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O60343

- TBCD4_HUMAN

UniProt

O60343 - TBCD4_HUMAN

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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

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
Complete GO annotation...

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
Complete GO annotation...

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 – 3411Phosphoserine3 Publications
Modified residuei344 – 3441Phosphoserine2 Publications
Modified residuei477 – 4771N6-acetyllysine1 Publication
Modified residuei566 – 5661Phosphoserine3 Publications
Modified residuei568 – 5681Phosphothreonine1 Publication
Modified residuei570 – 5701Phosphoserine2 Publications
Modified residuei588 – 5881Phosphoserine; by PKB/AKT15 Publications
Modified residuei591 – 5911Phosphoserine2 Publications
Modified residuei642 – 6421Phosphothreonine; by PKB/AKT12 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

BgeeiO60343.
CleanExiHS_TBC1D4.
ExpressionAtlasiO60343. baseline and differential.
GenevestigatoriO60343.

Organism-specific databases

HPAiCAB011623.
HPA040145.

Interactioni

Protein-protein interaction databases

BioGridi115213. 30 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 – 8774Combined sources
Helixi887 – 89610Combined sources
Helixi908 – 91710Combined sources
Turni921 – 9233Combined sources
Helixi924 – 93714Combined sources
Beta strandi943 – 9464Combined sources
Helixi952 – 9565Combined sources
Helixi963 – 9708Combined sources
Helixi978 – 9814Combined sources
Helixi986 – 100116Combined sources
Turni1002 – 10054Combined sources
Helixi1011 – 10199Combined sources
Helixi1024 – 103512Combined sources
Turni1036 – 10394Combined sources
Turni1041 – 10444Combined sources
Helixi1049 – 106315Combined sources
Helixi1067 – 10759Combined sources
Helixi1080 – 10834Combined sources
Helixi1085 – 10906Combined sources
Turni1091 – 10955Combined sources
Helixi1098 – 110811Combined sources
Turni1109 – 11113Combined sources
Helixi1115 – 112410Combined sources
Turni1128 – 11336Combined sources
Helixi1137 – 11448Combined sources
Turni1145 – 11495Combined sources
Helixi1153 – 116412Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00750000117238.
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

        10         20         30         40         50
MEPPSCIQDE PFPHPLEPEP GVSAQPGPGK PSDKRFRLWY VGGSCLDHRT
60 70 80 90 100
TLPMLPWLMA EIRRRSQKPE AGGCGAPAAR EVILVLSAPF LRCVPAPGAG
110 120 130 140 150
ASGGTSPSAT QPNPAVFIFE HKAQHISRFI HNSHDLTYFA YLIKAQPDDP
160 170 180 190 200
ESQMACHVFR ATDPSQVPDV ISSIRQLSKA AMKEDAKPSK DNEDAFYNSQ
210 220 230 240 250
KFEVLYCGKV TVTHKKAPSS LIDDCMEKFS LHEQQRLKIQ GEQRGPDPGE
260 270 280 290 300
DLADLEVVVP GSPGDCLPEE ADGTDTHLGL PAGASQPALT SSRVCFPERI
310 320 330 340 350
LEDSGFDEQQ EFRSRCSSVT GVQRRVHEGS QKSQPRRRHA SAPSHVQPSD
360 370 380 390 400
SEKNRTMLFQ VGRFEINLIS PDTKSVVLEK NFKDISSCSQ GIKHVDHFGF
410 420 430 440 450
ICRESPEPGL SQYICYVFQC ASESLVDEVM LTLKQAFSTA AALQSAKTQI
460 470 480 490 500
KLCEACPMHS LHKLCERIEG LYPPRAKLVI QRHLSSLTDN EQADIFERVQ
510 520 530 540 550
KMKPVSDQEE NELVILHLRQ LCEAKQKTHV HIGEGPSTIS NSTIPENATS
560 570 580 590 600
SGRFKLDILK NKAKRSLTSS LENIFSRGAN RMRGRLGSVD SFERSNSLAS
610 620 630 640 650
EKDYSPGDSP PGTPPASPPS SAWQTFPEED SDSPQFRRRA HTFSHPPSST
660 670 680 690 700
KRKLNLQDGR AQGVRSPLLR QSSSEQCSNL SSVRRMYKES NSSSSLPSLH
710 720 730 740 750
TSFSAPSFTA PSFLKSFYQN SGRLSPQYEN EIRQDTASES SDGEGRKRTS
760 770 780 790 800
STCSNESLSV GGTSVTPRRI SWRQRIFLRV ASPMNKSPSA MQQQDGLDRN
810 820 830 840 850
ELLPLSPLSP TMEEEPLVVF LSGEDDPEKI EERKKSKELR SLWRKAIHQQ
860 870 880 890 900
ILLLRMEKEN QKLEASRDEL QSRKVKLDYE EVGACQKEVL ITWDKKLLNC
910 920 930 940 950
RAKIRCDMED IHTLLKEGVP KSRRGEIWQF LALQYRLRHR LPNKQQPPDI
960 970 980 990 1000
SYKELLKQLT AQQHAILVDL GRTFPTHPYF SVQLGPGQLS LFNLLKAYSL
1010 1020 1030 1040 1050
LDKEVGYCQG ISFVAGVLLL HMSEEQAFEM LKFLMYDLGF RKQYRPDMMS
1060 1070 1080 1090 1100
LQIQMYQLSR LLHDYHRDLY NHLEENEISP SLYAAPWFLT LFASQFSLGF
1110 1120 1130 1140 1150
VARVFDIIFL QGTEVIFKVA LSLLSSQETL IMECESFENI VEFLKNTLPD
1160 1170 1180 1190 1200
MNTSEMEKII TQVFEMDISK QLHAYEVEYH VLQDELQESS YSCEDSETLE
1210 1220 1230 1240 1250
KLERANSQLK RQNMDLLEKL QVAHTKIQAL ESNLENLLTR ETKMKSLIRT
1260 1270 1280 1290
LEQEKMAYQK TVEQLRKLLP ADALVNCDLL LRDLNCNPNN KAKIGNKP
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 30 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.
GeneTreei ENSGT00750000117238.
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

Bgeei O60343.
CleanExi HS_TBC1D4.
ExpressionAtlasi O60343. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 130 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