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Calcineurin B homologous protein 1 (Calcineurin B-like protein) (Calcium-binding protein CHP) (Calcium-binding protein p22) (EF-hand calcium-binding domain-containing protein p22)

 CHP1_RAT                Reviewed;         195 AA.
P61023; Q62877;
26-APR-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
27-SEP-2017, entry version 119.
RecName: Full=Calcineurin B homologous protein 1;
AltName: Full=Calcineurin B-like protein;
AltName: Full=Calcium-binding protein CHP;
AltName: Full=Calcium-binding protein p22;
AltName: Full=EF-hand calcium-binding domain-containing protein p22;
Name=Chp1; Synonyms=Chp;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN EXOCYTIC MEMBRANE TRAFFIC,
CALCIUM-BINDING, MUTAGENESIS OF GLU-134, AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=8626580; DOI=10.1074/jbc.271.17.10183;
Barroso M.R., Bernd K.K., Dewitt N.D., Chang A., Mills K., Sztul E.S.;
"A novel Ca2+-binding protein, p22, is required for constitutive
membrane traffic.";
J. Biol. Chem. 271:10183-10187(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH STK17B.
TISSUE=Brain;
PubMed=11481038; DOI=10.1093/oxfordjournals.jbchem.a002975;
Matsumoto M., Miyake Y., Nagita M., Inoue H., Shitakubo D.,
Takemoto K., Ohtsuka C., Murakami H., Nakamura N., Kanazawa H.;
"A serine/threonine kinase which causes apoptosis-like cell death
interacts with a calcineurin B-like protein capable of binding Na+/H+
exchanger.";
J. Biochem. 130:217-225(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
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]
ASSOCIATION WITH MICROTUBULES, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=10512881; DOI=10.1091/mbc.10.10.3473;
Timm S., Titus B., Bernd K., Barroso M.;
"The EF-hand Ca(2+)-binding protein p22 associates with microtubules
in an N-myristoylation-dependent manner.";
Mol. Biol. Cell 10:3473-3488(1999).
[5]
INTERACTION WITH KIF1B, AND SUBCELLULAR LOCATION.
PubMed=12204119; DOI=10.1093/oxfordjournals.jbchem.a003246;
Nakamura N., Miyake Y., Matsushita M., Tanaka S., Inoue H.,
Kanazawa H.;
"KIF1Bbeta2, capable of interacting with CHP, is localized to synaptic
vesicles.";
J. Biochem. 132:483-491(2002).
[6]
FUNCTION AS STK17B KINASE INHIBITOR, AND INTERACTION WITH STK17B.
PubMed=12966074; DOI=10.1093/jb/mvg137;
Kuwahara H., Kamei J., Nakamura N., Matsumoto M., Inoue H.,
Kanazawa H.;
"The apoptosis-inducing protein kinase DRAK2 is inhibited in a
calcium-dependent manner by the calcium-binding protein CHP.";
J. Biochem. 134:245-250(2003).
[7]
SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNALS, AND MUTAGENESIS OF
VAL-138; LEU-139; VAL-143; VAL-145; ILE-147; VAL-179; LEU-180; VAL-183
AND VAL-185.
PubMed=14769882; DOI=10.1093/jb/mvg223;
Nagita M., Inoue H., Nakamura N., Kanazawa H.;
"Two nuclear export signals specify the cytoplasmic localization of
calcineurin B homologous protein 1.";
J. Biochem. 134:919-925(2003).
[8]
FUNCTION, INTERACTION WITH GAPDH, ASSOCIATION WITH MICROTUBULES,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15312048; DOI=10.1042/BJ20040622;
Andrade J., Pearce S.T., Zhao H., Barroso M.;
"Interactions among p22, glyceraldehyde-3-phosphate dehydrogenase and
microtubules.";
Biochem. J. 384:327-336(2004).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-134.
PubMed=14657246; DOI=10.1091/mbc.E03-07-0500;
Andrade J., Zhao H., Titus B., Timm Pearce S., Barroso M.;
"The EF-hand Ca2+-binding protein p22 plays a role in microtubule and
endoplasmic reticulum organization and dynamics with distinct Ca2+-
binding requirements.";
Mol. Biol. Cell 15:481-496(2004).
[10]
FUNCTION IN TRANSCRIPTION REGULATION, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF VAL-143; VAL-145; ILE-147; VAL-183 AND VAL-185.
PubMed=20720019; DOI=10.1074/jbc.M110.165555;
Jimenez-Vidal M., Srivastava J., Putney L.K., Barber D.L.;
"Nuclear-localized calcineurin homologous protein CHP1 interacts with
upstream binding factor and inhibits ribosomal RNA synthesis.";
J. Biol. Chem. 285:36260-36266(2010).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=21543739; DOI=10.1152/ajpcell.00404.2010;
Matsushita M., Tanaka H., Mitsui K., Kanazawa H.;
"Dual functional significance of calcineurin homologous protein 1
binding to Na(+)/H(+) exchanger isoform 1.";
Am. J. Physiol. 301:C280-C288(2011).
[12]
PRELIMINARY X-RAY CRYSTALLOGRAPHY.
PubMed=16511110; DOI=10.1107/S1744309105016325;
Naoe Y., Arita K., Hashimoto H., Kanazawa H., Sato M., Shimizu T.;
"Crystallization and preliminary X-ray crystallographic analysis of
rat calcineurin B homologous protein 1.";
Acta Crystallogr. F 61:612-613(2005).
[13]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS,
AND SUBUNIT.
PubMed=15987692; DOI=10.1074/jbc.M503390200;
Naoe Y., Arita K., Hashimoto H., Kanazawa H., Sato M., Shimizu T.;
"Structural characterization of calcineurin B homologous protein 1.";
J. Biol. Chem. 280:32372-32378(2005).
-!- FUNCTION: Calcium-binding protein involved in different processes
such as regulation of vesicular trafficking, plasma membrane
Na(+)/H(+) exchanger and gene transcription. Involved in the
constitutive exocytic membrane traffic. Mediates the association
between microtubules and membrane-bound organelles of the
endoplasmic reticulum and Golgi apparatus and is also required for
the targeting and fusion of transcytotic vesicles (TCV) with the
plasma membrane. Functions as an integral cofactor in cell pH
regulation by controlling plasma membrane-type Na(+)/H(+) exchange
activity. Affects the pH sensitivity of SLC9A1/NHE1 by increasing
its sensitivity at acidic pH. Required for the stabilization and
localization of SLC9A1/NHE1 at the plasma membrane. Inhibits
serum- and GTPase-stimulated Na(+)/H(+) exchange. Plays a role as
an inhibitor of ribosomal RNA transcription by repressing the
nucleolar UBF1 transcriptional activity. May sequester UBF1 in the
nucleoplasm and limit its translocation to the nucleolus.
Associates to the ribosomal gene promoter. Acts as a negative
regulator of the calcineurin/NFAT signaling pathway. Inhibits NFAT
nuclear translocation and transcriptional activity by suppressing
the calcium-dependent calcineurin phosphatase activity. Also
negatively regulates the kinase activity of the apoptosis-induced
kinase STK17B. Inhibits both STK17B auto- and substrate-
phosphorylations in a calcium-dependent manner.
{ECO:0000269|PubMed:12966074, ECO:0000269|PubMed:14657246,
ECO:0000269|PubMed:15312048, ECO:0000269|PubMed:20720019,
ECO:0000269|PubMed:21543739, ECO:0000269|PubMed:8626580}.
-!- SUBUNIT: Interacts with PPP3CA. Interacts with SLC9A1/NHE1 (via
the juxtamembrane region of the cytoplasmic C-terminal domain);
the interaction occurs at the plasma membrane in a calcium-
dependent manner and at a domain that is critical for growth
factor stimulation of the exchanger (By similarity). Monomer.
Interacts with STK17B; the interaction occurs in a calcium-
independent manner and induces the translocation of CHP1 from the
Golgi to the nucleus. Interacts with GAPDH; the interaction is
direct, occurs in a N-myristoylation-dependent manner and
facilitates the ability of CHP1 to bind microtubules. Interacts
with KIF1B (via the C-terminal end of the kinesin-motor domain);
the interaction occurs in a calcium-dependent manner. Associates
(via C-terminal domain) with microtubules; the association occurs
with polymerized microtubules during the cell cycle in a
myristoylation- and calcium-independent manner and is enhanced by
GAPDH. {ECO:0000250, ECO:0000269|PubMed:11481038,
ECO:0000269|PubMed:12204119, ECO:0000269|PubMed:12966074,
ECO:0000269|PubMed:15312048, ECO:0000269|PubMed:15987692}.
-!- INTERACTION:
P46406:GAPDH (xeno); NbExp=2; IntAct=EBI-917838, EBI-2750726;
P04797:Gapdh; NbExp=3; IntAct=EBI-917838, EBI-349219;
O88658-1:Kif1b; NbExp=4; IntAct=EBI-917838, EBI-6143515;
Q91XS8:Stk17b; NbExp=6; IntAct=EBI-917838, EBI-77460;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20720019}.
Cytoplasm {ECO:0000269|PubMed:12204119,
ECO:0000269|PubMed:14769882}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:10512881, ECO:0000269|PubMed:15312048}.
Endomembrane system {ECO:0000269|PubMed:15312048}. Endoplasmic
reticulum-Golgi intermediate compartment {ECO:0000305}.
Endoplasmic reticulum {ECO:0000269|PubMed:14657246}. Cell membrane
{ECO:0000269|PubMed:21543739}. Membrane
{ECO:0000250|UniProtKB:Q99653}; Lipid-anchor
{ECO:0000250|UniProtKB:Q99653}. Note=Localizes in cytoplasmic
compartments in dividing cells. Localizes in the nucleus in
quiescent cells. Exported from the nucleus to the cytoplasm
through a nuclear export signal (NES) and CRM1-dependent pathway.
May shuttle between nucleus and cytoplasm. Localizes with the
microtubule-organizing center (MTOC) and extends toward the
periphery along microtubules. Associates with membranes of the
early secretory pathway in a GAPDH-independent, N-
myristoylation- and calcium-dependent manner. Colocalizes with the
mitotic spindle microtubules. Colocalizes with GAPDH along
microtubules. Colocalizes with SLC9A1 at the reticulum endoplasmic
and plasma membrane. Colocalizes with STK17B at the plasma
membrane. {ECO:0000269|PubMed:14657246,
ECO:0000269|PubMed:15312048, ECO:0000269|PubMed:20720019,
ECO:0000269|PubMed:21543739}.
-!- TISSUE SPECIFICITY: Expressed in liver and kidney (at protein
level). Ubiquitously expressed. Expressed in the brain, lung,
testes, kidney, spleen and heart. {ECO:0000269|PubMed:10512881,
ECO:0000269|PubMed:15312048, ECO:0000269|PubMed:8626580}.
-!- PTM: Phosphorylated; decreased phosphorylation is associated with
an increase in SLC9A1/NHE1 Na(+)/H(+) exchange activity.
Phosphorylation occurs in serum-dependent manner. The
phosphorylation state may regulate the binding to SLC9A1/NHE1 (By
similarity). {ECO:0000250}.
-!- PTM: N-myristoylation is required for its association with
microtubules and interaction with GAPDH, but not for the
constitutive association to membranes. Both N-myristoylation and
calcium-mediated conformational changes are essential in exocytic
traffic.
-!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CHP subfamily. {ECO:0000305}.
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EMBL; U39875; AAB04146.1; -; mRNA.
EMBL; AB070350; BAB63369.1; -; mRNA.
EMBL; BC062029; AAH62029.1; -; mRNA.
RefSeq; NP_077053.1; NM_024139.2.
UniGene; Rn.11041; -.
PDB; 2CT9; X-ray; 2.20 A; A/B=1-195.
PDBsum; 2CT9; -.
ProteinModelPortal; P61023; -.
SMR; P61023; -.
IntAct; P61023; 11.
MINT; MINT-1786138; -.
STRING; 10116.ENSRNOP00000053243; -.
PhosphoSitePlus; P61023; -.
PaxDb; P61023; -.
PRIDE; P61023; -.
Ensembl; ENSRNOT00000056405; ENSRNOP00000053243; ENSRNOG00000004742.
GeneID; 64152; -.
KEGG; rno:64152; -.
UCSC; RGD:620447; rat.
CTD; 11261; -.
RGD; 620447; Chp1.
eggNOG; KOG0034; Eukaryota.
eggNOG; COG5126; LUCA.
GeneTree; ENSGT00860000133729; -.
HOGENOM; HOG000233019; -.
HOVERGEN; HBG105307; -.
InParanoid; P61023; -.
KO; K17610; -.
OMA; EFCRAME; -.
OrthoDB; EOG091G0LZ1; -.
PhylomeDB; P61023; -.
TreeFam; TF354284; -.
Reactome; R-RNO-2160916; Hyaluronan uptake and degradation.
EvolutionaryTrace; P61023; -.
PRO; PR:P61023; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000004742; -.
Genevisible; P61023; RN.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0030133; C:transport vesicle; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:RGD.
GO; GO:0048306; F:calcium-dependent protein binding; ISS:UniProtKB.
GO; GO:0019900; F:kinase binding; IDA:UniProtKB.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0004860; F:protein kinase inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0005215; F:transporter activity; IDA:UniProtKB.
GO; GO:0017156; P:calcium ion regulated exocytosis; IDA:RGD.
GO; GO:0019722; P:calcium-mediated signaling; TAS:RGD.
GO; GO:0071468; P:cellular response to acidic pH; ISS:UniProtKB.
GO; GO:0031122; P:cytoplasmic microtubule organization; IDA:UniProtKB.
GO; GO:0022406; P:membrane docking; IDA:UniProtKB.
GO; GO:0061025; P:membrane fusion; IDA:UniProtKB.
GO; GO:0061024; P:membrane organization; IDA:UniProtKB.
GO; GO:0001578; P:microtubule bundle formation; IDA:UniProtKB.
GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; ISS:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:0010923; P:negative regulation of phosphatase activity; ISS:UniProtKB.
GO; GO:0031953; P:negative regulation of protein autophosphorylation; IDA:UniProtKB.
GO; GO:0042308; P:negative regulation of protein import into nucleus; ISS:UniProtKB.
GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:UniProtKB.
GO; GO:0060050; P:positive regulation of protein glycosylation; IDA:UniProtKB.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
GO; GO:0051222; P:positive regulation of protein transport; IDA:UniProtKB.
GO; GO:0032417; P:positive regulation of sodium:proton antiporter activity; ISS:UniProtKB.
GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB.
GO; GO:0051259; P:protein oligomerization; IDA:UniProtKB.
GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
GO; GO:0051453; P:regulation of intracellular pH; ISS:UniProtKB.
GO; GO:1901214; P:regulation of neuron death; IEA:Ensembl.
CDD; cd00051; EFh; 1.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
Pfam; PF13499; EF-hand_7; 1.
SMART; SM00054; EFh; 2.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 1.
PROSITE; PS50222; EF_HAND_2; 3.
1: Evidence at protein level;
3D-structure; Calcium; Cell membrane; Complete proteome; Cytoplasm;
Cytoskeleton; Endoplasmic reticulum; Lipoprotein; Membrane;
Metal-binding; Myristate; Nucleus; Phosphoprotein;
Protein kinase inhibitor; Protein transport; Reference proteome;
Repeat; Transport.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q99653}.
CHAIN 2 195 Calcineurin B homologous protein 1.
/FTId=PRO_0000073846.
DOMAIN 26 61 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 71 106 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 110 145 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 151 186 EF-hand 4. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 123 134 1.
CA_BIND 164 175 2.
MOTIF 2 6 Necessary for association with
microtubule and interaction with GAPDH.
MOTIF 138 147 Nuclear export signal 1.
MOTIF 176 185 Nuclear export signal 2.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000250|UniProtKB:Q99653}.
MUTAGEN 134 134 E->A: Inhibits calcium-mediated
conformational changes. Loss of
transcytotic targeting/fusion function.
Reduces association with membranes. Does
not affect microtubule formation.
{ECO:0000269|PubMed:14657246,
ECO:0000269|PubMed:8626580}.
MUTAGEN 138 138 V->A: Predominantly located in the
cytoplasm; when associated with A-139.
Predominantly located in the nucleus;
when associated with A-139; A-179 and A-
180. {ECO:0000269|PubMed:14769882}.
MUTAGEN 139 139 L->A: Predominantly located in the
cytoplasm; when associated with A-138.
Predominantly located in the nucleus;
when associated with A-138; A-179 and A-
180. {ECO:0000269|PubMed:14769882}.
MUTAGEN 143 143 V->A: Predominantly located in the
cytoplasm; when associated with A-145 and
A-147. Predominantly located in the
nucleus; when associated with A-145; A-
147; A-183 and A-185.
{ECO:0000269|PubMed:14769882,
ECO:0000269|PubMed:20720019}.
MUTAGEN 145 145 V->A: Predominantly located in the
cytoplasm; when associated with A-143 and
A-147. Predominantly located in the
nucleus; when associated with A-143; A-
147; A-183 and A-185.
{ECO:0000269|PubMed:14769882,
ECO:0000269|PubMed:20720019}.
MUTAGEN 147 147 I->A: Predominantly located in the
cytoplasm; when associated with A-143 and
A-145. Predominantly located in the
nucleus; when associated with A-143; A-
145; A-183 and A-185.
{ECO:0000269|PubMed:14769882,
ECO:0000269|PubMed:20720019}.
MUTAGEN 179 179 V->A: Predominantly located in the
cytoplasm; when associated with A-180.
Predominantly located in the nucleus;
when associated with A-138; A-139 and A-
180. {ECO:0000269|PubMed:14769882}.
MUTAGEN 180 180 L->A: Predominantly located in the
cytoplasm; when associated with A-179.
Predominantly located in the nucleus;
when associated with A-138; A-139 and A-
179. {ECO:0000269|PubMed:14769882}.
MUTAGEN 183 183 V->A: Predominantly located in the
cytoplasm; when associated with A-185.
Predominantly located in the nucleus;
when associated with A-143; A-145; A-147
and A-185. {ECO:0000269|PubMed:14769882,
ECO:0000269|PubMed:20720019}.
MUTAGEN 185 185 V->A: Predominantly located in the
cytoplasm; when associated with A-183.
Predominantly located in the nucleus;
when associated with A-143; A-145; A-147
and A-183. {ECO:0000269|PubMed:14769882,
ECO:0000269|PubMed:20720019}.
HELIX 4 7 {ECO:0000244|PDB:2CT9}.
HELIX 11 21 {ECO:0000244|PDB:2CT9}.
HELIX 25 38 {ECO:0000244|PDB:2CT9}.
STRAND 43 46 {ECO:0000244|PDB:2CT9}.
HELIX 49 53 {ECO:0000244|PDB:2CT9}.
HELIX 55 58 {ECO:0000244|PDB:2CT9}.
HELIX 63 68 {ECO:0000244|PDB:2CT9}.
HELIX 80 88 {ECO:0000244|PDB:2CT9}.
HELIX 111 122 {ECO:0000244|PDB:2CT9}.
STRAND 127 130 {ECO:0000244|PDB:2CT9}.
HELIX 132 142 {ECO:0000244|PDB:2CT9}.
HELIX 149 163 {ECO:0000244|PDB:2CT9}.
STRAND 165 172 {ECO:0000244|PDB:2CT9}.
HELIX 173 178 {ECO:0000244|PDB:2CT9}.
TURN 179 182 {ECO:0000244|PDB:2CT9}.
HELIX 185 187 {ECO:0000244|PDB:2CT9}.
HELIX 189 195 {ECO:0000244|PDB:2CT9}.
SEQUENCE 195 AA; 22432 MW; 7B803EF0ABED829E CRC64;
MGSRASTLLR DEELEEIKKE TGFSHSQITR LYSRFTSLDK GENGTLSRED FQRIPELAIN
PLGDRIINAF FSEGEDQVNF RGFMRTLAHF RPIEDNEKSK DVNGPEPLNS RSNKLHFAFR
LYDLDKDDKI SRDELLQVLR MMVGVNISDE QLGSIADRTI QEADQDGDSA ISFTEFVKVL
EKVDVEQKMS IRFLH


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EIAAB12528 CAP-binding protein complex-interacting protein 1,DJ-1-binding protein,DJBP,DJBP,EFCAB6,EF-hand calcium-binding domain-containing protein 6,Homo sapiens,Human,KIAA1672
EIAAB05007 Cabyr,Calcium-binding protein 86,Calcium-binding tyrosine phosphorylation-regulated protein,Cbp86,Mouse,Mus musculus,Testis-specific calcium-binding protein CBP86
10-663-45600 S100 calcium binding Protein A4 (S100A4) Human - S100 calcium-binding protein A4; Metastasin; Protein Mts1; Placental calcium-binding protein; Calvasculin N_A 0.005 mg
10-663-45600 S100 calcium binding Protein A4 (S100A4) Human - S100 calcium-binding protein A4; Metastasin; Protein Mts1; Placental calcium-binding protein; Calvasculin N_A 0.01 mg
10-663-45600 S100 calcium binding Protein A4 (S100A4) Human - S100 calcium-binding protein A4; Metastasin; Protein Mts1; Placental calcium-binding protein; Calvasculin N_A 0.002 mg
EIAAB36663 Homo sapiens,Human,Protein S100-A7A,S100 calcium-binding protein A15,S100 calcium-binding protein A7A,S100 calcium-binding protein A7-like 1,S100A15,S100A7A,S100A7L1
EIAAB36537 Capl,Metastasin,Metastatic cell protein,Mouse,Mts1,Mus musculus,PEL98,Placental calcium-binding protein,Protein 18A2,Protein Mts1,Protein S100-A4,S100 calcium-binding protein A4,S100a4
EIAAB36540 Metastasin,Nerve growth factor-induced protein 42A,P9K,Placental calcium-binding protein,Protein S100-A4,Rat,Rattus norvegicus,S100 calcium-binding protein A4,S100a4
EIAAB12514 Calcium release-activated calcium channel regulator 2A,CRAC channel regulator 2A,CRACR2A,EFCAB4B,EF-hand calcium-binding domain-containing protein 4B,Homo sapiens,Human
EIAAB12512 Calcium release-activated calcium channel regulator 2B,CRAC channel regulator 2B,CRACR2B,EFCAB4A,EF-hand calcium-binding domain-containing protein 4A,Homo sapiens,Human
EIAAB12527 DJ-1-binding protein,DJBP,Djbp,Efcab6,EF-hand calcium-binding domain-containing protein 6,Kiaa1672,Mouse,Mus musculus
EIAAB36523 CABP,CABP9K,CALB3,Calbindin-D9k,Homo sapiens,Human,Protein S100-G,S100 calcium-binding protein G,S100D,S100G,Vitamin D-dependent calcium-binding protein, intestinal


 

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