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Tax1-binding protein 3 (Glutaminase-interacting protein 3) (Tax interaction protein 1) (TIP-1) (Tax-interacting protein 1)

 TX1B3_HUMAN             Reviewed;         124 AA.
O14907; B2RD53; D3DTJ6; Q7LCQ4;
02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 2.
25-OCT-2017, entry version 143.
RecName: Full=Tax1-binding protein 3;
AltName: Full=Glutaminase-interacting protein 3;
AltName: Full=Tax interaction protein 1;
Short=TIP-1;
AltName: Full=Tax-interacting protein 1;
Name=TAX1BP3 {ECO:0000312|HGNC:HGNC:30684};
Synonyms=TIP1 {ECO:0000312|EMBL:AAF43104.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAB84248.2}
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH HTLV-1 TAX.
TISSUE=Peripheral blood lymphocyte {ECO:0000312|EMBL:AAB84248.2};
PubMed=9482110; DOI=10.1038/sj.onc.1201567;
Rousset R., Fabre S., Desbois C., Bantignies F., Jalinot P.;
"The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction
with the PDZ domain of cellular proteins.";
Oncogene 16:643-654(1998).
[2] {ECO:0000312|EMBL:AAF43104.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10673275; DOI=10.1101/gr.10.2.165;
Touchman J.W., Anikster Y., Dietrich N.L., Maduro V.V.B., McDowell G.,
Shotelersuk V., Bouffard G.G., Beckstrom-Sternberg S.M., Gahl W.A.,
Green E.D.;
"The genomic region encompassing the nephropathic cystinosis gene
(CTNS): complete sequencing of a 200-kb segment and discovery of a
novel gene within the common cystinosis-causing deletion.";
Genome Res. 10:165-173(2000).
[3] {ECO:0000305, ECO:0000312|EMBL:AAG44368.1}
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH GLS2.
TISSUE=Brain {ECO:0000312|EMBL:AAG44368.1};
PubMed=11163757; DOI=10.1016/S0014-5793(00)02373-5;
Olalla L., Aledo J.C., Bannenberg G., Marquez J.;
"The C-terminus of human glutaminase L mediates association with PDZ
domain-containing proteins.";
FEBS Lett. 488:116-122(2001).
[4] {ECO:0000312|EMBL:AAK69111.1}
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovary {ECO:0000312|EMBL:AAK69111.1};
Honore B.;
"hPWP1-interacting proteins 2 and 11 (Tax-interacting protein 1).";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6] {ECO:0000312|EMBL:AAK69111.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7] {ECO:0000312|EMBL:AAH23980.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney {ECO:0000312|EMBL:AAH23980.1};
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).
[8] {ECO:0000305}
FUNCTION, INTERACTION WITH RTKN, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=10940294; DOI=10.1074/jbc.M000465200;
Reynaud C., Fabre S., Jalinot P.;
"The PDZ protein TIP-1 interacts with the Rho effector rhotekin and is
involved in Rho signaling to the serum response element.";
J. Biol. Chem. 275:33962-33968(2000).
[9]
FUNCTION, INTERACTION WITH KCNJ4, MUTAGENESIS OF LYS-20 AND HIS-90,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16855024; DOI=10.1091/mbc.E06-02-0129;
Alewine C., Olsen O., Wade J.B., Welling P.A.;
"TIP-1 has PDZ scaffold antagonist activity.";
Mol. Biol. Cell 17:4200-4211(2006).
[10]
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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, 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).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
FUNCTION, AND INTERACTION WITH ARHGEF16.
PubMed=21139582; DOI=10.1038/sj.bjc.6606026;
Oliver A.W., He X., Borthwick K., Donne A.J., Hampson L.,
Hampson I.N.;
"The HPV16 E6 binding protein Tip-1 interacts with ARHGEF16, which
activates Cdc42.";
Br. J. Cancer 104:324-331(2011).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
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).
[17]
STRUCTURE BY NMR, AND INTERACTION WITH KCNJ4.
PubMed=19685007; DOI=10.1007/s10858-009-9361-8;
Durney M.A., Birrane G., Anklin C., Soni A., Ladias J.A.;
"Solution structure of the human Tax-interacting protein-1.";
J. Biomol. NMR 45:329-334(2009).
[18]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), AND INTERACTION WITH KCNJ4.
PubMed=19635485; DOI=10.1016/j.jmb.2009.07.060;
Yan X., Zhou H., Zhang J., Shi C., Xie X., Wu Y., Tian C., Shen Y.,
Long J.;
"Molecular mechanism of inward rectifier potassium channel 2.3
regulation by tax-interacting protein-1.";
J. Mol. Biol. 392:967-976(2009).
[19] {ECO:0000312|EMBL:AAK69111.1}
X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 13-124.
Structural genomics consortium (SGC);
"The structure of the PDZ domain of TAX1BP.";
Submitted (FEB-2009) to the PDB data bank.
[20]
STRUCTURE BY NMR IN COMPLEX WITH GLS2, AND INTERACTION WITH GLS2.
PubMed=21417405; DOI=10.1021/bi102055y;
Zoetewey D.L., Ovee M., Banerjee M., Bhaskaran R., Mohanty S.;
"Promiscuous binding at the crossroads of numerous cancer pathways:
insight from the binding of glutaminase interacting protein with
glutaminase L.";
Biochemistry 50:3528-3539(2011).
[21]
STRUCTURE BY NMR IN COMPLEX WITH ADGRB2, AND INTERACTION WITH ADGRB2.
PubMed=21787750; DOI=10.1016/j.bbrc.2011.07.029;
Zencir S., Ovee M., Dobson M.J., Banerjee M., Topcu Z., Mohanty S.;
"Identification of brain-specific angiogenesis inhibitor 2 as an
interaction partner of glutaminase interacting protein.";
Biochem. Biophys. Res. Commun. 411:792-797(2011).
[22]
VARIANT THR-33, AND TISSUE SPECIFICITY.
PubMed=25645515; DOI=10.1002/humu.22759;
Reinstein E., Orvin K., Tayeb-Fligelman E., Stiebel-Kalish H.,
Tzur S., Pimienta A.L., Bazak L., Bengal T., Cohen L., Gaton D.D.,
Bormans C., Landau M., Kornowski R., Shohat M., Behar D.M.;
"Mutations in TAX1BP3 cause dilated cardiomyopathy with septo-optic
dysplasia.";
Hum. Mutat. 36:439-442(2015).
-!- FUNCTION: May regulate a number of protein-protein interactions by
competing for PDZ domain binding sites. Binds CTNNB1 and may
thereby act as an inhibitor of the Wnt signaling pathway. Competes
with LIN7A for KCNJ4 binding, and thereby promotes KCNJ4
internalization. May play a role in the Rho signaling pathway. May
play a role in activation of CDC42 by the viral protein HPV16 E6.
{ECO:0000269|PubMed:10940294, ECO:0000269|PubMed:16855024,
ECO:0000269|PubMed:21139582}.
-!- SUBUNIT: Interacts (via its PDZ domain) with GLS2. Interacts (via
its PDZ domain) with RTKN (via the C-terminal region); this
interaction facilitates Rho-mediated activation of the FOS serum
response element (SRE). Interacts (via its PDZ domain) with
CTNNB1; this interaction inhibits the transcriptional activity of
CTNNB1. Interacts with HTLV-1 TAX protein. Interacts (via PDZ
domain) with ARHGEF16. Interacts (via PDZ domain) with KCNJ4 (via
C-terminus). Competes with LIN7A for KCNJ4 binding. Interacts with
ADGRB2 (PubMed:21787750). {ECO:0000269|PubMed:10940294,
ECO:0000269|PubMed:11163757, ECO:0000269|PubMed:16855024,
ECO:0000269|PubMed:19635485, ECO:0000269|PubMed:19685007,
ECO:0000269|PubMed:21139582, ECO:0000269|PubMed:21417405,
ECO:0000269|PubMed:21787750, ECO:0000269|PubMed:9482110}.
-!- INTERACTION:
P03126:E6 (xeno); NbExp=2; IntAct=EBI-723259, EBI-1177242;
Q96D59:RNF183; NbExp=3; IntAct=EBI-723259, EBI-743938;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane;
Peripheral membrane protein; Cytoplasmic side. Note=Recruited to
the cell membrane by interaction with membrane proteins.
-!- TISSUE SPECIFICITY: Ubiquitous. Detected in brain, heart, kidney,
lung, small intestine and skeletal muscle. Detected in various
cell lines including HeLa. Weakly expressed in peripheral blood
leukocytes. {ECO:0000269|PubMed:10940294,
ECO:0000269|PubMed:16855024, ECO:0000269|PubMed:25645515}.
-!- SEQUENCE CAUTION:
Sequence=AAF43104.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF028823; AAB84248.2; -; mRNA.
EMBL; AF168787; AAF43104.1; ALT_INIT; Genomic_DNA.
EMBL; AF234997; AAG44368.1; -; mRNA.
EMBL; AF277318; AAK69111.1; -; mRNA.
EMBL; AK315408; BAG37800.1; -; mRNA.
EMBL; CH471108; EAW90491.1; -; Genomic_DNA.
EMBL; CH471108; EAW90492.1; -; Genomic_DNA.
EMBL; BC023980; AAH23980.1; -; mRNA.
CCDS; CCDS11032.1; -.
RefSeq; NP_001191627.1; NM_001204698.1.
RefSeq; NP_055419.1; NM_014604.3.
UniGene; Hs.12956; -.
UniGene; Hs.731607; -.
PDB; 2KG2; NMR; -; A=2-124.
PDB; 2L4S; NMR; -; A=1-124.
PDB; 2L4T; NMR; -; A=1-124.
PDB; 2VZ5; X-ray; 1.74 A; A=13-113.
PDB; 3GJ9; X-ray; 2.80 A; A/B=1-124.
PDB; 3SFJ; X-ray; 1.24 A; A/C=10-112.
PDB; 4E3B; X-ray; 1.50 A; A/B=11-112.
PDB; 4NNL; X-ray; 1.50 A; A/B=10-112.
PDB; 4NNM; X-ray; 1.60 A; A/B=10-120.
PDBsum; 2KG2; -.
PDBsum; 2L4S; -.
PDBsum; 2L4T; -.
PDBsum; 2VZ5; -.
PDBsum; 3GJ9; -.
PDBsum; 3SFJ; -.
PDBsum; 4E3B; -.
PDBsum; 4NNL; -.
PDBsum; 4NNM; -.
ProteinModelPortal; O14907; -.
SMR; O14907; -.
BioGrid; 119061; 44.
ELM; O14907; -.
IntAct; O14907; 16.
MINT; MINT-142501; -.
STRING; 9606.ENSP00000225525; -.
iPTMnet; O14907; -.
PhosphoSitePlus; O14907; -.
BioMuta; TAX1BP3; -.
UCD-2DPAGE; O14907; -.
EPD; O14907; -.
MaxQB; O14907; -.
PaxDb; O14907; -.
PeptideAtlas; O14907; -.
PRIDE; O14907; -.
TopDownProteomics; O14907; -.
DNASU; 30851; -.
Ensembl; ENST00000225525; ENSP00000225525; ENSG00000213977.
GeneID; 30851; -.
KEGG; hsa:30851; -.
UCSC; uc002fwc.4; human.
CTD; 30851; -.
DisGeNET; 30851; -.
EuPathDB; HostDB:ENSG00000213977.7; -.
GeneCards; TAX1BP3; -.
HGNC; HGNC:30684; TAX1BP3.
HPA; HPA046410; -.
HPA; HPA063078; -.
MIM; 616476; gene.
neXtProt; NX_O14907; -.
OpenTargets; ENSG00000213977; -.
PharmGKB; PA134950693; -.
eggNOG; KOG3553; Eukaryota.
eggNOG; ENOG4111IK0; LUCA.
GeneTree; ENSGT00390000002877; -.
HOGENOM; HOG000015753; -.
HOVERGEN; HBG052814; -.
InParanoid; O14907; -.
OMA; HKETEIN; -.
OrthoDB; EOG091G0UZR; -.
PhylomeDB; O14907; -.
TreeFam; TF318964; -.
BRENDA; 3.5.1.2; 2681.
Reactome; R-HSA-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
ChiTaRS; TAX1BP3; human.
EvolutionaryTrace; O14907; -.
GeneWiki; TAX1BP3; -.
GenomeRNAi; 30851; -.
PRO; PR:O14907; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000213977; -.
CleanEx; HS_TAX1BP3; -.
ExpressionAtlas; O14907; baseline and differential.
Genevisible; O14907; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0090630; P:activation of GTPase activity; IDA:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:2000009; P:negative regulation of protein localization to cell surface; IDA:UniProtKB.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB.
GO; GO:0007266; P:Rho protein signal transduction; IDA:UniProtKB.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
InterPro; IPR017268; Tax1-binding_p3.
PANTHER; PTHR23136; PTHR23136; 1.
Pfam; PF00595; PDZ; 1.
PIRSF; PIRSF037712; Tax1-binding_p3; 1.
SMART; SM00228; PDZ; 1.
SUPFAM; SSF50156; SSF50156; 1.
PROSITE; PS50106; PDZ; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cell membrane; Complete proteome;
Cytoplasm; Membrane; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Wnt signaling pathway.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
CHAIN 2 124 Tax1-binding protein 3.
/FTId=PRO_0000233943.
DOMAIN 15 112 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378}.
MOD_RES 61 61 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
VARIANT 33 33 I -> T (found in a patient with dilated
cardiomyopathy and septo-optic dysplasia;
unknown pathological significance).
{ECO:0000269|PubMed:25645515}.
/FTId=VAR_073966.
MUTAGEN 20 20 K->A: Abolishes interaction with KCNJ4.
{ECO:0000269|PubMed:16855024}.
MUTAGEN 90 90 H->A: Abolishes interaction with KCNJ4.
{ECO:0000269|PubMed:16855024}.
STRAND 9 11 {ECO:0000244|PDB:2KG2}.
STRAND 12 19 {ECO:0000244|PDB:3SFJ}.
STRAND 21 23 {ECO:0000244|PDB:3SFJ}.
STRAND 26 28 {ECO:0000244|PDB:3SFJ}.
STRAND 30 35 {ECO:0000244|PDB:3SFJ}.
STRAND 37 39 {ECO:0000244|PDB:2L4S}.
HELIX 41 43 {ECO:0000244|PDB:3SFJ}.
TURN 45 47 {ECO:0000244|PDB:2KG2}.
STRAND 48 50 {ECO:0000244|PDB:2L4S}.
STRAND 54 60 {ECO:0000244|PDB:3SFJ}.
STRAND 62 64 {ECO:0000244|PDB:2KG2}.
HELIX 65 69 {ECO:0000244|PDB:3SFJ}.
STRAND 76 80 {ECO:0000244|PDB:3SFJ}.
STRAND 83 85 {ECO:0000244|PDB:2L4T}.
HELIX 90 97 {ECO:0000244|PDB:3SFJ}.
STRAND 98 101 {ECO:0000244|PDB:2L4T}.
STRAND 103 111 {ECO:0000244|PDB:3SFJ}.
STRAND 115 118 {ECO:0000244|PDB:2KG2}.
TURN 121 123 {ECO:0000244|PDB:2KG2}.
SEQUENCE 124 AA; 13735 MW; FF0BCDF475F682CD CRC64;
MSYIPGQPVT AVVQRVEIHK LRQGENLILG FSIGGGIDQD PSQNPFSEDK TDKGIYVTRV
SEGGPAEIAG LQIGDKIMQV NGWDMTMVTH DQARKRLTKR SEEVVRLLVT RQSLQKAVQQ
SMLS


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EIAAB44595 Glutaminase-interacting protein 3,Homo sapiens,Human,Tax interaction protein 1,Tax1-binding protein 3,TAX1BP3,TIP1,TIP-1
EIAAB29754 Homo sapiens,HSPC218,Human,PABP-interacting protein 2,PAIP2,PAIP-2,PAIP2A,Poly(A)-binding protein-interacting protein 2,Polyadenylate-binding protein-interacting protein 2
EIAAB29748 Homo sapiens,Human,KIAA1155,PABP-interacting protein 2B,PAIP2B,PAIP-2B,Poly(A)-binding protein-interacting protein 2B,Polyadenylate-binding protein-interacting protein 2B
EIAAB39347 Mouse,Mus musculus,Spata24,Spermatogenesis-associated protein 24,TATA-binding protein-like factor-interacting protein,Testis protein T6441 homolog,Tipt,Tipt2,TLF-interacting protein,TRF2-interacting p
EIAAB29747 Kiaa1155,Mouse,Mus musculus,PABP-interacting protein 2B,Paip2b,PAIP-2B,Poly(A)-binding protein-interacting protein 2B,Polyadenylate-binding protein-interacting protein 2B
EIAAB29749 Homo sapiens,Human,PABP-interacting protein 1,PAIP1,PAIP-1,Poly(A)-binding protein-interacting protein 1,Polyadenylate-binding protein-interacting protein 1
EIAAB10371 AF9Q34,AIP1,ASK-interacting protein 1,DAB2 interaction protein,DAB2-interacting protein,DAB2IP,Disabled homolog 2-interacting protein,Homo sapiens,Human,KIAA1743
EIAAB29755 Mouse,Mus musculus,PABP-interacting protein 2,Paip2,PAIP-2,Poly(A)-binding protein-interacting protein 2,Polyadenylate-binding protein-interacting protein 2
EIAAB29752 Bos taurus,Bovine,PABP-interacting protein 2,PAIP2,PAIP-2,Poly(A)-binding protein-interacting protein 2,Polyadenylate-binding protein-interacting protein 2
EIAAB29751 PABP-interacting protein 2,Paip2,PAIP-2,Poly(A)-binding protein-interacting protein 2,Polyadenylate-binding protein-interacting protein 2,Rat,Rattus norvegicus
EIAAB29750 Mouse,Mus musculus,PABP-interacting protein 1,Paip1,PAIP-1,Poly(A)-binding protein-interacting protein 1,Polyadenylate-binding protein-interacting protein 1
15-288-22308F GIPC PDZ domain-containing protein 1 - RGS19-interacting protein 1; GAIP C-terminus-interacting protein; RGS-GAIP-interacting protein; Tax interaction protein 2; TIP-2 Polyclonal 0.1 mg
18-003-44197 PDZ domain-containing protein GIPC1 - RGS19-interacting protein 1; GAIP C-terminus-interacting protein; RGS-GAIP-interacting protein; Tax interaction protein 2; TIP-2 Polyclonal 0.05 mg Aff Pur
15-288-22308F GIPC PDZ domain-containing protein 1 - RGS19-interacting protein 1; GAIP C-terminus-interacting protein; RGS-GAIP-interacting protein; Tax interaction protein 2; TIP-2 Polyclonal 0.05 mg
10-288-22308F GIPC PDZ domain-containing protein 1 - RGS19-interacting protein 1; GAIP C-terminus-interacting protein; RGS-GAIP-interacting protein; Tax interaction protein 2; TIP-2 0.05 mg
10-288-22308F GIPC PDZ domain-containing protein 1 - RGS19-interacting protein 1; GAIP C-terminus-interacting protein; RGS-GAIP-interacting protein; Tax interaction protein 2; TIP-2 0.1 mg
EIAAB39603 54 kDa VacA-interacting protein,90 kDa N-WASP-interacting protein,90 kDa SH3 protein interacting with Nck,Mouse,Mus musculus,NCK-interacting protein with SH3 domain,Nckipsd,N-WASP-binding protein,SH3
18-003-43619 Polyadenylate-binding protein-interacting protein 1 - Poly(A)-binding protein-interacting protein 1; PABP-interacting protein 1; PAIP-1 Polyclonal 0.1 mg Protein A
10-288-21983F Calcium and integrin-binding protein 1 - Calmyrin; DNA-PKcs-interacting protein; Kinase-interacting protein; KIP; CIB; SNK-interacting protein 2-28; SIP2-28 0.05 mg
10-288-21983F Calcium and integrin-binding protein 1 - Calmyrin; DNA-PKcs-interacting protein; Kinase-interacting protein; KIP; CIB; SNK-interacting protein 2-28; SIP2-28 0.1 mg
EIAAB29753 Chicken,Gallus gallus,PABP-interacting protein 2,PAIP2,PAIP-2,Poly(A)-binding protein-interacting protein 2,Polyadenylate-binding protein-interacting protein 2,RCJMB04_16b5
EIAAB27017 45 kDa NF-AT-interacting protein,45 kDa NFAT-interacting protein,Homo sapiens,Human,NFATC2-interacting protein,NFATC2IP,NIP45,Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein
EIAAB27018 45 kDa NF-AT-interacting protein,45 kDa NFAT-interacting protein,Mouse,Mus musculus,NFATC2-interacting protein,Nfatc2ip,Nip45,Nuclear factor of activated T-cells, cytoplasmic 2-interacting protein
EIAAB31218 Homo sapiens,hPIP1,Human,p21-activated protein kinase-interacting protein 1,PAK_PLC-interacting protein 1,PAK1-interacting protein 1,PAK1IP1,PIP1,WD repeat-containing protein 84,WDR84
EIAAB46349 Homo sapiens,Human,Protein PRPL-2,WAS_WASL-interacting protein family member 1,WASP-interacting protein,WASPIP,WIP,WIPF1,Wiskott-Aldrich syndrome protein-interacting protein


 

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