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    14. "Upregulation of the transcript level of GTPase activating protein KIAA0603 in T cells from patients with atopic dermatitis."
      Matsumoto Y., Imai Y., Lu Yoshida N., Sugita Y., Tanaka T., Tsujimoto G., Saito H., Oshida T.
      FEBS Lett. 572:135-140(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    15. "Insulin-stimulated phosphorylation of the Akt substrate AS160 is impaired in skeletal muscle of type 2 diabetic subjects."
      Karlsson H.K.R., Zierath J.R., Kane S., Krook A., Lienhard G.E., Wallberg-Henriksson H.
      Diabetes 54:1692-1697(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    16. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: 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), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566; THR-568; SER-570 AND SER-588, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    20. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-477, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341; SER-566 AND SER-588, VARIANT [LARGE SCALE ANALYSIS] ILE-819, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341; SER-344; SER-588 AND SER-591, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Rab10 and myosin-Va mediate insulin-stimulated GLUT4 storage vesicle translocation in adipocytes."
      Chen Y., Wang Y., Zhang J., Deng Y., Jiang L., Song E., Wu X.S., Hammer J.A., Xu T., Lippincott-Schwartz J.
      J. Cell Biol. 198:545-560(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    25. "Crystal structures of human TBC1D1 and TBC1D4 (AS160) RabGTPase-activating protein (RabGAP) domains reveal critical elements for GLUT4 translocation."
      Park S.Y., Jin W., Woo J.R., Shoelson S.E.
      J. Biol. Chem. 286:18130-18138(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 874-1170.

    Entry informationi

    Entry nameiTBCD4_HUMAN
    AccessioniPrimary (citable) accession number: O60343
    Secondary accession number(s): A7E2X8
    , B4DU25, B4E235, B6ETN8, B6ETN9, Q5W0B9, Q68D14
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2002
    Last sequence update: June 7, 2005
    Last modified: October 1, 2014
    This is version 128 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3