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Calcineurin-binding protein cabin-1 (Calcineurin inhibitor) (CAIN)

 CABIN_HUMAN             Reviewed;        2220 AA.
Q9Y6J0; G5E9F3; Q6PHY0; Q9Y460;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
20-JUN-2018, entry version 171.
RecName: Full=Calcineurin-binding protein cabin-1;
AltName: Full=Calcineurin inhibitor;
Short=CAIN;
Name=CABIN1; Synonyms=KIAA0330;
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 1), FUNCTION, INTERACTION WITH
CALCINEURIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
PHOSPHORYLATION.
TISSUE=Kidney;
PubMed=9655484; DOI=10.1016/S1074-7613(00)80575-0;
Sun L., Youn H.-D., Loh C., Stolow M., He W., Liu J.O.;
"Cabin 1, a negative regulator for calcineurin signaling in T
lymphocytes.";
Immunity 8:703-711(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
GLN-853.
TISSUE=Testis;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 319-2220 (ISOFORM 1).
TISSUE=Brain;
PubMed=9205841; DOI=10.1093/dnares/4.2.141;
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VII.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 4:141-150(1997).
[6]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A
COMPLEX WITH ASF1A; HIRA; HISTONE H3.3 AND UBN1.
PubMed=14718166; DOI=10.1016/S0092-8674(03)01064-X;
Tagami H., Ray-Gallet D., Almouzni G., Nakatani Y.;
"Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways
dependent or independent of DNA synthesis.";
Cell 116:51-61(2004).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2151 AND THR-2154, 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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66 AND SER-1439, 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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-11; THR-12;
SER-20; SER-66; SER-433; SER-450; SER-673; SER-1439; THR-1924 AND
SER-2094, 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).
[11]
PHOSPHORYLATION BY ATM AND CHK2, AND UBIQUITINATION.
PubMed=23303793; DOI=10.1093/nar/gks1319;
Choi S.Y., Jang H., Roe J.S., Kim S.T., Cho E.J., Youn H.D.;
"Phosphorylation and ubiquitination-dependent degradation of CABIN1
releases p53 for transactivation upon genotoxic stress.";
Nucleic Acids Res. 41:2180-2190(2013).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2156-2190 IN COMPLEX WITH
MEF2B AND DNA, AND MUTAGENESIS OF LEU-2172.
PubMed=12700764; DOI=10.1038/nature01555;
Han A., Pan F., Stroud J.C., Youn H.-D., Liu J.O., Chen L.;
"Sequence-specific recruitment of transcriptional co-repressor Cabin1
by myocyte enhancer factor-2.";
Nature 422:730-734(2003).
-!- FUNCTION: May be required for replication-independent chromatin
assembly. May serve as a negative regulator of T-cell receptor
(TCR) signaling via inhibition of calcineurin. Inhibition of
activated calcineurin is dependent on both PKC and calcium
signals. Acts as a negative regulator of p53/TP53 by keeping p53
in an inactive state on chromatin at promoters of a subset of it's
target genes. {ECO:0000269|PubMed:14718166,
ECO:0000269|PubMed:9655484}.
-!- SUBUNIT: Component of a complex that includes at least ASF1A,
CABIN1, HIRA, histone H3.3 and UBN1. Interacts with calcineurin.
Interacts with MEF2B. {ECO:0000269|PubMed:12700764,
ECO:0000269|PubMed:14718166, ECO:0000269|PubMed:9655484}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9655484}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Y6J0-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y6J0-2; Sequence=VSP_054161, VSP_054162;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed in different tissues.
{ECO:0000269|PubMed:9655484}.
-!- PTM: Activated through PKC-mediated hyperphosphorylation.
Phosphorylation by the DNA damage kinases ATM and CHK2 enhances
ubiquitination. {ECO:0000269|PubMed:23303793,
ECO:0000269|PubMed:9655484}.
-!- PTM: Upon genotoxic stress, ubiquitination by the DCX(DDB2) E3
ubiquitin-protein ligase complex targets CABIN1 for proteasomal
degradation, leading to the release of p53/TP53.
{ECO:0000269|PubMed:23303793}.
-!- SEQUENCE CAUTION:
Sequence=BAA20788.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF072441; AAD40846.1; -; mRNA.
EMBL; AP000351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP000352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP000353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471095; EAW59639.1; -; Genomic_DNA.
EMBL; BC054497; AAH54497.1; -; mRNA.
EMBL; Z92546; CAB62954.1; -; Genomic_DNA.
EMBL; AB002328; BAA20788.2; ALT_INIT; mRNA.
CCDS; CCDS13823.1; -. [Q9Y6J0-1]
RefSeq; NP_001186210.1; NM_001199281.1. [Q9Y6J0-1]
RefSeq; NP_001188358.1; NM_001201429.1.
RefSeq; NP_036427.1; NM_012295.3. [Q9Y6J0-1]
RefSeq; XP_016884172.1; XM_017028683.1. [Q9Y6J0-2]
UniGene; Hs.517478; -.
PDB; 1N6J; X-ray; 2.20 A; G=2156-2190.
PDBsum; 1N6J; -.
ProteinModelPortal; Q9Y6J0; -.
SMR; Q9Y6J0; -.
BioGrid; 117070; 29.
CORUM; Q9Y6J0; -.
IntAct; Q9Y6J0; 4.
MINT; Q9Y6J0; -.
STRING; 9606.ENSP00000263119; -.
iPTMnet; Q9Y6J0; -.
PhosphoSitePlus; Q9Y6J0; -.
BioMuta; CABIN1; -.
DMDM; 6685261; -.
EPD; Q9Y6J0; -.
PaxDb; Q9Y6J0; -.
PeptideAtlas; Q9Y6J0; -.
PRIDE; Q9Y6J0; -.
ProteomicsDB; 86699; -.
Ensembl; ENST00000263119; ENSP00000263119; ENSG00000099991. [Q9Y6J0-1]
Ensembl; ENST00000398319; ENSP00000381364; ENSG00000099991. [Q9Y6J0-1]
Ensembl; ENST00000405822; ENSP00000384694; ENSG00000099991. [Q9Y6J0-2]
GeneID; 23523; -.
KEGG; hsa:23523; -.
UCSC; uc002zzi.1; human. [Q9Y6J0-1]
CTD; 23523; -.
DisGeNET; 23523; -.
EuPathDB; HostDB:ENSG00000099991.16; -.
GeneCards; CABIN1; -.
HGNC; HGNC:24187; CABIN1.
HPA; HPA043296; -.
MIM; 604251; gene.
neXtProt; NX_Q9Y6J0; -.
OpenTargets; ENSG00000099991; -.
PharmGKB; PA164717549; -.
eggNOG; ENOG410IFFG; Eukaryota.
eggNOG; ENOG410XY91; LUCA.
GeneTree; ENSGT00390000008529; -.
HOGENOM; HOG000111281; -.
HOVERGEN; HBG050758; -.
InParanoid; Q9Y6J0; -.
KO; K17613; -.
OMA; AEPTCSQ; -.
OrthoDB; EOG091G008Y; -.
PhylomeDB; Q9Y6J0; -.
TreeFam; TF323227; -.
Reactome; R-HSA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
SIGNOR; Q9Y6J0; -.
ChiTaRS; CABIN1; human.
EvolutionaryTrace; Q9Y6J0; -.
GeneWiki; CABIN1; -.
GenomeRNAi; 23523; -.
PRO; PR:Q9Y6J0; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000099991; -.
CleanEx; HS_CABIN1; -.
ExpressionAtlas; Q9Y6J0; baseline and differential.
Genevisible; Q9Y6J0; HS.
GO; GO:0016235; C:aggresome; IDA:HPA.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0004864; F:protein phosphatase inhibitor activity; NAS:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; NAS:UniProtKB.
GO; GO:0006336; P:DNA replication-independent nucleosome assembly; IDA:UniProtKB.
CDD; cd13839; MEF2_binding; 1.
Gene3D; 1.25.40.10; -; 2.
InterPro; IPR033053; Hir3/CABIN1.
InterPro; IPR015134; MEF2-bd.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
PANTHER; PTHR15502; PTHR15502; 1.
Pfam; PF09047; MEF2_binding; 1.
SMART; SM00028; TPR; 5.
SUPFAM; SSF48452; SSF48452; 3.
PROSITE; PS50005; TPR; 4.
PROSITE; PS50293; TPR_REGION; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator;
Complete proteome; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; TPR repeat; Ubl conjugation.
CHAIN 1 2220 Calcineurin-binding protein cabin-1.
/FTId=PRO_0000106275.
REPEAT 36 69 TPR 1.
REPEAT 90 123 TPR 2.
REPEAT 125 157 TPR 3.
REPEAT 615 648 TPR 4.
REPEAT 1055 1088 TPR 5.
REPEAT 1106 1139 TPR 6.
REGION 2116 2153 Required for interaction with
calcineurin. {ECO:0000250}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 12 12 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 66 66 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 433 433 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 450 450 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 673 673 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1439 1439 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1924 1924 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2094 2094 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2151 2151 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 2154 2154 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
VAR_SEQ 220 269 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054161.
VAR_SEQ 1344 1372 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054162.
VARIANT 56 56 A -> T (in dbSNP:rs5760185).
/FTId=VAR_052607.
VARIANT 225 225 D -> N (in dbSNP:rs17004823).
/FTId=VAR_052608.
VARIANT 517 517 S -> R (in dbSNP:rs9624393).
/FTId=VAR_052609.
VARIANT 660 660 R -> S (in dbSNP:rs9624395).
/FTId=VAR_052610.
VARIANT 853 853 R -> Q (in dbSNP:rs17854874).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_052611.
VARIANT 921 921 Q -> E (in dbSNP:rs12166151).
/FTId=VAR_052612.
MUTAGEN 2172 2172 L->A,K,W: Abrogates binding to MEF2B.
{ECO:0000269|PubMed:12700764}.
HELIX 2166 2177 {ECO:0000244|PDB:1N6J}.
SEQUENCE 2220 AA; 246352 MW; BA4AD1741056C233 CRC64;
MIRIAALNAS STIEDDHEGS FKSHKTQTKE AQEAEAFALY HKALDLQKHD RFEESAKAYH
ELLEASLLRE AVSSGDEKEG LKHPGLILKY STYKNLAQLA AQREDLETAM EFYLEAVMLD
STDVNLWYKI GHVALRLIRI PLARHAFEEG LRCNPDHWPC LDNLITVLYT LSDYTTCLYF
ICKALEKDCR YSKGLVLKEK IFEEQPCLRK DSLRMFLKCD MSIHDVSVSA AETQAIVDEA
LGLRKKRQAL IVREKEPDLK LVQPIPFFTW KCLGESLLAM YNHLTTCEPP RPSLGKRIDL
SDYQDPSQPL ESSMVVTPVN VIQPSTVSTN PAVAVAEPVV SYTSVATTSF PLHSPGLLET
GAPVGDISGG DKSKKGVKRK KISEESGETA KRRSARVRNT KCKKEEKVDF QELLMKFLPS
RLRKLDPEEE DDSFNNYEVQ SEAKLESFPS IGPQRLSFDS ATFMESEKQD VHEFLLENLT
NGGILELMMR YLKAMGHKFL VRWPPGLAEV VLSVYHSWRR HSTSLPNPLL RDCSNKHIKD
MMLMSLSCME LQLDQWLLTK GRSSAVSPRN CPAGMVNGRF GPDFPGTHCL GDLLQLSFAS
SQRDLFEDGW LEFVVRVYWL KARFLALQGD MEQALENYDI CTEMLQSSTA IQVEAGAERR
DIVIRLPNLH NDSVVSLEEI DKNLKSLERC QSLEEIQRLY EAGDYKAVVH LLRPTLCTSG
FDRAKHLEFM TSIPERPAQL LLLQDSLLRL KDYRQCFECS DVALNEAVQQ MVNSGEAAAK
EEWVATVTQL LMGIEQALSA DSSGSILKVS SSTTGLVRLT NNLIQVIDCS MAVQEEAKEP
HVSSVLPWII LHRIIWQEED TFHSLCHQQQ LQNPAEEGMS ETPMLPSSLM LLNTAHEYLG
RRSWCCNSDG ALLRFYVRVL QKELAASTSE DTHPYKEELE TALEQCFYCL YSFPSKKSKA
RYLEEHSAQQ VDLIWEDALF MFEYFKPKTL PEFDSYKTST VSADLANLLK RIATIVPRTE
RPALSLDKVS AYIEGTSTEV PCLPEGADPS PPVVNELYYL LADYHFKNKE QSKAIKFYMH
DICICPNRFD SWAGMALARA SRIQDKLNSN ELKSDGPIWK HATPVLNCFR RALEIDSSNL
SLWIEYGTMS YALHSFASRQ LKQWRGELPP ELVQQMEGRR DSMLETAKHC FTSAARCEGD
GDEEEWLIHY MLGKVAEKQQ QPPTVYLLHY RQAGHYLHEE AARYPKKIHY HNPPELAMEA
LEVYFRLHAS ILKLLGKPDS GVGAEVLVNF MKEAAEGPFA RGEEKNTPKA SEKEKACLVD
EDSHSSAGTL PGPGASLPSS SGPGLTSPPY TATPIDHDYV KCKKPHQQAT PDDRSQDSTA
VALSDSSSTQ DFFNEPTSLL EGSRKSYTEK RLPILSSQAG ATGKDLQGAT EERGKNEESL
ESTEGFRAAE QGVQKPAAET PASACIPGKP SASTPTLWDG KKRGDLPGEP VAFPQGLPAG
AEEQRQFLTE QCIASFRLCL SRFPQHYKSL YRLAFLYTYS KTHRNLQWAR DVLLGSSIPW
QQLQHMPAQG LFCERNKTNF FNGIWRIPVD EIDRPGSFAW HMNRSIVLLL KVLAQLRDHS
TLLKVSSMLQ RTPDQGKKYL RDADRQVLAQ RAFILTVKVL EDTLSELAEG SERPGPKVCG
LPGARMTTDV SHKASPEDGQ EGLPQPKKPP LADGSGPGPE PGGKVGLLNH RPVAMDAGDS
ADQSGERKDK ESPRAGPTEP MDTSEATVCH SDLERTPPLL PGRPARDRGP ESRPTELSLE
ELSISARQQP TPLTPAQPAP APAPATTTGT RAGGHPEEPL SRLSRKRKLL EDTESGKTLL
LDAYRVWQQG QKGVAYDLGR VERIMSETYM LIKQVDEEAA LEQAVKFCQV HLGAAAQRQA
SGDTPTTPKH PKDSRENFFP VTVVPTAPDP VPADSVQRPS DAHTKPRPAL AAATTIITCP
PSASASTLDQ SKDPGPPRPH RPEATPSMAS LGPEGEELAR VAEGTSFPPQ EPRHSPQVKM
APTSSPAEPH CWPAEAALGT GAEPTCSQEG KLRPEPRRDG EAQEAASETQ PLSSPPTAAS
SKAPSSGSAQ PPEGHPGKPE PSRAKSRPLP NMPKLVIPSA ATKFPPEITV TPPTPTLLSP
KGSISEETKQ KLKSAILSAQ SAANVRKESL CQPALEVLET SSQESSLESE TDEDDDYMDI


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Catalog number Product name Quantity
EIAAB04979 Cabin1,CAIN,Calcineurin inhibitor,Calcineurin-binding protein cabin-1,Rat,Rattus norvegicus
EIAAB04978 CABIN1,CAIN,Calcineurin inhibitor,Calcineurin-binding protein cabin-1,Homo sapiens,Human,KIAA0330
CSB-EL004384RA Rat Calcineurin-binding protein cabin-1(CABIN1) ELISA kit 96T
CSB-EL004384HU Human Calcineurin-binding protein cabin-1(CABIN1) ELISA kit 96T
CSB-EL004384RA Rat Calcineurin-binding protein cabin-1(CABIN1) ELISA kit SpeciesRat 96T
CSB-EL004384HU Human Calcineurin-binding protein cabin-1(CABIN1) ELISA kit SpeciesHuman 96T
CABIN_HUMAN ELISA Kit FOR Calcineurin-binding protein cabin-1; organism: Human; gene name: CABIN1 96T
EIAAB07238 Calcineurin B homolog,Calcineurin homologous protein,Calcium-binding protein CHP,Calcium-binding protein p22,CHP,Homo sapiens,Human
EIAAB07235 Bos taurus,Bovine,Calcineurin B homolog,Calcineurin homologous protein,Calcium-binding protein CHP,Calcium-binding protein p22,CHP
EIAAB05266 Calcineurin BII,Calcineurin B-like protein,Calcineurin subunit B type 2,CBLP,CBLP,CNBII,Homo sapiens,Human,PPP3R1-like,PPP3R2,PPP3RL,Protein phosphatase 2B regulatory subunit 2,Protein phosphatase 3 r
25-642 RCAN3 inhibits calcineurin-dependent transcriptional responses by binding to the catalytic domain of calcineurin A. It could play a role during central nervous system development. 0.05 mg
EIAAB34092 Calcineurin inhibitory protein ZAKI-4,Calcipressin-2,Down syndrome candidate region 1-like protein 1,Dscr1l1,Rat,Rattus norvegicus,Rcan2,Regulator of calcineurin 2,Zaki4
18-272-195665 Calcineurin A - Rabbit polyclonal to Calcineurin A; EC 3.1.3.16; Calmodulin-dependent calcineurin A subunit alpha isoform; CAM-PRP catalytic subunit Polyclonal 0.05 mg
EIAAB34094 Calcipressin-3,Down syndrome candidate region 1-like protein 2,Dscr1l2,MCIP3,Mouse,Mus musculus,Myocyte-enriched calcineurin-interacting protein 3,Rcan3,Regulator of calcineurin 3
EIAAB34090 Calcineurin inhibitory protein ZAKI-4,Calcipressin-2,Down syndrome candidate region 1-like protein 1,Dscr1l1,MCIP2,Mouse,Mus musculus,Myocyte-enriched calcineurin-interacting protein 2,Rcan2,Regulator
EIAAB34095 Calcipressin-3,Down syndrome candidate region 1-like protein 2,DSCR1L2,Homo sapiens,Human,MCIP3,Myocyte-enriched calcineurin-interacting protein 3,RCAN3,Regulator of calcineurin 3
EIAAB34086 Calcipressin-1,Down syndrome critical region protein 1 homolog,Dscr1,MCIP1,Mouse,Mus musculus,Myocyte-enriched calcineurin-interacting protein 1,Rcan1,Regulator of calcineurin 1
EIAAB34085 Calcipressin-1,Down syndrome critical region protein 1 homolog,Dscr1,MCIP1,Myocyte-enriched calcineurin-interacting protein 1,Rat,Rattus norvegicus,Rcan1,Regulator of calcineurin 1
EIAAB34089 Calcipressin-2,Down syndrome candidate region 1-like 1,DSCR1L1,Homo sapiens,Human,MCIP2,Myocyte-enriched calcineurin-interacting protein 2,RCAN2,Regulator of calcineurin 2,Thyroid hormone-responsive p
EIAAB34088 Adapt78,ADAPT78,Calcipressin-1,CSP1,Down syndrome critical region protein 1,DSC1,DSCR1,Homo sapiens,Human,MCIP1,Myocyte-enriched calcineurin-interacting protein 1,RCAN1,Regulator of calcineurin 1
148067-21-4 Calcineurin Autoinhibitory Peptide Calcineurin Autoinhibito 1g
3075BP-50 Calcineurin A Blocking Peptide target: Calcineurin A 50 μg
25-434 RCAN1 interacts with calcineurin A and inhibits calcineurin-dependent signaling pathways, possibly affecting central nervous system development. This gene is located in the minimal candidate region fo 0.05 mg
MA1008 Monoclonal Anti-Calcineurin alpha, Clone number: CC-6, Ig type: mouse IgG1, Immunogen: Bovine brain calcineurin., Specificity: Human;rat. No cross reactivity with other proteins. 100μg/vial
EIAAB31927 Calcineurin, testis-specific catalytic subunit,Calmodulin-dependent calcineurin A subunit gamma isoform,Calnc,CAM-PRP catalytic subunit,Mouse,Mus musculus,Ppp3cc,Serine_threonine-protein phosphatase 2


 

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