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Ankyrin repeat domain-containing protein 11 (Ankyrin repeat-containing cofactor 1)

 ANR11_HUMAN             Reviewed;        2663 AA.
Q6UB99; Q6NTG1; Q6QMF8;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
28-MAR-2018, entry version 127.
RecName: Full=Ankyrin repeat domain-containing protein 11;
AltName: Full=Ankyrin repeat-containing cofactor 1;
Name=ANKRD11; Synonyms=ANCO1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
Powell J.A., Settasatian C., Lower K., Callen D.F.;
"ANKRD11 and ANKRD12 are novel 9kb genes encoding nuclear-located
proteins with ankyrin domains.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH
P160.
PubMed=15184363; DOI=10.1074/jbc.M403997200;
Zhang A., Yeung P.L., Li C.-W., Tsai S.-C., Dinh G.K., Wu X., Li H.,
Chen J.D.;
"Identification of a novel family of ankyrin repeats-containing
cofactors for p160 nuclear receptor coactivators.";
J. Biol. Chem. 279:33799-33805(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-451.
TISSUE=Pancreas;
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).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1509, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276; SER-408; THR-410;
SER-411; SER-834; THR-1120; SER-1123; THR-1419; SER-1792; SER-1847 AND
SER-1859, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276; SER-408; THR-410
AND SER-411, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276; SER-408; THR-410;
SER-411; SER-834 AND THR-1419, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[9]
INVOLVEMENT IN KBGS.
PubMed=21782149; DOI=10.1016/j.ajhg.2011.06.007;
Sirmaci A., Spiliopoulos M., Brancati F., Powell E., Duman D.,
Abrams A., Bademci G., Agolini E., Guo S., Konuk B., Kavaz A.,
Blanton S., Digilio M.C., Dallapiccola B., Young J., Zuchner S.,
Tekin M.;
"Mutations in ANKRD11 cause KBG syndrome, characterized by
intellectual disability, skeletal malformations, and macrodontia.";
Am. J. Hum. Genet. 89:289-294(2011).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408; THR-410; SER-411
AND SER-834, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276; SER-834; THR-1419;
SER-1792 AND SER-1990, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=25556659; DOI=10.1016/j.devcel.2014.11.031;
Gallagher D., Voronova A., Zander M.A., Cancino G.I., Bramall A.,
Krause M.P., Abad C., Tekin M., Neilsen P.M., Callen D.F.,
Scherer S.W., Keller G.M., Kaplan D.R., Walz K., Miller F.D.;
"Ankrd11 is a chromatin regulator involved in autism that is essential
for neural development.";
Dev. Cell 32:31-42(2015).
[13]
SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PROTEASOMAL DEGRADATION,
AND VARIANT KBGS GLN-2512.
PubMed=25413698; DOI=10.1007/s00439-014-1509-2;
Walz K., Cohen D., Neilsen P.M., Foster J. II, Brancati F., Demir K.,
Fisher R., Moffat M., Verbeek N.E., Bjoergo K., Lo Castro A.,
Curatolo P., Novelli G., Abad C., Lei C., Zhang L., Diaz-Horta O.,
Young J.I., Callen D.F., Tekin M.;
"Characterization of ANKRD11 mutations in humans and mice related to
KBG syndrome.";
Hum. Genet. 134:181-190(2015).
-!- FUNCTION: Chromatin regulator which modulates histone acetylation
and gene expression in neural precursor cells (By similarity). May
recruit histone deacetylases (HDACs) to the p160
coactivators/nuclear receptor complex to inhibit ligand-dependent
transactivation (PubMed:15184363). Has a role in proliferation and
development of cortical neural precursors (PubMed:25556659). May
also regulate bone homeostasis (By similarity).
{ECO:0000250|UniProtKB:E9Q4F7, ECO:0000269|PubMed:15184363,
ECO:0000269|PubMed:25556659}.
-!- SUBUNIT: Interacts with the PAS region of the p160 coactivators.
{ECO:0000269|PubMed:15184363}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15184363,
ECO:0000269|PubMed:25413698, ECO:0000269|PubMed:25556659,
ECO:0000269|Ref.1}. Note=Localizes to chromatin during
prometaphase. {ECO:0000269|PubMed:25413698}.
-!- DEVELOPMENTAL STAGE: Expression levels are regulated during the
cell cycle, reaching maximal levels at M phase and then rapidly
declining after late M phase. {ECO:0000269|PubMed:25413698}.
-!- PTM: Subject to proteasomal degradation which is probably
essential to regulate its activity. {ECO:0000269|PubMed:25413698}.
-!- DISEASE: KBG syndrome (KBGS) [MIM:148050]: A syndrome
characterized by macrodontia of the upper central incisors,
distinctive craniofacial findings, short stature, skeletal
anomalies, and neurologic involvement that includes global
developmental delay, seizures, and intellectual disability.
{ECO:0000269|PubMed:21782149, ECO:0000269|PubMed:25413698}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAH69013.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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EMBL; AY373756; AAR25661.1; -; mRNA.
EMBL; AY533563; AAS45544.1; -; mRNA.
EMBL; AC137932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC069013; AAH69013.1; ALT_SEQ; mRNA.
CCDS; CCDS32513.1; -.
RefSeq; NP_001243111.1; NM_001256182.1.
RefSeq; NP_001243112.1; NM_001256183.1.
RefSeq; NP_037407.4; NM_013275.5.
RefSeq; XP_011521353.1; XM_011523051.2.
RefSeq; XP_011521355.1; XM_011523053.2.
RefSeq; XP_016878671.1; XM_017023182.1.
RefSeq; XP_016878672.1; XM_017023183.1.
RefSeq; XP_016878673.1; XM_017023184.1.
RefSeq; XP_016878674.1; XM_017023185.1.
RefSeq; XP_016878675.1; XM_017023186.1.
RefSeq; XP_016878676.1; XM_017023187.1.
UniGene; Hs.335003; -.
UniGene; Hs.740440; -.
ProteinModelPortal; Q6UB99; -.
SMR; Q6UB99; -.
BioGrid; 118888; 27.
CORUM; Q6UB99; -.
IntAct; Q6UB99; 16.
STRING; 9606.ENSP00000301030; -.
CarbonylDB; Q6UB99; -.
iPTMnet; Q6UB99; -.
PhosphoSitePlus; Q6UB99; -.
BioMuta; ANKRD11; -.
DMDM; 296439440; -.
EPD; Q6UB99; -.
MaxQB; Q6UB99; -.
PaxDb; Q6UB99; -.
PeptideAtlas; Q6UB99; -.
PRIDE; Q6UB99; -.
Ensembl; ENST00000301030; ENSP00000301030; ENSG00000167522.
Ensembl; ENST00000378330; ENSP00000367581; ENSG00000167522.
GeneID; 29123; -.
KEGG; hsa:29123; -.
UCSC; uc002fmx.3; human.
CTD; 29123; -.
DisGeNET; 29123; -.
EuPathDB; HostDB:ENSG00000167522.14; -.
GeneCards; ANKRD11; -.
H-InvDB; HIX0013356; -.
HGNC; HGNC:21316; ANKRD11.
HPA; CAB019288; -.
HPA; HPA041593; -.
HPA; HPA049470; -.
MalaCards; ANKRD11; -.
MIM; 148050; phenotype.
MIM; 611192; gene.
neXtProt; NX_Q6UB99; -.
OpenTargets; ENSG00000167522; -.
Orphanet; 261250; 16q24.3 microdeletion syndrome.
Orphanet; 2332; KBG syndrome.
PharmGKB; PA134861925; -.
eggNOG; ENOG410IJ47; Eukaryota.
eggNOG; ENOG4110UQU; LUCA.
GeneTree; ENSGT00760000119090; -.
HOGENOM; HOG000168254; -.
HOVERGEN; HBG106759; -.
InParanoid; Q6UB99; -.
KO; K21436; -.
OMA; SCPSYEE; -.
OrthoDB; EOG091G05O7; -.
PhylomeDB; Q6UB99; -.
TreeFam; TF326440; -.
ChiTaRS; ANKRD11; human.
GenomeRNAi; 29123; -.
PRO; PR:Q6UB99; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000167522; -.
CleanEx; HS_ANKRD11; -.
ExpressionAtlas; Q6UB99; baseline and differential.
Genevisible; Q6UB99; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0060348; P:bone development; IEA:Ensembl.
GO; GO:0060325; P:face morphogenesis; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
CDD; cd00204; ANK; 1.
Gene3D; 1.25.40.20; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
Pfam; PF00023; Ank; 1.
Pfam; PF12796; Ank_2; 1.
SMART; SM00248; ANK; 3.
SUPFAM; SSF48403; SSF48403; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 3.
1: Evidence at protein level;
ANK repeat; Complete proteome; Disease mutation; Dwarfism;
Mental retardation; Nucleus; Phosphoprotein; Reference proteome;
Repeat.
CHAIN 1 2663 Ankyrin repeat domain-containing protein
11.
/FTId=PRO_0000066907.
REPEAT 167 196 ANK 1.
REPEAT 200 229 ANK 2.
REPEAT 233 262 ANK 3.
REPEAT 266 292 ANK 4.
REGION 2369 2663 Important for protein degradation.
{ECO:0000269|PubMed:25413698}.
COMPBIAS 478 588 Ser-rich.
COMPBIAS 621 1655 Lys-rich.
COMPBIAS 1824 2365 Pro-rich.
MOD_RES 276 276 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 408 408 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 410 410 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 411 411 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 834 834 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1079 1079 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q4F7}.
MOD_RES 1120 1120 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1123 1123 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1419 1419 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1509 1509 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 1692 1692 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q4F7}.
MOD_RES 1792 1792 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1847 1847 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1850 1850 Phosphotyrosine.
{ECO:0000250|UniProtKB:E9Q4F7}.
MOD_RES 1851 1851 Phosphotyrosine.
{ECO:0000250|UniProtKB:E9Q4F7}.
MOD_RES 1852 1852 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q4F7}.
MOD_RES 1859 1859 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1990 1990 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 2512 2512 R -> Q (in KBGS; unknown pathological
significance).
{ECO:0000269|PubMed:25413698}.
/FTId=VAR_075870.
CONFLICT 76 76 E -> EE (in Ref. 1; AAR25661).
{ECO:0000305}.
CONFLICT 971 971 A -> V (in Ref. 1; AAR25661 and 2;
AAS45544). {ECO:0000305}.
SEQUENCE 2663 AA; 297913 MW; 845B04094AF37CFE CRC64;
MPKGGCPKAP QQEELPLSSD MVEKQTGKKD KDKVSLTKTP KLERGDGGKE VRERASKRKL
PFTAGANGEQ KDSDTEKQGP ERKRIKKEPV TRKAGLLFGM GLSGIRAGYP LSERQQVALL
MQMTAEESAN SPVDTTPKHP SQSTVCQKGT PNSASKTKDK VNKRNERGET RLHRAAIRGD
ARRIKELISE GADVNVKDFA GWTALHEACN RGYYDVAKQL LAAGAEVNTK GLDDDTPLHD
AANNGHYKVV KLLLRYGGNP QQSNRKGETP LKVANSPTMV NLLLGKGTYT SSEESSTESS
EEEDAPSFAP SSSVDGNNTD SEFEKGLKHK AKNPEPQKAT APVKDEYEFD EDDEQDRVPP
VDDKHLLKKD YRKETKSNSF ISIPKMEVKS YTKNNTIAPK KASHRILSDT SDEEDASVTV
GTGEKLRLSA HTILPGSKTR EPSNAKQQKE KNKVKKKRKK ETKGREVRFG KRSDKFCSSE
SESESSESGE DDRDSLGSSG CLKGSPLVLK DPSLFSSLSA SSTSSHGSSA AQKQNPSHTD
QHTKHWRTDN WKTISSPAWS EVSSLSDSTR TRLTSESDYS SEGSSVESLK PVRKRQEHRK
RASLSEKKSP FLSSAEGAVP KLDKEGKVVK KHKTKHKHKN KEKGQCSISQ ELKLKSFTYE
YEDSKQKSDK AILLENDLST ENKLKVLKHD RDHFKKEEKL SKMKLEEKEW LFKDEKSLKR
IKDTNKDISR SFREEKDRSN KAEKERSLKE KSPKEEKLRL YKEERKKKSK DRPSKLEKKN
DLKEDKISKE KEKIFKEDKE KLKKEKVYRE DSAFDEYCNK NQFLENEDTK FSLSDDQRDR
WFSDLSDSSF DFKGEDSWDS PVTDYRDMKS DSVAKLILET VKEDSKERRR DSRAREKRDY
REPFFRKKDR DYLDKNSEKR KEQTEKHKSV PGYLSEKDKK RRESAEAGRD RKDALESCKE
RRDGRAKPEE AHREELKECG CESGFKDKSD GDFGKGLEPW ERHHPAREKE KKDGPDKERK
EKTKPERYKE KSSDKDKSEK SILEKCQKDK EFDKCFKEKK DTKEKHKDTH GKDKERKASL
DQGKEKKEKA FPGIISEDFS EKKDDKKGKE KSWYIADIFT DESEDDRDSC MGSGFKMGEA
SDLPRTDGLQ EKEEGREAYA SDRHRKSSDK QHPERQKDKE PRDRRKDRGA ADAGRDKKEK
VFEKHKEKKD KESTEKYKDR KDRASVDSTQ DKKNKQKLPE KAEKKHAAED KAKSKHKEKS
DKEHSKERKS SRSADAEKSL LEKLEEEALH EYREDSNDKI SEVSSDSFTD RGQEPGLTAF
LEVSFTEPPG DDKPRESACL PEKLKEKERH RHSSSSSKKS HDRERAKKEK AEKKEKGEDY
KEGGSRKDSG QYEKDFLEAD AYGVSYNMKA DIEDELDKTI ELFSTEKKDK NDSEREPSKK
IEKELKPYGS SAINILKEKK KREKHREKWR DEKERHRDRH ADGLLRHHRD ELLRHHRDEQ
KPATRDKDSP PRVLKDKSRD EGPRLGDAKL KEKFKDGAEK EKGDPVKMSN GNDKVAPSKD
PGKKDARPRE KLLGDGDLMM TSFERMLSQK DLEIEERHKR HKERMKQMEK LRHRSGDPKL
KEKAKPADDG RKKGLDIPAK KPPGLDPPFK DKKLKESTPI PPAAENKLHP ASGADSKDWL
AGPHMKEVLP ASPRPDQSRP TGVPTPTSVL SCPSYEEVMH TPRTPSCSAD DYADLVFDCA
DSQHSTPVPT APTSACSPSF FDRFSVASSG LSENASQAPA RPLSTNLYRS VSVDIRRTPE
EEFSVGDKLF RQQSVPAASS YDSPMPPSME DRAPLPPVPA EKFACLSPGY YSPDYGLPSP
KVDALHCPPA AVVTVTPSPE GVFSSLQAKP SPSPRAELLV PSLEGALPPD LDTSEDQQAT
AAIIPPEPSY LEPLDEGPFS AVITEEPVEW AHPSEQALAS SLIGGTSENP VSWPVGSDLL
LKSPQRFPES PKRFCPADPL HSAAPGPFSA SEAPYPAPPA SPAPYALPVA EPGLEDVKDG
VDAVPAAIST SEAAPYAPPS GLESFFSNCK SLPEAPLDVA PEPACVAAVA QVEALGPLEN
SFLDGSRGLS HLGQVEPVPW ADAFAGPEDD LDLGPFSLPE LPLQTKDAAD GEAEPVEESL
APPEEMPPGA PGVINGGDVS TVVAEEPPAL PPDQASTRLP AELEPEPSGE PKLDVALEAA
VEAETVPEER ARGDPDSSVE PAPVPPEQRP LGSGDQGAEA EGPPAASLCA PDGPAPNTVA
QAQAADGAGP EDDTEASRAA APAEGPPGGI QPEAAEPKPT AEAPKAPRVE EIPQRMTRNR
AQMLANQSKQ GPPPSEKECA PTPAPVTRAK ARGSEDDDAQ AQHPRKRRFQ RSTQQLQQQL
NTSTQQTREV IQQTLAAIVD AIKLDAIEPY HSDRANPYFE YLQIRKKIEE KRKILCCITP
QAPQCYAEYV TYTGSYLLDG KPLSKLHIPV IAPPPSLAEP LKELFRQQEA VRGKLRLQHS
IEREKLIVSC EQEILRVHCR AARTIANQAV PFSACTMLLD SEVYNMPLES QGDENKSVRD
RFNARQFISW LQDVDDKYDR MKTCLLMRQQ HEAAALNAVQ RMEWQLKVQE LDPAGHKSLC
VNEVPSFYVP MVDVNDDFVL LPA


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Catalog number Product name Quantity
18-003-42394 Ankyrin repeat domain-containing protein 12 - Ankyrin repeat-containing cofactor 2; GAC-1 protein Polyclonal 0.1 mg Protein A
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
26-655 ASB12 is a member of the ankyrin repeat and SOCS box-containing (ASB) family of proteins. They contain ankyrin repeat sequence and a SOCS box domain. The SOCS box serves to couple suppressor of cytoki 0.05 mg
LF-PA40055 anti-Ankyrin Repeat Domain 32 (ANKRD32) , Rabbit polyclonal to Ankyrin Repeat Domain 32 (ANKRD32) , Isotype IgG, Host Rabbit 50 ug
EIAAB31841 A26B3,ANKRD21,ANKRD26-like family B member 3,Ankyrin repeat domain-containing protein 21,Homo sapiens,Human,POTE,POTE ankyrin domain family member D,POTED,Prostate, ovary, testis-expressed protein,Pro
EIAAB41359 Homo sapiens,Human,KIAA1728,Protein TANC1,TANC1,Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1
EIAAB41360 Homo sapiens,Human,KIAA1148,KIAA1636,Protein TANC2,TANC2,Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 2
EIAAB41361 Kiaa1148,Mouse,Mus musculus,Protein TANC2,Tanc2,Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 2
EIAAB41358 Mouse,Mus musculus,Protein TANC1,Tanc1,Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1
EH1832 Ankyrin repeat domain-containing protein 30A Elisa Kit 96T
ANKL2_RAT Rat ELISA Kit FOR Ankyrin repeat and LEM domain-containing protein 2 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
E1432h Rat ELISA Kit FOR Ankyrin repeat and SAM domain-containing protein 3 96T
ABTB1_RAT Rat ELISA Kit FOR Ankyrin repeat and BTB per POZ domain-containing protein 1 96T
E02A0077 Rat Ankyrin repeat domain-containing protein 1 ELISA 96T/kit
20-783-72857 MOUSE ANTI HUMAN ANKYRIN B (SPECTRIN BINDING DOMAIN) - Brain ankyrin; Ankyrin-B; Non-erythroid ankyrin Monoclonal 0.1 mg
E7271h Human Ankyrin Repeat Domain Protein 13B ELISA Kit 96T
E7326h Human Ankyrin Repeat Domain Protein 42 ELISA Kit 96T
E1076m Mouse ELISA Kit FOR Ankyrin repeat and SAM domain-containing protein 4B 96T
E1075r Mouse ELISA Kit FOR Ankyrin repeat domain-containing protein 6 96T
ANR24_HUMAN Human ELISA Kit FOR Ankyrin repeat domain-containing protein 24 96T
ANR62_HUMAN Human ELISA Kit FOR Ankyrin repeat domain-containing protein 62 96T
E7267h Human Ankyrin Repeat Domain Protein 35 ELISA Kit 96T
E10995r Human ELISA Kit FOR Ankyrin repeat domain-containing protein 26 96T


 

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