Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

CD2 antigen cytoplasmic tail-binding protein 2 (CD2 cytoplasmic domain-binding protein 2) (CD2 tail-binding protein 2) (U5 snRNP 52K protein) (U5-52K)

 CD2B2_HUMAN             Reviewed;         341 AA.
O95400; B2RDX2; Q9ULP2;
30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
25-OCT-2017, entry version 153.
RecName: Full=CD2 antigen cytoplasmic tail-binding protein 2;
Short=CD2 cytoplasmic domain-binding protein 2;
Short=CD2 tail-binding protein 2;
AltName: Full=U5 snRNP 52K protein;
Short=U5-52K;
Name=CD2BP2; Synonyms=KIAA1178;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CD2.
PubMed=9843987; DOI=10.1073/pnas.95.25.14897;
Nishizawa K., Freund C., Li J., Wagner G., Reinherz E.L.;
"Identification of a proline-binding motif regulating CD2-triggered T
lymphocyte activation.";
Proc. Natl. Acad. Sci. U.S.A. 95:14897-14902(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
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).
[3]
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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 218-341.
TISSUE=Brain;
PubMed=10574461; DOI=10.1093/dnares/6.5.329;
Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
"Characterization of cDNA clones selected by the GeneMark analysis
from size-fractionated cDNA libraries from human brain.";
DNA Res. 6:329-336(1999).
[6]
FUNCTION, SUBUNIT, INTERACTION WITH PRPF6 AND TXNL4A, AND SUBCELLULAR
LOCATION.
PubMed=15840814; DOI=10.1261/rna.2300805;
Laggerbauer B., Liu S., Makarov E., Vornlocher H.P., Makarova O.,
Ingelfinger D., Achsel T., Luhrmann R.;
"The human U5 snRNP 52K protein (CD2BP2) interacts with U5-102K
(hPrp6), a U4/U6.U5 tri-snRNP bridging protein, but dissociates upon
tri-snRNP formation.";
RNA 11:598-608(2005).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
SUBUNIT.
PubMed=16723661; DOI=10.1261/rna.55406;
Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.;
"The network of protein-protein interactions within the human U4/U6.U5
tri-snRNP.";
RNA 12:1418-1430(2006).
[9]
SUBCELLULAR LOCATION.
PubMed=17906334; DOI=10.1093/intimm/dxm100;
Heinze M., Kofler M., Freund C.;
"Investigating the functional role of CD2BP2 in T cells.";
Int. Immunol. 19:1313-1318(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
network: indicating the involvement of ribonucleoside-diphosphate
reductase M2 subunit phosphorylation at residue serine 20 in canonical
Wnt signal transduction.";
Mol. Cell. Proteomics 6:1952-1967(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[12]
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-118; SER-194 AND
SER-195, 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).
[15]
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, 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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND SER-195, 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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-49, AND
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).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-26, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[20]
STRUCTURE BY NMR OF 280-341.
PubMed=10404223; DOI=10.1038/10712;
Freund C., Dotsch V., Nishizawa K., Reinherz E.L., Wagner G.;
"The GYF domain is a novel structural fold that is involved in
lymphoid signaling through proline-rich sequences.";
Nat. Struct. Biol. 6:656-660(1999).
[21]
STRUCTURE BY NMR OF 280-341, INTERACTION WITH CD2 PEPTIDE, AND
SUBCELLULAR LOCATION.
PubMed=12426371; DOI=10.1093/emboj/cdf602;
Freund C., Kuhne R., Yang H., Park S., Reinherz E.L., Wagner G.;
"Dynamic interaction of CD2 with the GYF and the SH3 domain of
compartmentalized effector molecules.";
EMBO J. 21:5985-5995(2002).
[22]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 256-341 IN COMPLEX WITH
TXNL4A, AND INTERACTION WITH TXNL4A.
PubMed=17467737; DOI=10.1016/j.jmb.2007.03.077;
Nielsen T.K., Liu S., Luhrmann R., Ficner R.;
"Structural basis for the bifunctionality of the U5 snRNP 52K protein
(CD2BP2).";
J. Mol. Biol. 369:902-908(2007).
[23]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 280-341 IN COMPLEX WITH
PQBP1 AND TXNL4A, AND SUBUNIT.
PubMed=24781215; DOI=10.1038/ncomms4822;
Mizuguchi M., Obita T., Serita T., Kojima R., Nabeshima Y.,
Okazawa H.;
"Mutations in the PQBP1 gene prevent its interaction with the
spliceosomal protein U5-15 kD.";
Nat. Commun. 5:3822-3822(2014).
-!- FUNCTION: Involved in pre-mRNA splicing as component of the U5
snRNP complex that is involved in spliceosome assembly.
{ECO:0000269|PubMed:15840814}.
-!- SUBUNIT: Component of the U5 snRNP complex composed of the U5
snRNA and at least PRPF6, PRPF8, SNRNP200, EFTUD2, SNRNP40, DDX23,
TXNL4A and CD2BP2. Interacts directly with TXNL4A and PRPF6.
Interacts (via GYF domain) with CD2 (via Pro-rich sequence in the
cytoplasmic domain). Interacts with PQBP1.
{ECO:0000269|PubMed:12426371, ECO:0000269|PubMed:15840814,
ECO:0000269|PubMed:16723661, ECO:0000269|PubMed:17467737,
ECO:0000269|PubMed:24781215, ECO:0000269|PubMed:9843987}.
-!- INTERACTION:
P06729:CD2; NbExp=3; IntAct=EBI-768015, EBI-3912464;
P62136:PPP1CA; NbExp=2; IntAct=EBI-768015, EBI-357253;
P36873:PPP1CC; NbExp=3; IntAct=EBI-768015, EBI-356283;
O94906:PRPF6; NbExp=5; IntAct=EBI-768015, EBI-536755;
P14678-2:SNRPB; NbExp=5; IntAct=EBI-768015, EBI-372475;
P83876:TXNL4A; NbExp=2; IntAct=EBI-768015, EBI-746539;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly
nuclear.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF104222; AAC84141.1; -; mRNA.
EMBL; AK315708; BAG38069.1; -; mRNA.
EMBL; CH471192; EAW52260.1; -; Genomic_DNA.
EMBL; BC000495; AAH00495.1; -; mRNA.
EMBL; BC001947; AAH01947.1; -; mRNA.
EMBL; AB033004; BAA86492.1; -; mRNA.
CCDS; CCDS10675.1; -.
RefSeq; NP_001230575.1; NM_001243646.1.
RefSeq; NP_006101.1; NM_006110.2.
UniGene; Hs.202677; -.
PDB; 1GYF; NMR; -; A=280-341.
PDB; 1L2Z; NMR; -; A=280-341.
PDB; 1SYX; X-ray; 2.34 A; B/D/F=262-341.
PDB; 4BWS; X-ray; 2.50 A; C/F=280-341.
PDBsum; 1GYF; -.
PDBsum; 1L2Z; -.
PDBsum; 1SYX; -.
PDBsum; 4BWS; -.
ProteinModelPortal; O95400; -.
SMR; O95400; -.
BioGrid; 115690; 81.
CORUM; O95400; -.
ELM; O95400; -.
IntAct; O95400; 26.
MINT; MINT-99472; -.
STRING; 9606.ENSP00000304903; -.
iPTMnet; O95400; -.
PhosphoSitePlus; O95400; -.
BioMuta; CD2BP2; -.
EPD; O95400; -.
MaxQB; O95400; -.
PaxDb; O95400; -.
PeptideAtlas; O95400; -.
PRIDE; O95400; -.
DNASU; 10421; -.
Ensembl; ENST00000305596; ENSP00000304903; ENSG00000169217.
Ensembl; ENST00000569466; ENSP00000456935; ENSG00000169217.
GeneID; 10421; -.
KEGG; hsa:10421; -.
UCSC; uc002dxr.4; human.
CTD; 10421; -.
DisGeNET; 10421; -.
EuPathDB; HostDB:ENSG00000169217.8; -.
GeneCards; CD2BP2; -.
HGNC; HGNC:1656; CD2BP2.
HPA; HPA041508; -.
HPA; HPA061309; -.
MIM; 604470; gene.
neXtProt; NX_O95400; -.
OpenTargets; ENSG00000169217; -.
PharmGKB; PA26209; -.
eggNOG; KOG2950; Eukaryota.
eggNOG; ENOG4111KF5; LUCA.
GeneTree; ENSGT00390000012483; -.
HOGENOM; HOG000007061; -.
HOVERGEN; HBG056920; -.
InParanoid; O95400; -.
KO; K13099; -.
OMA; TGNMDIY; -.
OrthoDB; EOG091G0MVR; -.
PhylomeDB; O95400; -.
TreeFam; TF313042; -.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
ChiTaRS; CD2BP2; human.
EvolutionaryTrace; O95400; -.
GeneWiki; CD2BP2; -.
GenomeRNAi; 10421; -.
PRO; PR:O95400; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000169217; -.
CleanEx; HS_CD2BP2; -.
ExpressionAtlas; O95400; baseline and differential.
Genevisible; O95400; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0005682; C:U5 snRNP; IDA:BHF-UCL.
GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:BHF-UCL.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0010923; P:negative regulation of phosphatase activity; IDA:UniProtKB.
GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; NAS:BHF-UCL.
CDD; cd00072; GYF; 1.
Gene3D; 3.30.1490.40; -; 1.
InterPro; IPR003169; GYF.
InterPro; IPR035445; GYF-like_domain.
Pfam; PF02213; GYF; 1.
SMART; SM00444; GYF; 1.
SUPFAM; SSF55277; SSF55277; 1.
PROSITE; PS50829; GYF; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation.
CHAIN 1 341 CD2 antigen cytoplasmic tail-binding
protein 2.
/FTId=PRO_0000089437.
DOMAIN 280 338 GYF. {ECO:0000255|PROSITE-
ProRule:PRU00101}.
MOD_RES 44 44 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9CWK3}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 49 49 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17693683,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:19367720,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 194 194 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 195 195 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
CROSSLNK 26 26 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 231 231 G -> D (in dbSNP:rs13330462).
/FTId=VAR_050772.
VARIANT 262 262 T -> I (in dbSNP:rs34391305).
/FTId=VAR_050773.
STRAND 282 293 {ECO:0000244|PDB:1SYX}.
STRAND 296 300 {ECO:0000244|PDB:1SYX}.
HELIX 301 309 {ECO:0000244|PDB:1SYX}.
STRAND 318 324 {ECO:0000244|PDB:1SYX}.
HELIX 332 334 {ECO:0000244|PDB:1SYX}.
HELIX 337 340 {ECO:0000244|PDB:1SYX}.
SEQUENCE 341 AA; 37646 MW; 8E9A7EE0C40474D5 CRC64;
MPKRKVTFQG VGDEEDEDEI IVPKKKLVDP VAGSGGPGSR FKGKHSLDSD EEEDDDDGGS
SKYDILASED VEGQEAATLP SEGGVRITPF NLQEEMEEGH FDADGNYFLN RDAQIRDSWL
DNIDWVKIRE RPPGQRQASD SEEEDSLGQT SMSAQALLEG LLELLLPRET VAGALRRLGA
RGGGKGRKGP GQPSSPQRLD RLSGLADQMV ARGNLGVYQE TRERLAMRLK GLGCQTLGPH
NPTPPPSLDM FAEELAEEEL ETPTPTQRGE AESRGDGLVD VMWEYKWENT GDAELYGPFT
SAQMQTWVSE GYFPDGVYCR KLDPPGGQFY NSKRIDFDLY T


Related products :

Catalog number Product name Quantity
EIAAB06308 CD2 antigen cytoplasmic tail-binding protein 2,CD2 cytoplasmic domain-binding protein 2,CD2 tail-binding protein 2,CD2BP2,Homo sapiens,Human,KIAA1178
EIAAB06309 CD2 antigen cytoplasmic tail-binding protein 2,CD2 cytoplasmic domain-binding protein 2,CD2 tail-binding protein 2,Cd2bp2,Mouse,Mus musculus
CD2B2_MOUSE Mouse ELISA Kit FOR CD2 antigen cytoplasmic tail-binding protein 2 96T
CSB-EL004915HU Human CD2 antigen cytoplasmic tail-binding protein 2(CD2BP2) ELISA kit 96T
CSB-EL004915MO Mouse CD2 antigen cytoplasmic tail-binding protein 2(CD2BP2) ELISA kit 96T
CSB-EL004915MO Mouse CD2 antigen cytoplasmic tail-binding protein 2(CD2BP2) ELISA kit SpeciesMouse 96T
CSB-EL004915HU Human CD2 antigen cytoplasmic tail-binding protein 2(CD2BP2) ELISA kit SpeciesHuman 96T
CD2B2_MOUSE ELISA Kit FOR CD2 antigen cytoplasmic tail-binding protein 2; organism: Mouse; gene name: Cd2bp2 96T
CD2B2_HUMAN ELISA Kit FOR CD2 antigen cytoplasmic tail-binding protein 2; organism: Human; gene name: CD2BP2 96T
APPL2 APPBP2 Gene amyloid beta precursor protein (cytoplasmic tail) binding protein 2
CD300C CD2BP2 Gene CD2 (cytoplasmic tail) binding protein 2
CSB-EL001951RA Rat amyloid beta precursor protein (cytoplasmic tail) binding protein 2 (APPBP2) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL001951HU Human amyloid beta precursor protein (cytoplasmic tail) binding protein 2 (APPBP2) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL001951MO Mouse amyloid beta precursor protein (cytoplasmic tail) binding protein 2 (APPBP2) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
EIAAB31641 Mouse,Mus musculus,PMF-1-binding protein,Pmfbp1,Polyamine-modulated factor 1-binding protein 1,Sperm tail-associated protein,Stap
CSB-PA001951GA01HU Rabbit anti-human amyloid beta precursor protein (cytoplasmic tail) binding protein 2 polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
CSB-PA001951GA01HU Rabbit anti-human amyloid beta precursor protein (cytoplasmic tail) binding protein 2 polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
CSB-EL004915HU Human CD2 (cytoplasmic tail) binding protein 2 (CD2BP2) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL004915MO Mouse CD2 (cytoplasmic tail) binding protein 2 (CD2BP2) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
EIAAB09918 ATPBD3,ATP-binding domain-containing protein 3,Cancer-associated gene protein,CTU1,Cytoplasmic tRNA 2-thiolation protein 1,Cytoplasmic tRNA adenylyltransferase 1,Homo sapiens,Human,NCS6
15-288-22028F 1.2-dihydroxy-3-keto-5-methylthiopentene dioxygenase - EC 1.13.-.-; Aci-reductone dioxygenase; ARD; Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1; MTCBP-1; Submergence-in 0.1 mg
15-288-22028F 1.2-dihydroxy-3-keto-5-methylthiopentene dioxygenase - EC 1.13.-.-; Aci-reductone dioxygenase; ARD; Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1; MTCBP-1; Submergence-in 0.05 mg
10-288-22028F 1.2-dihydroxy-3-keto-5-methylthiopentene dioxygenase - EC 1.13.-.-; Aci-reductone dioxygenase; ARD; Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1; MTCBP-1; Submergence-in 0.05 mg
10-288-22028F 1.2-dihydroxy-3-keto-5-methylthiopentene dioxygenase - EC 1.13.-.-; Aci-reductone dioxygenase; ARD; Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1; MTCBP-1; Submergence-in 0.1 mg
EIAAB09916 Atpbd3,ATP-binding domain-containing protein 3,Ctu1,Cytoplasmic tRNA 2-thiolation protein 1,Cytoplasmic tRNA adenylyltransferase 1,Mouse,Mus musculus,Ncs6


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur