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Ankyrin repeat domain-containing protein 27 (VPS9 domain-containing protein) (VPS9-ankyrin-repeat protein)

 ANR27_MOUSE             Reviewed;        1048 AA.
Q3UMR0; Q6KAU0; Q6P1F9; Q7TNY8; Q8BUD2; Q91W65;
06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
06-FEB-2007, sequence version 2.
20-JUN-2018, entry version 116.
RecName: Full=Ankyrin repeat domain-containing protein 27;
AltName: Full=VPS9 domain-containing protein;
AltName: Full=VPS9-ankyrin-repeat protein;
Name=Ankrd27; Synonyms=Varp;
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 [MRNA] (ISOFORM 1).
STRAIN=BALB/cJ; TISSUE=Testis;
PubMed=16525121; DOI=10.1242/jcs.02810;
Zhang X., He X., Fu X.-Y., Chang Z.;
"Varp is a Rab21 guanine nucleotide exchange factor and regulates
endosome dynamics.";
J. Cell Sci. 119:1053-1062(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Heart, and Lung;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Kidney;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 371-1048 (ISOFORM 3).
TISSUE=Embryonic tail;
PubMed=15449545; DOI=10.1093/dnares/11.2.127;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of FLJ genes:
the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs
identified by screening of terminal sequences of cDNA clones randomly
sampled from size-fractionated libraries.";
DNA Res. 11:127-135(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-961, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
FUNCTION, INTERACTION WITH VAMP7, AND SUBCELLULAR LOCATION.
PubMed=19745841; DOI=10.1038/embor.2009.186;
Burgo A., Sotirakis E., Simmler M.C., Verraes A., Chamot C.,
Simpson J.C., Lanzetti L., Proux-Gillardeaux V., Galli T.;
"Role of Varp, a Rab21 exchange factor and TI-VAMP/VAMP7 partner, in
neurite growth.";
EMBO Rep. 10:1117-1124(2009).
[7]
FUNCTION, INTERACTION WITH RAB32 AND RAB38, AND SUBCELLULAR LOCATION.
PubMed=19403694; DOI=10.1091/mbc.E08-12-1161;
Tamura K., Ohbayashi N., Maruta Y., Kanno E., Itoh T., Fukuda M.;
"Varp is a novel Rab32/38-binding protein that regulates Tyrp1
trafficking in melanocytes.";
Mol. Biol. Cell 20:2900-2908(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-961, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, and Spleen;
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).
[9]
FUNCTION, INTERACTION WITH RAB32; RAB38 AND VAMP7, AND MUTAGENESIS OF
GLN-509; TYR-550; TRP-575 AND TYR-577.
PubMed=21187289; DOI=10.1074/jbc.M110.191205;
Tamura K., Ohbayashi N., Ishibashi K., Fukuda M.;
"Structure-function analysis of VPS9-ankyrin-repeat protein (Varp) in
the trafficking of tyrosinase-related protein 1 in melanocytes.";
J. Biol. Chem. 286:7507-7521(2011).
[10]
FUNCTION, AND MUTAGENESIS OF ASP-310; TYR-350; GLN-509 AND TYR-550.
PubMed=22171327; DOI=10.1091/mbc.E11-04-0324;
Ohbayashi N., Yatsu A., Tamura K., Fukuda M.;
"The Rab21-GEF activity of Varp, but not its Rab32/38 effector
function, is required for dendrite formation in melanocytes.";
Mol. Biol. Cell 23:669-678(2012).
[11]
FUNCTION.
PubMed=26620560; DOI=10.1074/jbc.M115.684043;
Marubashi S., Shimada H., Fukuda M., Ohbayashi N.;
"RUTBC1 functions as a GTPase-activating protein for Rab32/38 and
regulates melanogenic enzyme trafficking in melanocytes.";
J. Biol. Chem. 291:1427-1440(2016).
-!- FUNCTION: May be a guanine exchange factor (GEF) for Rab21, Rab32
and Rab38 and regulate endosome dynamics (By similarity). May
regulate the participation of VAMP7 in membrane fusion events; in
vitro inhibits VAMP7-mediated SNARE complex formation by trapping
VAMP7 in a closed, fusogenically inactive conformation (By
similarity). Involved in peripheral melanosomal distribution of
TYRP1 in melanocytes; the function, which probably is implicating
vesicle-trafficking, includes cooperation with Rab32, Rab38 and
VAMP7 (PubMed:19403694, PubMed:21187289). Involved in the
regulation of neurite growth; the function seems to require its
GEF activity, probably towards Rab21, and VAMP7 but not Rab32/38
(PubMed:19745841, PubMed:22171327). Proposed to be involved in
Golgi sorting of VAMP7 and transport of VAMP7 vesicles to the cell
surface; the function seems to implicate kinesin heavy chain
isoform 5 proteins, GOLGA4, RAB21 and MACF1. Required for the
colocalization of VAMP7 and Rab21, probably on TGN sites (By
similarity). Involved in GLUT1 endosome-to-plasma membrane
trafficking; the function is dependent of association with VPS29
(By similarity). Regulates the proper trafficking of melanogenic
enzymes TYR, TYRP1 and DCT/TYRP2 to melanosomes in melanocytes
(PubMed:26620560). {ECO:0000250|UniProtKB:Q96NW4,
ECO:0000269|PubMed:19403694, ECO:0000269|PubMed:21187289,
ECO:0000269|PubMed:26620560}.
-!- SUBUNIT: Interacts with RAB21 (GDP-bound form), VPS29, KIF5A,
KIF5C, GOLGA4 (By similarity). Interacts with RAB32 (GTP-bound
form), RAB38 (GTP-bound form), VAMP7 (PubMed:19403694,
PubMed:21187289). Interacts with low affinity with RAB5 (By
similarity). ANKRD27:RAB32 heterodimers can homodimerize to form
tetramers (By similarity). Can interact with RAB38 or RAB32, VPS29
and VAMP7 simultaneously (By similarity). A decreased interaction
with RAB32 seen in the presence of SGSM2 (By similarity).
{ECO:0000250|UniProtKB:Q96NW4, ECO:0000269|PubMed:16525121,
ECO:0000269|PubMed:19403694, ECO:0000269|PubMed:21187289}.
-!- INTERACTION:
Q8QZZ8:Rab38; NbExp=5; IntAct=EBI-1993429, EBI-1993463;
-!- SUBCELLULAR LOCATION: Early endosome
{ECO:0000250|UniProtKB:Q96NW4}. Late endosome
{ECO:0000250|UniProtKB:Q96NW4}. Cytoplasmic vesicle membrane
{ECO:0000250|UniProtKB:Q96NW4}. Lysosome
{ECO:0000250|UniProtKB:Q96NW4}. Cell membrane
{ECO:0000250|UniProtKB:Q96NW4}. Melanosome
{ECO:0000269|PubMed:19403694}. Cytoplasmic vesicle
{ECO:0000269|PubMed:19403694}. Note=Colocalizes with VAMP7 in
transport vesicles in the shaft of hippocampal neurons.
{ECO:0000269|PubMed:19745841}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q3UMR0-1; Sequence=Displayed;
Name=2;
IsoId=Q3UMR0-2; Sequence=VSP_022792;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q3UMR0-3; Sequence=VSP_022791;
Note=No experimental confirmation available.;
-!- SEQUENCE CAUTION:
Sequence=AAP94281.1; Type=Frameshift; Positions=920, 929; Evidence={ECO:0000305};
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EMBL; AY336500; AAP94281.1; ALT_FRAME; mRNA.
EMBL; AK085796; BAC39537.1; -; mRNA.
EMBL; AK144733; BAE26038.1; -; mRNA.
EMBL; BC016493; AAH16493.1; -; mRNA.
EMBL; BC065093; AAH65093.1; -; mRNA.
EMBL; AK131117; BAD21367.1; -; Transcribed_RNA.
CCDS; CCDS21154.1; -. [Q3UMR0-1]
RefSeq; NP_663608.3; NM_145633.3. [Q3UMR0-1]
RefSeq; NP_839994.1; NM_178263.3.
UniGene; Mm.272620; -.
ProteinModelPortal; Q3UMR0; -.
SMR; Q3UMR0; -.
BioGrid; 232848; 1.
IntAct; Q3UMR0; 2.
STRING; 10090.ENSMUSP00000041751; -.
iPTMnet; Q3UMR0; -.
PhosphoSitePlus; Q3UMR0; -.
MaxQB; Q3UMR0; -.
PaxDb; Q3UMR0; -.
PRIDE; Q3UMR0; -.
DNASU; 245886; -.
Ensembl; ENSMUST00000040844; ENSMUSP00000041751; ENSMUSG00000034867. [Q3UMR0-1]
Ensembl; ENSMUST00000190503; ENSMUSP00000140259; ENSMUSG00000034867. [Q3UMR0-2]
GeneID; 245886; -.
KEGG; mmu:245886; -.
UCSC; uc009gkd.1; mouse. [Q3UMR0-1]
UCSC; uc012fin.1; mouse. [Q3UMR0-2]
CTD; 84079; -.
MGI; MGI:2444103; Ankrd27.
eggNOG; ENOG410IQ81; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00920000149074; -.
HOGENOM; HOG000033958; -.
HOVERGEN; HBG080845; -.
InParanoid; Q3UMR0; -.
KO; K20175; -.
OMA; IDCLFKH; -.
OrthoDB; EOG091G07HY; -.
PhylomeDB; Q3UMR0; -.
TreeFam; TF351261; -.
Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
ChiTaRS; Ankrd27; mouse.
PRO; PR:Q3UMR0; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000034867; -.
CleanEx; MM_ANKRD27; -.
ExpressionAtlas; Q3UMR0; baseline and differential.
Genevisible; Q3UMR0; MM.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0005769; C:early endosome; ISO:MGI.
GO; GO:0005770; C:late endosome; ISO:MGI.
GO; GO:0005764; C:lysosome; ISO:MGI.
GO; GO:0042470; C:melanosome; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0030133; C:transport vesicle; IDA:UniProtKB.
GO; GO:0097422; C:tubular endosome; ISO:MGI.
GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
GO; GO:0017137; F:Rab GTPase binding; IDA:UniProtKB.
GO; GO:0000149; F:SNARE binding; IDA:UniProtKB.
GO; GO:0045022; P:early endosome to late endosome transport; ISO:MGI.
GO; GO:0035646; P:endosome to melanosome transport; IDA:UniProtKB.
GO; GO:0035544; P:negative regulation of SNARE complex assembly; ISO:MGI.
GO; GO:0048812; P:neuron projection morphogenesis; IMP:UniProtKB.
GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:1990126; P:retrograde transport, endosome to plasma membrane; ISO:MGI.
CDD; cd00204; ANK; 2.
Gene3D; 1.20.1050.80; -; 1.
Gene3D; 1.25.40.20; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR003123; VPS9.
InterPro; IPR037191; VPS9_dom_sf.
Pfam; PF12796; Ank_2; 2.
Pfam; PF02204; VPS9; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 8.
SMART; SM00167; VPS9; 1.
SUPFAM; SSF109993; SSF109993; 1.
SUPFAM; SSF48403; SSF48403; 3.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 8.
PROSITE; PS51205; VPS9; 1.
1: Evidence at protein level;
Alternative splicing; ANK repeat; Cell membrane; Complete proteome;
Cytoplasmic vesicle; Endosome; GTPase activation;
Guanine-nucleotide releasing factor; Lysosome; Membrane;
Phosphoprotein; Protein transport; Reference proteome; Repeat;
Transport.
CHAIN 1 1048 Ankyrin repeat domain-containing protein
27.
/FTId=PRO_0000274557.
DOMAIN 233 371 VPS9. {ECO:0000255|PROSITE-
ProRule:PRU00550}.
REPEAT 396 426 ANK 1.
REPEAT 462 491 ANK 2.
REPEAT 495 524 ANK 3.
REPEAT 528 557 ANK 4.
REPEAT 564 593 ANK 5.
REPEAT 597 627 ANK 6.
REPEAT 668 698 ANK 7.
REPEAT 742 771 ANK 8.
REPEAT 775 804 ANK 9.
REPEAT 808 837 ANK 10.
REPEAT 841 870 ANK 11.
REGION 1 372 Sufficient for GEF activity towards
RAB21. {ECO:0000250|UniProtKB:Q96NW4}.
REGION 396 460 Sufficient for interaction with VPS29.
{ECO:0000250|UniProtKB:Q96NW4}.
REGION 451 729 Interaction with RAB32.
{ECO:0000269|PubMed:19403694}.
REGION 451 600 Interaction with RAB38.
{ECO:0000269|PubMed:19403694}.
REGION 658 707 Required for interaction with VAMP7.
{ECO:0000250|UniProtKB:Q96NW4,
ECO:0000269|PubMed:19745841}.
REGION 692 745 Sufficient for interaction with VPS29.
{ECO:0000250|UniProtKB:Q96NW4}.
MOD_RES 961 961 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 969 969 Phosphoserine.
{ECO:0000250|UniProtKB:Q96NW4}.
MOD_RES 1022 1022 Phosphothreonine.
{ECO:0000250|UniProtKB:Q96NW4}.
VAR_SEQ 630 670 Missing (in isoform 3).
{ECO:0000303|PubMed:15449545}.
/FTId=VSP_022791.
VAR_SEQ 670 724 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_022792.
MUTAGEN 310 310 D->A: Inhibits dendrite formation.
{ECO:0000269|PubMed:22171327}.
MUTAGEN 350 350 Y->A: Inhibits dendrite formation.
{ECO:0000269|PubMed:22171327}.
MUTAGEN 509 509 Q->A: Disrupts interaction with RAB32 and
RAB38; inhibits peripheral distribution
of TYRP1 in melanocytes; no effect on
dendrite formation in melanocytes.
{ECO:0000269|PubMed:21187289,
ECO:0000269|PubMed:22171327}.
MUTAGEN 550 550 Y->A: Disrupts interaction with RAB32 and
RAB38; inhibits peripheral distribution
of TYRP1 in melanocytes; no effect on
dendrite formation in melanocytes.
{ECO:0000269|PubMed:21187289,
ECO:0000269|PubMed:22171327}.
MUTAGEN 575 575 W->A: Impairs interaction with RAB32 and
RAB38. {ECO:0000269|PubMed:21187289}.
MUTAGEN 577 577 Y->A: Impairs interaction with RAB32 and
RAB38. {ECO:0000269|PubMed:21187289}.
CONFLICT 281 310 QQKLLCLRKVVQLMTQSPSQRVNLETMCAD -> TAEAAVP
EEGGPAHDTISQPESELGDHVCR (in Ref. 2;
BAC39537). {ECO:0000305}.
CONFLICT 371 372 TP -> PQ (in Ref. 4; BAD21367).
{ECO:0000305}.
CONFLICT 373 377 DAEGF -> VRSPC (in Ref. 3; AAH16493).
{ECO:0000305}.
CONFLICT 601 601 P -> Q (in Ref. 2; BAE26038).
{ECO:0000305}.
CONFLICT 609 609 K -> KV (in Ref. 4; BAD21367).
{ECO:0000305}.
CONFLICT 730 730 S -> P (in Ref. 1; AAP94281).
{ECO:0000305}.
SEQUENCE 1048 AA; 116809 MW; 63636820D0CC4D2C CRC64;
MALYDEDLLK NPFYLALQKW RPDLCSKVAQ IHGIVLVPCR GSLPGSVQAS CQFESYVLVP
TEGHFQTLDG KAVVIEGNRI KLGAGFACLL SVPILFEETF YNEKEESFSI LCIAHPLERR
ETSEEPSAPA DPFSLKTIED VREFLGRHSE KFDKNIASFH RTFRECERKS LRHHIDSVNA
LYTKCLQQLL RDSHLKVLAK QEAQMNLMKQ AVEMYVHHDI YDLIFKYVGT MEASEDAAFN
KITRSLQDLQ QKDIGVKPEF SFNIPRAKRE LGQLNKCTSP QQKLLCLRKV VQLMTQSPSQ
RVNLETMCAD DLLSVLLYLL VKTEIPNWMA NLSYIKNFRF SSSAKDELGY CLTSVEAAIE
YIRQGSLSTK TPDAEGFGDR LFLKQRMNLL SQMTSTPIDC LFKHIASGNQ KEVERLLSQD
DQDKDAMQKM CHPLCSCEDC EKLISGRLND PSVVTPFSRD DRGQTPLHVA ALCGQASLID
FLVSKGAVVN ATDYHGSTPL HLACQKGFQS VTLLLLHYKA STEVQDNNGN TPLHLACTYG
QEDCVKALVY YDVQACRLDI GNEKGDTALH IAARWGYEGI IETLLQNGAP TAVQNRLKET
PLKCALNSKI LSIMEAHHLS SDRRPRPSEV PAQSPTRSVD SISQGSSTSS FSSISVSFRQ
EEVKKDYREV EKLLRAVADG DLEMVRYLLE WTEDDLDDVE DAISTVDLEF CHPLCQCPKC
APAQKLARIS ANGLSVNVTN QDGFSPLHMA ALHGRTDLVP LLLKHGAYSG ARNTSQAVPL
HLACQQGHFQ VAKCLLDSNA KPNKKDLSGN TPLICACSAG HHEVAALLLQ HGASINACNN
KGNTALHEAV MGRHTLVVEL LLFYGASVDI LNKRQYTAAD CAEQDSKIME LLQVVPGCVA
SLDSVEEADH EGYVTVEIRR KWNPKMYNLP EEPLRRQFCL INPGGRFQER TSRETMGRDR
SVPDLAGRSL QEPEKQRVTG KQSDLSDLSR YQTSEEGNKG LPERPVSRQA APGHRPMVRR
HTVNDAAILQ VPEVTVHLTT HEASVPQS


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EIAAB41357 Protein TANC1,Rat,Rattus norvegicus,Tanc,Tanc1,TPR domain, ankyrin-repeat and coiled-coil domain-containing protein 1
CSB-EL001732MO Mouse Ankyrin repeat and protein kinase domain-containing protein 1(ANKK1) ELISA kit 96T
CSB-EL001732HU Human Ankyrin repeat and protein kinase domain-containing protein 1(ANKK1) ELISA kit 96T
ANKL2_RAT Rat ELISA Kit FOR Ankyrin repeat and LEM domain-containing protein 2 96T
E02A0077 Rat Ankyrin repeat domain-containing protein 1 ELISA 96T/kit
EH1832 Ankyrin repeat domain-containing protein 30A Elisa Kit 96T
E1432h Rat ELISA Kit FOR Ankyrin repeat and SAM domain-containing protein 3 96T
ANR54_RAT Rat ELISA Kit FOR Ankyrin repeat domain-containing protein 54 96T
ANKS6_RAT Rat ELISA Kit FOR Ankyrin repeat and SAM domain-containing protein 6 96T
ABTB1_RAT Rat ELISA Kit FOR Ankyrin repeat and BTB per POZ domain-containing protein 1 96T
CSB-EL001732MO Mouse Ankyrin repeat and protein kinase domain-containing protein 1(ANKK1) ELISA kit SpeciesMouse 96T
CSB-EL001732HU Human Ankyrin repeat and protein kinase domain-containing protein 1(ANKK1) ELISA kit SpeciesHuman 96T
AR26L_HUMAN ELISA Kit FOR Putative ankyrin repeat domain-containing protein 26-like protein; organism: Human; gene name: ANKRD26P1 96T
30-770 ASB11 is a member of the ankyrin repeat and SOCS box-containing (ASB) family of proteins. They contain ankyrin repeat sequence and SOCS box domain. The SOCS box serves to couple suppressor of cytokine 0.05 mg


 

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