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Coronin-1A (Coronin-like protein A) (Clipin-A) (Coronin-like protein p57) (Tryptophan aspartate-containing coat protein) (TACO)

 COR1A_HUMAN             Reviewed;         461 AA.
P31146; B2RBL1; Q2YD73;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
22-NOV-2017, entry version 175.
RecName: Full=Coronin-1A;
AltName: Full=Coronin-like protein A;
Short=Clipin-A;
AltName: Full=Coronin-like protein p57;
AltName: Full=Tryptophan aspartate-containing coat protein;
Short=TACO;
Name=CORO1A; Synonyms=CORO1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Peripheral blood leukocyte;
PubMed=7758584; DOI=10.1016/0014-5793(95)00393-N;
Suzuki K., Nishihata J., Arai Y., Honma N., Yamamoto K., Irimura T.,
Toyoshima S.;
"Molecular cloning of a novel actin-binding protein, p57, with a WD
repeat and a leucine zipper motif.";
FEBS Lett. 364:283-288(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Grogan A., Keep N.H., Reeves E., Segal A.W.;
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
Liau G., Popa I., Argraves K., Argraves W.S.;
Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Kohchi C., Inagawa H., Makino K., Terada H., Soma G.;
"A new therapeutic strategy of mycobacterium infection by use of anti-
TACO sequence.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thymus;
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]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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]
PROTEIN SEQUENCE OF 2-9; 50-65; 242-252; 433-448 AND 453-460, CLEAVAGE
OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=T-cell;
Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
Submitted (MAY-2006) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 355-374.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[10]
ROLE IN PHAGOSOME TRAFFICKING.
PubMed=10338208; DOI=10.1016/S0092-8674(00)80754-0;
Ferrari G., Langen H., Naito M., Pieters J.;
"A coat protein on phagosomes involved in the intracellular survival
of mycobacteria.";
Cell 97:435-447(1999).
[11]
INVOLVEMENT IN IMD8.
PubMed=19097825; DOI=10.1016/j.clim.2008.11.002;
Shiow L.R., Paris K., Akana M.C., Cyster J.G., Sorensen R.U.,
Puck J.M.;
"Severe combined immunodeficiency (SCID) and attention deficit
hyperactivity disorder (ADHD) associated with a Coronin-1A mutation
and a chromosome 16p11.2 deletion.";
Clin. Immunol. 131:24-30(2009).
[12]
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).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-449, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[14]
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).
[15]
UBIQUITINATION BY RNF128.
PubMed=22016387; DOI=10.1074/jbc.M111.222711;
Ichikawa D., Mizuno M., Yamamura T., Miyake S.;
"GRAIL (gene related to anergy in lymphocytes) regulates cytoskeletal
reorganization through ubiquitination and degradation of Arp2/3
subunit 5 and coronin 1A.";
J. Biol. Chem. 286:43465-43474(2011).
[16]
PHOSPHORYLATION AT SER-2 AND THR-412, AND INTERACTION WITH ACTIN.
PubMed=23100250; DOI=10.1074/jbc.M112.349829;
Oku T., Nakano M., Kaneko Y., Ando Y., Kenmotsu H., Itoh S.,
Tsuiji M., Seyama Y., Toyoshima S., Tsuji T.;
"Constitutive turnover of phosphorylation at Thr-412 of human
p57/coronin-1 regulates the interaction with actin.";
J. Biol. Chem. 287:42910-42920(2012).
[17]
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).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[19]
VARIANT IMD8 MET-134, AND CHARACTERIZATION OF VARIANT IMD8 MET-134.
PubMed=23522482; DOI=10.1016/j.jaci.2013.01.042;
Moshous D., Martin E., Carpentier W., Lim A., Callebaut I.,
Canioni D., Hauck F., Majewski J., Schwartzentruber J., Nitschke P.,
Sirvent N., Frange P., Picard C., Blanche S., Revy P., Fischer A.,
Latour S., Jabado N., de Villartay J.P.;
"Whole-exome sequencing identifies Coronin-1A deficiency in 3 siblings
with immunodeficiency and EBV-associated B-cell lymphoproliferation.";
J. Allergy Clin. Immunol. 131:1594-1603(2013).
-!- FUNCTION: May be a crucial component of the cytoskeleton of highly
motile cells, functioning both in the invagination of large pieces
of plasma membrane, as well as in forming protrusions of the
plasma membrane involved in cell locomotion. In mycobacteria-
infected cells, its retention on the phagosomal membrane prevents
fusion between phagosomes and lysosomes.
{ECO:0000269|PubMed:10338208}.
-!- SUBUNIT: Binds actin.
-!- INTERACTION:
A1L4K1:FSD2; NbExp=5; IntAct=EBI-1046676, EBI-5661036;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-1046676, EBI-618309;
P43364:MAGEA11; NbExp=4; IntAct=EBI-1046676, EBI-739552;
P40763:STAT3; NbExp=2; IntAct=EBI-1046676, EBI-518675;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
Cytoplasm, cell cortex {ECO:0000250}. Cytoplasmic vesicle,
phagosome membrane {ECO:0000250}. Note=In non-infected
macrophages, associated with the cortical microtubule network. In
mycobacteria-infected macrophages, becomes progressively
relocalized and retained around the mycobacterial phagosomes.
Retention on the phagosomal membrane is strictly dependent on
mycobacterial viability and not due to impaired acidification (By
similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in brain, thymus, spleen, bone
marrow and lymph node. Low in lung and gut.
-!- PTM: phosphorylation at Thr-412 by PKC strongly down-regulates the
association with actin. {ECO:0000269|PubMed:23100250}.
-!- PTM: Polyubiquitinated by RNF128 with 'Lys-48'-linked chains,
leading to proteasomal degradation. {ECO:0000269|PubMed:22016387}.
-!- DISEASE: Immunodeficiency 8 (IMD8) [MIM:615401]: A disease of the
immune system leading to recurrent infections, and characterized
by CD4+ T-cells lymphopenia. Patients can develop B-cell
lymphoproliferation associated with Epstein-Barr virus infection.
{ECO:0000269|PubMed:19097825, ECO:0000269|PubMed:23522482}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the WD repeat coronin family.
{ECO:0000305}.
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EMBL; D44497; BAA07940.1; -; mRNA.
EMBL; X89109; CAA61482.1; -; mRNA.
EMBL; U34690; AAA77058.1; -; mRNA.
EMBL; AF495470; AAM18516.1; -; mRNA.
EMBL; AK314714; BAG37258.1; -; mRNA.
EMBL; CH471238; EAW79906.1; -; Genomic_DNA.
EMBL; BC110374; AAI10375.1; -; mRNA.
EMBL; BC126385; AAI26386.1; -; mRNA.
EMBL; BC126387; AAI26388.1; -; mRNA.
CCDS; CCDS10673.1; -.
PIR; S65665; S65665.
RefSeq; NP_001180262.1; NM_001193333.2.
RefSeq; NP_009005.1; NM_007074.3.
RefSeq; XP_011544016.1; XM_011545714.2.
UniGene; Hs.415067; -.
ProteinModelPortal; P31146; -.
SMR; P31146; -.
BioGrid; 116322; 57.
IntAct; P31146; 24.
MINT; MINT-263387; -.
STRING; 9606.ENSP00000219150; -.
iPTMnet; P31146; -.
PhosphoSitePlus; P31146; -.
SwissPalm; P31146; -.
BioMuta; CORO1A; -.
DMDM; 1706004; -.
OGP; P31146; -.
UCD-2DPAGE; P31146; -.
EPD; P31146; -.
MaxQB; P31146; -.
PaxDb; P31146; -.
PeptideAtlas; P31146; -.
PRIDE; P31146; -.
TopDownProteomics; P31146; -.
DNASU; 11151; -.
Ensembl; ENST00000219150; ENSP00000219150; ENSG00000102879.
Ensembl; ENST00000570045; ENSP00000455552; ENSG00000102879.
GeneID; 11151; -.
KEGG; hsa:11151; -.
UCSC; uc002dww.4; human.
CTD; 11151; -.
DisGeNET; 11151; -.
EuPathDB; HostDB:ENSG00000102879.15; -.
GeneCards; CORO1A; -.
HGNC; HGNC:2252; CORO1A.
HPA; CAB046473; -.
HPA; HPA051132; -.
MalaCards; CORO1A; -.
MIM; 605000; gene.
MIM; 615401; phenotype.
neXtProt; NX_P31146; -.
OpenTargets; ENSG00000102879; -.
Orphanet; 228003; Severe combined immunodeficiency due to CORO1A deficiency.
PharmGKB; PA26768; -.
eggNOG; KOG0303; Eukaryota.
eggNOG; ENOG410XQAD; LUCA.
GeneTree; ENSGT00760000119195; -.
HOGENOM; HOG000166356; -.
HOVERGEN; HBG059978; -.
InParanoid; P31146; -.
KO; K13882; -.
OMA; CYDDIRI; -.
OrthoDB; EOG091G03H5; -.
PhylomeDB; P31146; -.
TreeFam; TF314280; -.
SignaLink; P31146; -.
SIGNOR; P31146; -.
GeneWiki; CORO1A; -.
GenomeRNAi; 11151; -.
PRO; PR:P31146; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000102879; -.
CleanEx; HS_CORO1A; -.
ExpressionAtlas; P31146; baseline and differential.
Genevisible; P31146; HS.
GO; GO:0005884; C:actin filament; IDA:UniProtKB.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0030864; C:cortical actin cytoskeleton; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0005769; C:early endosome; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0001772; C:immunological synapse; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0001891; C:phagocytic cup; IDA:UniProtKB.
GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0003779; F:actin binding; IPI:UniProtKB.
GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
GO; GO:0003785; F:actin monomer binding; IMP:UniProtKB.
GO; GO:0008092; F:cytoskeletal protein binding; ISS:UniProtKB.
GO; GO:0032036; F:myosin heavy chain binding; IPI:UniProtKB.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IDA:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0030036; P:actin cytoskeleton organization; IMP:UniProtKB.
GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
GO; GO:0006816; P:calcium ion transport; IEA:Ensembl.
GO; GO:0031589; P:cell-substrate adhesion; IMP:UniProtKB.
GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
GO; GO:0061502; P:early endosome to recycling endosome transport; IEA:Ensembl.
GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
GO; GO:0045087; P:innate immune response; NAS:UniProtKB.
GO; GO:0030595; P:leukocyte chemotaxis; IEA:Ensembl.
GO; GO:0006928; P:movement of cell or subcellular component; NAS:UniProtKB.
GO; GO:0043320; P:natural killer cell degranulation; IMP:UniProtKB.
GO; GO:0051126; P:negative regulation of actin nucleation; IDA:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0031339; P:negative regulation of vesicle fusion; IEA:Ensembl.
GO; GO:0038180; P:nerve growth factor signaling pathway; IEA:Ensembl.
GO; GO:0006909; P:phagocytosis; IMP:UniProtKB.
GO; GO:0001845; P:phagolysosome assembly; IMP:UniProtKB.
GO; GO:0050918; P:positive chemotaxis; IDA:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
GO; GO:0032796; P:uropod organization; IEA:Ensembl.
Gene3D; 2.120.10.30; -; 1.
Gene3D; 2.130.10.10; -; 2.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR029508; CORO1A.
InterPro; IPR015505; Coronin.
InterPro; IPR015048; DUF1899.
InterPro; IPR015049; Trimer_CC.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR10856; PTHR10856; 1.
PANTHER; PTHR10856:SF18; PTHR10856:SF18; 1.
Pfam; PF08953; DUF1899; 1.
Pfam; PF08954; Trimer_CC; 1.
Pfam; PF00400; WD40; 3.
SMART; SM01166; DUF1899; 1.
SMART; SM00320; WD40; 3.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 2.
PROSITE; PS50082; WD_REPEATS_2; 2.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Acetylation; Actin-binding; Coiled coil; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Cytoskeleton; Direct protein sequencing;
Disease mutation; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Ubl conjugation; WD repeat.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.8}.
CHAIN 2 461 Coronin-1A.
/FTId=PRO_0000050920.
REPEAT 13 63 WD 1.
REPEAT 73 110 WD 2.
REPEAT 123 160 WD 3.
REPEAT 164 204 WD 4.
REPEAT 207 251 WD 5.
REPEAT 258 296 WD 6.
REPEAT 302 349 WD 7.
COILED 424 460 {ECO:0000255}.
MOD_RES 2 2 N-acetylserine. {ECO:0000269|Ref.8}.
MOD_RES 2 2 Phosphoserine; by PKC.
{ECO:0000269|PubMed:23100250}.
MOD_RES 412 412 Phosphothreonine; by PKC.
{ECO:0000269|PubMed:23100250}.
MOD_RES 422 422 Phosphoserine.
{ECO:0000250|UniProtKB:O89053}.
MOD_RES 449 449 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VARIANT 134 134 V -> M (in IMD8; the mutation causes a
decrease in protein stability; patient T-
cell blasts show delayed activation of
signaling molecules MAPK3 and MAPK1;
dbSNP:rs397514755).
{ECO:0000269|PubMed:23522482}.
/FTId=VAR_070447.
VARIANT 415 415 R -> K (in dbSNP:rs1804109).
/FTId=VAR_011956.
CONFLICT 8 8 S -> T (in Ref. 3; AAA77058).
{ECO:0000305}.
CONFLICT 245 245 R -> W (in Ref. 3; AAA77058).
{ECO:0000305}.
SEQUENCE 461 AA; 51026 MW; DE3FEDA57041515E CRC64;
MSRQVVRSSK FRHVFGQPAK ADQCYEDVRV SQTTWDSGFC AVNPKFVALI CEASGGGAFL
VLPLGKTGRV DKNAPTVCGH TAPVLDIAWC PHNDNVIASG SEDCTVMVWE IPDGGLMLPL
REPVVTLEGH TKRVGIVAWH TTAQNVLLSA GCDNVIMVWD VGTGAAMLTL GPEVHPDTIY
SVDWSRDGGL ICTSCRDKRV RIIEPRKGTV VAEKDRPHEG TRPVRAVFVS EGKILTTGFS
RMSERQVALW DTKHLEEPLS LQELDTSSGV LLPFFDPDTN IVYLCGKGDS SIRYFEITSE
APFLHYLSMF SSKESQRGMG YMPKRGLEVN KCEIARFYKL HERRCEPIAM TVPRKSDLFQ
EDLYPPTAGP DPALTAEEWL GGRDAGPLLI SLKDGYVPPK SRELRVNRGL DTGRRRAAPE
ASGTPSSDAV SRLEEEMRKL QATVQELQKR LDRLEETVQA K


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E0023h ELISA kit Clipin-A,CORO1,CORO1A,Coronin-1A,Coronin-like protein A,Coronin-like protein p57,Homo sapiens,Human,TACO,Tryptophan aspartate-containing coat protein 96T
U0023h CLIA Clipin-A,CORO1,CORO1A,Coronin-1A,Coronin-like protein A,Coronin-like protein p57,Homo sapiens,Human,TACO,Tryptophan aspartate-containing coat protein 96T
U0023b CLIA Bos taurus,Bovine,Clipin-A,CORO1,CORO1A,Coronin-1A,Coronin-like protein A,Coronin-like protein p57,TACO,Tryptophan aspartate-containing coat protein 96T
E0023b ELISA Bos taurus,Bovine,Clipin-A,CORO1,CORO1A,Coronin-1A,Coronin-like protein A,Coronin-like protein p57,TACO,Tryptophan aspartate-containing coat protein 96T
E0023m ELISA kit Clipin-A,Coro1,Coro1a,Coronin-1A,Coronin-like protein A,Coronin-like protein p57,Mouse,Mus musculus,TACO,Tryptophan aspartate-containing coat protein 96T
U0023m CLIA Clipin-A,Coro1,Coro1a,Coronin-1A,Coronin-like protein A,Coronin-like protein p57,Mouse,Mus musculus,TACO,Tryptophan aspartate-containing coat protein 96T
E0023b ELISA kit Bos taurus,Bovine,Clipin-A,CORO1,CORO1A,Coronin-1A,Coronin-like protein A,Coronin-like protein p57,TACO,Tryptophan aspartate-containing coat protein 96T
E0023m ELISA Clipin-A,Coro1,Coro1a,Coronin-1A,Coronin-like protein A,Coronin-like protein p57,Mouse,Mus musculus,TACO,Tryptophan aspartate-containing coat protein 96T
18-003-43872 Coronin-1A - Coronin-like protein p57; Coronin-like protein A; Clipin-A; Tryptophan aspartate-containing coat protein; TACO Polyclonal 0.1 mg Protein A
E0023r ELISA kit Clipin-A,Coro1,Coro1a,Coronin-1A,Coronin-like protein A,Rat,Rattus norvegicus,TACO,Tryptophan aspartate-containing coat protein 96T
U0023r CLIA Clipin-A,Coro1,Coro1a,Coronin-1A,Coronin-like protein A,Rat,Rattus norvegicus,TACO,Tryptophan aspartate-containing coat protein 96T
E0023r ELISA Clipin-A,Coro1,Coro1a,Coronin-1A,Coronin-like protein A,Rat,Rattus norvegicus,TACO,Tryptophan aspartate-containing coat protein 96T
EIAAB08668 Clipin-C,CORO2B,Coronin-2B,Coronin-like protein C,Homo sapiens,Human,KIAA0925,Protein FC96
EIAAB08677 Clipin-E,Coro6,Coronin-6,Coronin-like protein E,Mouse,Mus musculus
EIAAB08676 Clipin-E,CORO6,Coronin-6,Coronin-like protein E,Homo sapiens,Human,PP1009,PP1782,PP1881
EIAAB08660 CORO1B,Coronin-1B,Coronin-like protein pp66,Coroninse,Oryctolagus cuniculus,Rabbit
EIAAB08663 CORO1C,Coronin-1C,Coronin-3,CRNN4,hCRNN4,Homo sapiens,Human
ER-14-0362 Goat Anti-Coronin 3 _ coronin 1C, with HRP-conjugated secondary antibody 100
ER-14-0362 Goat Anti-Human Coronin 3 _ coronin 1C, (C Terminus) Antibodies 100 μg
EIAAB08662 CORO1B,Coronin-1B,Coronin-2,Homo sapiens,Human
CA17468-100 Antibodies: Coronin 3 _ coronin 1C HOST: Goat Clonality: pAb 100
EIAAB08661 Coro1b,Coronin-1B,Coronin-2,Rat,Rattus norvegicus
EIAAB08664 Coro1c,Coronin-1C,Coronin-3,Mouse,Mus musculus
EIAAB08659 Coro1b,Coronin-1B,Coronin-2,Mouse,Mus musculus


 

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