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O60343 (TBCD4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
TBC1 domain family member 4
Alternative name(s):
Akt substrate of 160 kDa
Short name=AS160
Gene names
Name:TBC1D4
Synonyms:AS160, KIAA0603
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1298 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.10 Ref.24

Subcellular location

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

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. Ref.1 Ref.13 Ref.14

Post-translational modification

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. Ref.1 Ref.8 Ref.15

Sequence similarities

Contains 2 PID domains.

Contains 1 Rab-GAP TBC domain.

Sequence caution

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

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60343-1)

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.
Isoform 2 (identifier: O60343-2)

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.
Isoform 3 (identifier: O60343-3)

Also known as: AS160_tv3;

The sequence of this isoform differs from the canonical sequence as follows:
     733-740: Missing.
Isoform 4 (identifier: O60343-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-783: Missing.
     865-917: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: O60343-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-783: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12981298TBC1 domain family member 4
PRO_0000208026

Regions

Domain53 – 209157PID 1
Domain312 – 468157PID 2
Domain918 – 1112195Rab-GAP TBC
Compositional bias672 – 75988Ser-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.18
Modified residue3181Phosphoserine; by PKB/AKT1 By similarity
Modified residue3411Phosphoserine Ref.17 Ref.21 Ref.23
Modified residue3441Phosphoserine Ref.11 Ref.23
Modified residue4771N6-acetyllysine Ref.20
Modified residue5661Phosphoserine Ref.17 Ref.19 Ref.21
Modified residue5681Phosphothreonine Ref.19
Modified residue5701Phosphoserine Ref.17 Ref.19
Modified residue5881Phosphoserine; by PKB/AKT1 Ref.8 Ref.12 Ref.19 Ref.21 Ref.23
Modified residue5911Phosphoserine Ref.12 Ref.23
Modified residue6421Phosphothreonine; by PKB/AKT1 Ref.1 Ref.8
Modified residue7511Phosphoserine; by PKB/AKT1 By similarity

Natural variations

Alternative sequence1 – 783783Missing in isoform 4 and isoform 5.
VSP_036868
Alternative sequence678 – 74063Missing in isoform 2.
VSP_036869
Alternative sequence733 – 7408Missing in isoform 3.
VSP_036870
Alternative sequence865 – 91753Missing in isoform 4.
VSP_036871
Natural variant6191P → L.
Corresponds to variant rs56223054 [ dbSNP | Ensembl ].
VAR_061891
Natural variant8191V → I. Ref.2 Ref.3 Ref.6 Ref.7 Ref.21
Corresponds to variant rs1062087 [ dbSNP | Ensembl ].
VAR_059855
Natural variant11191V → A.
Corresponds to variant rs58232698 [ dbSNP | Ensembl ].
VAR_061892
Natural variant11471T → M.
Corresponds to variant rs9600455 [ dbSNP | Ensembl ].
VAR_052534
Natural variant12751V → A. Ref.2 Ref.3 Ref.6
Corresponds to variant rs557337 [ dbSNP | Ensembl ].
VAR_052535
Natural variant12841L → I.
Corresponds to variant rs11616741 [ dbSNP | Ensembl ].
VAR_054862

Experimental info

Mutagenesis3181S → A: 80% reduction of insulin-stimulated GLUT4 translocation; when associated with A-588; A-642 and A-751. Ref.9
Mutagenesis5881S → A: 80% reduction of insulin-stimulated GLUT4 translocation; when associated with A-318; A-642 and A-751. Ref.9
Mutagenesis6421T → A: 80% reduction of insulin-stimulated GLUT4 translocation; when associated with A-318; A-588 and A-751. Ref.9
Mutagenesis7511S → A: 80% reduction of insulin-stimulated GLUT4 translocation; when associated with A-318; A-588 and A-642. Ref.9
Mutagenesis9721R → 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. Ref.9 Ref.10
Sequence conflict6441S → G in CAH18416. Ref.7
Sequence conflict8451K → E in CAH18416. Ref.7
Sequence conflict8641E → EG in BAH16628. Ref.2
Sequence conflict8641E → EG in BAA25529. Ref.3
Sequence conflict8641E → EG in AAI51240. Ref.6
Sequence conflict8671R → G in CAH18416. Ref.7
Sequence conflict11371F → L in CAH18416. Ref.7
Sequence conflict11781E → G in BAG62187. Ref.4

Secondary structure

................................................. 1298
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: 8DC70CE887C0B311

FASTA1,298146,563
        10         20         30         40         50         60 
MEPPSCIQDE PFPHPLEPEP GVSAQPGPGK PSDKRFRLWY VGGSCLDHRT TLPMLPWLMA 

        70         80         90        100        110        120 
EIRRRSQKPE AGGCGAPAAR EVILVLSAPF LRCVPAPGAG ASGGTSPSAT QPNPAVFIFE 

       130        140        150        160        170        180 
HKAQHISRFI HNSHDLTYFA YLIKAQPDDP ESQMACHVFR ATDPSQVPDV ISSIRQLSKA 

       190        200        210        220        230        240 
AMKEDAKPSK DNEDAFYNSQ KFEVLYCGKV TVTHKKAPSS LIDDCMEKFS LHEQQRLKIQ 

       250        260        270        280        290        300 
GEQRGPDPGE DLADLEVVVP GSPGDCLPEE ADGTDTHLGL PAGASQPALT SSRVCFPERI 

       310        320        330        340        350        360 
LEDSGFDEQQ EFRSRCSSVT GVQRRVHEGS QKSQPRRRHA SAPSHVQPSD SEKNRTMLFQ 

       370        380        390        400        410        420 
VGRFEINLIS PDTKSVVLEK NFKDISSCSQ GIKHVDHFGF ICRESPEPGL SQYICYVFQC 

       430        440        450        460        470        480 
ASESLVDEVM LTLKQAFSTA AALQSAKTQI KLCEACPMHS LHKLCERIEG LYPPRAKLVI 

       490        500        510        520        530        540 
QRHLSSLTDN EQADIFERVQ KMKPVSDQEE NELVILHLRQ LCEAKQKTHV HIGEGPSTIS 

       550        560        570        580        590        600 
NSTIPENATS SGRFKLDILK NKAKRSLTSS LENIFSRGAN RMRGRLGSVD SFERSNSLAS 

       610        620        630        640        650        660 
EKDYSPGDSP PGTPPASPPS SAWQTFPEED SDSPQFRRRA HTFSHPPSST KRKLNLQDGR 

       670        680        690        700        710        720 
AQGVRSPLLR QSSSEQCSNL SSVRRMYKES NSSSSLPSLH TSFSAPSFTA PSFLKSFYQN 

       730        740        750        760        770        780 
SGRLSPQYEN EIRQDTASES SDGEGRKRTS STCSNESLSV GGTSVTPRRI SWRQRIFLRV 

       790        800        810        820        830        840 
ASPMNKSPSA MQQQDGLDRN ELLPLSPLSP TMEEEPLVVF LSGEDDPEKI EERKKSKELR 

       850        860        870        880        890        900 
SLWRKAIHQQ ILLLRMEKEN QKLEASRDEL QSRKVKLDYE EVGACQKEVL ITWDKKLLNC 

       910        920        930        940        950        960 
RAKIRCDMED IHTLLKEGVP KSRRGEIWQF LALQYRLRHR LPNKQQPPDI SYKELLKQLT 

       970        980        990       1000       1010       1020 
AQQHAILVDL GRTFPTHPYF SVQLGPGQLS LFNLLKAYSL LDKEVGYCQG ISFVAGVLLL 

      1030       1040       1050       1060       1070       1080 
HMSEEQAFEM LKFLMYDLGF RKQYRPDMMS LQIQMYQLSR LLHDYHRDLY NHLEENEISP 

      1090       1100       1110       1120       1130       1140 
SLYAAPWFLT LFASQFSLGF VARVFDIIFL QGTEVIFKVA LSLLSSQETL IMECESFENI 

      1150       1160       1170       1180       1190       1200 
VEFLKNTLPD MNTSEMEKII TQVFEMDISK QLHAYEVEYH VLQDELQESS YSCEDSETLE 

      1210       1220       1230       1240       1250       1260 
KLERANSQLK RQNMDLLEKL QVAHTKIQAL ESNLENLLTR ETKMKSLIRT LEQEKMAYQK 

      1270       1280       1290 
TVEQLRKLLP ADALVNCDLL LRDLNCNPNN KAKIGNKP 

« Hide

Isoform 2 (AS160_tv2) [UniParc].

Checksum: 2A688BE2C17FD422
Show »

FASTA1,235139,556
Isoform 3 (AS160_tv3) [UniParc].

Checksum: 38A0D7A205A0D252
Show »

FASTA1,290145,689
Isoform 4 [UniParc].

Checksum: B063DE6885C060DA
Show »

FASTA46253,850
Isoform 5 [UniParc].

Checksum: 18CDA70728CE1CBB
Show »

FASTA51560,095

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
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.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS41901.1. [O60343-1]
CCDS66563.1. [O60343-2]
CCDS66564.1. [O60343-3]
PIRT00261.
RefSeqNP_001273587.1. NM_001286658.1. [O60343-3]
NP_001273588.1. NM_001286659.1. [O60343-2]
NP_055647.2. NM_014832.3. [O60343-1]
UniGeneHs.210891.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QYBX-ray3.50A874-1170[»]
ProteinModelPortalO60343.
SMRO60343. Positions 874-1168.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115213. 21 interactions.
IntActO60343. 20 interactions.
MINTMINT-5005871.
STRING9606.ENSP00000366863.

PTM databases

PhosphoSiteO60343.

Proteomic databases

MaxQBO60343.
PaxDbO60343.
PRIDEO60343.

Protocols and materials databases

DNASU9882.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000377625; ENSP00000366852; ENSG00000136111. [O60343-2]
ENST00000377636; ENSP00000366863; ENSG00000136111. [O60343-1]
ENST00000425511; ENSP00000390654; ENSG00000136111. [O60343-4]
ENST00000431480; ENSP00000395986; ENSG00000136111. [O60343-3]
GeneID9882.
KEGGhsa:9882.
UCSCuc001vjl.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

CTD9882.
GeneCardsGC13M075858.
H-InvDBHIX0017963.
HGNCHGNC:19165. TBC1D4.
HPACAB011623.
HPA040145.
MIM612465. gene.
neXtProtNX_O60343.
PharmGKBPA38807.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5210.
HOVERGENHBG059376.
InParanoidO60343.
KOK17902.
OMAFPHPLEP.
OrthoDBEOG76T9QM.
PhylomeDBO60343.
TreeFamTF317184.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpressO60343.
BgeeO60343.
CleanExHS_TBC1D4.
GenevestigatorO60343.

Family and domain databases

Gene3D2.30.29.30. 3 hits.
InterProIPR021785. DUF3350.
IPR011993. PH_like_dom.
IPR006020. PTB/PI_dom.
IPR000195. Rab-GTPase-TBC_dom.
[Graphical view]
PfamPF11830. DUF3350. 1 hit.
PF00640. PID. 2 hits.
PF00566. RabGAP-TBC. 1 hit.
[Graphical view]
SMARTSM00462. PTB. 2 hits.
SM00164. TBC. 1 hit.
[Graphical view]
SUPFAMSSF47923. SSF47923. 2 hits.
PROSITEPS01179. PID. 1 hit.
PS50086. TBC_RABGAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTBC1D4. human.
EvolutionaryTraceO60343.
GeneWikiTBC1D4.
GenomeRNAi9882.
NextBio37248.
PMAP-CutDBO60343.
PROO60343.
SOURCESearch...

Entry information

Entry nameTBCD4_HUMAN
AccessionPrimary (citable) accession number: O60343
Secondary accession number(s): A7E2X8 expand/collapse secondary AC list , B4DU25, B4E235, B6ETN8, B6ETN9, Q5W0B9, Q68D14
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: June 7, 2005
Last modified: July 9, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM