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Calcium-binding protein 1 (CaBP1) (Calbrain) (Caldendrin)

 CABP1_HUMAN             Reviewed;         370 AA.
Q9NZU7; O95663; Q8N6H5; Q9NZU8;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
31-MAY-2011, sequence version 5.
25-OCT-2017, entry version 152.
RecName: Full=Calcium-binding protein 1;
Short=CaBP1;
AltName: Full=Calbrain;
AltName: Full=Caldendrin;
Name=CABP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CALBRAIN).
TISSUE=Cerebellum;
PubMed=9920909; DOI=10.1074/jbc.274.6.3610;
Yamaguchi K., Yamaguchi F., Miyamoto O., Sugimoto K., Konishi R.,
Hatase O.;
"Calbrain, a novel two EF-hand calcium-binding protein that suppresses
Ca2+/calmodulin-dependent protein kinase II activity in the brain.";
J. Biol. Chem. 274:3610-3616(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS L-CABP1 AND S-CABP1),
MYRISTOYLATION AT GLY-2 (ISOFORMS L-CABP1 AND S-CABP1), PALMITOYLATION
AT CYS-4 (ISOFORMS L-CABP1 AND S-CABP1), AND SUBCELLULAR LOCATION.
TISSUE=Retina;
PubMed=10625670; DOI=10.1074/jbc.275.2.1247;
Haeseleer F., Sokal I., Verlinde C.L.M.J., Erdjument-Bromage H.,
Tempst P., Pronin A.N., Benovic J.L., Fariss R.N., Palczewski K.;
"Five members of a novel Ca(2+)-binding protein (CABP) subfamily with
similarity to calmodulin.";
J. Biol. Chem. 275:1247-1260(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CALDENDRIN).
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]
ALTERNATIVE SPLICING (ISOFORM CALDENDRIN).
PubMed=9694893; DOI=10.1074/jbc.273.33.21324;
Seidenbecher C.I., Langnaese K., Sanmarti-Vila L., Boeckers T.M.,
Smalla K.-H., Sabel B.A., Garner C.C., Gundelfinger E.D., Kreutz M.R.;
"Caldendrin, a novel neuronal calcium-binding protein confined to the
somato-dendritic compartment.";
J. Biol. Chem. 273:21324-21331(1998).
[6]
INTERACTION WITH ITPR1; ITPR2 AND ITPR3, AND MUTAGENESIS OF ASP-238;
ASP-240; ASP-315; ASN-317; ASP-352 AND ASN-354.
PubMed=12032348; DOI=10.1073/pnas.102006299;
Yang J., McBride S., Mak D.-O.D., Vardi N., Palczewski K.,
Haeseleer F., Foskett J.K.;
"Identification of a family of calcium sensors as protein ligands of
inositol trisphosphate receptor Ca(2+) release channels.";
Proc. Natl. Acad. Sci. U.S.A. 99:7711-7716(2002).
[7]
FUNCTION, AND INTERACTION WITH CACNA1A.
PubMed=11865310; DOI=10.1038/nn805;
Lee A., Westenbroek R.E., Haeseleer F., Palczewski K., Scheuer T.,
Catterall W.A.;
"Differential modulation of Ca(v)2.1 channels by calmodulin and Ca2+-
binding protein 1.";
Nat. Neurosci. 5:210-217(2002).
[8]
PHOSPHORYLATION AT SER-323, MUTAGENESIS OF SER-323, SUBCELLULAR
LOCATION, AND INTERACTION WITH ITPR1.
PubMed=14685260; DOI=10.1038/sj.emboj.7600037;
Kasri N.N., Holmes A.M., Bultynck G., Parys J.B., Bootman M.D.,
Rietdorf K., Missiaen L., McDonald F., De Smedt H., Conway S.J.,
Holmes A.B., Berridge M.J., Roderick H.L.;
"Regulation of InsP3 receptor activity by neuronal Ca2+-binding
proteins.";
EMBO J. 23:312-321(2004).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=14570872; DOI=10.1074/jbc.M309617200;
Haynes L.P., Tepikin A.V., Burgoyne R.D.;
"Calcium-binding protein 1 is an inhibitor of agonist-evoked, inositol
1,4,5-trisphosphate-mediated calcium signaling.";
J. Biol. Chem. 279:547-555(2004).
[10]
INTERACTION WITH MAP1LC3B.
PubMed=15095872; DOI=10.1016/j.jmb.2003.12.054;
Seidenbecher C.I., Landwehr M., Smalla K.H., Kreutz M.,
Dieterich D.C., Zuschratter W., Reissner C., Hammarback J.A.,
Bockers T.M., Gundelfinger E.D., Kreutz M.R.;
"Caldendrin but not calmodulin binds to light chain 3 of MAP1A/B: an
association with the microtubule cytoskeleton highlighting exclusive
binding partners for neuronal Ca(2+)-sensor proteins.";
J. Mol. Biol. 336:957-970(2004).
[11]
FUNCTION, AND INTERACTION WITH CACNA1C.
PubMed=15140941; DOI=10.1523/JNEUROSCI.5523-03.2004;
Zhou H., Kim S.-A., Kirk E.A., Tippens A.L., Sun H., Haeseleer F.,
Lee A.;
"Ca2+-binding protein-1 facilitates and forms a postsynaptic complex
with Cav1.2 (L-type) Ca2+ channels.";
J. Neurosci. 24:4698-4708(2004).
[12]
FUNCTION, AND INTERACTION WITH CACNA1C.
PubMed=15980432; DOI=10.1074/jbc.M504167200;
Zhou H., Yu K., McCoy K.L., Lee A.;
"Molecular mechanism for divergent regulation of Cav1.2 Ca2+ channels
by calmodulin and Ca2+-binding protein-1.";
J. Biol. Chem. 280:29612-29619(2005).
[13]
FUNCTION, AND INTERACTION WITH TRPC5.
PubMed=15895247; DOI=10.1007/s00424-005-1419-1;
Kinoshita-Kawada M., Tang J., Xiao R., Kaneko S., Foskett J.K.,
Zhu M.X.;
"Inhibition of TRPC5 channels by Ca2+-binding protein 1 in Xenopus
oocytes.";
Pflugers Arch. 450:345-354(2005).
[14]
SUBUNIT, CALCIUM-BINDING, AND MAGNESIUM-BINDING.
PubMed=16147998; DOI=10.1074/jbc.M508541200;
Wingard J.N., Chan J., Bosanac I., Haeseleer F., Palczewski K.,
Ikura M., Ames J.B.;
"Structural analysis of Mg2+ and Ca2+ binding to CaBP1, a neuron-
specific regulator of calcium channels.";
J. Biol. Chem. 280:37461-37470(2005).
[15]
STRUCTURE BY NMR OF 219-294 AND 299-370 IN COMPLEX WITH MAGNESIUM AND
CALCIUM, AND MUTAGENESIS OF ASP-238; ASP-240; ASP-242 AND ASP-249.
PubMed=19008222; DOI=10.1074/jbc.M806513200;
Li C., Chan J., Haeseleer F., Mikoshiba K., Palczewski K., Ikura M.,
Ames J.B.;
"Structural insights into Ca2+-dependent regulation of inositol 1,4,5-
trisphosphate receptors by CaBP1.";
J. Biol. Chem. 284:2472-2481(2009).
-!- FUNCTION: Modulates calcium-dependent activity of inositol 1,4,5-
triphosphate receptors (ITPRs). Inhibits agonist-induced
intracellular calcium signaling. Enhances inactivation and does
not support calcium-dependent facilitation of voltage-dependent
P/Q-type calcium channels. Causes calcium-dependent facilitation
and inhibits inactivation of L-type calcium channels by binding to
the same sites as calmodulin in the C-terminal domain of CACNA1C,
but resulting in an opposit effects on channel function.
Suppresses the calcium-dependent inactivation of CACNA1D (By
similarity). Inhibits TRPC5 channels. Prevents NMDA receptor-
induced cellular degeneration (By similarity). {ECO:0000250,
ECO:0000269|PubMed:11865310, ECO:0000269|PubMed:14570872,
ECO:0000269|PubMed:15140941, ECO:0000269|PubMed:15895247,
ECO:0000269|PubMed:15980432}.
-!- SUBUNIT: Homodimer; when bound to calcium or magnesium. Interacts
(via C-terminus) with ITPR1, ITPR2 and ITPR3. This binding is
calcium dependent and the interaction correlates with calcium
concentration. An additional calcium-independent interaction with
the N-terminus of ITPR1 results in a decreased InsP(3) binding to
the receptor. Interacts with CACNA1A (via C-terminal CDB motif) in
the pre- and postsynaptic membranes. Interacts with CACNA1C (via
C-terminal C and IQ motifs). The binding to the C motif is calcium
independent whereas the binding to IQ requires the presence of
calcium and is mutually exclusive with calmodulin binding.
Interacts with CACNA1D (By similarity). Interacts with TRPC5 (via
C-terminus). Interacts (via EF-hands 1 and 2) at microtubules with
MAP1LC3B. Interacts with MYO1C (By similarity). Interacts (via EF-
hands 1 and 2) with NSMF (via the central NLS-containing motif
region), the interaction occurs in a calcium dependent manner
after synaptic NMDA receptor stimulation and prevents nuclear
import of NSMF. Interacts with SPACA9 (By similarity).
{ECO:0000250|UniProtKB:O88751, ECO:0000250|UniProtKB:Q9JLK7,
ECO:0000269|PubMed:11865310, ECO:0000269|PubMed:12032348,
ECO:0000269|PubMed:15095872, ECO:0000269|PubMed:15140941,
ECO:0000269|PubMed:15895247, ECO:0000269|PubMed:15980432}.
-!- INTERACTION:
Q13936:CACNA1C; NbExp=4; IntAct=EBI-907894, EBI-1038838;
Q13936-20:CACNA1C; NbExp=2; IntAct=EBI-15896740, EBI-15896749;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:10625670}. Cytoplasm, perinuclear region
{ECO:0000269|PubMed:14685260}. Cell membrane
{ECO:0000269|PubMed:10625670, ECO:0000269|PubMed:14570872,
ECO:0000269|PubMed:14685260}; Lipid-anchor; Cytoplasmic side.
Golgi apparatus {ECO:0000269|PubMed:14570872,
ECO:0000269|PubMed:14685260}. Cell junction, synapse, postsynaptic
cell membrane, postsynaptic density {ECO:0000305}. Note=L-CaBP1 is
associated most likely with the cytoskeletal structures, whereas
S-CaBP1 is localized at or near the plasma membrane.
{ECO:0000269|PubMed:10625670}.
-!- SUBCELLULAR LOCATION: Isoform L-CaBP1: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:10625670}. Note=L-CaBP1 is associated most
likely with the cytoskeletal structures.
{ECO:0000269|PubMed:10625670}.
-!- SUBCELLULAR LOCATION: Isoform S-CaBP1: Cytoplasm, cell cortex.
Cell membrane {ECO:0000305|PubMed:10625670}; Lipid-anchor
{ECO:0000305}. Note=S-CaBP1 is localized at or near the plasma
membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Experimental confirmation may be lacking for some
isoforms.;
Name=Caldendrin;
IsoId=Q9NZU7-4; Sequence=Displayed;
Name=L-CaBP1; Synonyms=Caldendrin-S2;
IsoId=Q9NZU7-1; Sequence=VSP_037938, VSP_037939;
Note=Initiator Met-1 is removed. Contains a N-myristoyl glycine
at position 2. Contains a S-palmitoyl cysteine at position 4.
{ECO:0000269|PubMed:10625670, ECO:0000303|PubMed:10625670};
Name=S-CaBP1; Synonyms=Caldendrin-S1;
IsoId=Q9NZU7-2; Sequence=VSP_037937, VSP_037940;
Note=Initiator Met-1 is removed. Contains a N-myristoyl glycine
at position 2. Contains a S-palmitoyl cysteine at position 4.
{ECO:0000269|PubMed:10625670, ECO:0000303|PubMed:10625670};
Name=Calbrain;
IsoId=Q9NZU7-3; Sequence=VSP_037936;
Note=It is currently uncertain whether calbrain represent a
spliced isoform.;
-!- TISSUE SPECIFICITY: Retina and brain. Somatodendritic compartment
of neurons. Calbrain was found exclusively in brain where it is
abundant in the hippocampus, habenular area in the epithalamus and
in the cerebellum.
-!- DOMAIN: EF-1 binds magnesium constitutively under physiological
conditions, EF-3 and EF-4 bind calcium cooperatively and EF-2
binds neither calcium nor magnesium.
-!- PTM: Phosphorylated. The phosphorylation regulates the activity.
{ECO:0000269|PubMed:14685260}.
-!- CAUTION: The interaction with CACNA1A is described as calcium
independent in PubMed:11865310 while it is shown to be acutely
calcium dependent in PubMed:14570872. PubMed:12032348 describes a
stimulatory effect of CABP1 during agonist-induced intracellular
calcium signaling while PubMed:14570872 and PubMed:11865310 show
an inhibitory effect. {ECO:0000305}.
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EMBL; X94700; CAA64361.1; -; mRNA.
EMBL; AF169148; AAF25782.1; -; mRNA.
EMBL; AF169149; AAF25783.1; -; mRNA.
EMBL; AC069234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC030201; AAH30201.2; -; mRNA.
CCDS; CCDS31913.1; -. [Q9NZU7-4]
CCDS; CCDS9204.1; -. [Q9NZU7-2]
CCDS; CCDS9205.1; -. [Q9NZU7-1]
RefSeq; NP_001028849.1; NM_001033677.1. [Q9NZU7-4]
RefSeq; NP_004267.2; NM_004276.4. [Q9NZU7-2]
RefSeq; NP_112482.1; NM_031205.3. [Q9NZU7-1]
UniGene; Hs.458482; -.
PDB; 2K7B; NMR; -; A=219-294.
PDB; 2K7C; NMR; -; A=299-370.
PDB; 2K7D; NMR; -; A=299-370.
PDB; 2LAN; NMR; -; A=219-370.
PDB; 2LAP; NMR; -; A=219-370.
PDB; 3OX5; X-ray; 2.90 A; A/B/C/D/E/F=219-370.
PDB; 3OX6; X-ray; 2.40 A; A/B/C/D/E/F=219-370.
PDBsum; 2K7B; -.
PDBsum; 2K7C; -.
PDBsum; 2K7D; -.
PDBsum; 2LAN; -.
PDBsum; 2LAP; -.
PDBsum; 3OX5; -.
PDBsum; 3OX6; -.
ProteinModelPortal; Q9NZU7; -.
SMR; Q9NZU7; -.
BioGrid; 114863; 8.
DIP; DIP-35477N; -.
IntAct; Q9NZU7; 4.
STRING; 9606.ENSP00000317310; -.
iPTMnet; Q9NZU7; -.
PhosphoSitePlus; Q9NZU7; -.
BioMuta; CABP1; -.
DMDM; 334302962; -.
PaxDb; Q9NZU7; -.
PeptideAtlas; Q9NZU7; -.
PRIDE; Q9NZU7; -.
DNASU; 9478; -.
Ensembl; ENST00000288616; ENSP00000288616; ENSG00000157782. [Q9NZU7-1]
Ensembl; ENST00000316803; ENSP00000317310; ENSG00000157782. [Q9NZU7-4]
Ensembl; ENST00000351200; ENSP00000288615; ENSG00000157782. [Q9NZU7-2]
GeneID; 9478; -.
KEGG; hsa:9478; -.
UCSC; uc001tyu.4; human. [Q9NZU7-4]
CTD; 9478; -.
EuPathDB; HostDB:ENSG00000157782.9; -.
GeneCards; CABP1; -.
HGNC; HGNC:1384; CABP1.
HPA; HPA051438; -.
MIM; 605563; gene.
neXtProt; NX_Q9NZU7; -.
OpenTargets; ENSG00000157782; -.
PharmGKB; PA26000; -.
eggNOG; KOG0027; Eukaryota.
eggNOG; COG5126; LUCA.
GeneTree; ENSGT00760000118901; -.
HOGENOM; HOG000233018; -.
HOVERGEN; HBG012180; -.
InParanoid; Q9NZU7; -.
OrthoDB; EOG091G0PB4; -.
PhylomeDB; Q9NZU7; -.
TreeFam; TF334804; -.
ChiTaRS; CABP1; human.
EvolutionaryTrace; Q9NZU7; -.
GenomeRNAi; 9478; -.
PRO; PR:Q9NZU7; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000157782; -.
CleanEx; HS_CABP1; -.
ExpressionAtlas; Q9NZU7; baseline and differential.
Genevisible; Q9NZU7; HS.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
GO; GO:0004857; F:enzyme inhibitor activity; TAS:ProtInc.
GO; GO:0008139; F:nuclear localization sequence binding; ISS:UniProtKB.
GO; GO:0042308; P:negative regulation of protein import into nucleus; ISS:UniProtKB.
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; 2.
SMART; SM00054; EFh; 3.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 3.
PROSITE; PS50222; EF_HAND_2; 4.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell junction;
Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton;
Golgi apparatus; Lipoprotein; Magnesium; Membrane; Metal-binding;
Myristate; Phosphoprotein; Postsynaptic cell membrane;
Reference proteome; Repeat; Synapse.
INIT_MET 1 1 Removed. {ECO:0000255}.
CHAIN 2 370 Calcium-binding protein 1.
/FTId=PRO_0000073513.
DOMAIN 225 260 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 261 296 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 302 337 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 339 370 EF-hand 4. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 238 249 1.
CA_BIND 315 326 2.
CA_BIND 352 363 3.
COMPBIAS 45 48 Poly-Pro.
COMPBIAS 74 79 Poly-Ala.
COMPBIAS 86 164 Pro-rich.
METAL 238 238 Magnesium. {ECO:0000269|PubMed:19008222}.
METAL 240 240 Magnesium. {ECO:0000269|PubMed:19008222}.
METAL 242 242 Magnesium. {ECO:0000269|PubMed:19008222}.
METAL 244 244 Magnesium; via carbonyl oxygen.
{ECO:0000269|PubMed:19008222}.
METAL 315 315 Calcium 1. {ECO:0000269|PubMed:19008222}.
METAL 317 317 Calcium 1. {ECO:0000269|PubMed:19008222}.
METAL 319 319 Calcium 1. {ECO:0000269|PubMed:19008222}.
METAL 321 321 Calcium 1; via carbonyl oxygen.
{ECO:0000269|PubMed:19008222}.
METAL 326 326 Calcium 1. {ECO:0000269|PubMed:19008222}.
METAL 352 352 Calcium 2. {ECO:0000269|PubMed:19008222}.
METAL 353 353 Calcium 2; via amide nitrogen.
{ECO:0000269|PubMed:19008222}.
METAL 354 354 Calcium 2. {ECO:0000269|PubMed:19008222}.
METAL 356 356 Calcium 2. {ECO:0000269|PubMed:19008222}.
METAL 357 357 Calcium 2; via amide nitrogen.
{ECO:0000269|PubMed:19008222}.
METAL 358 358 Calcium 2; via carbonyl oxygen.
{ECO:0000269|PubMed:19008222}.
METAL 360 360 Calcium 2. {ECO:0000269|PubMed:19008222}.
METAL 363 363 Calcium 2. {ECO:0000269|PubMed:19008222}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000269|PubMed:14685260}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000255}.
VAR_SEQ 1 300 Missing (in isoform Calbrain).
{ECO:0000303|PubMed:9920909}.
/FTId=VSP_037936.
VAR_SEQ 1 203 Missing (in isoform S-CaBP1).
{ECO:0000303|PubMed:10625670}.
/FTId=VSP_037937.
VAR_SEQ 1 143 Missing (in isoform L-CaBP1).
{ECO:0000303|PubMed:10625670}.
/FTId=VSP_037938.
VAR_SEQ 144 218 RPREALPAAASRPSPSSPLPPARGRDGEERGLSPALGLRGS
LRARGRGDSVPAAASEADPFLHRLRPMLSSAFGQ -> MGN
CVKYPLRNLSRKMCQEEQTSYMVVQTSEEGLAADAELPGPL
LMLAQNCAVMHNLLGPACIFLRKGFAENRQP (in
isoform L-CaBP1).
{ECO:0000303|PubMed:10625670}.
/FTId=VSP_037939.
VAR_SEQ 204 218 FLHRLRPMLSSAFGQ -> MGNCVKYPLRNLSRK (in
isoform S-CaBP1).
{ECO:0000303|PubMed:10625670}.
/FTId=VSP_037940.
MUTAGEN 238 238 D->A: Loss of magnesium-binding. Loss of
binding to ITPRs; when associated with A-
240; A-315; A-317; A-352 and A-354.
{ECO:0000269|PubMed:12032348,
ECO:0000269|PubMed:19008222}.
MUTAGEN 240 240 D->A: Loss of magnesium-binding. Loss of
binding to ITPRs; when associated with A-
238; A-315; A-317; A-352 and A-354.
{ECO:0000269|PubMed:12032348,
ECO:0000269|PubMed:19008222}.
MUTAGEN 242 242 D->A: Loss of magnesium-binding.
{ECO:0000269|PubMed:19008222}.
MUTAGEN 249 249 D->A: No effect on magnesium-binding.
{ECO:0000269|PubMed:19008222}.
MUTAGEN 315 315 D->A: Loss of binding to ITPRs; when
associated with A-238; A-240; A-317; A-
352 and A-354.
{ECO:0000269|PubMed:12032348}.
MUTAGEN 317 317 N->A: Loss of binding to ITPRs; when
associated with A-238; A-240; A-315; A-
352 and A-354.
{ECO:0000269|PubMed:12032348}.
MUTAGEN 323 323 S->A: Loss of phosphorylation and loss of
calcium release by InsP(3).
{ECO:0000269|PubMed:14685260}.
MUTAGEN 352 352 D->A: Loss of binding to ITPRs; when
associated with A-238; A-240; A-315; A-
317 and A-354.
{ECO:0000269|PubMed:12032348}.
MUTAGEN 354 354 N->A: Loss of binding to ITPRs; when
associated with A-238; A-240; A-315; A-
317 and A-352.
{ECO:0000269|PubMed:12032348}.
CONFLICT 140 140 Q -> R (in Ref. 4; AAH30201).
{ECO:0000305}.
HELIX 224 240 {ECO:0000244|PDB:3OX6}.
STRAND 242 244 {ECO:0000244|PDB:3OX6}.
HELIX 247 256 {ECO:0000244|PDB:3OX6}.
HELIX 263 274 {ECO:0000244|PDB:3OX6}.
STRAND 277 279 {ECO:0000244|PDB:2K7B}.
HELIX 283 294 {ECO:0000244|PDB:3OX6}.
HELIX 299 302 {ECO:0000244|PDB:3OX6}.
HELIX 304 314 {ECO:0000244|PDB:3OX6}.
STRAND 319 322 {ECO:0000244|PDB:3OX6}.
HELIX 324 335 {ECO:0000244|PDB:3OX6}.
STRAND 337 339 {ECO:0000244|PDB:2K7C}.
HELIX 341 351 {ECO:0000244|PDB:3OX6}.
STRAND 353 359 {ECO:0000244|PDB:3OX6}.
HELIX 361 367 {ECO:0000244|PDB:3OX6}.
SEQUENCE 370 AA; 39838 MW; 3444721152E01AA7 CRC64;
MGGGDGAAFK RPGDGARLQR VLGLGSRREP RSLPAGGPAP RRTAPPPPGH ASAGPAAMSS
HIAKSESKTS LLKAAAAAAS GGSRAPRHGP ARDPGLPSRR LPGSCPATPQ SSGDPSSRRP
LCRPAPREEG ARGSQRVLPQ AHCRPREALP AAASRPSPSS PLPPARGRDG EERGLSPALG
LRGSLRARGR GDSVPAAASE ADPFLHRLRP MLSSAFGQDR SLRPEEIEEL REAFREFDKD
KDGYINCRDL GNCMRTMGYM PTEMELIELS QQINMNLGGH VDFDDFVELM GPKLLAETAD
MIGVKELRDA FREFDTNGDG EISTSELREA MRKLLGHQVG HRDIEEIIRD VDLNGDGRVD
FEEFVRMMSR


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