Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

TBC1 domain family member 4 (Akt substrate of 160 kDa) (AS160)

 TBCD4_MOUSE             Reviewed;        1307 AA.
Q8BYJ6; Q149C0; Q149C1; Q3T9E8; Q3TAQ5; Q5DU23; Q66JU2; Q6P2M2;
Q8BMH6; Q8BXM2;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 2.
22-NOV-2017, entry version 124.
RecName: Full=TBC1 domain family member 4;
AltName: Full=Akt substrate of 160 kDa;
Short=AS160;
Name=Tbc1d4; Synonyms=As160, Kiaa0603;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-840 (ISOFORM 1).
STRAIN=C57BL/6J, and NOD;
TISSUE=Forelimb, Retina, Spinal cord, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-844 (ISOFORM 2).
STRAIN=NMRI; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 289-1307 (ISOFORM 2).
TISSUE=Fetal brain;
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene.
The complete nucleotide sequences of mouse KIAA-homologous cDNAs
identified by screening of terminal sequences of cDNA clones randomly
sampled from size-fractionated libraries.";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[4]
PHOSPHORYLATION AT SER-595 AND THR-649, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=11994271; DOI=10.1074/jbc.C200198200;
Kane S., Sano H., Liu S.C.H., Asara J.M., Lane W.S., Garner C.C.,
Lienhard G.E.;
"A method to identify serine kinase substrates. Akt phosphorylates a
novel adipocyte protein with a Rab GTPase-activating protein (GAP)
domain.";
J. Biol. Chem. 277:22115-22118(2002).
[5]
PHOSPHORYLATION AT SER-324; SER-348; SER-577; SER-595; THR-649 AND
SER-758.
PubMed=12637568; DOI=10.1074/jbc.C300063200;
Sano H., Kane S., Sano E., Miinea C.P., Asara J.M., Lane W.S.,
Garner C.W., Lienhard G.E.;
"Insulin-stimulated phosphorylation of a Rab GTPase-activating protein
regulates GLUT4 translocation.";
J. Biol. Chem. 278:14599-14602(2003).
[6]
EFFECT ON GLUT4 TRANSLOCATION.
PubMed=15254270; DOI=10.1091/mbc.E04-04-0333;
Zeigerer A., McBrayer M.K., McGraw T.E.;
"Insulin stimulation of GLUT4 exocytosis, but not its inhibition of
endocytosis, is dependent on RabGAP AS160.";
Mol. Biol. Cell 15:4406-4415(2004).
[7]
PHOSPHORYLATION BY AMPK.
PubMed=16804075; DOI=10.2337/db06-0175;
Treebak J.T., Glund S., Deshmukh A., Klein D.K., Long Y.C.,
Jensen T.E., Jorgensen S.B., Viollet B., Andersson L., Neumann D.,
Wallimann T., Richter E.A., Chibalin A.V., Zierath J.R.,
Wojtaszewski J.F.;
"AMPK-mediated AS160 phosphorylation in skeletal muscle is dependent
on AMPK catalytic and regulatory subunits.";
Diabetes 55:2051-2058(2006).
[8]
PHOSPHORYLATION BY AMPK.
PubMed=16804077; DOI=10.2337/db06-0150;
Kramer H.F., Witczak C.A., Fujii N., Jessen N., Taylor E.B.,
Arnolds D.E., Sakamoto K., Hirshman M.F., Goodyear L.J.;
"Distinct signals regulate AS160 phosphorylation in response to
insulin, AICAR, and contraction in mouse skeletal muscle.";
Diabetes 55:2067-2076(2006).
[9]
TISSUE SPECIFICITY.
PubMed=18276765; DOI=10.2337/db07-1469;
Bouzakri K., Ribaux P., Tomas A., Parnaud G., Rickenbach K.,
Halban P.A.;
"Rab GTPase-activating protein AS160 is a major downstream effector of
protein kinase B/Akt signaling in pancreatic beta-cells.";
Diabetes 57:1195-1204(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-261; SER-573;
SER-577; SER-598; SER-616; THR-620; SER-624; SER-761; SER-764 AND
THR-770, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-584, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: May act as a GTPase-activating protein for RAB2A, RAB8A,
RAB10 and RAB14. Promotes insulin-induced glucose transporter
SLC2A4/GLUT4 translocation at the plasma membrane, thus increasing
glucose uptake (By similarity). {ECO:0000250}.
-!- INTERACTION:
P62259:Ywhae; NbExp=6; IntAct=EBI-7920707, EBI-356480;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11994271}.
Note=Cytoplasmic perinuclear. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q8BYJ6-1; Sequence=Displayed;
Name=2;
IsoId=Q8BYJ6-2; Sequence=VSP_013891, VSP_036876, VSP_036878;
Name=3;
IsoId=Q8BYJ6-3; Sequence=VSP_036874, VSP_036876, VSP_036878;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q8BYJ6-4; Sequence=VSP_036873, VSP_013891, VSP_036876,
VSP_036878;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q8BYJ6-5; Sequence=VSP_036872, VSP_036875, VSP_036877;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed, including in pancreatic beta
cells. {ECO:0000269|PubMed:11994271, ECO:0000269|PubMed:18276765}.
-!- PTM: Phosphorylated by AKT1; insulin-induced. Also phosphorylated
by AMPK in response to insulin. Insulin-stimulated phosphorylation
is required for SLC2A4/GLUT4 translocation. Has no effect on
SLC2A4/GLUT4 internalization. {ECO:0000269|PubMed:11994271,
ECO:0000269|PubMed:12637568, ECO:0000269|PubMed:16804075,
ECO:0000269|PubMed:16804077}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AK039337; BAC30322.2; -; mRNA.
EMBL; AK044719; BAC32048.1; -; mRNA.
EMBL; AK031120; BAC27263.1; -; mRNA.
EMBL; AK171689; BAE42613.1; -; mRNA.
EMBL; AK172575; BAE43074.1; -; mRNA.
EMBL; BC064433; AAH64433.1; -; mRNA.
EMBL; BC080762; AAH80762.1; -; mRNA.
EMBL; BC117869; AAI17870.1; -; mRNA.
EMBL; BC117870; AAI17871.1; -; mRNA.
EMBL; AK220347; BAD90243.1; -; mRNA.
RefSeq; NP_001074747.2; NM_001081278.2.
RefSeq; XP_006518822.1; XM_006518759.3. [Q8BYJ6-1]
RefSeq; XP_011243304.1; XM_011245002.2. [Q8BYJ6-2]
UniGene; Mm.320639; -.
ProteinModelPortal; Q8BYJ6; -.
SMR; Q8BYJ6; -.
BioGrid; 229182; 1.
IntAct; Q8BYJ6; 2.
MINT; MINT-4113377; -.
STRING; 10090.ENSMUSP00000125509; -.
iPTMnet; Q8BYJ6; -.
PhosphoSitePlus; Q8BYJ6; -.
PaxDb; Q8BYJ6; -.
PeptideAtlas; Q8BYJ6; -.
PRIDE; Q8BYJ6; -.
GeneID; 210789; -.
KEGG; mmu:210789; -.
UCSC; uc007uvl.1; mouse. [Q8BYJ6-5]
UCSC; uc007uvo.2; mouse. [Q8BYJ6-3]
UCSC; uc007uvp.2; mouse. [Q8BYJ6-4]
UCSC; uc007uvq.2; mouse. [Q8BYJ6-2]
UCSC; uc007uvr.2; mouse. [Q8BYJ6-1]
CTD; 9882; -.
MGI; MGI:2429660; Tbc1d4.
eggNOG; KOG4436; Eukaryota.
eggNOG; ENOG410YWJY; LUCA.
HOVERGEN; HBG059376; -.
InParanoid; Q8BYJ6; -.
KO; K17902; -.
PhylomeDB; Q8BYJ6; -.
PRO; PR:Q8BYJ6; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_TBC1D4; -.
GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005622; C:intracellular; IBA:GO_Central.
GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
GO; GO:0017137; F:Rab GTPase binding; IBA:GO_Central.
GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0031338; P:regulation of vesicle fusion; IBA:GO_Central.
GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
Gene3D; 2.30.29.30; -; 2.
InterPro; IPR021785; DUF3350.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR006020; PTB/PI_dom.
InterPro; IPR000195; Rab-GTPase-TBC_dom.
InterPro; IPR035969; Rab-GTPase_TBC_sf.
InterPro; IPR033564; TBC1D4.
PANTHER; PTHR22957:SF195; PTHR22957:SF195; 1.
Pfam; PF11830; DUF3350; 1.
Pfam; PF00640; PID; 2.
Pfam; PF00566; RabGAP-TBC; 1.
SMART; SM00462; PTB; 2.
SMART; SM00164; TBC; 1.
SUPFAM; SSF47923; SSF47923; 2.
SUPFAM; SSF50729; SSF50729; 3.
PROSITE; PS01179; PID; 1.
PROSITE; PS50086; TBC_RABGAP; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
GTPase activation; Methylation; Phosphoprotein; Reference proteome;
Repeat.
CHAIN 1 1307 TBC1 domain family member 4.
/FTId=PRO_0000208027.
DOMAIN 53 209 PID 1. {ECO:0000255|PROSITE-
ProRule:PRU00148}.
DOMAIN 319 475 PID 2. {ECO:0000255|PROSITE-
ProRule:PRU00148}.
DOMAIN 927 1121 Rab-GAP TBC. {ECO:0000255|PROSITE-
ProRule:PRU00163}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:O60343}.
MOD_RES 258 258 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 261 261 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 320 320 Phosphoserine.
{ECO:0000250|UniProtKB:O60343}.
MOD_RES 324 324 Phosphoserine; by PKB/AKT1.
{ECO:0000269|PubMed:12637568}.
MOD_RES 348 348 Phosphoserine; by PKB/AKT1.
{ECO:0000269|PubMed:12637568}.
MOD_RES 351 351 Phosphoserine.
{ECO:0000250|UniProtKB:O60343}.
MOD_RES 484 484 N6-acetyllysine.
{ECO:0000250|UniProtKB:O60343}.
MOD_RES 573 573 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 575 575 Phosphothreonine.
{ECO:0000250|UniProtKB:O60343}.
MOD_RES 577 577 Phosphoserine; by PKB/AKT1.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:12637568}.
MOD_RES 584 584 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 595 595 Phosphoserine; by PKB/AKT1.
{ECO:0000269|PubMed:11994271,
ECO:0000269|PubMed:12637568}.
MOD_RES 598 598 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 616 616 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 620 620 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 624 624 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 649 649 Phosphothreonine; by PKB/AKT1.
{ECO:0000269|PubMed:11994271,
ECO:0000269|PubMed:12637568}.
MOD_RES 673 673 Phosphoserine.
{ECO:0000250|UniProtKB:O60343}.
MOD_RES 758 758 Phosphoserine; by PKB/AKT1.
{ECO:0000269|PubMed:12637568}.
MOD_RES 761 761 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 764 764 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 770 770 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 793 Missing (in isoform 5).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_036872.
VAR_SEQ 508 508 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_036873.
VAR_SEQ 685 747 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|Ref.3}.
/FTId=VSP_013891.
VAR_SEQ 685 739 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_036874.
VAR_SEQ 794 802 SPSAMQQQK -> MPLTVFFSA (in isoform 5).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_036875.
VAR_SEQ 873 873 E -> G (in isoform 2, isoform 3 and
isoform 4). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|Ref.3}.
/FTId=VSP_036876.
VAR_SEQ 873 873 Missing (in isoform 5).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_036877.
VAR_SEQ 874 1307 Missing (in isoform 2, isoform 3 and
isoform 4). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|Ref.3}.
/FTId=VSP_036878.
CONFLICT 171 171 I -> V (in Ref. 1; BAC30322).
{ECO:0000305}.
CONFLICT 631 631 H -> Y (in Ref. 1; BAC30322).
{ECO:0000305}.
CONFLICT 840 840 E -> A (in Ref. 1; BAC30322).
{ECO:0000305}.
CONFLICT 840 840 E -> K (in Ref. 2; AAH64433).
{ECO:0000305}.
CONFLICT 844 844 S -> K (in Ref. 2; AAH80762).
{ECO:0000305}.
CONFLICT 880 880 Q -> L (in Ref. 1; BAE42613).
{ECO:0000305}.
CONFLICT 914 914 R -> K (in Ref. 1; BAE42613).
{ECO:0000305}.
CONFLICT 974 974 A -> T (in Ref. 1; BAE42613).
{ECO:0000305}.
SEQUENCE 1307 AA; 147451 MW; 60B37CC6ED1D2F55 CRC64;
MESPSCIQDE PFPHPLEPEP SAPAQPGATK PGDKRFRLWY VGGSCLDRRT TLPMLPWLMA
EIRRRSQKPD AGGCGAPAAR EVILVLSAPF LRCVPAPGAG VGGGAGSGAV QPNTGVFIFE
HKAQHISRFI HNSHDLTYFA YLIKAQPDDP ESQMACHVFR ATDPNQVPDV ISSIRQLSKA
AMKEDSKPSK DNEDAFYNSQ KFEVLYCGRV IVTHKKAPSS LIDDCKDKFS LHEQQRLKLQ
GERGGDPGDE MGVLEVESPV SPDDSLPEKA DGTVNSPRAL PSLASLPALA SQPALASSRV
CFPERILEDC GFDEQQEFRS RCSSVTGVMQ KKVHENNQKT QPRRRHASAP SHVQPSDSEK
NRTMLFQVGR FEINLISPDT KSVVLEKNFK DISSCSQGIK HVDHFGFICR ESPEPGLSQY
ICYVFQCANE SLVDEVMLTL KQAFSTAAAL QSAKTQIKLC ETCPMHSLHK LCERIEGLYP
PRAKLVIQRH LSSLTDNEQA DIFERVQKMK PISDQEENEL VILHLRQLCE AKQRTHVHIG
EGPAIISNST IPENVTSGGR FKLDVLKNKA KRSLTSSLEN IFSRGANRMR GRLGSMDSFE
RANSLASEKD FSPGDSPPGT PPASPLSSAW HAFPEEDSDS PQFRRRAHTF SHPPSSSRRK
LNLQDGKAHG LRSPLLRQSS SEQCSIVPSA RRMYKESNSS CSLPSLHTSF SAPSFTAPSF
LKSFYQNSGR LSPQYENEIR QDTASESSDG EGRKRTSSTC SNESLNAGGT PVTPRRVSWR
QRIFLRVASP VNKSPSAMQQ QKDGLDRTEL LPLSPLSPTM EEEPLIIFLS GDEDTEKVEE
KKKSKELKSL WKKAIHQQIL LLRMEKENQK LEEARRDELQ SRKVKLDYEE VGTCQKEILI
AWDKKLLNCR TKIRCDMEDI HTSLKEGVPK SRRGEIWQFL ALQYRLRHRL PNKHQPPDTS
YKELLKQLTA QQHAILVDLG RTFPTHPYFS VQLGAGQLSL FNLLKAYSLL DKEVGYCQGI
SFVAGVLLLH MSEEQAFEML KFLMYDLGFR KQYRPDMMSL QIQMYQLSRL LHDYHRELYN
HLEENEISPS LYAAPWFLTL FASQFPLGFV ARVFDIIFLQ GTEVIFKVAL SLLSSQEALI
MECENFENIV EFLKSTLPDM NTTEMEKIIT QVFEMDISKQ LHAYEVEYHV LQDELLESSY
ACEDNESLEK LERANNQLKR QNMDLLEKLQ VAHAKIQALE SNLETLLTRE TKMKALIRTL
EQDKMAYQKT VEQIRKLLPA DALANCELLL KDLTHPTNDK AKAGNKP


Related products :

Catalog number Product name Quantity
EIAAB41537 Akt substrate of 160 kDa,AS160,As160,Kiaa0603,Mouse,Mus musculus,TBC1 domain family member 4,Tbc1d4
EIAAB41538 Akt substrate of 160 kDa,AS160,AS160,Homo sapiens,Human,KIAA0603,TBC1 domain family member 4,TBC1D4
EIAAB41546 Homo sapiens,Human,KIAA0882,TBC1 domain family member 9,TBC1 domain family member 9A,TBC1D9,TBC1D9A
3954BP-50 AS160-TBC1 Blocking Peptide target: AS160-TBC1 50 μg
EIAAB41534 Kiaa1108,Mouse,Mus musculus,Tbc1,TBC1 domain family member 1,Tbc1d1
E12649r Rat ELISA Kit FOR TBC1 domain family member 2A 96T
ARP55029_P050 TBC1D22A(TBC1 domain family, member 22A) 50 µg
ARP55029_P050 TBC1D22A(TBC1 domain family, member 22A) 50 µg
Y050697 Anti_TBC1D1(TBC1 domain family member 1) 100ug
EH2275 TBC1 domain family member 1 Elisa Kit 96T
TB10B_HUMAN Human ELISA Kit FOR TBC1 domain family member 10B 96T
KISHA_BOVIN Mouse ELISA Kit FOR TBC1 domain family member 2B 96T
TBC9B_MOUSE Mouse ELISA Kit FOR TBC1 domain family member 9B 96T
E4046h Human TBC1 Domain Family, Member 3B ELISA Kit 96T
E0478r Mouse ELISA Kit FOR TBC1 domain family member 10B 96T
TBC17_HUMAN Human ELISA Kit FOR TBC1 domain family member 17 96T
TBC8B_MOUSE Mouse ELISA Kit FOR TBC1 domain family member 8B 96T
TBC13_MOUSE Mouse ELISA Kit FOR TBC1 domain family member 13 96T
201-20-5771 TBC1D5{TBC1 domain family, member 5}rabbit.pAb 0.2ml
201-20-5769 TBC1D22A{TBC1 domain family, member 22A}rabbit.pAb 0.2ml
E8275h Human TBC1 Domain Family, Member 22A ELISA Kit 96T
LRC51_RAT Bovine ELISA Kit FOR TBC1 domain family member 20 96T
RPGP2_HUMAN Mouse ELISA Kit FOR TBC1 domain family member 10B 96T
E1264h Human ELISA Kit FOR TBC1 domain family member 14 96T
E4738h Human TBC1 Domain Family, Member 2 ELISA Kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur